NCBI Conserved Domain Search

Conserved domains on [gi|1331970929|gb|PNK12315|]

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hypothetical protein CEP09_15005 [Cylindrospermopsis raciborskii S06]

Protein Classification

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

PksD

COG3321

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...

673-2008

0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 1320.26 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  673 DSNDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDELEQTL----PELFNNPAYVKAGAVLEGVELFDATFFGYS 748
Cdd:COG3321      2 ADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAyydpDPDAPGKTYVRWGGFLDDVDEFDALFFGIS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  749 PKEAAVTDPQQRILLECAWEAFERAGYNPETYP-EPVGVYAGSSLSTYLLNNIGSALGIiteqpfietdmeQFQAKIGND 827
Cdd:COG3321     82 PREAEAMDPQQRLLLEVAWEALEDAGYDPESLAgSRTGVFVGASSNDYALLLLADPEAI------------DAYALTGNA 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  828 RSYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFD 907
Cdd:COG3321    150 KSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFD 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  908 AEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGALKmGYTAPSVDGQADVISEAIAIADIDASTIGYVEA 987
Cdd:COG3321    230 ADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEA 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  988 HGTATQLGDPIEVAGLARAFQRSTDsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRID 1067
Cdd:COG3321    309 HGTGTPLGDPIEAAALTAAFGQGRP---ADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1068 FDATPFFVNTELREWSRNGYPRRAGVSSFGVGGTNSHIVLEESPVKQPTlfSSLPERSHHLLTLSAHTQEALHELVQRYI 1147
Cdd:COG3321    386 FENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPA--AAAAARPPQLLVLSAKTEEALRALAARLA 463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1148 QHNETHLDINLGDLCFTANTGRKHFEHRLAVVAESIPGLQAQLETAQTAISAQ-----KKNAPPTIAFLFTGQGSQYINM 1222
Cdd:COG3321    464 AFLEAHPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPgvvtgAAAAAPKVAFLFPGQGSQYVGM 543

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1223 GRTLYDTESTFRAALDRCETILQNLGIESILSVIFGSSEHGLsLDDTAYTQPALFAIEYALYQLWKSWGIQPSVVIGHSV 1302
Cdd:COG3321    544 GRELYETEPVFRAALDECDALLRPHLGWSLREVLFPDEEESR-LDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSV 622

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1303 GEYVSACVAGVFSLEDGLKLIAERGRLIQALPRDGSMVSVMASEKRIADIILPYGGqVGIAAINGPQSVVISGQQQAIDA 1382
Cdd:COG3321    623 GEYAAACVAGVLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAGYDG-VSIAAVNGPRSTVVSGPAEAVEA 701

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1383 ICAILETEGIKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHEscpdelpITTAEYWVRHVR 1462
Cdd:COG3321    702 LAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGE-------ALDADYWVRHLR 774

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1463 QPVRFAAGMESLEGQGVNVFIEIGPKPVLLGMGRDCLTEQE-GLWLPSLRPKQDDWQQVLSSLRDLYLAGVTVDWSSFDQ 1541
Cdd:COG3321    775 QPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAGdAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYP 854

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1542 GYARRRVPLPTYPWQRERHWVEPIIRQRQSVLQATNTTKLTRNASVAQHPLLGQRLHLSRTQEIYFQTFIHSDFPIWVAD 1621
Cdd:COG3321    855 GRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVA 934

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1622 HKVFGNVIIPGVAYFEMALAAGKALKPDSIFWLEDVSIAQALIIPDEGQTVQIVLSPQEESAyffeILSLEKENSWVLHA 1701
Cdd:COG3321    935 LAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAAL----AAAAALALLAAAAL 1010

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1702 SGKLVAQEQVLETEPIDLIALQAHCSEEVSVDVLYQEEMARRLDMGPMMRGVKQLWRYPLSFAKSHDAIALAKVSLPEIL 1781
Cdd:COG3321   1011 LLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAAL 1090

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1782 LHESNAYQFHPVILDAGLQMITVSYPEANQGQTYVPVGIEGLQVYGRPSSELWCRAQYRPPLDTDQRQGIDLLPKKLIAD 1861
Cdd:COG3321   1091 AAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAA 1170

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1862 LHLFDTQGRVVAIMFGVQSVLVGREAMLRSQDTWRNWLYQVLWKPQACFGLLPNYLPTPDKIRKRLETKLATLIIEANLA 1941
Cdd:COG3321   1171 AALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAA 1250

                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331970929 1942 TYAIAYTQLERLSLAYVVAAFRQMGWLFQPGERFSTAQKVSALGIVDQHRQLFARLLDILAEADILR 2008
Cdd:COG3321   1251 AAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAA 1317

EntF

COG1020

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...

5-663

0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 601.46 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    5 ESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERS 83
Cdd:COG1020    457 ERQQLLAEWNATAAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERS 536

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   84 AELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLaltiPALQeCQTVYLDQEifeydfhflai 163
Cdd:COG1020    537 LEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL----PELG-VPVLALDAL----------- 600

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  164 akllhnqylrllhfyfytLIQQCQATSVSQGIQtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:COG1020    601 ------------------ALAAEPATNPPVPVT----PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPG 658

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  244 VRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNgnkSTSLALCE 323
Cdd:COG1020    659 DRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP---EALPSLRL 735

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  324 VITTGEQmqITPAVANLFQKT--GAMLHNHYGATEFQ-DATTHTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVPLG 400
Cdd:COG1020    736 VLVGGEA--LPPELVRRWRARlpGARLVNLYGPTETTvDSTYYEVTPPDADGGS-VPIGRPIANTRVYVLDAHLQPVPVG 812

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  401 GEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANEnaKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIES 480
Cdd:COG1020    813 VPGELYIGGAGLARGYLNRPELTAERFVADPFGFPG--ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEA 890

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  481 VLASHQAVRECAVVAREIA-GHTQLVGYIIAKDTLnlsfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:COG1020    891 ALLQHPGVREAVVVAREDApGDKRLVAYVVPEAGA----AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  560 ALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYP 639
Cdd:COG1020    967 ALPAP--AAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAA 1044

                          650       660
                   ....*....|....*....|....
gi 1331970929  640 TIQTLAQYIDCQGDTTSSDTASRH 663
Cdd:COG1020   1045 AAAAAAAAAAAAAAAAAPLAAAAA 1068

KR_2_FAS_SDR_x

cd08955

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...

2353-2747

5.06e-127

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187658 [Multi-domain] Cd Length: 376 Bit Score: 405.13 E-value: 5.06e-127

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2353 LLNRVPNIQEIVHCWSM----VSTDLDRATIFSCSSTLHLVQAL--ANYPKNPRLSLVTLGAQAVN-EHHVQNVVGAALW 2425
Cdd:cd08955      1 ALLGSAPLAGVVHLWSLdaprEEPADAASQELGCASALHLVQALskAGLRRAPRLWLVTRGAQSVLaDGEPVSPAQAPLW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2426 GMGKVIALEHPELQVAQMDLDPNGKVKAQVEVLRDELLARKDpasamsvpdlqtrphEKQIAFREQTRYVARLSPLDRPN 2505
Cdd:cd08955     81 GLGRVIALEHPELRCGLVDLDPEATAAEEAEALLAELLAADA---------------EDQVALRGGARYVARLVRAPARP 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2506 pgekgtqealtFRDDGSYLIAGGLGGLGLVVARFLVTNGAKYLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAE 2585
Cdd:cd08955    146 -----------LRPDATYLITGGLGGLGLLVAEWLVERGARHLVLTGRRAPSAAARQAIAALEEAGAEVVVLAADVSDRD 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2586 QLAQALSAV--TYPPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQ 2663
Cdd:cd08955    215 ALAAALAQIraSLPPLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLDFFVLFSSVASLLGSPGQ 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2664 ANHAAANAFLDGLASYRRHLGLPSLSINWGTWSEVGIAARLELDKLSSKQGEGTITLGQGLQILEQLLKDENGvyQVGVM 2743
Cdd:cd08955    295 ANYAAANAFLDALAHYRRARGLPALSINWGPWAEVGMAASLARQARLEARGVGAISPAAGLQALGQLLRTGST--QVGVA 372


                   ....
gi 1331970929 2744 PINW 2747
Cdd:cd08955    373 PVDW 376

Methyltransf_12

pfam08242

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

2113-2213

7.00e-25

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 100.91 E-value: 7.00e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2113 LEIGAGTGGTTAYLLPHLPGdqTKYVFTDISAFFLAKAEERFKDYPFVRYQVLDIEQAPQAQGFEPQiYDLIVAADVLHA 2192
Cdd:pfam08242    1 LEIGCGTGTLLRALLEALPG--LEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGS-FDVVVASNVLHH 77

                           90       100
                   ....*....|....*....|.
gi 1331970929 2193 TSDLRQTLVHIRQLLAPGGML 2213
Cdd:pfam08242   78 LADPRAVLRNIRRLLKPGGVL 98

PKS_PP

smart00823

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...

2795-2881

9.49e-25

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.

Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 100.02 E-value: 9.49e-25

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  2795 LENAPPKEGLTLLQAHVREQVSQVLGIDTKTLLaEQDVGFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQALV 2874
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAI-DPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79


                    ....*..
gi 1331970929  2875 NYLANEL 2881
Cdd:smart00823   80 EHLAAEL 86

Name

Accession

Description

Interval

E-value

PksD

COG3321

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...

673-2008

0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 1320.26 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  673 DSNDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDELEQTL----PELFNNPAYVKAGAVLEGVELFDATFFGYS 748
Cdd:COG3321      2 ADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAyydpDPDAPGKTYVRWGGFLDDVDEFDALFFGIS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  749 PKEAAVTDPQQRILLECAWEAFERAGYNPETYP-EPVGVYAGSSLSTYLLNNIGSALGIiteqpfietdmeQFQAKIGND 827
Cdd:COG3321     82 PREAEAMDPQQRLLLEVAWEALEDAGYDPESLAgSRTGVFVGASSNDYALLLLADPEAI------------DAYALTGNA 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  828 RSYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFD 907
Cdd:COG3321    150 KSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFD 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  908 AEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGALKmGYTAPSVDGQADVISEAIAIADIDASTIGYVEA 987
Cdd:COG3321    230 ADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEA 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  988 HGTATQLGDPIEVAGLARAFQRSTDsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRID 1067
Cdd:COG3321    309 HGTGTPLGDPIEAAALTAAFGQGRP---ADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1068 FDATPFFVNTELREWSRNGYPRRAGVSSFGVGGTNSHIVLEESPVKQPTlfSSLPERSHHLLTLSAHTQEALHELVQRYI 1147
Cdd:COG3321    386 FENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPA--AAAAARPPQLLVLSAKTEEALRALAARLA 463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1148 QHNETHLDINLGDLCFTANTGRKHFEHRLAVVAESIPGLQAQLETAQTAISAQ-----KKNAPPTIAFLFTGQGSQYINM 1222
Cdd:COG3321    464 AFLEAHPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPgvvtgAAAAAPKVAFLFPGQGSQYVGM 543

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1223 GRTLYDTESTFRAALDRCETILQNLGIESILSVIFGSSEHGLsLDDTAYTQPALFAIEYALYQLWKSWGIQPSVVIGHSV 1302
Cdd:COG3321    544 GRELYETEPVFRAALDECDALLRPHLGWSLREVLFPDEEESR-LDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSV 622

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1303 GEYVSACVAGVFSLEDGLKLIAERGRLIQALPRDGSMVSVMASEKRIADIILPYGGqVGIAAINGPQSVVISGQQQAIDA 1382
Cdd:COG3321    623 GEYAAACVAGVLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAGYDG-VSIAAVNGPRSTVVSGPAEAVEA 701

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1383 ICAILETEGIKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHEscpdelpITTAEYWVRHVR 1462
Cdd:COG3321    702 LAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGE-------ALDADYWVRHLR 774

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1463 QPVRFAAGMESLEGQGVNVFIEIGPKPVLLGMGRDCLTEQE-GLWLPSLRPKQDDWQQVLSSLRDLYLAGVTVDWSSFDQ 1541
Cdd:COG3321    775 QPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAGdAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYP 854

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1542 GYARRRVPLPTYPWQRERHWVEPIIRQRQSVLQATNTTKLTRNASVAQHPLLGQRLHLSRTQEIYFQTFIHSDFPIWVAD 1621
Cdd:COG3321    855 GRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVA 934

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1622 HKVFGNVIIPGVAYFEMALAAGKALKPDSIFWLEDVSIAQALIIPDEGQTVQIVLSPQEESAyffeILSLEKENSWVLHA 1701
Cdd:COG3321    935 LAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAAL----AAAAALALLAAAAL 1010

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1702 SGKLVAQEQVLETEPIDLIALQAHCSEEVSVDVLYQEEMARRLDMGPMMRGVKQLWRYPLSFAKSHDAIALAKVSLPEIL 1781
Cdd:COG3321   1011 LLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAAL 1090

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1782 LHESNAYQFHPVILDAGLQMITVSYPEANQGQTYVPVGIEGLQVYGRPSSELWCRAQYRPPLDTDQRQGIDLLPKKLIAD 1861
Cdd:COG3321   1091 AAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAA 1170

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1862 LHLFDTQGRVVAIMFGVQSVLVGREAMLRSQDTWRNWLYQVLWKPQACFGLLPNYLPTPDKIRKRLETKLATLIIEANLA 1941
Cdd:COG3321   1171 AALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAA 1250

                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331970929 1942 TYAIAYTQLERLSLAYVVAAFRQMGWLFQPGERFSTAQKVSALGIVDQHRQLFARLLDILAEADILR 2008
Cdd:COG3321   1251 AAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAA 1317

PKS

cd00833

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...

675-1107

0e+00

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.

Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 609.94 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  675 NDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDELEQTL---PELFNNPAYVKAGAVLEGVELFDATFFGYSPKE 751
Cdd:cd00833      1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGyypDPGKPGKTYTRRGGFLDDVDAFDAAFFGISPRE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  752 AAVTDPQQRILLECAWEAFERAGYNPET-YPEPVGVYAGSSLSTYLLNNIGSALGIiteqpfietdmEQFQAkIGNDRSY 830
Cdd:cd00833     81 AEAMDPQQRLLLEVAWEALEDAGYSPESlAGSRTGVFVGASSSDYLELLARDPDEI-----------DAYAA-TGTSRAF 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  831 LATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFDAEA 910
Cdd:cd00833    149 LANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADA 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  911 QGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGALKmGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGT 990
Cdd:cd00833    229 DGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTK-GITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGT 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  991 ATQLGDPIEVAGLARAFQRSTDsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDA 1070
Cdd:cd00833    308 GTPLGDPIEVEALAKVFGGSRS---ADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEE 384

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1331970929 1071 TPFFVNTELREWSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00833    385 SPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421

EntF

COG1020

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...

5-663

0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 601.46 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    5 ESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERS 83
Cdd:COG1020    457 ERQQLLAEWNATAAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERS 536

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   84 AELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLaltiPALQeCQTVYLDQEifeydfhflai 163
Cdd:COG1020    537 LEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL----PELG-VPVLALDAL----------- 600

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  164 akllhnqylrllhfyfytLIQQCQATSVSQGIQtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:COG1020    601 ------------------ALAAEPATNPPVPVT----PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPG 658

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  244 VRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNgnkSTSLALCE 323
Cdd:COG1020    659 DRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP---EALPSLRL 735

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  324 VITTGEQmqITPAVANLFQKT--GAMLHNHYGATEFQ-DATTHTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVPLG 400
Cdd:COG1020    736 VLVGGEA--LPPELVRRWRARlpGARLVNLYGPTETTvDSTYYEVTPPDADGGS-VPIGRPIANTRVYVLDAHLQPVPVG 812

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  401 GEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANEnaKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIES 480
Cdd:COG1020    813 VPGELYIGGAGLARGYLNRPELTAERFVADPFGFPG--ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEA 890

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  481 VLASHQAVRECAVVAREIA-GHTQLVGYIIAKDTLnlsfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:COG1020    891 ALLQHPGVREAVVVAREDApGDKRLVAYVVPEAGA----AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  560 ALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYP 639
Cdd:COG1020    967 ALPAP--AAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAA 1044

                          650       660
                   ....*....|....*....|....
gi 1331970929  640 TIQTLAQYIDCQGDTTSSDTASRH 663
Cdd:COG1020   1045 AAAAAAAAAAAAAAAAAPLAAAAA 1068

A_NRPS_VisG_like

cd17651

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...

29-562

0e+00

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 576.60 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   29 FEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYP 108
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  109 GDRIEYMLRDSDARILLTSTDVAKKLALTIPALqecqtVYLDQEifeydfhflaiakllhnqylrllhfyfytliQQCQA 188
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPALAGELAVELVAV-----TLLDQP-------------------------------GAAAG 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  189 TSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLG 268
Cdd:cd17651    125 ADAEPDPALD--ADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAG 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  269 GILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMQITPAVANLFQK-TGAM 347
Cdd:cd17651    203 ATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGlPGLR 282

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  348 LHNHYGATEFQDATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKF 427
Cdd:cd17651    283 LHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERF 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  428 IPNPFGANEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE-IAGHTQLVG 506
Cdd:cd17651    363 VPDPFVPGA---RMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREdRPGEKRLVA 439

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929  507 YIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17651    440 YVVGDPEAPVDAAE----LRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491

mycolic_Pks13

NF040607

polyketide synthase Pks13;

628-1563

4.22e-170

polyketide synthase Pks13;

Pssm-ID: 468580 [Multi-domain] Cd Length: 1671 Bit Score: 573.41 E-value: 4.22e-170

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  628 INLSAVSLFQYPTIQTLAQYIdCQGDTTSSDTASRHKKVRKKQSGDSNDIAIISVAGRFPGA-ETIEQFWHNLCNGVESI 706
Cdd:NF040607    54 VTLTATVAYQHPTIASLATRI-IEGEPEVAADDDDDADWSRRPRSDAHDIAIVGLATRFPGAgNTPEEMWEALIEGRDGI 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  707 TLFSDDELEqtlpELFNNPAYVKA-------GAVLEGVELFDATFFGYSPKEAAVTDPQQRILLECAWEAFERAGYNPET 779
Cdd:NF040607   133 TDLPEGRWS----EFAADPRIAERvakantrGGYLDDIKGFDAEFFALSPLEAENVDPQQRLALELTWEALEHARIPASS 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  780 YP-EPVGVYAGSSLSTY-LLnnigSALGIITEQPFietdmeqfqAKIGNDRSYLATRISYKLNLKGPSVNVQTACSTSLV 857
Cdd:NF040607   209 LRgEPVGVFIGSSNNDYqML----AVADPAEAHPY---------ALTGTSSSIIANRVSYFFDFRGPSVAVDTACSSSLV 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  858 AVHMACQSLISGECQMALAGGISVVVPQKGGYLYEE-GMVRSQDGHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDN 936
Cdd:NF040607   276 AVHQAVRALRSGEADVAVAGGVNMLLTPAVTLGFDElGGVLAPDGRIKAFSSDADGMVRSEGGGVVVLKRLADARRDGDT 355

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  937 IMAVIKATAINNDGAlKMGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARafqrstdsVLG 1016
Cdd:NF040607   356 ILAVIAGSAVNSDGR-SNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDPIEADALGR--------VVG 426

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1017 KQQCA-----IGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFVNTELREWSR-NGYPrR 1090
Cdd:NF040607   427 RGRDAdkpalLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPYIDFDAEHLKVVDEPTEWPRySGHA-V 505

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1091 AGVSSFGVGGTNSHIVLEE------SPVKQPTLFSSLPERShhLLTLSAHTQEALHELVQRYIQHNETHLDINL------ 1158
Cdd:NF040607   506 AGVSGFGFGGTNAHVVVREvlpadlVEPEAQPDEDTEAELA--GLTAEAKRLLAEAELAAEFAPAAPEGPVVPLpvsgfl 583

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1159 ----------------------GDLCFTANT--GRKHFEHRLAVVA----ESIPGLQAQLE--TAQTAISAqkkNAPPTI 1208
Cdd:NF040607   584 psrrraaaadladwleseegraTPLADVARAlaRRNHGRSRAVVLAhtheEAIKGLRAVAEgkPGPGVFSA---DAPAAN 660

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1209 --AFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGIESILSVIfgssehglsLDD-----TAYTQPALFAIEY 1281
Cdd:NF040607   661 gpVWVLSGFGSQHRKMAKQLYLENPVFAARIDEVDELVQDESGYSIVELI---------LDDeqtydIETAQVGIFAIQI 731

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1282 ALYQLWKSWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLI----QALPRD--GSMVSVMASEKRIADIILP 1355
Cdd:NF040607   732 ALADLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAVRVICHRSRLMgegeAMLPGDdiRLMALVEYSAEEIETVLAD 811

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1356 YGGqVGIAAINGPQSVVISGQQQAIDAICAILETEGIKSKKLNVSHAFHSplveAMLDSFL-QVAQEVTYSQPQ---IKL 1431
Cdd:NF040607   812 FPD-LEVCVYAAPTHTVIGGPREQVDAIVARAEAEGKFARKLQTKGASHT----SQMDPLLgELAAELAGIEPQpltVGL 886

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1432 ISNV-TGTL--ASHEscpdelPITTAEYWVRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLgMGRDCLTEQEGL--- 1505
Cdd:NF040607   887 YSSVdRGTFyrPGHE------PIHDVDYWVKGLRHSVWFTQAVRKAVDAGHTTFLELAPNPVAL-MSVAATTFAAGLhda 959

                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331970929 1506 -WLPSLRPKQDDWQQVLSSLRDLYLAGVTVDWSS-FDQG-YArrrvPLPTYPWQRERHWVE 1563
Cdd:NF040607   960 qLIPTLKRKEDESESVLNALAQLYVHGHDVDLRSlFGAGdYA----DIPRTRFKRKPYWLD 1016

PKS_KS

smart00825

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...

677-1109

1.29e-151

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.

Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 472.20 E-value: 1.29e-151

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   677 IAIISVAGRFPGAETIEQFWHNLCNGvesitlfsddeleqtlpelfnnpayvkagavLEGVELFDATFFGYSPKEAAVTD 756
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG-------------------------------LDDVDLFDAAFFGISPREAEAMD 49

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   757 PQQRILLECAWEAFERAGYNPETYPE-PVGVYAGSSLSTYllnnigsalgiiteqpfietdmeqfqakigndrsylatri 835
Cdd:smart00825   50 PQQRLLLEVAWEALEDAGIDPESLRGsRTGVFVGVSSSDY---------------------------------------- 89

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   836 syklnlkgpSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFDAEAQGTIF 915
Cdd:smart00825   90 ---------SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVR 160

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   916 GNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAlKMGYTAPSVDGqadviseaiaiadidastigyveahgtatqlg 995
Cdd:smart00825  161 GEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGR-SNGITAPSGPA-------------------------------- 207

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   996 dpievaglarafqrstdsvlgkqQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFV 1075
Cdd:smart00825  208 -----------------------QLLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRV 264

                           410       420       430
                    ....*....|....*....|....*....|....
gi 1331970929  1076 NTELREWSRNGYPRRAGVSSFGVGGTNSHIVLEE 1109
Cdd:smart00825  265 PTELTPWPPPGRPRRAGVSSFGFGGTNAHVILEE 298

PRK12467

peptide synthase; Provisional

5-645

7.38e-148

peptide synthase; Provisional

Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 519.72 E-value: 7.38e-148

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    5 ESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERS 83
Cdd:PRK12467  1555 ERRQILEGWNATHTGYPlARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERS 1634

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   84 AELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQEifeydfhflai 163
Cdd:PRK12467  1635 LEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL----PLPDGLRSLVLDQE----------- 1699

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  164 akllhnqylrllhfyfytliQQCQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:PRK12467  1700 --------------------DDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAA 1759

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  244 VRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKL-FLPVI--ALLQLAEAVNGnkstSLA 320
Cdd:PRK12467  1760 DVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLhFVPSMlqQLLQMDEQVEH----PLS 1835

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  321 LCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATEFQDATTHTL--KGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVP 398
Cdd:PRK12467  1836 LRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTcrRKDLEGRDS-VPIGQPIANLSTYILDASLNPVP 1914

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  399 LGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGanENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEI 478
Cdd:PRK12467  1915 IGVAGELYLGGVGLARGYLNRPALTAERFVADPFG--TVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEI 1992

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  479 ESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDK----LEPILRQYSEAVLPEYMIPTRFINISNMPLTPSG 554
Cdd:PRK12467  1993 EARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDDEaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTPNG 2072

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  555 KLDRRALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKfLCETFNINLSAVS 634
Cdd:PRK12467  2073 KLDRKALPAP--DASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVS-RARQAGIRFTPKD 2149

                          650
                   ....*....|.
gi 1331970929  635 LFQYPTIQTLA 645
Cdd:PRK12467  2150 LFQHQTVQSLA 2160

AA-adenyl-dom

TIGR01733

amino acid adenylation domain; This model represents a domain responsible for the specific ...

50-493

4.43e-140

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.

Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 444.40 E-value: 4.43e-140

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   50 TYGELNVRANHLAQHLLSLGC-QPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTST 128
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGGvGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  129 DVAKKLAltipalqecqtvYLDQEIFEYDFHFLAIAkllhnqylrllhfyfytliqqcQATSVSQGIQTQVLPNNLAYCI 208
Cdd:TIGR01733   81 ALASRLA------------GLVLPVILLDPLELAAL----------------------DDAPAPPPPDAPSGPDDLAYVI 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  209 YTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFAL-AE 287
Cdd:TIGR01733  127 YTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAA 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  288 FISQQKIEKLFLPVIALLQLAEAVNGNKSTslaLCEVITTGEQmqITPAVANLFQKT--GAMLHNHYGATEFQ-DATTHT 364
Cdd:TIGR01733  207 LIAEHPVTVLNLTPSLLALLAAALPPALAS---LRLVILGGEA--LTPALVDRWRARgpGARLINLYGPTETTvWSTATL 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  365 LKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANENAKkLYRT 444
Cdd:TIGR01733  282 VDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGAR-LYRT 360

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1331970929  445 GDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV 493
Cdd:TIGR01733  361 GDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409

KR_2_FAS_SDR_x

cd08955

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...

2353-2747

5.06e-127

Pssm-ID: 187658 [Multi-domain] Cd Length: 376 Bit Score: 405.13 E-value: 5.06e-127

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2353 LLNRVPNIQEIVHCWSM----VSTDLDRATIFSCSSTLHLVQAL--ANYPKNPRLSLVTLGAQAVN-EHHVQNVVGAALW 2425
Cdd:cd08955      1 ALLGSAPLAGVVHLWSLdaprEEPADAASQELGCASALHLVQALskAGLRRAPRLWLVTRGAQSVLaDGEPVSPAQAPLW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2426 GMGKVIALEHPELQVAQMDLDPNGKVKAQVEVLRDELLARKDpasamsvpdlqtrphEKQIAFREQTRYVARLSPLDRPN 2505
Cdd:cd08955     81 GLGRVIALEHPELRCGLVDLDPEATAAEEAEALLAELLAADA---------------EDQVALRGGARYVARLVRAPARP 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2506 pgekgtqealtFRDDGSYLIAGGLGGLGLVVARFLVTNGAKYLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAE 2585
Cdd:cd08955    146 -----------LRPDATYLITGGLGGLGLLVAEWLVERGARHLVLTGRRAPSAAARQAIAALEEAGAEVVVLAADVSDRD 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2586 QLAQALSAV--TYPPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQ 2663
Cdd:cd08955    215 ALAAALAQIraSLPPLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLDFFVLFSSVASLLGSPGQ 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2664 ANHAAANAFLDGLASYRRHLGLPSLSINWGTWSEVGIAARLELDKLSSKQGEGTITLGQGLQILEQLLKDENGvyQVGVM 2743
Cdd:cd08955    295 ANYAAANAFLDALAHYRRARGLPALSINWGPWAEVGMAASLARQARLEARGVGAISPAAGLQALGQLLRTGST--QVGVA 372


                   ....
gi 1331970929 2744 PINW 2747
Cdd:cd08955    373 PVDW 376

omega_3_PfaA

TIGR02813

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...

677-1554

2.79e-115

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.

Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 412.09 E-value: 2.79e-115

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  677 IAIISVAGRFPGAETIEQFWHNLCNGVESIT-----------LFSDDELEQtlpelfnNPAYVKAGAVLEGVElFDATFF 745
Cdd:TIGR02813    9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITdvpsdhwakddYYDSDKSEA-------DKSYCKRGGFLPEVD-FNPMEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  746 GYSPKEAAVTDPQQRILLECAWEAFERAGYnPETYPE-----PVGVYAGSSLSTYL--------LNNIGSALGIITE--- 809
Cdd:TIGR02813   81 GLPPNILELTDISQLLSLVVAKEVLNDAGL-PDGYDRdkigiTLGVGGGQKQSSSLnarlqypvLKKVFKASGVEDEdse 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  810 -------QPFIETDMEQFQAKIGNdrsYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGisvV 882
Cdd:TIGR02813  160 mlikkfqDQYIHWEENSFPGSLGN---VISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---V 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  883 VPQKGGYLYeegMVRSQ------DGHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGALKMGY 956
Cdd:TIGR02813  234 CTDNSPFMY---MSFSKtpafttNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIY 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  957 tAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARAFQRSTDSvlgKQQCAIGSVKTNIGHLDEAA 1036
Cdd:TIGR02813  311 -APRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQ---KQHIALGSVKSQIGHTKSTA 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1037 GIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFVNTELREWSR--NGYPRRAGVSSFGVGGTNSHIVLEE-SP-- 1111
Cdd:TIGR02813  387 GTAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPWMQreDGTPRRAGISSFGFGGTNFHMVLEEySPkh 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1112 ----------VKQPTLFSS------LPERSHHLLTLSAHTQEALHELVQRYIQHNETHLDINLGDLCFTANTGrkhfEHR 1175
Cdd:TIGR02813  467 qrddqyrqraVAQTLLFTAanekalVSSLKDWKNKLSAKADDQPYAFNALAVENTLRTIAVALARLGFVAKNA----DEL 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1176 LAVVAESIPGLQAQ-LETAQ--TAISAQKK---NAPPTIAFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGI 1249
Cdd:TIGR02813  543 ITMLEQAITQLEAKsCEEWQlpSGISYRKSalvVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGK 622

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1250 ESILSVIF--------GSSEHGLSLDDTAYTQPALFAIEYALYQLWKSWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLK 1321
Cdd:TIGR02813  623 GALSPVLYpipvfndeSRKAQEEALTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMM 702

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1322 LIAERGRLIQALPRD---GSMVSVMASEKRIADIILPYGGQ---VGIAAINGPQSVVISG----QQQAIDAicaiLETEG 1391
Cdd:TIGR02813  703 LAFSRGQAMAAPTGEadiGFMYAVILAVVGSPTVIANCIKDfegVSIANYNSPTQLVIAGvstqIQIAAKA----LKEKG 778

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1392 IKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHescpDELPITTAeyWVRHVRQPVRFAAGM 1471
Cdd:TIGR02813  779 FKAIPLPVSGAFHTPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSN----DAAAIKKA--LKNHMLQSVHFSEQL 852

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1472 ESLEGQGVNVFIEIGPKPVLLGMGRDCLTEQEG-LWLPSL--RPKQDDWQQVLSSLRDLYLAGVTVDwsSFDQGYARRRV 1548
Cdd:TIGR02813  853 EAMYAAGARVFVEFGPKNILQKLVENTLKDKENeLCAISInpNPKGDSDMQLRQAAVQLAVLGLELT--EIDPYQAEKRP 930


                   ....*.
gi 1331970929 1549 PLPTYP 1554
Cdd:TIGR02813  931 PAATSP 936

AMP-binding

pfam00501

AMP-binding enzyme;

29-469

3.42e-98

AMP-binding enzyme;

Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 323.88 E-value: 3.42e-98

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   29 FEDQAAKRPDAIALIDGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  108 PGDRIEYMLRDSDARILLTstDVAKKLALTIPALQECQTVYldqeifeydfHFLAIAKLLHNQYLRLLHFYFYTLIQQCQ 187
Cdd:pfam00501   81 PAEELAYILEDSGAKVLIT--DDALKLEELLEALGKLEVVK----------LVLVLDRDPVLKEEPLPEEAKPADVPPPP 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  188 ATSVSqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGV----RTLQFCAVSFDFS-CHEIF 262
Cdd:pfam00501  149 PPPPD--------PDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLgpddRVLSTLPLFHDFGlSLGLL 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  263 STLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLP---VIALLQlAEAVNGNKSTSLalcEVITTGeQMQITPAVAN 339
Cdd:pfam00501  221 GPLLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVptlLNMLLE-AGAPKRALLSSL---RLVLSG-GAPLPPELAR 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  340 -LFQKTGAMLHNHYGATEfqdATTHTLKGNPEGWPTLVP--VGRPLHNVQVYILDEA-QQPVPLGGEGEFCIGGIGLARG 415
Cdd:pfam00501  296 rFRELFGGALVNGYGLTE---TTGVVTTPLPLDEDLRSLgsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKG 372

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1331970929  416 YHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIR 469
Cdd:pfam00501  373 YLNDPELTAEAFDEDGW---------YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417

ketoacyl-synt

pfam00109

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...

675-930

2.44e-79

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.

Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 262.96 E-value: 2.44e-79

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  675 NDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDELE----QTLPELFNNPAYVKAGAvLEGVELFDATFFGYSPK 750
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDpdklYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  751 EAAVTDPQQRILLECAWEAFERAGYNPETYPEP-VGVYAGSSLSTY----LLNNIGSALGIiteQPFIetdmeqfqakIG 825
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSrTGVFIGSGIGDYaallLLDEDGGPRRG---SPFA----------VG 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  826 NDRSYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRA 905
Cdd:pfam00109  147 TMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKA 226

                          250       260
                   ....*....|....*....|....*
gi 1331970929  906 FDAEAQGTIFGNGGGLVLLKRLQDA 930
Cdd:pfam00109  227 FDPFADGFVRGEGVGAVVLKRLSDA 251

PKS_KR

smart00822

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...

2535-2697

9.30e-74

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.

Pssm-ID: 214833 [Multi-domain] Cd Length: 180 Bit Score: 243.93 E-value: 9.30e-74

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  2535 VVARFLVTNGAKYLVLVGRRGAREEQQAQL-SELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLND 2611
Cdd:smart00822   15 ALARWLAERGARRLVLLSRSGPDAPGAAALlAELEAAGARVTVVACDVADRDALAAVLAAIpaVEGPLTGVIHAAGVLDD 94

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  2612 GILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLASYRRHLGLPSLSIN 2691
Cdd:smart00822   95 GVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRRARGLPALSIA 174


                    ....*.
gi 1331970929  2692 WGTWSE 2697
Cdd:smart00822  175 WGAWAE 180

pfam08659

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...

2521-2697

5.33e-71

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.

Pssm-ID: 430138 [Multi-domain] Cd Length: 180 Bit Score: 236.30 E-value: 5.33e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2521 GSYLIAGGLGGLGLVVARFLVTNGAKYLVLVGRRGA-REEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYP 2597
Cdd:pfam08659    1 GTYLITGGLGGLGRELARWLAERGARHLVLLSRSAApRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIkaEGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2598 PLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:pfam08659   81 PIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANAFLDALA 160

                          170       180
                   ....*....|....*....|
gi 1331970929 2678 SYRRHLGLPSLSINWGTWSE 2697
Cdd:pfam08659  161 EYRRSQGLPATSINWGPWAE 180

PLN02752

[acyl-carrier protein] S-malonyltransferase

1206-1494

1.07e-36

[acyl-carrier protein] S-malonyltransferase

Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 143.36 E-value: 1.07e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1206 PTIAFLFTGQGSQYINMGRTLYDTEstfrAALDRCETILQNLGIEsILSV-IFGSSEhglSLDDTAYTQPALFAIEYALY 1284
Cdd:PLN02752    38 PTTAFLFPGQGAQAVGMGKEAAEVP----AAKALFDKASEILGYD-LLDVcVNGPKE---KLDSTVVSQPAIYVASLAAV 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1285 QLWKSWGIQPSVV------IGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQAL--PRDGSMVSV--MASEKrIADIIL 1354
Cdd:PLN02752   110 EKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAadAGPSGMVSVigLDSDK-VQELCA 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1355 PYGGQVG------IAAINGPQSVVISGQQQAIDAICAILETEG-IKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQP 1427
Cdd:PLN02752   189 AANEEVGeddvvqIANYLCPGNYAVSGGKKGIDAVEAKAKSFKaRMTVRLAVAGAFHTSFMEPAVDALEAALAAVEIRTP 268

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331970929 1428 QIKLISNVTGtlASHeSCPDELPITTAeywvRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLGM 1494
Cdd:PLN02752   269 RIPVISNVDA--QPH-SDPATIKKILA----RQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGI 328

Methyltransf_12

pfam08242

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

2113-2213

7.00e-25

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 100.91 E-value: 7.00e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2113 LEIGAGTGGTTAYLLPHLPGdqTKYVFTDISAFFLAKAEERFKDYPFVRYQVLDIEQAPQAQGFEPQiYDLIVAADVLHA 2192
Cdd:pfam08242    1 LEIGCGTGTLLRALLEALPG--LEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGS-FDVVVASNVLHH 77

                           90       100
                   ....*....|....*....|.
gi 1331970929 2193 TSDLRQTLVHIRQLLAPGGML 2213
Cdd:pfam08242   78 LADPRAVLRNIRRLLKPGGVL 98

PKS_PP

smart00823

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...

2795-2881

9.49e-25

Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 100.02 E-value: 9.49e-25

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  2795 LENAPPKEGLTLLQAHVREQVSQVLGIDTKTLLaEQDVGFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQALV 2874
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAI-DPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79


                    ....*..
gi 1331970929  2875 NYLANEL 2881
Cdd:smart00823   80 EHLAAEL 86

UbiE

COG2226

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...

2100-2224

1.06e-23

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis

Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 99.30 E-value: 1.06e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2100 ALEQLPPERGWRILEIGAGTGGTTAYLLPHlpgdQTKYVFTDISAFFLAKAEERFKDYPF-VRYQVLDIEQAPqaqgFEP 2178
Cdd:COG2226     14 LLAALGLRPGARVLDLGCGTGRLALALAER----GARVTGVDISPEMLELARERAAEAGLnVEFVVGDAEDLP----FPD 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1331970929 2179 QIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILMEDSEPARW 2224
Cdd:COG2226     86 GSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLA 131

YqjQ

COG0300

Short-chain dehydrogenase [General function prediction only];

2536-2693

1.66e-19

Short-chain dehydrogenase [General function prediction only];

Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 90.70 E-value: 1.66e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGAKyLVLVGRRGAREEQQAQlsELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:COG0300     21 LARALAARGAR-VVLVARDAERLEALAA--ELRAAGARVEVVALDVTDPDAVAALAEAVlaRFGPIDVLVNNAGVGGGGP 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2614 LQQQSWQAFKEVMNPKVAGAWNLHILT----KNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA-SYR---RHLGL 2685
Cdd:COG0300     98 FEELDLEDLRRVFEVNVFGPVRLTRALlplmRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSeSLRaelAPTGV 177


                   ....*...
gi 1331970929 2686 PSLSINWG 2693
Cdd:COG0300    178 RVTAVCPG 185

BioC

TIGR02072

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...

2097-2215

1.81e-13

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]

Pssm-ID: 273953 [Multi-domain] Cd Length: 240 Bit Score: 72.70 E-value: 1.81e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2097 LLSALEQLPPERGWRILEIGAGTGGTTAYLLPHLPgdQTKYVFTDISAFFLAKAEERFKdyPFVRYQVLDIEQAPqaqgF 2176
Cdd:TIGR02072   23 LLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFP--QAEFIALDISAGMLAQAKTKLS--ENVQFICGDAEKLP----L 94

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1331970929 2177 EPQIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:TIGR02072   95 EDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAF 133

AcpP

COG0236

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...

2805-2881

2.07e-13

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 67.57 E-value: 2.07e-13

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929 2805 TLLQAHVREQVSQVLGIDTKTLLAEQDvgFFT-LGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQALVNYLANEL 2881
Cdd:COG0236      4 EELEERLAEIIAEVLGVDPEEITPDDS--FFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79

fabG

PRK12825

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

2540-2677

2.16e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 237218 [Multi-domain] Cd Length: 249 Bit Score: 66.82 E-value: 2.16e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2540 LVTNGAK--------------YLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVI 2603
Cdd:PRK12825    10 LVTGAARglgraialrlaragADVVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAveRFGRIDILV 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2604 HAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNL-----HILTKNQpldF--FVLFSSATSLLGNAGQANHAAANAFLDGL 2676
Cdd:PRK12825    90 NNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLlravvPPMRKQR---GgrIVNISSVAGLPGWPGRSNYAAAKAGLVGL 166


                   .
gi 1331970929 2677 A 2677
Cdd:PRK12825   167 T 167

PP-binding

pfam00550

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...

2811-2869

1.58e-09

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.

Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 56.03 E-value: 1.58e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1331970929 2811 VREQVSQVLGIDTKTLLAEQDvgFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPT 2869
Cdd:pfam00550    3 LRELLAEVLGVPAEEIDPDTD--LFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPT 59

AdoMet_MTases

cd02440

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...

2111-2216

4.87e-09

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).

Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 56.28 E-value: 4.87e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2111 RILEIGAGTGGTTAYLLPHLPGdqtKYVFTDISAFFLAKAEERFKDYPFVRYQVL--DIEQAPQaqgFEPQIYDLIVAAD 2188
Cdd:cd02440      1 RVLDLGCGTGALALALASGPGA---RVTGVDISPVALELARKAAAALLADNVEVLkgDAEELPP---EADESFDVIISDP 74

                           90       100
                   ....*....|....*....|....*....
gi 1331970929 2189 VLHATSDLRQTLVH-IRQLLAPGGMLILM 2216
Cdd:cd02440     75 PLHHLVEDLARFLEeARRLLKPGGVLVLT 103

PRK06060

p-hydroxybenzoic acid--AMP ligase FadD22;

2801-2893

1.35e-06

p-hydroxybenzoic acid--AMP ligase FadD22;

Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 1.35e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2801 KEGLTLLQAHVREQVSQVLGIDTKTLLAE-------QDVGFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQAL 2873
Cdd:PRK06060   532 RERLVALRQERQRLVVDAVCAEAAKMLGEpdpwsvdQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGL 611

                           90       100
                   ....*....|....*....|
gi 1331970929 2874 VNYLANELLGTPEQLQEPES 2893
Cdd:PRK06060   612 AQYLEAELAGGHGRLKSAGP 631

PKS_PP

smart00823

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...

595-648

6.46e-06

Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 46.47 E-value: 6.46e-06

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1331970929   595 AVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQTLAQYI 648
Cdd:smart00823   29 AAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82

PRK08317

hypothetical protein; Provisional

2100-2217

6.03e-05

hypothetical protein; Provisional

Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 47.24 E-value: 6.03e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2100 ALEQLPPERGWRILEIGAGTGGTTAYlLPHLPGDQTKYVFTDISAFFLAKAEERFK-DYPFVRYQVLDIEQAPqaqgFEP 2178
Cdd:PRK08317    11 TFELLAVQPGDRVLDVGCGPGNDARE-LARRVGPEGRVVGIDRSEAMLALAKERAAgLGPNVEFVRGDADGLP----FPD 85

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1331970929 2179 QIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILME 2217
Cdd:PRK08317    86 GSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLD 124

Name

Accession

Description

Interval

E-value

PksD

COG3321

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...

673-2008

0e+00

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 1320.26 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  673 DSNDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDELEQTL----PELFNNPAYVKAGAVLEGVELFDATFFGYS 748
Cdd:COG3321      2 ADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAyydpDPDAPGKTYVRWGGFLDDVDEFDALFFGIS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  749 PKEAAVTDPQQRILLECAWEAFERAGYNPETYP-EPVGVYAGSSLSTYLLNNIGSALGIiteqpfietdmeQFQAKIGND 827
Cdd:COG3321     82 PREAEAMDPQQRLLLEVAWEALEDAGYDPESLAgSRTGVFVGASSNDYALLLLADPEAI------------DAYALTGNA 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  828 RSYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFD 907
Cdd:COG3321    150 KSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFD 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  908 AEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGALKmGYTAPSVDGQADVISEAIAIADIDASTIGYVEA 987
Cdd:COG3321    230 ADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSN-GLTAPNGPAQAAVIRRALADAGVDPATVDYVEA 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  988 HGTATQLGDPIEVAGLARAFQRSTDsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRID 1067
Cdd:COG3321    309 HGTGTPLGDPIEAAALTAAFGQGRP---ADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1068 FDATPFFVNTELREWSRNGYPRRAGVSSFGVGGTNSHIVLEESPVKQPTlfSSLPERSHHLLTLSAHTQEALHELVQRYI 1147
Cdd:COG3321    386 FENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPA--AAAAARPPQLLVLSAKTEEALRALAARLA 463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1148 QHNETHLDINLGDLCFTANTGRKHFEHRLAVVAESIPGLQAQLETAQTAISAQ-----KKNAPPTIAFLFTGQGSQYINM 1222
Cdd:COG3321    464 AFLEAHPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPgvvtgAAAAAPKVAFLFPGQGSQYVGM 543

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1223 GRTLYDTESTFRAALDRCETILQNLGIESILSVIFGSSEHGLsLDDTAYTQPALFAIEYALYQLWKSWGIQPSVVIGHSV 1302
Cdd:COG3321    544 GRELYETEPVFRAALDECDALLRPHLGWSLREVLFPDEEESR-LDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSV 622

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1303 GEYVSACVAGVFSLEDGLKLIAERGRLIQALPRDGSMVSVMASEKRIADIILPYGGqVGIAAINGPQSVVISGQQQAIDA 1382
Cdd:COG3321    623 GEYAAACVAGVLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAGYDG-VSIAAVNGPRSTVVSGPAEAVEA 701

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1383 ICAILETEGIKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHEscpdelpITTAEYWVRHVR 1462
Cdd:COG3321    702 LAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGE-------ALDADYWVRHLR 774

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1463 QPVRFAAGMESLEGQGVNVFIEIGPKPVLLGMGRDCLTEQE-GLWLPSLRPKQDDWQQVLSSLRDLYLAGVTVDWSSFDQ 1541
Cdd:COG3321    775 QPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAGdAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYP 854

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1542 GYARRRVPLPTYPWQRERHWVEPIIRQRQSVLQATNTTKLTRNASVAQHPLLGQRLHLSRTQEIYFQTFIHSDFPIWVAD 1621
Cdd:COG3321    855 GRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVA 934

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1622 HKVFGNVIIPGVAYFEMALAAGKALKPDSIFWLEDVSIAQALIIPDEGQTVQIVLSPQEESAyffeILSLEKENSWVLHA 1701
Cdd:COG3321    935 LAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAAL----AAAAALALLAAAAL 1010

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1702 SGKLVAQEQVLETEPIDLIALQAHCSEEVSVDVLYQEEMARRLDMGPMMRGVKQLWRYPLSFAKSHDAIALAKVSLPEIL 1781
Cdd:COG3321   1011 LLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAAL 1090

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1782 LHESNAYQFHPVILDAGLQMITVSYPEANQGQTYVPVGIEGLQVYGRPSSELWCRAQYRPPLDTDQRQGIDLLPKKLIAD 1861
Cdd:COG3321   1091 AAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAA 1170

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1862 LHLFDTQGRVVAIMFGVQSVLVGREAMLRSQDTWRNWLYQVLWKPQACFGLLPNYLPTPDKIRKRLETKLATLIIEANLA 1941
Cdd:COG3321   1171 AALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAA 1250

                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331970929 1942 TYAIAYTQLERLSLAYVVAAFRQMGWLFQPGERFSTAQKVSALGIVDQHRQLFARLLDILAEADILR 2008
Cdd:COG3321   1251 AAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAA 1317

PKS

cd00833

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...

675-1107

0e+00

Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 609.94 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  675 NDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDELEQTL---PELFNNPAYVKAGAVLEGVELFDATFFGYSPKE 751
Cdd:cd00833      1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGyypDPGKPGKTYTRRGGFLDDVDAFDAAFFGISPRE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  752 AAVTDPQQRILLECAWEAFERAGYNPET-YPEPVGVYAGSSLSTYLLNNIGSALGIiteqpfietdmEQFQAkIGNDRSY 830
Cdd:cd00833     81 AEAMDPQQRLLLEVAWEALEDAGYSPESlAGSRTGVFVGASSSDYLELLARDPDEI-----------DAYAA-TGTSRAF 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  831 LATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFDAEA 910
Cdd:cd00833    149 LANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADA 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  911 QGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGALKmGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGT 990
Cdd:cd00833    229 DGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTK-GITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGT 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  991 ATQLGDPIEVAGLARAFQRSTDsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDA 1070
Cdd:cd00833    308 GTPLGDPIEVEALAKVFGGSRS---ADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEE 384

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1331970929 1071 TPFFVNTELREWSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00833    385 SPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421

EntF

COG1020

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...

5-663

0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 601.46 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    5 ESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERS 83
Cdd:COG1020    457 ERQQLLAEWNATAAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERS 536

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   84 AELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLaltiPALQeCQTVYLDQEifeydfhflai 163
Cdd:COG1020    537 LEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL----PELG-VPVLALDAL----------- 600

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  164 akllhnqylrllhfyfytLIQQCQATSVSQGIQtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:COG1020    601 ------------------ALAAEPATNPPVPVT----PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPG 658

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  244 VRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNgnkSTSLALCE 323
Cdd:COG1020    659 DRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP---EALPSLRL 735

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  324 VITTGEQmqITPAVANLFQKT--GAMLHNHYGATEFQ-DATTHTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVPLG 400
Cdd:COG1020    736 VLVGGEA--LPPELVRRWRARlpGARLVNLYGPTETTvDSTYYEVTPPDADGGS-VPIGRPIANTRVYVLDAHLQPVPVG 812

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  401 GEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANEnaKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIES 480
Cdd:COG1020    813 VPGELYIGGAGLARGYLNRPELTAERFVADPFGFPG--ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEA 890

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  481 VLASHQAVRECAVVAREIA-GHTQLVGYIIAKDTLnlsfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:COG1020    891 ALLQHPGVREAVVVAREDApGDKRLVAYVVPEAGA----AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  560 ALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYP 639
Cdd:COG1020    967 ALPAP--AAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAA 1044

                          650       660
                   ....*....|....*....|....
gi 1331970929  640 TIQTLAQYIDCQGDTTSSDTASRH 663
Cdd:COG1020   1045 AAAAAAAAAAAAAAAAAPLAAAAA 1068

A_NRPS_VisG_like

cd17651

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...

29-562

0e+00

Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 576.60 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   29 FEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYP 108
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  109 GDRIEYMLRDSDARILLTSTDVAKKLALTIPALqecqtVYLDQEifeydfhflaiakllhnqylrllhfyfytliQQCQA 188
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPALAGELAVELVAV-----TLLDQP-------------------------------GAAAG 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  189 TSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLG 268
Cdd:cd17651    125 ADAEPDPALD--ADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAG 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  269 GILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMQITPAVANLFQK-TGAM 347
Cdd:cd17651    203 ATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGlPGLR 282

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  348 LHNHYGATEFQDATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKF 427
Cdd:cd17651    283 LHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERF 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  428 IPNPFGANEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE-IAGHTQLVG 506
Cdd:cd17651    363 VPDPFVPGA---RMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREdRPGEKRLVA 439

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929  507 YIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17651    440 YVVGDPEAPVDAAE----LRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491

A_NRPS

cd05930

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...

37-561

4.65e-177

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 551.75 E-value: 4.65e-177

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYML 116
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  117 RDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd05930     81 EDSGAKLVLTD--------------------------------------------------------------------- 91

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  197 tqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPE 276
Cdd:cd05930     92 ----PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPE 167

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  277 AVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALceVITTGEQMqiTPAVANLFQKT--GAMLHNHYGA 354
Cdd:cd05930    168 EVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRL--VLVGGEAL--PPDLVRRWRELlpGARLVNLYGP 243

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  355 TEFQ-DATTHTLKGNPEGwPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFG 433
Cdd:cd05930    244 TEATvDATYYRVPPDDEE-DGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG 322

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  434 ANEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE-IAGHTQLVGYIIAKD 512
Cdd:cd05930    323 PGE---RMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREdGDGEKRLVAYVVPDE 399

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1331970929  513 TLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05930    400 GGELDEEE----LRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444

mycolic_Pks13

NF040607

polyketide synthase Pks13;

628-1563

4.22e-170

polyketide synthase Pks13;

Pssm-ID: 468580 [Multi-domain] Cd Length: 1671 Bit Score: 573.41 E-value: 4.22e-170

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  628 INLSAVSLFQYPTIQTLAQYIdCQGDTTSSDTASRHKKVRKKQSGDSNDIAIISVAGRFPGA-ETIEQFWHNLCNGVESI 706
Cdd:NF040607    54 VTLTATVAYQHPTIASLATRI-IEGEPEVAADDDDDADWSRRPRSDAHDIAIVGLATRFPGAgNTPEEMWEALIEGRDGI 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  707 TLFSDDELEqtlpELFNNPAYVKA-------GAVLEGVELFDATFFGYSPKEAAVTDPQQRILLECAWEAFERAGYNPET 779
Cdd:NF040607   133 TDLPEGRWS----EFAADPRIAERvakantrGGYLDDIKGFDAEFFALSPLEAENVDPQQRLALELTWEALEHARIPASS 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  780 YP-EPVGVYAGSSLSTY-LLnnigSALGIITEQPFietdmeqfqAKIGNDRSYLATRISYKLNLKGPSVNVQTACSTSLV 857
Cdd:NF040607   209 LRgEPVGVFIGSSNNDYqML----AVADPAEAHPY---------ALTGTSSSIIANRVSYFFDFRGPSVAVDTACSSSLV 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  858 AVHMACQSLISGECQMALAGGISVVVPQKGGYLYEE-GMVRSQDGHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDN 936
Cdd:NF040607   276 AVHQAVRALRSGEADVAVAGGVNMLLTPAVTLGFDElGGVLAPDGRIKAFSSDADGMVRSEGGGVVVLKRLADARRDGDT 355

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  937 IMAVIKATAINNDGAlKMGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARafqrstdsVLG 1016
Cdd:NF040607   356 ILAVIAGSAVNSDGR-SNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDPIEADALGR--------VVG 426

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1017 KQQCA-----IGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFVNTELREWSR-NGYPrR 1090
Cdd:NF040607   427 RGRDAdkpalLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPYIDFDAEHLKVVDEPTEWPRySGHA-V 505

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1091 AGVSSFGVGGTNSHIVLEE------SPVKQPTLFSSLPERShhLLTLSAHTQEALHELVQRYIQHNETHLDINL------ 1158
Cdd:NF040607   506 AGVSGFGFGGTNAHVVVREvlpadlVEPEAQPDEDTEAELA--GLTAEAKRLLAEAELAAEFAPAAPEGPVVPLpvsgfl 583

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1159 ----------------------GDLCFTANT--GRKHFEHRLAVVA----ESIPGLQAQLE--TAQTAISAqkkNAPPTI 1208
Cdd:NF040607   584 psrrraaaadladwleseegraTPLADVARAlaRRNHGRSRAVVLAhtheEAIKGLRAVAEgkPGPGVFSA---DAPAAN 660

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1209 --AFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGIESILSVIfgssehglsLDD-----TAYTQPALFAIEY 1281
Cdd:NF040607   661 gpVWVLSGFGSQHRKMAKQLYLENPVFAARIDEVDELVQDESGYSIVELI---------LDDeqtydIETAQVGIFAIQI 731

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1282 ALYQLWKSWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLI----QALPRD--GSMVSVMASEKRIADIILP 1355
Cdd:NF040607   732 ALADLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAVRVICHRSRLMgegeAMLPGDdiRLMALVEYSAEEIETVLAD 811

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1356 YGGqVGIAAINGPQSVVISGQQQAIDAICAILETEGIKSKKLNVSHAFHSplveAMLDSFL-QVAQEVTYSQPQ---IKL 1431
Cdd:NF040607   812 FPD-LEVCVYAAPTHTVIGGPREQVDAIVARAEAEGKFARKLQTKGASHT----SQMDPLLgELAAELAGIEPQpltVGL 886

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1432 ISNV-TGTL--ASHEscpdelPITTAEYWVRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLgMGRDCLTEQEGL--- 1505
Cdd:NF040607   887 YSSVdRGTFyrPGHE------PIHDVDYWVKGLRHSVWFTQAVRKAVDAGHTTFLELAPNPVAL-MSVAATTFAAGLhda 959

                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331970929 1506 -WLPSLRPKQDDWQQVLSSLRDLYLAGVTVDWSS-FDQG-YArrrvPLPTYPWQRERHWVE 1563
Cdd:NF040607   960 qLIPTLKRKEDESESVLNALAQLYVHGHDVDLRSlFGAGdYA----DIPRTRFKRKPYWLD 1016

A_NRPS_Bac

cd17655

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...

28-564

8.13e-161

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 507.25 E-value: 8.13e-161

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:cd17655      2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  108 PGDRIEYMLRDSDARILLTSTDVAKKLALTipalqecQTVYL--DQEIFEYDFHFLAIakllhnqylrllhfyfytliqq 185
Cdd:cd17655     82 PEERIQYILEDSGADILLTQSHLQPPIAFI-------GLIDLldEDTIYHEESENLEP---------------------- 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  186 cqatsVSQgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTL 265
Cdd:cd17655    133 -----VSK-------SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASL 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  266 CLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAvngNKSTSLALCEVITTGEQMqiTPAVANLFQK-- 343
Cdd:cd17655    201 LSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAA---DDSEGLSLKHLIVGGEAL--STELAKKIIElf 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  344 -TGAMLHNHYGATEFQ-DATTHTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPD 421
Cdd:cd17655    276 gTNPTITNAYGPTETTvDASIYQYEPETDQQVS-VPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPE 354

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  422 LTNEKFIPNPFGANEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIA-G 500
Cdd:cd17655    355 LTAEKFVDDPFVPGE---RMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEqG 431

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331970929  501 HTQLVGYIIAKDTLNLSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPDP 564
Cdd:cd17655    432 QNYLCAYIVSEKELPVA------QLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489

A_NRPS_ApnA-like

cd17644

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...

24-562

1.25e-155

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 491.18 E-value: 1.25e-155

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   24 CIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPL 103
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  104 DVGYPGDRIEYMLRDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytli 183
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLTQ-------------------------------------------------------- 104

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  184 qqcqatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFS 263
Cdd:cd17644    105 -----------------PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYV 167

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  264 TLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSL-ALCEVITTGEQMQitPAVANLFQ 342
Cdd:cd17644    168 TLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPsSLRLVIVGGEAVQ--PELVRQWQ 245

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  343 KTGA---MLHNHYGATEFQ-DATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHN 418
Cdd:cd17644    246 KNVGnfiQLINVYGPTEATiAATVCRLTQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLN 325

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  419 LPDLTNEKFIPNPFGANEnAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE- 497
Cdd:cd17644    326 RPELTAEKFISHPFNSSE-SERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREd 404

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331970929  498 IAGHTQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17644    405 QPGNKRLVAYIVPHYEESPSTVE----LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465

PKS_KS

smart00825

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...

677-1109

1.29e-151

Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 472.20 E-value: 1.29e-151

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   677 IAIISVAGRFPGAETIEQFWHNLCNGvesitlfsddeleqtlpelfnnpayvkagavLEGVELFDATFFGYSPKEAAVTD 756
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAG-------------------------------LDDVDLFDAAFFGISPREAEAMD 49

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   757 PQQRILLECAWEAFERAGYNPETYPE-PVGVYAGSSLSTYllnnigsalgiiteqpfietdmeqfqakigndrsylatri 835
Cdd:smart00825   50 PQQRLLLEVAWEALEDAGIDPESLRGsRTGVFVGVSSSDY---------------------------------------- 89

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   836 syklnlkgpSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFDAEAQGTIF 915
Cdd:smart00825   90 ---------SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVR 160

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   916 GNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAlKMGYTAPSVDGqadviseaiaiadidastigyveahgtatqlg 995
Cdd:smart00825  161 GEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGR-SNGITAPSGPA-------------------------------- 207

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   996 dpievaglarafqrstdsvlgkqQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFV 1075
Cdd:smart00825  208 -----------------------QLLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRV 264

                           410       420       430
                    ....*....|....*....|....*....|....
gi 1331970929  1076 NTELREWSRNGYPRRAGVSSFGVGGTNSHIVLEE 1109
Cdd:smart00825  265 PTELTPWPPPGRPRRAGVSSFGFGGTNAHVILEE 298

A_NRPS_Srf_like

cd12117

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...

28-561

2.32e-150

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.

Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 477.08 E-value: 2.32e-150

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:cd12117      2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  108 PGDRIEYMLRDSDARILLTSTDVAKKLALTIPALqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytLIQQCQ 187
Cdd:cd12117     82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAV----------------------------------------VIDEAL 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  188 ATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNmLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCL 267
Cdd:cd12117    122 DAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR-LVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLN 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  268 GGILVLVPEAVRQNPFALAEFISQQKIEKLFLpvIALL--QLAEAVNGnkstSLA-LCEVITTGEQMQItPAVANLFQKT 344
Cdd:cd12117    201 GARLVLAPKGTLLDPDALGALIAEEGVTVLWL--TAALfnQLADEDPE----CFAgLRELLTGGEVVSP-PHVRRVLAAC 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  345 GAM-LHNHYGATE---FqdATTHTLkGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLP 420
Cdd:cd12117    274 PGLrLVNGYGPTEnttF--TTSHVV-TELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRP 350

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  421 DLTNEKFIPNPFGANEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIA- 499
Cdd:cd12117    351 ALTAERFVADPFGPGE---RLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAg 427

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331970929  500 GHTQLVGYIIAKDTLNlsfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd12117    428 GDKRLVAYVVAEGALD------AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483

A_NRPS_ProA

cd17656

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...

37-562

1.10e-148

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 471.96 E-value: 1.10e-148

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYML 116
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  117 RDSDARILLTSTDVAKKLAltipalqecqtvyldqeiFEYDFHFLAiakllhnqylrllhfyfYTLIQQCQAtsvsQGIQ 196
Cdd:cd17656     82 LDSGVRVVLTQRHLKSKLS------------------FNKSTILLE-----------------DPSISQEDT----SNID 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  197 TQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPE 276
Cdd:cd17656    123 YINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIRE 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  277 AVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATE 356
Cdd:cd17656    203 ETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSE 282

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  357 FQDATTHTLKGNPEgWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANe 436
Cdd:cd17656    283 THVVTTYTINPEAE-IPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPN- 360

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  437 naKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR-EIAGHTQLVGYIIAKDTLN 515
Cdd:cd17656    361 --ERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKaDDKGEKYLCAYFVMEQELN 438

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1331970929  516 LSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17656    439 IS------QLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479

PRK12467

peptide synthase; Provisional

5-645

7.38e-148

peptide synthase; Provisional

Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 519.72 E-value: 7.38e-148

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    5 ESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERS 83
Cdd:PRK12467  1555 ERRQILEGWNATHTGYPlARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERS 1634

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   84 AELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQEifeydfhflai 163
Cdd:PRK12467  1635 LEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL----PLPDGLRSLVLDQE----------- 1699

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  164 akllhnqylrllhfyfytliQQCQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:PRK12467  1700 --------------------DDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAA 1759

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  244 VRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKL-FLPVI--ALLQLAEAVNGnkstSLA 320
Cdd:PRK12467  1760 DVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLhFVPSMlqQLLQMDEQVEH----PLS 1835

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  321 LCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATEFQDATTHTL--KGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVP 398
Cdd:PRK12467  1836 LRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTcrRKDLEGRDS-VPIGQPIANLSTYILDASLNPVP 1914

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  399 LGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGanENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEI 478
Cdd:PRK12467  1915 IGVAGELYLGGVGLARGYLNRPALTAERFVADPFG--TVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEI 1992

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  479 ESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDK----LEPILRQYSEAVLPEYMIPTRFINISNMPLTPSG 554
Cdd:PRK12467  1993 EARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDDEaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTPNG 2072

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  555 KLDRRALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKfLCETFNINLSAVS 634
Cdd:PRK12467  2073 KLDRKALPAP--DASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVS-RARQAGIRFTPKD 2149

                          650
                   ....*....|.
gi 1331970929  635 LFQYPTIQTLA 645
Cdd:PRK12467  2150 LFQHQTVQSLA 2160

PRK12316

peptide synthase; Provisional

1-658

5.96e-147

peptide synthase; Provisional

Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 517.20 E-value: 5.96e-147

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    1 MQKRESPQILFDGNGTQSEFPDS-CIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAIC 79
Cdd:PRK12316  4528 LEKAEQQRIVALWNRTDAGYPATrCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIA 4607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   80 IERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQEIFEYDFH 159
Cdd:PRK12316  4608 MERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRL----PIPDGLASLALDRDEDWEGFP 4683

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  160 FLAIAKLLHnqylrllhfyfytliqqcqatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRP 239
Cdd:PRK12316  4684 AHDPAVRLH--------------------------------PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYE 4731

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  240 SVQGVRTLQFCAVSFDFSCHEIFSTLCLGGiLVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAE--AVNGNkst 317
Cdd:PRK12316  4732 LTPDDRVLQFMSFSFDGSHEGLYHPLINGA-SVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEhaERDGE--- 4807

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  318 SLALCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATEFQDATTH--TLKGNPEGwPTLVPVGRPLHNVQVYILDEAQQ 395
Cdd:PRK12316  4808 PPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLwkARDGDACG-AAYMPIGTPLGNRSGYVLDGQLN 4886

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  396 PVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVEL 475
Cdd:PRK12316  4887 PLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAP--GGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIEL 4964

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  476 GEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYSEA----VLPEYMIPTRFINISNMPLT 551
Cdd:PRK12316  4965 GEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAalreRLPEYMVPAHLVFLARMPLT 5044

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  552 PSGKLDRRALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLS 631
Cdd:PRK12316  5045 PNGKLDRKALPQP--DASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELP 5122

                          650       660
                   ....*....|....*....|....*..
gi 1331970929  632 AVSLFQYPTIQTLAQYIDCQGDTTSSD 658
Cdd:PRK12316  5123 LRELFQTPTLAAFVELAAAAGSGDDEK 5149

A_NRPS_AB3403-like

cd17646

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...

26-561

3.18e-146

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 465.21 E-value: 3.18e-146

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   26 HHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDV 105
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  106 GYPGDRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYldqeifeydfhflaiakllhnqylrllhfyfytliqq 185
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEAL------------------------------------- 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  186 cqATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTL 265
Cdd:cd17646    124 --AAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPL 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  266 CLGGILVLVPEAVRQNPFALAEFISQQKIEKL-FLPVI--ALLQLAEAvngnkSTSLALCEVITTGEQMqiTPAVANLF- 341
Cdd:cd17646    202 VAGARLVVARPGGHRDPAYLAALIREHGVTTChFVPSMlrVFLAEPAA-----GSCASLRRVFCSGEAL--PPELAARFl 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  342 QKTGAMLHNHYGATEFQ-DATTHTLKGNPEGWPtlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLP 420
Cdd:cd17646    275 ALPGAELHNLYGPTEAAiDVTHWPVRGPAETPS--VPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRP 352

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  421 DLTNEKFIPNPFGANEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREI-A 499
Cdd:cd17646    353 ALTAERFVPDPFGPGS---RMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAApA 429

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331970929  500 GHTQLVGYIIAKDTlnlSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17646    430 GAARLVGYVVPAAG---AAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488

PRK12467

peptide synthase; Provisional

3-648

9.18e-145

peptide synthase; Provisional

Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 509.70 E-value: 9.18e-145

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    3 KRESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIE 81
Cdd:PRK12467  3074 AHERRQVLHAWNATAAAYPsERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVE 3153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   82 RSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQEIFEydfhfl 161
Cdd:PRK12467  3154 RSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQL----PAPAGDTALTLDRLDLN------ 3223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  162 aiAKLLHNqylrllhfyfytliqqcqatsvsqgIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSV 241
Cdd:PRK12467  3224 --GYSENN-------------------------PSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELD 3276

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  242 QGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRqNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLAl 321
Cdd:PRK12467  3277 ANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLD- 3354

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  322 cEVITTGEQMQITpAVANLFQKTG-AMLHNHYGATEFQDATTH-TLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPL 399
Cdd:PRK12467  3355 -IYVFGGEAVPPA-AFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPV 3432

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  400 GGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIE 479
Cdd:PRK12467  3433 GVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGS--GGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 3510

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  480 SVLASHQAVRECAVVAREIAGHTQLVGYIIAKDtlnLSFDKLEpILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:PRK12467  3511 ARLLQHPSVREAVVLARDGAGGKQLVAYVVPAD---PQGDWRE-TLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRK 3586

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  560 ALPDPKGDrpaLSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYP 639
Cdd:PRK12467  3587 ALPDPDAK---GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAP 3663


                   ....*....
gi 1331970929  640 TIQTLAQYI 648
Cdd:PRK12467  3664 TIAELAGYS 3672

PRK12467

peptide synthase; Provisional

5-657

3.34e-143

peptide synthase; Provisional

Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 504.70 E-value: 3.34e-143

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    5 ESPQILFDGNGTQSEFPDSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSA 84
Cdd:PRK12467   494 ERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSI 573

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   85 ELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLALtiPAlqecqtvyldqeifeydfhflAIA 164
Cdd:PRK12467   574 EMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPV--PA---------------------GLR 630

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  165 KLLHNQYLRLLhfyfytliQQCQATSVSqgiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGV 244
Cdd:PRK12467   631 SLCLDEPADLL--------CGYSGHNPE----VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD 698

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  245 RTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAvnGNKSTSLALCEV 324
Cdd:PRK12467   699 SMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA--SRVALPRPQRAL 776

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  325 ITTGEQMQITpAVANLFQKT-GAMLHNHYGATEFQ-DATTHTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVPLGGE 402
Cdd:PRK12467   777 VCGGEALQVD-LLARVRALGpGARLINHYGPTETTvGVSTYELSDEERDFGN-VPIGQPLANLGLYILDHYLNPVPVGVV 854

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  403 GEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVL 482
Cdd:PRK12467   855 GELYIGGAGLARGYHRRPALTAERFVPDPFGAD--GGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARL 932

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  483 ASHQAVRECAVVAREIAGHTQLVGYII----AKDTLNLSF-DKLEPILRQyseaVLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:PRK12467   933 LAQPGVREAVVLAQPGDAGLQLVAYLVpaavADGAEHQATrDELKAQLRQ----VLPDYMVPAHLLLLDSLPLTPNGKLD 1008

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  558 RRALPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQ 637
Cdd:PRK12467  1009 RKALPKP--DASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFE 1086

                          650       660
                   ....*....|....*....|
gi 1331970929  638 YPTIQTLAQYIDCQGDTTSS 657
Cdd:PRK12467  1087 HQTLAGFAQAVAAQQQGAQP 1106

PRK12316

peptide synthase; Provisional

5-646

2.50e-141

peptide synthase; Provisional

Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 499.10 E-value: 2.50e-141

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    5 ESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERS 83
Cdd:PRK12316   492 ERGQLVEGWNATAAEYPlQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERS 571

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   84 AELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQEIFEYDFHFlai 163
Cdd:PRK12316   572 IEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL----PLAAGVQVLDLDRPAAWLEGYS--- 644

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  164 akllhnqylrllhfyfytliqqcqatsvSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:PRK12316   645 ----------------------------EENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVG 696

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  244 VRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALce 323
Cdd:PRK12316   697 DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRR-- 774

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  324 VITTGEQMQITpAVANLFQK-TGAMLHNHYGATEFQDATTHTLKGNpEGWPTlVPVGRPLHNVQVYILDEAQQPVPLGGE 402
Cdd:PRK12316   775 IVCSGEALPAD-AQEQVFAKlPQAGLYNLYGPTEAAIDVTHWTCVE-EGGDS-VPIGRPIANLACYILDANLEPVPVGVL 851

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  403 GEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVL 482
Cdd:PRK12316   852 GELYLAGRGLARGYHGRPGLTAERFVPSPFVAGE---RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 928

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  483 ASHQAVRECAVVAreiAGHTQLVGYIIAKDTLNlsfdKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:PRK12316   929 LEHPWVREAAVLA---VDGKQLVGYVVLESEGG----DWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALP 1001

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  563 DPKGDRPALStpLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKfLCETFNINLSAVSLFQYPTIQ 642
Cdd:PRK12316  1002 APEASVAQQG--YVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVS-RARQAGIQLSPRDLFQHQTIR 1078


                   ....
gi 1331970929  643 TLAQ 646
Cdd:PRK12316  1079 SLAL 1082

AA-adenyl-dom

TIGR01733

amino acid adenylation domain; This model represents a domain responsible for the specific ...

50-493

4.43e-140

Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 444.40 E-value: 4.43e-140

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   50 TYGELNVRANHLAQHLLSLGC-QPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTST 128
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGGvGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  129 DVAKKLAltipalqecqtvYLDQEIFEYDFHFLAIAkllhnqylrllhfyfytliqqcQATSVSQGIQTQVLPNNLAYCI 208
Cdd:TIGR01733   81 ALASRLA------------GLVLPVILLDPLELAAL----------------------DDAPAPPPPDAPSGPDDLAYVI 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  209 YTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFAL-AE 287
Cdd:TIGR01733  127 YTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAA 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  288 FISQQKIEKLFLPVIALLQLAEAVNGNKSTslaLCEVITTGEQmqITPAVANLFQKT--GAMLHNHYGATEFQ-DATTHT 364
Cdd:TIGR01733  207 LIAEHPVTVLNLTPSLLALLAAALPPALAS---LRLVILGGEA--LTPALVDRWRARgpGARLINLYGPTETTvWSTATL 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  365 LKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANENAKkLYRT 444
Cdd:TIGR01733  282 VDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGAR-LYRT 360

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1331970929  445 GDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV 493
Cdd:TIGR01733  361 GDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409

PKS_AT

smart00827

Acyl transferase domain in polyketide synthase (PKS) enzymes;

1211-1513

4.82e-139

Acyl transferase domain in polyketide synthase (PKS) enzymes;

Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 436.45 E-value: 4.82e-139

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  1211 LFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGIESILSVIFGSSEHGlSLDDTAYTQPALFAIEYALYQLWKSW 1290
Cdd:smart00827    1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLLGEDGAA-SLLDTEVAQPALFAVQVALARLLRSW 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  1291 GIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQALPRDGSMVSVMASEKRIADIILPYGGQVGIAAINGPQS 1370
Cdd:smart00827   80 GVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLSEEEVEPLLAGVPDRVSVAAVNSPSS 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  1371 VVISGQQQAIDAICAILETEGIKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHEScpdelp 1450
Cdd:smart00827  160 VVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAE------ 233

                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331970929  1451 ITTAEYWVRHVRQPVRFAAGMESL-EGQGVNVFIEIGPKPVLLGMGRDCLTEQEG-LWLPSLRPK 1513
Cdd:smart00827  234 LDDADYWVRNLREPVRFADAVRALlAEGGVTVFLEVGPHPVLTGPIKQTLAAAGSaVVLPSLRRG 298

A_NRPS_CmdD_like

cd17652

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...

37-562

1.27e-137

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).

Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 438.23 E-value: 1.27e-137

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYML 116
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  117 RDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd17652     81 ADARPALLLTT--------------------------------------------------------------------- 91

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  197 tqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNM---LWWHQQTRPsvqGVRTLQFCAVSFDFSCHEIFSTLCLGGILVL 273
Cdd:cd17652     92 ----PDNLAYVIYTSGSTGRPKGVVVTHRGLANLaaaQIAAFDVGP---GSRVLQFASPSFDASVWELLMALLAGATLVL 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  274 VPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAvngnksTSLALCEVITTGEQmqITPAVANLFQKTGAMLhNHYG 353
Cdd:cd17652    165 APAEELLPGEPLADLLREHRITHVTLPPAALAALPPD------DLPDLRTLVVAGEA--CPAELVDRWAPGRRMI-NAYG 235

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  354 ATEfqdATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFG 433
Cdd:cd17652    236 PTE---TTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFG 312

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  434 ANenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREI-AGHTQLVGYIIAKD 512
Cdd:cd17652    313 AP--GSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDrPGDKRLVAYVVPAP 390

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1331970929  513 TLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17652    391 GAAPTAAE----LRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436

A_NRPS_Ta1_like

cd12116

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...

37-561

2.05e-136

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.

Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 436.34 E-value: 2.05e-136

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYML 116
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  117 RDSDARILLTSTDVAKKLALTIPALqecqtvyldqeifeydfhflaiakLLHNQYLRLLHfyfytliqqcqatsvsQGIQ 196
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVL------------------------LLALAAAAAAP----------------AAPR 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  197 TQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQtRPSVQ-GVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVP 275
Cdd:cd12116    121 TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE-RLGLGpGDRLLAVTTYAFDISLLELLLPLLAGARVVIAP 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  276 EAVRQNPFALAEFISQQKIeKLFLPVIALLQLAEAVNGNKSTSL-ALCevitTGEQMQitPAVANLFQKTGAMLHNHYGA 354
Cdd:cd12116    200 RETQRDPEALARLIEAHSI-TVMQATPATWRMLLDAGWQGRAGLtALC----GGEALP--PDLAARLLSRVGSLWNLYGP 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  355 TEfqdATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGa 434
Cdd:cd12116    273 TE---TTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFA- 348

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  435 nENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTl 514
Cdd:cd12116    349 -GPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAG- 426

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1331970929  515 nLSFDKLEpiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd12116    427 -AAPDAAA--LRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470

A_NRPS_Cytc1-like

cd17643

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...

37-561

3.23e-136

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 434.81 E-value: 3.23e-136

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYML 116
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  117 RDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd17643     81 ADSGPSLLLTD--------------------------------------------------------------------- 91

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  197 tqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPE 276
Cdd:cd17643     92 ----PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPY 167

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  277 AVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMQItPAVANLFQKTGAM---LHNHYG 353
Cdd:cd17643    168 EVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEA-AMLRPWAGRFGLDrpqLVNMYG 246

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  354 ATEFQDATTHTLKGNPEGWP-TLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPF 432
Cdd:cd17643    247 ITETTVHVTFRPLDAADLPAaAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF 326

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  433 GANenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE-IAGHTQLVGYIIAK 511
Cdd:cd17643    327 GGP--GSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREdEPGDTRLVAYVVAD 404

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1331970929  512 DtlnlSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17643    405 D----GAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450

A_NRPS_Sfm_like

cd12115

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...

25-561

1.54e-135

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.

Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 432.90 E-value: 1.54e-135

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  105 VGYPGDRIEYMLRDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliq 184
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLTD--------------------------------------------------------- 103

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  185 qcqatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFST 264
Cdd:cd12115    104 ----------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGP 167

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  265 LCLGGILVLVpeavrQNPFALAEFISQQK---IEKLFLPVIALLQLAEAVNGNKSTSLAlcevittGEQMQITpAVANLF 341
Cdd:cd12115    168 LATGGKVVLA-----DNVLALPDLPAAAEvtlINTVPSAAAELLRHDALPASVRVVNLA-------GEPLPRD-LVQRLY 234

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  342 QK-TGAMLHNHYGATEfqDATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLP 420
Cdd:cd12115    235 ARlQVERVVNLYGPSE--DTTYSTVAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRP 312

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  421 DLTNEKFIPNPFGANEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE-IA 499
Cdd:cd12115    313 GLTAERFLPDPFGPGA---RLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGdAA 389

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331970929  500 GHTQLVGYIIAKDTLNLSFDKLEPILRQyseaVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd12115    390 GERRLVAYIVAEPGAAGLVEDLRRHLGT----RLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447

A_NRPS_PvdJ-like

cd17649

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...

37-562

1.99e-135

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 432.56 E-value: 1.99e-135

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYML 116
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  117 RDSDARILLTSTdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd17649     81 EDSGAGLLLTHH-------------------------------------------------------------------- 92

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  197 tqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNmlwwHQQTRPSVQGV----RTLQFCAVSFDFSCHEIFSTLCLGGILV 272
Cdd:cd17649     93 ----PRQLAYVIYTSGSTGTPKGVAVSHGPLAA----HCQATAERYGLtpgdRELQFASFNFDGAHEQLLPPLICGACVV 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  273 LVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLA-EAVNGNKSTSLALCEVITTGEQMqiTPAVANLFQKTGAMLHNH 351
Cdd:cd17649    165 LRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAeEADRTGDGRPPSLRLYIFGGEAL--SPELLRRWLKAPVRLFNA 242

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  352 YGATEfqdAT-THTL----KGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEK 426
Cdd:cd17649    243 YGPTE---ATvTPLVwkceAGAARAGAS-MPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAER 318

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  427 FIPNPFGANenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVG 506
Cdd:cd17649    319 FVPDPFGAP--GSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVA 396

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929  507 YIIAKDTLNLSFDKLEpiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17649    397 YVVLRAAAAQPELRAQ--LRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450

A_NRPS_PpsD_like

cd17650

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...

37-561

3.66e-134

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 428.81 E-value: 3.66e-134

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYML 116
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  117 RDSDARILLTstdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd17650     81 EDSGAKLLLT---------------------------------------------------------------------- 90

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  197 tqvLPNNLAYCIYTSGSTGNPKGILMEHRSLVNM-LWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVP 275
Cdd:cd17650     91 ---QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAaHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICP 167

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  276 EAVRQNPFALAEFISQQKIEKL-FLPVIALLQLAE-AVNGNKSTSLalcEVITTGEQMQITPAVANLFQKTGA--MLHNH 351
Cdd:cd17650    168 DEVKLDPAALYDLILKSRITLMeSTPALIRPVMAYvYRNGLDLSAM---RLLIVGSDGCKAQDFKTLAARFGQgmRIINS 244

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  352 YGATEFQ-DATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPN 430
Cdd:cd17650    245 YGVTEATiDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVEN 324

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  431 PFGANENakkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIA-GHTQLVGYII 509
Cdd:cd17650    325 PFAPGER---MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKgGEARLCAYVV 401

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1331970929  510 AKDTLNLSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17650    402 AAATLNTA------ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447

entF

PRK10252

enterobactin non-ribosomal peptide synthetase EntF;

8-653

6.60e-132

enterobactin non-ribosomal peptide synthetase EntF;

Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 450.65 E-value: 6.60e-132

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    8 QILFDGNGTQSEFPDSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELF 87
Cdd:PRK10252   443 AQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLT 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   88 IGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLAlTIPalqecqtvylDQEIFEYDFHFLAiakll 167
Cdd:PRK10252   523 LALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFA-DVP----------DLTSLCYNAPLAP----- 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  168 hnqylrllhfyfytliQQCQATSVSQgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTL 247
Cdd:PRK10252   587 ----------------QGAAPLQLSQ-------PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVL 643

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  248 QFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKL-FLP-VIALLQLAEAVNGNKSTSLALCEVI 325
Cdd:PRK10252   644 QKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTThFVPsMLAAFVASLTPEGARQSCASLRQVF 723

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  326 TTGEQMqiTPAVANLFQK-TGAMLHNHYGATE----------FQDATTHTlKGNPegwptlVPVGRPLHNVQVYILDEAQ 394
Cdd:PRK10252   724 CSGEAL--PADLCREWQQlTGAPLHNLYGPTEaavdvswypaFGEELAAV-RGSS------VPIGYPVWNTGLRILDARM 794

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  395 QPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVE 474
Cdd:PRK10252   795 RPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGE---RMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIE 871

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  475 LGEIESVLASHQAVRECAVVAREI-------AGHTQLVGYIIAKDTLNLSFDKLEPILRqyseAVLPEYMIPTRFINISN 547
Cdd:PRK10252   872 LGEIDRAMQALPDVEQAVTHACVInqaaatgGDARQLVGYLVSQSGLPLDTSALQAQLR----ERLPPHMVPVVLLQLDQ 947

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  548 MPLTPSGKLDRRALPDPKgdrPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFN 627
Cdd:PRK10252   948 LPLSANGKLDRKALPLPE---LKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFA 1024

                          650       660
                   ....*....|....*....|....*.
gi 1331970929  628 INLSAVSLFQYPTIQTLAQYIDCQGD 653
Cdd:PRK10252  1025 RQVTPGQVMVASTVAKLATLLDAEED 1050

PRK12316

peptide synthase; Provisional

5-645

1.90e-130

peptide synthase; Provisional

Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 463.27 E-value: 1.90e-130

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    5 ESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERS 83
Cdd:PRK12316  1984 ERQRILADWDRTPEAYPrGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERS 2063

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   84 AELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLALtiPALQECQTVYLDQEIFEYDfhflai 163
Cdd:PRK12316  2064 FELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPL--PAGVARLPLDRDAEWADYP------ 2135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  164 akllhnqylrllhfyfytliqqcqatsvSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:PRK12316  2136 ----------------------------DTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPA 2187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  244 VRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRqNPFALAEFISQQKIEKLFLPVIALLQLAE--AVNGNKstsLAL 321
Cdd:PRK12316  2188 DCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEhaERDGRP---PAV 2263

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  322 CEVITTGEQMQITPAVANLFQKTGAMLHNHYGATE-FQDATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLG 400
Cdd:PRK12316  2264 RVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEaVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPG 2343

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  401 GEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIES 480
Cdd:PRK12316  2344 MAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAS--GERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEA 2421

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  481 VLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLsfdkLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRA 560
Cdd:PRK12316  2422 RLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAED----LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKA 2497

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  561 LPDPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPT 640
Cdd:PRK12316  2498 LPKP--DVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPT 2575


                   ....*
gi 1331970929  641 IQTLA 645
Cdd:PRK12316  2576 LAAFA 2580

A_NRPS_SidN3_like

cd05918

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...

25-561

3.03e-127

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 410.40 E-value: 3.03e-127

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  105 VGYPGDRIEYMLRDSDARILLTSTdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliq 184
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTSS-------------------------------------------------------- 104

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  185 qcqatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFST 264
Cdd:cd05918    105 ----------------PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTT 168

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  265 LCLGGILVLVPEAVRQNpfALAEFISQQKIEKLFLP--VIALLQLAEAVNgnkstslaLCEVITTGEQMqiTPAVANLFQ 342
Cdd:cd05918    169 LAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLTpsVARLLDPEDVPS--------LRTLVLGGEAL--TQSDVDTWA 236

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  343 KtGAMLHNHYGATEfqdATTHTLKGNPEGWPTLVPVGRPLhNVQVYILDEA--QQPVPLGGEGEFCIGGIGLARGYHNLP 420
Cdd:cd05918    237 D-RVRLINAYGPAE---CTIAATVSPVVPSTDPRNIGRPL-GATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDP 311

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  421 DLTNEKFIPNPF----GANENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA- 495
Cdd:cd05918    312 EKTAAAFIEDPAwlkqEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEv 391

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  496 ---REIAGHTQLVGYIIAKDT-------------LNLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:cd05918    392 vkpKDGSSSPQLVAFVVLDGSssgsgdgdslflePSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRR 471


                   ..
gi 1331970929  560 AL 561
Cdd:cd05918    472 AL 473

KR_2_FAS_SDR_x

cd08955

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...

2353-2747

5.06e-127

Pssm-ID: 187658 [Multi-domain] Cd Length: 376 Bit Score: 405.13 E-value: 5.06e-127

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2353 LLNRVPNIQEIVHCWSM----VSTDLDRATIFSCSSTLHLVQAL--ANYPKNPRLSLVTLGAQAVN-EHHVQNVVGAALW 2425
Cdd:cd08955      1 ALLGSAPLAGVVHLWSLdaprEEPADAASQELGCASALHLVQALskAGLRRAPRLWLVTRGAQSVLaDGEPVSPAQAPLW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2426 GMGKVIALEHPELQVAQMDLDPNGKVKAQVEVLRDELLARKDpasamsvpdlqtrphEKQIAFREQTRYVARLSPLDRPN 2505
Cdd:cd08955     81 GLGRVIALEHPELRCGLVDLDPEATAAEEAEALLAELLAADA---------------EDQVALRGGARYVARLVRAPARP 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2506 pgekgtqealtFRDDGSYLIAGGLGGLGLVVARFLVTNGAKYLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAE 2585
Cdd:cd08955    146 -----------LRPDATYLITGGLGGLGLLVAEWLVERGARHLVLTGRRAPSAAARQAIAALEEAGAEVVVLAADVSDRD 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2586 QLAQALSAV--TYPPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQ 2663
Cdd:cd08955    215 ALAAALAQIraSLPPLRGVIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLDFFVLFSSVASLLGSPGQ 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2664 ANHAAANAFLDGLASYRRHLGLPSLSINWGTWSEVGIAARLELDKLSSKQGEGTITLGQGLQILEQLLKDENGvyQVGVM 2743
Cdd:cd08955    295 ANYAAANAFLDALAHYRRARGLPALSINWGPWAEVGMAASLARQARLEARGVGAISPAAGLQALGQLLRTGST--QVGVA 372


                   ....
gi 1331970929 2744 PINW 2747
Cdd:cd08955    373 PVDW 376

PRK12316

peptide synthase; Provisional

5-646

1.05e-122

peptide synthase; Provisional

Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 437.85 E-value: 1.05e-122

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    5 ESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERS 83
Cdd:PRK12316  3038 ERGQLLEAWNATAAEYPlERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERS 3117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   84 AELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDvakklaLTIPALQECQTVYLDQEIFEYDFHFLAI 163
Cdd:PRK12316  3118 LEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSH------LRLPLAQGVQVLDLDRGDENYAEANPAI 3191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  164 akllhnqylrllhfyfytliqqcqatsvsqgiqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:PRK12316  3192 ----------------------------------RTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVG 3237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  244 VRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCe 323
Cdd:PRK12316  3238 DRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRI- 3316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  324 vITTGEQMqitPAVANLFQKTGAMLHNHYGATEFQ-DATTHTLKGNPEGWPtlvPVGRPLHNVQVYILDEAQQPVPLGGE 402
Cdd:PRK12316  3317 -VCGGEAL---PADLQQQVFAGLPLYNLYGPTEATiTVTHWQCVEEGKDAV---PIGRPIANRACYILDGSLEPVPVGAL 3389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  403 GEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVL 482
Cdd:PRK12316  3390 GELYLGGEGLARGYHNRPGLTAERFVPDPFVPGE---RLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARL 3466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  483 ASHQAVRECAVVAREiagHTQLVGYIIAKDtlnlSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:PRK12316  3467 LEHPWVREAVVLAVD---GRQLVAYVVPED----EAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALP 3539

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  563 DPkgDRPALSTPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKfLCETFNINLSAVSLFQYPTIQ 642
Cdd:PRK12316  3540 RP--DAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVS-RARQAGIRFTPKDLFQHQTIQ 3616


                   ....
gi 1331970929  643 TLAQ 646
Cdd:PRK12316  3617 GLAR 3620

A_NRPS_LgrA-like

cd17645

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...

26-562

1.82e-122

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.

Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 395.00 E-value: 1.82e-122

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   26 HHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDV 105
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  106 GYPGDRIEYMLRDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqq 185
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLTN---------------------------------------------------------- 102

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  186 cqatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTL 265
Cdd:cd17645    103 ---------------PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHL 167

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  266 CLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPViallQLAEAVNGNKSTSLALceVITTGEQMqitpavaNLFQKTG 345
Cdd:cd17645    168 TAGAALHVVPSERRLDLDALNDYFNQEGITISFLPT----GAAEQFMQLDNQSLRV--LLTGGDKL-------KKIERKG 234

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  346 AMLHNHYGATEFQDATTHTLKGNPEGwptLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNE 425
Cdd:cd17645    235 YKLVNNYGPTENTVVATSFEIDKPYA---NIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAE 311

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  426 KFIPNPFGANEnakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGH-TQL 504
Cdd:cd17645    312 KFIVHPFVPGE---RMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGrKYL 388

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929  505 VGYIIAKDTLNLSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17645    389 VAYVTAPEEIPHE------ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440

omega_3_PfaA

TIGR02813

polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...

677-1554

2.79e-115

Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 412.09 E-value: 2.79e-115

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  677 IAIISVAGRFPGAETIEQFWHNLCNGVESIT-----------LFSDDELEQtlpelfnNPAYVKAGAVLEGVElFDATFF 745
Cdd:TIGR02813    9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITdvpsdhwakddYYDSDKSEA-------DKSYCKRGGFLPEVD-FNPMEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  746 GYSPKEAAVTDPQQRILLECAWEAFERAGYnPETYPE-----PVGVYAGSSLSTYL--------LNNIGSALGIITE--- 809
Cdd:TIGR02813   81 GLPPNILELTDISQLLSLVVAKEVLNDAGL-PDGYDRdkigiTLGVGGGQKQSSSLnarlqypvLKKVFKASGVEDEdse 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  810 -------QPFIETDMEQFQAKIGNdrsYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGisvV 882
Cdd:TIGR02813  160 mlikkfqDQYIHWEENSFPGSLGN---VISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---V 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  883 VPQKGGYLYeegMVRSQ------DGHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGALKMGY 956
Cdd:TIGR02813  234 CTDNSPFMY---MSFSKtpafttNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIY 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  957 tAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARAFQRSTDSvlgKQQCAIGSVKTNIGHLDEAA 1036
Cdd:TIGR02813  311 -APRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQ---KQHIALGSVKSQIGHTKSTA 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1037 GIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPFFVNTELREWSR--NGYPRRAGVSSFGVGGTNSHIVLEE-SP-- 1111
Cdd:TIGR02813  387 GTAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPFYLNTETRPWMQreDGTPRRAGISSFGFGGTNFHMVLEEySPkh 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1112 ----------VKQPTLFSS------LPERSHHLLTLSAHTQEALHELVQRYIQHNETHLDINLGDLCFTANTGrkhfEHR 1175
Cdd:TIGR02813  467 qrddqyrqraVAQTLLFTAanekalVSSLKDWKNKLSAKADDQPYAFNALAVENTLRTIAVALARLGFVAKNA----DEL 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1176 LAVVAESIPGLQAQ-LETAQ--TAISAQKK---NAPPTIAFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGI 1249
Cdd:TIGR02813  543 ITMLEQAITQLEAKsCEEWQlpSGISYRKSalvVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGK 622

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1250 ESILSVIF--------GSSEHGLSLDDTAYTQPALFAIEYALYQLWKSWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLK 1321
Cdd:TIGR02813  623 GALSPVLYpipvfndeSRKAQEEALTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMM 702

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1322 LIAERGRLIQALPRD---GSMVSVMASEKRIADIILPYGGQ---VGIAAINGPQSVVISG----QQQAIDAicaiLETEG 1391
Cdd:TIGR02813  703 LAFSRGQAMAAPTGEadiGFMYAVILAVVGSPTVIANCIKDfegVSIANYNSPTQLVIAGvstqIQIAAKA----LKEKG 778

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1392 IKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTLASHescpDELPITTAeyWVRHVRQPVRFAAGM 1471
Cdd:TIGR02813  779 FKAIPLPVSGAFHTPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSN----DAAAIKKA--LKNHMLQSVHFSEQL 852

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1472 ESLEGQGVNVFIEIGPKPVLLGMGRDCLTEQEG-LWLPSL--RPKQDDWQQVLSSLRDLYLAGVTVDwsSFDQGYARRRV 1548
Cdd:TIGR02813  853 EAMYAAGARVFVEFGPKNILQKLVENTLKDKENeLCAISInpNPKGDSDMQLRQAAVQLAVLGLELT--EIDPYQAEKRP 930


                   ....*.
gi 1331970929 1549 PLPTYP 1554
Cdd:TIGR02813  931 PAATSP 936

PRK05691

peptide synthase; Validated

28-637

6.19e-114

peptide synthase; Validated

Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 408.79 E-value: 6.19e-114

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:PRK05691  1136 LLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDY 1215

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  108 PGDRIEYMLRDSDARILLTSTDVAKKLaltiPALQECQTVYLDQeifeydfhflaiakllhnqylrlLHFYFYTliqqcq 187
Cdd:PRK05691  1216 PAERLAYMLADSGVELLLTQSHLLERL----PQAEGVSAIALDS-----------------------LHLDSWP------ 1262

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  188 atsvSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCL 267
Cdd:PRK05691  1263 ----SQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLIT 1338

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  268 GGILVLVPEAVRQNPFALAEFISQQKIEKL-FLPviALLQL-AEAVNGNKSTSLALceVITTGEQMqiTPAVAN--LFQK 343
Cdd:PRK05691  1339 GCRLVLAGPGEHRDPQRIAELVQQYGVTTLhFVP--PLLQLfIDEPLAAACTSLRR--LFSGGEAL--PAELRNrvLQRL 1412

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  344 TGAMLHNHYGATEFQDATTHTLKGNPEGwpTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLT 423
Cdd:PRK05691  1413 PQVQLHNRYGPTETAINVTHWQCQAEDG--ERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALT 1490

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  424 NEKFIPNPFGanENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQ 503
Cdd:PRK05691  1491 AERFVPDPLG--EDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQ 1568

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  504 LVGYIIAKDTLNLSFDKLEPILrqysEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPDPKGDRpalsTPLVKPRTQTE 583
Cdd:PRK05691  1569 LVGYYTGEAGQEAEAERLKAAL----AAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ----REHVEPRTELQ 1640

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1331970929  584 KRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQ 637
Cdd:PRK05691  1641 QQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFE 1694

A_NRPS_ACVS-like

cd17648

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...

37-562

2.39e-113

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.

Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 369.04 E-value: 2.39e-113

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGC-QPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYM 115
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEiRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  116 LRDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgi 195
Cdd:cd17648     81 LEDTGARVVITN-------------------------------------------------------------------- 92

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  196 qtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMlwwHQQTRPSVQGVRT-----LQFCAVSFDFSCHEIFSTLCLGGI 270
Cdd:cd17648     93 -----STDLAYAIYTSGTTGKPKGVLVEHGSVVNL---RTSLSERYFGRDNgdeavLFFSNYVFDFFVEQMTLALLNGQK 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  271 LVLVPEAVRQNPFALAEFISQQKIEKLF-LP-VIALLQLAEAvngnksTSLALceVITTGEQMQiTPAVANLFQKTGAML 348
Cdd:cd17648    165 LVVPPDEMRFDPDRFYAYINREKVTYLSgTPsVLQQYDLARL------PHLKR--VDAAGEEFT-APVFEKLRSRFAGLI 235

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  349 HNHYGATEFqdATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFI 428
Cdd:cd17648    236 INAYGPTET--TVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFL 313

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  429 PNPFGANENAK-----KLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQ 503
Cdd:cd17648    314 PNPFQTEQERArgrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQ 393

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331970929  504 ------LVGYIIAkDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:cd17648    394 sriqkyLVGYYLP-EPGHVP----ESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453

PRK05691

peptide synthase; Validated

1-672

1.11e-112

peptide synthase; Validated

Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 404.55 E-value: 1.11e-112

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929    1 MQKRESPQILFDGNGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAIC 79
Cdd:PRK05691  2165 LAAAEQQQLLDSLAGEAGEARlDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLA 2244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   80 IERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLAlTIPA------LQECQTVYLDQEI 153
Cdd:PRK05691  2245 LERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALG-ELPAgvarwcLEDDAAALAAYSD 2323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  154 FEYDFhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVnmlwW 233
Cdd:PRK05691  2324 APLPF---------------------------------------LSLPQHQAYLIYTSGSTGKPKGVVVSHGEIA----M 2360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  234 HQQTRPSVQGVRT----LQFCAVSFDFSCHEIFSTLCLGGILVLVpeavRQNPFA---LAEFISQQKIEKL-FLPVIALl 305
Cdd:PRK05691  2361 HCQAVIERFGMRAddceLHFYSINFDAASERLLVPLLCGARVVLR----AQGQWGaeeICQLIREQQVSILgFTPSYGS- 2435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  306 QLAEAVNG-NKSTSLALCevIT-----TGEQMQitpAVANLFQKtgAMLHNHYGATEFQDATTHTLKGN--PEGWPTlVP 377
Cdd:PRK05691  2436 QLAQWLAGqGEQLPVRMC--ITggealTGEHLQ---RIRQAFAP--QLFFNAYGPTETVVMPLACLAPEqlEEGAAS-VP 2507

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  378 VGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANenAKKLYRTGDLARYLPDGTIE 457
Cdd:PRK05691  2508 IGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAD--GGRLYRTGDLVRLRADGLVE 2585

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  458 HLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAK--DTLNLSFDKLEPILRQYSEAVLPE 535
Cdd:PRK05691  2586 YVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAvaGQDDEAQAALREALKAHLKQQLPD 2665

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  536 YMIPTRFINISNMPLTPSGKLDRRAL--PDPKGDRPAlstpLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSL 613
Cdd:PRK05691  2666 YMVPAHLILLDSLPLTANGKLDRRALpaPDPELNRQA----YQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSI 2741

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1331970929  614 LLTQAHKfLCETFNINLSAVSLFQYPTIQTLAQYIdcqgdtTSSDTASRHKKVRKKQSG 672
Cdd:PRK05691  2742 LSIQVVS-RARQLGIHFSPRDLFQHQTVQTLAAVA------THSEAAQAEQGPLQGASG 2793

A_NRPS_GliP_like

cd17653

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...

27-561

1.94e-109

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 357.00 E-value: 1.94e-109

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   27 HLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  107 YPGDRIEYMLRDSDARILLTSTDvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqc 186
Cdd:cd17653     81 LPSARIQAILRTSGATLLLTTDS--------------------------------------------------------- 103

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  187 qatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLC 266
Cdd:cd17653    104 --------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLC 169

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  267 LGGILVLVPEAvrqNPFA-LAEFISqqkieklFLP----VIALLQLAEAVNgnkstslaLCEVITTGEQmqITPAVANLF 341
Cdd:cd17653    170 NGGTLVLADPS---DPFAhVARTVD-------ALMstpsILSTLSPQDFPN--------LKTIFLGGEA--VPPSLLDRW 229

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  342 QKtGAMLHNHYGATE--FQDATTHTLKGNPegwptlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNL 419
Cdd:cd17653    230 SP-GRRLYNAYGPTEctISSTMTELLPGQP------VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGN 302

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  420 PDLTNEKFIPNPFganENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQA-VRECAVVAREi 498
Cdd:cd17653    303 PALTASKFVPDPF---WPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPeVTQAAAIVVN- 378

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331970929  499 aghTQLVGYiIAKDTLNLSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17653    379 ---GRLVAF-VTPETVDVD------GLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431

A_NRPS_TlmIV_like

cd12114

The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...

37-561

1.18e-103

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.

Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 342.33 E-value: 1.18e-103

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYML 116
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  117 RDSDARILLTSTDVAKKLALTIPALqecqtvyldqeifeydfhflaiakllhnqylrllhfyfyTLIQQCQATSvSQGIQ 196
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAVFDVL---------------------------------------ILDLDALAAP-APPPP 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  197 TQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQtRPSVQGV-RTLQFCAVSFDFSCHEIFSTLCLGGILVLVP 275
Cdd:cd12114    121 VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR-RFAVGPDdRVLALSSLSFDLSVYDIFGALSAGATLVLPD 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  276 EAVRQNPFALAEFISQQKIeKLFLPVIALLQL----AEAVNGNKStSLALceVITTGE--QMQITPAVANLFqkTGAMLH 349
Cdd:cd12114    200 EARRRDPAHWAELIERHGV-TLWNSVPALLEMlldvLEAAQALLP-SLRL--VLLSGDwiPLDLPARLRALA--PDARLI 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  350 NHYGATEfqdAT----THTLKGNPEGWPTlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNE 425
Cdd:cd12114    274 SLGGATE---ASiwsiYHPIDEVPPDWRS-IPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAA 349

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  426 KFIPNPFGAnenakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLV 505
Cdd:cd12114    350 RFVTHPDGE-----RLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLA 424

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929  506 GYIIAKDTLNLSFdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd12114    425 AFVVPDNDGTPIA---PDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477

AMP-binding

pfam00501

AMP-binding enzyme;

29-469

3.42e-98

AMP-binding enzyme;

Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 323.88 E-value: 3.42e-98

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   29 FEDQAAKRPDAIALIDGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  108 PGDRIEYMLRDSDARILLTstDVAKKLALTIPALQECQTVYldqeifeydfHFLAIAKLLHNQYLRLLHFYFYTLIQQCQ 187
Cdd:pfam00501   81 PAEELAYILEDSGAKVLIT--DDALKLEELLEALGKLEVVK----------LVLVLDRDPVLKEEPLPEEAKPADVPPPP 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  188 ATSVSqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGV----RTLQFCAVSFDFS-CHEIF 262
Cdd:pfam00501  149 PPPPD--------PDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLgpddRVLSTLPLFHDFGlSLGLL 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  263 STLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLP---VIALLQlAEAVNGNKSTSLalcEVITTGeQMQITPAVAN 339
Cdd:pfam00501  221 GPLLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVptlLNMLLE-AGAPKRALLSSL---RLVLSG-GAPLPPELAR 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  340 -LFQKTGAMLHNHYGATEfqdATTHTLKGNPEGWPTLVP--VGRPLHNVQVYILDEA-QQPVPLGGEGEFCIGGIGLARG 415
Cdd:pfam00501  296 rFRELFGGALVNGYGLTE---TTGVVTTPLPLDEDLRSLgsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKG 372

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1331970929  416 YHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIR 469
Cdd:pfam00501  373 YLNDPELTAEAFDEDGW---------YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417

PRK05691

peptide synthase; Validated

10-662

5.15e-98

peptide synthase; Validated

Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 356.40 E-value: 5.15e-98

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   10 LFDG-NGTQSEFP-DSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELF 87
Cdd:PRK05691  3705 LLDGcNRSERDYPlEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLL 3784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   88 IGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTStdvAKKLALTIPALQECQTVyldqeifeydfhflAIAKLL 167
Cdd:PRK05691  3785 GMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCS---AACREQARALLDELGCA--------------NRPRLL 3847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  168 hnqylrllhfyFYTLIQQCQATSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNmlwwHQQTR-P----SVQ 242
Cdd:PRK05691  3848 -----------VWEEVQAGEVASHNPGIYSG--PDNLAYVIYTSGSTGLPKGVMVEQRGMLN----NQLSKvPylalSEA 3910

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  243 GVrTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLfLPVIALLQ--LAEavngNKSTSLA 320
Cdd:PRK05691  3911 DV-IAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVL-ESVPSLIQgmLAE----DRQALDG 3984

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  321 LCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATEFQD--ATTHTLKGNPEGwpTLVPVGRPLHNVQVYILDEAQQPVP 398
Cdd:PRK05691  3985 LRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDdvAFFRVDLASTRG--SYLPIGSPTDNNRLYLLDEALELVP 4062

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  399 LGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGANenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEI 478
Cdd:PRK05691  4063 LGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAP--GERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEI 4140

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  479 ESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDKLEPIlRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:PRK05691  4141 EARLHEQAEVREAAVAVQEGVNGKHLVGYLVPHQTVLAQGALLERI-KQRLRAELPDYMVPLHWLWLDRLPLNANGKLDR 4219

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  559 RALPDPkgDRPAL-STPLVKPRTQTEKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQ 637
Cdd:PRK05691  4220 KALPAL--DIGQLqSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFE 4297

                          650       660
                   ....*....|....*....|....*.
gi 1331970929  638 YPTIQTLAQYID-CQGDTTSSDTASR 662
Cdd:PRK05691  4298 CSTVEELAEYIEgLAGSAIDEQKVDR 4323

DltA

cd05945

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...

33-561

4.18e-96

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 319.19 E-value: 4.18e-96

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRI 112
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  113 EYMLRDSDARILLTStdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvs 192
Cdd:cd05945     81 REILDAAKPALLIAD----------------------------------------------------------------- 95

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  193 qgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILV 272
Cdd:cd05945     96 --------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLV 167

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  273 LVPEAVRQNPFALAEFISQQKIEKLF-LP-VIALLQLAEAVNGNKSTSLALceVITTGEQMQItPAVANLFQKT-GAMLH 349
Cdd:cd05945    168 PVPRDATADPKQLFRFLAEHGITVWVsTPsFAAMCLLSPTFTPESLPSLRH--FLFCGEVLPH-KTARALQQRFpDARIY 244

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  350 NHYGATEFQDATT------HTLKGNPEgwptlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLT 423
Cdd:cd05945    245 NTYGPTEATVAVTyievtpEVLDGYDR-----LPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKT 319

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  424 NEKFIPNPfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR-EIAGHT 502
Cdd:cd05945    320 AAAFFPDE------GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKyKGEKVT 393

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1331970929  503 QLVGYIIAKDTLNlsfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05945    394 ELIAFVVPKPGAE---AGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449

MenE/FadK

COG0318

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...

25-563

3.60e-94

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis

Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 313.67 E-value: 3.60e-94

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  105 VGYPGDRIEYMLRDSDARILLTstdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliq 184
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT---------------------------------------------------------- 102

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  185 qcqatsvsqgiqtqvlpnnlAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFS-CHEIFS 263
Cdd:COG0318    103 --------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLA 162

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  264 TLCLGGILVLVPeavRQNPFALAEFISQQKIEKLFLP---VIALLQLAEAvNGNKSTSLALceVITTGEQMqiTPAVANL 340
Cdd:COG0318    163 PLLAGATLVLLP---RFDPERVLELIERERVTVLFGVptmLARLLRHPEF-ARYDLSSLRL--VVSGGAPL--PPELLER 234

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  341 FQK-TGAMLHNHYGATEfqdaTTHTLKGNPE--GWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYH 417
Cdd:COG0318    235 FEErFGVRIVEGYGLTE----TSPVVTVNPEdpGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYW 310

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  418 NLPDLTNEKFiPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE 497
Cdd:COG0318    311 NDPEATAEAF-RDGW---------LRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVP 380

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331970929  498 IAGHTQ-LVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:COG0318    381 DEKWGErVVAFVVLRPGAELD----AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443

KR_FAS_SDR_x

cd05274

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...

2381-2746

1.83e-93

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187582 [Multi-domain] Cd Length: 375 Bit Score: 308.93 E-value: 1.83e-93

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2381 SCSSTLHLVQALAN--YPKNPRLSLVTLGAQAVNEHHVQNVVGAALWGMGKVIALEHPELQVAQMDLDPNgkvkaqvevl 2458
Cdd:cd05274     29 ALAALLALVAALLAayASTGPPLWLVTRGAEAVSADDVAALAQAALWGLLRVLALEHPELWGGLVDLDAA---------- 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2459 rdellaRKDPASAMSVPDLQTRPHEKQIAFREQTRYVARLSPLDRPNPgekgTQEALTFRDDGSYLIAGGLGGLGLVVAR 2538
Cdd:cd05274     99 ------DAADEAAALAALLAGAPGEDELALRGGQRLVPRLVRAPAAAL----ELAAAPGGLDGTYLITGGLGGLGLLVAR 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2539 FLVTNGAKYLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV-TYPPLRGVIHAAGTLNDGILQQQ 2617
Cdd:cd05274    169 WLAARGARHLVLLSRRGPAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAELaAGGPLAGVIHAAGVLRDALLAEL 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2618 SWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLASYRRHLGLPSLSINWGTWSE 2697
Cdd:cd05274    249 TPAAFAAVLAAKVAGALNLHELTPDLPLDFFVLFSSVAALLGGAGQAAYAAANAFLDALAAQRRRRGLPATSVQWGAWAG 328

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1331970929 2698 VGIAARLELDKLSSKQGEGTITLGQGLQILEQLLKDENGvyQVGVMPIN 2746
Cdd:cd05274    329 GGMAAAAALRARLARSGLGPLAPAEALEALEALLASDAP--QAVVASVD 375

ketoacyl-synt

pfam00109

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...

675-930

2.44e-79

Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 262.96 E-value: 2.44e-79

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  675 NDIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDELE----QTLPELFNNPAYVKAGAvLEGVELFDATFFGYSPK 750
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDpdklYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  751 EAAVTDPQQRILLECAWEAFERAGYNPETYPEP-VGVYAGSSLSTY----LLNNIGSALGIiteQPFIetdmeqfqakIG 825
Cdd:pfam00109   80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSrTGVFIGSGIGDYaallLLDEDGGPRRG---SPFA----------VG 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  826 NDRSYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRA 905
Cdd:pfam00109  147 TMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKA 226

                          250       260
                   ....*....|....*....|....*
gi 1331970929  906 FDAEAQGTIFGNGGGLVLLKRLQDA 930
Cdd:pfam00109  227 FDPFADGFVRGEGVGAVVLKRLSDA 251

FabD

COG0331

Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...

1207-1494

2.02e-75

Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 253.90 E-value: 2.02e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1207 TIAFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQnlgiESILSVIFGSSEHglSLDDTAYTQPALFAIEYALYQL 1286
Cdd:COG0331      2 KLAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEALG----YDLSALCFEGPEE--ELNLTENTQPAILAASVAAYRA 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1287 WKSWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQAL--PRDGSMVSVM-ASEKRIADII--LPYGGQVG 1361
Cdd:COG0331     76 LEEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAvpAGPGGMAAVLgLDDEEVEALCaeAAQGEVVE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1362 IAAINGPQSVVISGQQQAIDAICAILETEGIK-SKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTGTla 1440
Cdd:COG0331    156 IANYNSPGQIVISGEKEAVEAAAELAKEAGAKrAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAA-- 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929 1441 shescpdelPITTAEYW----VRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLGM 1494
Cdd:COG0331    234 ---------PVTDPEEIrellVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGL 282

PKS_KR

smart00822

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...

2535-2697

9.30e-74

Pssm-ID: 214833 [Multi-domain] Cd Length: 180 Bit Score: 243.93 E-value: 9.30e-74

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  2535 VVARFLVTNGAKYLVLVGRRGAREEQQAQL-SELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLND 2611
Cdd:smart00822   15 ALARWLAERGARRLVLLSRSGPDAPGAAALlAELEAAGARVTVVACDVADRDALAAVLAAIpaVEGPLTGVIHAAGVLDD 94

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  2612 GILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLASYRRHLGLPSLSIN 2691
Cdd:smart00822   95 GVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRRARGLPALSIA 174


                    ....*.
gi 1331970929  2692 WGTWSE 2697
Cdd:smart00822  175 WGAWAE 180

pfam08659

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...

2521-2697

5.33e-71

Pssm-ID: 430138 [Multi-domain] Cd Length: 180 Bit Score: 236.30 E-value: 5.33e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2521 GSYLIAGGLGGLGLVVARFLVTNGAKYLVLVGRRGA-REEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYP 2597
Cdd:pfam08659    1 GTYLITGGLGGLGRELARWLAERGARHLVLLSRSAApRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIkaEGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2598 PLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:pfam08659   81 PIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANAFLDALA 160

                          170       180
                   ....*....|....*....|
gi 1331970929 2678 SYRRHLGLPSLSINWGTWSE 2697
Cdd:pfam08659  161 EYRRSQGLPATSINWGPWAE 180

alpha_am_amid

TIGR03443

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...

24-690

5.27e-70

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.

Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 261.54 E-value: 5.27e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   24 CIHHLFEDQAAKRPDAIALI---------DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGIL 94
Cdd:TIGR03443  237 AIHDIFADNAEKHPDRTCVVetpsfldpsSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVL 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   95 KAGCAYVPLDVGYPGDRIEYMLRDSDARIL-----------LTSTDVAKKLAL--TIPAL--QECQTV---YLDQEifEY 156
Cdd:TIGR03443  317 KAGATFSVIDPAYPPARQTIYLSVAKPRALiviekagtldqLVRDYIDKELELrtEIPALalQDDGSLvggSLEGG--ET 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  157 DFhfLAiakllhnQYLRLlhfyfytliqQCQATSVSQGiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQ 236
Cdd:TIGR03443  395 DV--LA-------PYQAL----------KDTPTGVVVG------PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAK 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  237 TRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILvLVPEAVR-QNPFALAEFISQQKIEKLFL-PVIALLQLAEAVNGN 314
Cdd:TIGR03443  450 RFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQL-LVPTADDiGTPGRLAEWMAKYGATVTHLtPAMGQLLSAQATTPI 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  315 KSTSLA--LCEVITTGEQMQITPAVANLFqktgamLHNHYGATEFQDATTH----TLKGNPEGWPTL---VPVGRPLHNV 385
Cdd:TIGR03443  529 PSLHHAffVGDILTKRDCLRLQTLAENVC------IVNMYGTTETQRAVSYfeipSRSSDSTFLKNLkdvMPAGKGMKNV 602

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  386 QVYILD--EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFGAN--------ENAK-----------KLYRT 444
Cdd:TIGR03443  603 QLLVVNrnDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPshwidldkENNKperefwlgprdRLYRT 682

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  445 GDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRE-CAVVAREIAGHTQLVGYIIAKDTLNlSFDKL-- 521
Cdd:TIGR03443  683 GDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnVTLVRRDKDEEPTLVSYIVPQDKSD-ELEEFks 761

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  522 --------EPI---LRQYSEAV----------LPEYMIPTRFINISNMPLTPSGKLDRRALPDPKGDRPALSTPLVKPR- 579
Cdd:TIGR03443  762 evddeessDPVvkgLIKYRKLIkdireylkkkLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSASa 841

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  580 -----TQTEKRLAEIWGSYL--AVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQTLAQYID--C 650
Cdd:TIGR03443  842 adeefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDrlK 921

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|...
gi 1331970929  651 QGDTTSSDTASRHKKVRKKQSGD-SNDIA--IISVAGRFPGAE 690
Cdd:TIGR03443  922 KGEELADEGDSEIEEEETVLELDyAKDAKtlVDSLPKSYPSRK 964

PRK04813

D-alanine--poly(phosphoribitol) ligase subunit DltA;

29-561

6.28e-69

D-alanine--poly(phosphoribitol) ligase subunit DltA;

Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 242.49 E-value: 6.28e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   29 FEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLgcQPDDLLAICI--ERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:PRK04813     8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSL--KLPDKSPIIVfgHMSPEMLATFLGAVKAGHAYIPVDVS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  107 YPGDRIEYMLRDSDARILLTSTDvakkLALTIpalQECQTVYLD--QEIFEYDFHFlaiakllhnqylrllhfyfytliq 184
Cdd:PRK04813    86 SPAERIEMIIEVAKPSLIIATEE----LPLEI---LGIPVITLDelKDIFATGNPY------------------------ 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  185 qcQATSvsqgiqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFST 264
Cdd:PRK04813   135 --DFDH-------AVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPT 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  265 LCLGGILVLVPEAVRQNPFALAEFISQQKIEklflpV---------IALLqlAEAVNGNKSTSLA---LCevittGEQMq 332
Cdd:PRK04813   206 LASGGTLVALPKDMTANFKQLFETLPQLPIN-----VwvstpsfadMCLL--DPSFNEEHLPNLThflFC-----GEEL- 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  333 iTPAVA-NLFQK-TGAMLHNHYGATEFQDATThTLKGNPE---GWPTLvPVGRPLHNVQVYILDEAQQPVPLGGEGEFCI 407
Cdd:PRK04813   273 -PHKTAkKLLERfPSATIYNTYGPTEATVAVT-SIEITDEmldQYKRL-PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI 349

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  408 GGIGLARGYHNLPDLTNEKFIPnpfganENAKKLYRTGDLArYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQA 487
Cdd:PRK04813   350 SGPSVSKGYLNNPEKTAEAFFT------FDGQPAYHTGDAG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSY 422

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929  488 VRECAVVAREIAGH-TQLVGYIIAKDTlnlSFDK---LEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK04813   423 VESAVVVPYNKDHKvQYLIAYVVPKEE---DFERefeLTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497

D-ala-DACP-lig

TIGR01734

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...

25-561

1.60e-68

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 241.20 E-value: 1.60e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEdQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:TIGR01734    3 IEAIQA-FAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  105 VGYPGDRIEYMLRDSDARILLTSTDvakkLALTIPAlQECQTVYLDQEIFEydfhflaiakllhnqylrllhfyfytliq 184
Cdd:TIGR01734   82 TSIPSERIEMIIEAAGPELVIHTAE----LSIDAVG-TQIITLSALEQAET----------------------------- 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  185 qcQATSVSQgiQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFST 264
Cdd:TIGR01734  128 --SGGPVSF--DHAVKGDDNYYIIYTSGSTGNPKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPC 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  265 LCLGGILVLVPEAVRQNPFALAEFISQQKI-EKLFLPVIA-LLQLAEAVNGNKSTSLAlcEVITTGEQMQITPAVANLFQ 342
Cdd:TIGR01734  204 LASGGTLHCLDKDITNNFKLLFEELPKTGLnVWVSTPSFVdMCLLDPNFNQENYPHLT--HFLFCGEELPVKTAKALLER 281

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  343 KTGAMLHNHYGATEFQDA------TTHTLKGNPEgwptlVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGY 416
Cdd:TIGR01734  282 FPKATIYNTYGPTEATVAvtsvkiTQEILDQYPR-----LPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGY 356

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  417 HNLPDLTNEKFIpnpfgaNENAKKLYRTGDLArYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR 496
Cdd:TIGR01734  357 LNNPEKTAEAFF------SHEGQPAYRTGDAG-TITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPK 429

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  497 EIAGH--TQLVGYIIAKDTlnlSFDKLEPILRQYSE---AVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:TIGR01734  430 YNKDHkvEYLIAAIVPETE---DFEKEFQLTKAIKKelkKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496

KR_3_FAS_SDR_x

cd08956

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...

2364-2703

3.51e-68

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187659 [Multi-domain] Cd Length: 448 Bit Score: 238.32 E-value: 3.51e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2364 VHCWSMVSTDLDRATIFSCSSTLHLVQA-LANyPK--NPRLSLVTLGAQAVN-EHHVQNVVGAALWGMGKVIALEHPeLQ 2439
Cdd:cd08956     58 VPCPAAAGGDLAAAAHAAAARALALLQAwLAD-PRlaDSRLVVVTRGAVAAGpDEDVPDLAAAAVWGLVRSAQAEHP-GR 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2440 VAQMDLDPngkvkaqvevlrDELLARKDPASAMSVpdlqtrphEKQIAFREQTRYVARLSpldRPNPGEKGTQEALTFRD 2519
Cdd:cd08956    136 FVLVDLDD------------DAASAAALPAALASG--------EPQLALRDGRLLVPRLA---RVAPAATLPPVPRPLDP 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2520 DGSYLIAGGLGGLGLVVARFLVTN-GAKYLVLVGRRGAREEQQAQL-SELEQLGASVKVLQADIADAEQLAQALSAVTY- 2596
Cdd:cd08956    193 DGTVLITGGTGTLGALLARHLVTEhGVRHLLLVSRRGPDAPGAAELvAELAALGAEVTVAACDVADRAALAALLAAVPAd 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2597 PPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGL 2676
Cdd:cd08956    273 HPLTAVVHAAGVLDDGVLTSLTPERLDAVLRPKVDAAWHLHELTRDLDLAAFVLFSSAAGVLGSPGQANYAAANAFLDAL 352

                          330       340
                   ....*....|....*....|....*..
gi 1331970929 2677 ASYRRHLGLPSLSINWGTWSEVGIAAR 2703
Cdd:cd08956    353 AQHRRARGLPATSLAWGLWAQASGMTA 379

KR_2_SDR_x

cd08953

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...

2344-2731

1.31e-66

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187656 [Multi-domain] Cd Length: 436 Bit Score: 233.41 E-value: 1.31e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2344 PGDIEEwqqLLNRVPNIQEIVHCWSMVSTDLDRATIFSCSSTLHLVQALA--------NYPKNPRLSL-VTLGAQAVNEH 2414
Cdd:cd08953     42 PAALAS---AFLALAYEAALLGLAAAEAALLDALSALDPAAALQLLESLQrllkagllAARASGRALLqVVTGLPGALGL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2415 HVQNVVGAALWGMGKVIALEHPELQVAQMDLDPngkvkaqvEVLRDELLARKdpasamsVPDLQTRPHEKQIAFREQTRY 2494
Cdd:cd08953    119 DALDPAGAGLAGLLRTLAQEYPGLTCRLIDLDA--------GEASAEALARE-------LAAELAAPGAAEVRYRDGLRY 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2495 VARLspldRPNPGEKGTQEALTFRDDGSYLIAGGLGGLGLVVARFLVTNGAKYLVLVGRRGAREEQQAQLS---ELEQLG 2571
Cdd:cd08953    184 VQTL----EPLPLPAGAAASAPLKPGGVYLVTGGAGGIGRALARALARRYGARLVLLGRSPLPPEEEWKAQtlaALEALG 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2572 ASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQPLDFFV 2649
Cdd:cd08953    260 ARVLYISADVTDAAAVRRLLEKVreRYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFV 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2650 LFSSATSLLGNAGQANHAAANAFLDGLASYRR--HLGLPSLSINWGTWSEVGIAARLELDKLSSKQGEGTITLGQGLQIL 2727
Cdd:cd08953    340 LFSSVSAFFGGAGQADYAAANAFLDAFAAYLRqrGPQGRVLSINWPAWREGGMAADLGARELLARAGLLPIEPEEGLQAL 419


                   ....
gi 1331970929 2728 EQLL 2731
Cdd:cd08953    420 EQAL 423

KR_1_SDR_x

cd08952

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...

2385-2702

4.58e-66

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187655 [Multi-domain] Cd Length: 480 Bit Score: 233.22 E-value: 4.58e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2385 TLHLVQALANYPKNPRLSLVTLGAQAVNEH-HVQNVVGAALWGMGKVIALEHPELQVAQMDLdPngkvkaqvEVLRDELL 2463
Cdd:cd08952    116 TLALVQALGDAGVDAPLWCVTRGAVAVGPDdPLPDPAQAAVWGLGRVAALEHPDRWGGLVDL-P--------ADLDARAL 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2464 ARKdpASAmsvpdLQTRPHEKQIAFREQTRYVARLSPLDRPNPGEKgtqealTFRDDGSYLIAGGLGGLGLVVARFLVTN 2543
Cdd:cd08952    187 RRL--AAV-----LAGAGGEDQVAVRASGVFARRLVRAPAPAPAAR------PWRPRGTVLVTGGTGALGAHVARWLARR 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2544 GAKYLVLVGRRGAREEQQAQL-SELEQLGASVKVLQADIADAEQLAQALSAVTY-PPLRGVIHAAGTLNDGILQQQSWQA 2621
Cdd:cd08952    254 GAEHLVLTSRRGPDAPGAAELvAELTALGARVTVAACDVADRDALAALLAALPAgHPLTAVVHAAGVLDDGPLDDLTPER 333

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2622 FKEVMNPKVAGAWNLHILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLASYRRHLGLPSLSINWGTWSEVGIA 2701
Cdd:cd08952    334 LAEVLRAKVAGARHLDELTRDRDLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALAERRRARGLPATSVAWGPWAGGGMA 413


                   .
gi 1331970929 2702 A 2702
Cdd:cd08952    414 A 414

PS-DH

pfam14765

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...

1590-1890

3.63e-63

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.

Pssm-ID: 434191 Cd Length: 296 Bit Score: 218.40 E-value: 3.63e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1590 HPLLGQRLHLSRTQEIYFQTFIHSDFPIWVADHKVFGNVIIPGVAYFEMALAAGKALKPDSIFW-LEDVSIAQALIIP-D 1667
Cdd:pfam14765    1 HPLLGSRVPSPSDLEPVWRNRLRLADLPWLRDHRVGGTVVLPGAGYLEMALEAARQLFGGSGAVaLRDVSILKALVLPeD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1668 EGQTVQIVLSPQEESAYF---FEILSLEKE-NSWVLHASGKLVAqEQVLETEPIDLIALQAHCSEE-----VSVDVLYQE 1738
Cdd:pfam14765   81 DPVEVQTSLTPEEDGADSwweFEIFSRAGGgWEWTLHATGTVRL-APGEPAAPVDLESLPARCAQPadprsVSSAEFYER 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1739 EMARRLDMGPMMRGVKQLWRYPLSfakshdaiALAKVSLPEILLHESNAYQFHPVILDAGLQMITVSYPEA--NQGQTYV 1816
Cdd:pfam14765  160 LAARGLFYGPAFQGLRRIWRGDGE--------ALAEARLPEAAAGGESPYLLHPALLDAALQLLGAALPAEaeHADQAYL 231

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929 1817 PVGIEGLQVYG--RPSSELWCRAQYRPPLDTDqrqgidllpkkLIADLHLFDTQGRVVAIMFGVQSVLVGREAMLR 1890
Cdd:pfam14765  232 PVGIERLRIYRslPPGEPLWVHARLERRGGRT-----------IVGDLTLVDEDGRVVARIEGLRLRRVEREALLR 296

Acs

COG0365

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];

26-576

1.66e-59

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];

Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 216.90 E-value: 1.66e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   26 HHLFEDQAAKRPDAIALI----DGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAY 100
Cdd:COG0365     12 YNCLDRHAEGRGDKVALIwegeDGEeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  101 VPLDVGYPGDRIEYMLRDSDARILLTST---------DVAKKLAltiPALQECQTV-------YLDQEIF---EYDFH-F 160
Cdd:COG0365     92 SPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVD---EALEELPSLehvivvgRTGADVPmegDLDWDeL 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  161 LAIAKllhnqylrllhfyfytliQQCQATSVSqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRS-LVNMLWWHQQtrp 239
Cdd:COG0365    169 LAAAS------------------AEFEPEPTD--------ADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKY--- 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  240 sVQGVR---TLqFCAVSFDF-SCH--EIFSTLCLGGILVLVPEA-VRQNPFALAEFISQQKIEKLFLP--VIALLQLAEA 310
Cdd:COG0365    220 -VLDLKpgdVF-WCTADIGWaTGHsyIVYGPLLNGATVVLYEGRpDFPDPGRLWELIEKYGVTVFFTAptAIRALMKAGD 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  311 VNGNKS--TSLALCevITTGEQmqITPAVAN-LFQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPtLVP--VGRPLHNV 385
Cdd:COG0365    298 EPLKKYdlSSLRLL--GSAGEP--LNPEVWEwWYEAVGVPIVDGWGQTE----TGGIFISNLPGLP-VKPgsMGKPVPGY 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  386 QVYILDEAQQPVPLGGEGEFCIGG--IGLARGYHNLPDLTNEKFipnpFGANENakkLYRTGDLARYLPDGTIEHLGRID 463
Cdd:COG0365    369 DVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETY----FGRFPG---WYRTGDGARRDEDGYFWILGRSD 441

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  464 HQVKIRGFRVELGEIESVLASHQAVRECAVVAR--EIAGhTQLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIPTR 541
Cdd:COG0365    442 DVINVSGHRIGTAEIESALVSHPAVAEAAVVGVpdEIRG-QVVKAFVVLKPGVEPS-DELAKELQAHVREELGPYAYPRE 519

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 1331970929  542 FINISNMPLTPSGKLDRRALPD-----PKGDRPALSTPLV 576
Cdd:COG0365    520 IEFVDELPKTRSGKIMRRLLRKiaegrPLGDTSTLEDPEA 559

KAS_I_II

cd00834

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...

677-1107

7.41e-58

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.

Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 207.01 E-value: 7.41e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  677 IAIISvagrfPGAETIEQFWHNLCNGVESITLFSDDELEQTlpelfnnpaYVKAGAVlegVELFDATFFGySPKEAAVTD 756
Cdd:cd00834      8 LGAVT-----PLGNGVEEFWEALLAGRSGIRPITRFDASGF---------PSRIAGE---VPDFDPEDYL-DRKELRRMD 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  757 PQQRILLECAWEAFERAGYNPETY-PEPVGVYAGSSLSTylLNNIGSALGIITEQPFIETDMEQFQAKIGNDrsyLATRI 835
Cdd:cd00834     70 RFAQFALAAAEEALADAGLDPEELdPERIGVVIGSGIGG--LATIEEAYRALLEKGPRRVSPFFVPMALPNM---AAGQV 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  836 SYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVpqkggylyEEGMV-----------RSQD--GH 902
Cdd:cd00834    145 AIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALI--------TPLTLagfaalralstRNDDpeKA 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  903 CRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgALKMgyTAPSVD--GQADVISEAIAIADIDAS 980
Cdd:cd00834    217 SRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSD-AYHI--TAPDPDgeGAARAMRAALADAGLSPE 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  981 TIGYVEAHGTATQLGDPIEVAGLARAFQRSTDSVlgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYA 1060
Cdd:cd00834    294 DIDYINAHGTSTPLNDAAESKAIKRVFGEHAKKV------PVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLE 367

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1331970929 1061 NPNPRIDFDatpfFVNTELREWsrngyPRRAGVS-SFGVGGTNSHIVL 1107
Cdd:cd00834    368 EPDPECDLD----YVPNEAREA-----PIRYALSnSFGFGGHNASLVF 406

FC-FACS_FadD_like

cd05936

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...

27-561

1.02e-57

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.

Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 208.57 E-value: 1.02e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   27 HLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:cd05936      3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  107 YPGDRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVyldqeifeydfhflaiakllhnqylrllhfyfytliqqc 186
Cdd:cd05936     83 YTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALT--------------------------------------- 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  187 qatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMlwwhQQTRPSVQGVRTLQ---FCAV----SFDFSC 258
Cdd:cd05936    124 --------------PEDVAVLQYTSGTTGVPKGAMLTHRNLVaNA----LQIKAWLEDLLEGDdvvLAALplfhVFGLTV 185

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  259 HeIFSTLCLGGILVLVPeavRQNPFALAEFISQQKIEkLFLPV----IALLQLAEAVNGNKStSLALCevITTGeqMQIT 334
Cdd:cd05936    186 A-LLLPLALGATIVLIP---RFRPIGVLKEIRKHRVT-IFPGVptmyIALLNAPEFKKRDFS-SLRLC--ISGG--APLP 255

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  335 PAVANLF-QKTGAMLHNHYGATEFQDATThtlkGNPEGWPTlVP--VGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIG 411
Cdd:cd05936    256 VEVAERFeELTGVPIVEGYGLTETSPVVA----VNPLDGPR-KPgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQ 330

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  412 LARGYHNLPDLTNEKFIPNPFganenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVREC 491
Cdd:cd05936    331 VMKGYWNRPEETAEAFVDGWL----------RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEA 400

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331970929  492 AVVA--REIAGHTqLVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05936    401 AVVGvpDPYSGEA-VKAFVVLKEGASLT----EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467

Acyl_transf_1

pfam00698

Acyl transferase domain;

1210-1534

2.88e-56

Acyl transferase domain;

Pssm-ID: 395567 Cd Length: 319 Bit Score: 199.62 E-value: 2.88e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1210 FLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNLGIESILSVIFgSSEHGLsLDDTAYTQPALFAIEYALYQLWKS 1289
Cdd:pfam00698    2 FVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVLR-NNPEGT-LDGTQFVQPALFAMQIALAALLQS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1290 WGIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQALPRDGSMVSVMASEKRIADIILPyggQVGIAAINGPQ 1369
Cdd:pfam00698   80 YGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPD---DVVGAVVNSPR 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1370 SVVISGQQQAIDAICAILETEGIKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISnvtgtlaSHESCPDEL 1449
Cdd:pfam00698  157 SVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFIS-------STSIDPSDQ 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1450 PITTAEYWVRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLGMGRDCLTEQEGL----WLPSLRPKQDDWQQVLSSLR 1525
Cdd:pfam00698  230 RTLSAEYWVRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTLKSASDGkvatLVGTLIRDQTDFLVTFLYIL 309

                          330
                   ....*....|
gi 1331970929 1526 D-LYLAGVTV 1534
Cdd:pfam00698  310 AvAHLTGSAP 319

decarbox_cond_enzymes

cd00825

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...

758-1107

3.15e-56

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).

Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 199.78 E-value: 3.15e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  758 QQRILLECAWEAFERAGYNPETYPEP-VGVYAGSSLSTYLLNNIGSAlGIITEQPFIETdmeqfqakiGNDRSYLATRIS 836
Cdd:cd00825     11 VSILGFEAAERAIADAGLSREYQKNPiVGVVVGTGGGSPRFQVFGAD-AMRAVGPYVVT---------KAMFPGASGQIA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  837 YKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMVRSQDGHCRAFDAEAQGTIFG 916
Cdd:cd00825     81 TPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  917 NGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAlKMGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGD 996
Cdd:cd00825    161 DGAGALVVEELEHALARGAHIYAEIVGTAATIDGA-GMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  997 PIEvaglarafQRSTDSVLGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPffvn 1076
Cdd:cd00825    240 VKE--------LKLLRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTE---- 307

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1331970929 1077 telrewSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00825    308 ------TTPRELRTALLNGFGLGGTNATLVL 332

fabD

TIGR00128

malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...

1208-1494

3.57e-55

malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]

Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 195.38 E-value: 3.57e-55

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1208 IAFLFTGQGSQYINMGRTLYDTESTFRAALDRCETILQNlgieSILSVIFGSSEhgLSLDDTAYTQPALFAIEYALYQLW 1287
Cdd:TIGR00128    3 IAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASEALGY----DLKKLCQEGPA--EELNKTQYTQPALYVVSAILYLKL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1288 K-SWGIQPSVVIGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQ-ALP-RDGSMVSVMA-SEKRIADIILPYGGQ-VGI 1362
Cdd:TIGR00128   77 KeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQeAVPeGGGAMAAVIGlDEEQLAQACEEATENdVDL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1363 AAINGPQSVVISGQQQAIDAICAILETEGIK-SKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQPQIKLISNVTgtlAS 1441
Cdd:TIGR00128  157 ANFNSPGQVVISGTKDGVEAAAALFKEMGAKrAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVD---AK 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1331970929 1442 HESCPDELpittAEYWVRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLGM 1494
Cdd:TIGR00128  234 PYTNGDRI----KEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGL 282

FabB

COG0304

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...

687-1107

4.34e-55

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 199.17 E-value: 4.34e-55

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  687 PGAETIEQFWHNLCNG---VESITLFSDDELEQTLpelfnnpayvkAGAVLEgvelFDATFFgYSPKEAAVTDPQQRILL 763
Cdd:COG0304     13 PLGNGVEEFWEALLAGrsgIRPITRFDASGLPVRI-----------AGEVKD----FDPEEY-LDRKELRRMDRFTQYAL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  764 ECAWEAFERAGYNPETY-PEPVGVYAGSSLSTylLNNIGSALGIITEQ------PFIETDMeqfqakIGNDrsyLATRIS 836
Cdd:COG0304     77 AAAREALADAGLDLDEVdPDRTGVIIGSGIGG--LDTLEEAYRALLEKgprrvsPFFVPMM------MPNM---AAGHVS 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  837 YKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISvvvpqkgGYLYEEGM----------VRSQD--GHCR 904
Cdd:COG0304    146 IRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAE-------AAITPLGLagfdalgalsTRNDDpeKASR 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  905 AFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgALKMGYTAPSVDGQADVISEAIAIADIDASTIGY 984
Cdd:COG0304    219 PFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSD-AYHITAPAPDGEGAARAMRAALKDAGLSPEDIDY 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  985 VEAHGTATQLGDPIEVAGLARAFQRSTDSVlgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNP 1064
Cdd:COG0304    298 INAHGTSTPLGDAAETKAIKRVFGDHAYKV------PVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDP 371

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1331970929 1065 RIDFDatpfFVNTELREWsrngyPRRAGVS-SFGVGGTNSHIVL 1107
Cdd:COG0304    372 ECDLD----YVPNEAREA-----KIDYALSnSFGFGGHNASLVF 406

AFD_class_I

cd04433

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...

204-557

1.03e-53

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.

Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 192.50 E-value: 1.03e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  204 LAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLqfCAVSFDFSCH--EIFSTLCLGGILVLVPeavRQN 281
Cdd:cd04433      2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFL--STLPLFHIGGlfGLLGALLAGGTVVLLP---KFD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  282 PFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMqiTPAVANLF-QKTGAMLHNHYGATEFQDA 360
Cdd:cd04433     77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPL--PPELLERFeEAPGIKLVNGYGLTETGGT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  361 TTHTLKGNPEGWPTlvPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNpfganenakk 440
Cdd:cd04433    155 VATGPPDDDARKPG--SVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG---------- 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  441 LYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVG-YIIAKDTLNLSFD 519
Cdd:cd04433    223 WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVaVVVLRPGADLDAE 302

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1331970929  520 KlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:cd04433    303 E----LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336

PRK06187

long-chain-fatty-acid--CoA ligase; Validated

25-564

1.83e-51

long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 191.94 E-value: 1.83e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:PRK06187     8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  105 VGYPGDRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVyldqeIFEYDFHFLAIAKLLHNqylrllhfyFYTLIq 184
Cdd:PRK06187    88 IRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTV-----IVEGDGPAAPLAPEVGE---------YEELL- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  185 qcqATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMlwwhqqtrpsvqgvrTLQFCAVsFDFSCHEIF-- 262
Cdd:PRK06187   153 ---AAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLH---------------SLAVCAW-LKLSRDDVYlv 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  263 ---------STLCLGGILV----LVPEavRQNPFALAEFISQQKIEKLFL-PVI--ALLQLAEAvNGNKSTSLALceVIT 326
Cdd:PRK06187   214 ivpmfhvhaWGLPYLALMAgakqVIPR--RFDPENLLDLIETERVTFFFAvPTIwqMLLKAPRA-YFVDFSSLRL--VIY 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  327 TGEQMqiTPAVANLFQ-KTGAMLHNHYGATEfqdaTTHTL------KGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPL 399
Cdd:PRK06187   289 GGAAL--PPALLREFKeKFGIDLVQGYGMTE----TSPVVsvlppeDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPP 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  400 GGE--GEFCIGGIGLARGYHNLPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGE 477
Cdd:PRK06187   363 DGGevGEIIVRGPWLMQGYWNRPEATAETI----------DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRE 432

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  478 IESVLASHQAVRECAVVAR--EIAGHTQLVgYIIAKDTLNLSFDKLepilRQYSEAVLPEYMIPTRFINISNMPLTPSGK 555
Cdd:PRK06187   433 LEDALYGHPAVAEVAVIGVpdEKWGERPVA-VVVLKPGATLDAKEL----RAFLRGRLAKFKLPKRIAFVDELPRTSVGK 507


                   ....*....
gi 1331970929  556 LDRRALPDP 564
Cdd:PRK06187   508 ILKRVLREQ 516

Ketoacyl-synt_C

pfam02801

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...

938-1059

2.34e-49

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.

Pssm-ID: 426989 Cd Length: 118 Bit Score: 171.60 E-value: 2.34e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  938 MAVIKATAINNDGAlKMGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARAFQRSTDsvlgK 1017
Cdd:pfam02801    1 YAVIKGSAVNHDGR-HNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGAR----K 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1331970929 1018 QQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHY 1059
Cdd:pfam02801   76 QPLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117

A_NRPS_alphaAR

cd17647

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...

47-564

5.26e-49

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.

Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 184.64 E-value: 5.26e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   47 QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRieymlrdsdarillt 126
Cdd:cd17647     19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR--------------- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  127 stdvakklaltipalqecQTVYLDqeifeydfhflaIAKllhnqylrllhfyfytliqqCQATSVSQGIQTQVLPNNLAY 206
Cdd:cd17647     84 ------------------QNIYLG------------VAK--------------------PRGLIVIRAAGVVVGPDSNPT 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  207 CIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILvLVPEAVRQ-NPFAL 285
Cdd:cd17647    114 LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQL-LVPTQDDIgTPGRL 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  286 AEFISQQKIEKLFL-PVIALLQLAEAVNGNKSTSLA--LCEVITTGEQMQITPAVANLfqktgaMLHNHYGATEFQDATT 362
Cdd:cd17647    193 AEWMAKYGATVTHLtPAMGQLLTAQATTPFPKLHHAffVGDILTKRDCLRLQTLAENV------RIVNMYGTTETQRAVS 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  363 H----TLKGNP---EGWPTLVPVGRPLHNVQVYILD--EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPF- 432
Cdd:cd17647    267 YfevpSRSSDPtflKNLKDVMPAGRGMLNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFv 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  433 ----------GANENAK--------KLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRE-CAV 493
Cdd:cd17647    347 epdhwnyldkDNNEPWRqfwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnITL 426

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  494 VAREIAGHTQLVGYIIAKDTLNLSFDKL----------EPI-------------LRQYSEAVLPEYMIPTRFINISNMPL 550
Cdd:cd17647    427 VRRDKDEEPTLVSYIVPRFDKPDDESFAqedvpkevstDPIvkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPL 506

                          570
                   ....*....|....
gi 1331970929  551 TPSGKLDRRALPDP 564
Cdd:cd17647    507 NPNGKVDKPKLQFP 520

elong_cond_enzymes

cd00828

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...

688-1107

9.73e-47

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.

Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 174.55 E-value: 9.73e-47

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  688 GAETIEQFWHNLCNGVESITLFsddeleqtlpelfNNPAYVKAGAVLEGVELFDatFFGYSPKEAAVTDPQQRILLECAW 767
Cdd:cd00828     17 GCDEVEEFWEALREGRSGIAPV-------------ARLKSRFDRGVAGQIPTGD--IPGWDAKRTGIVDRTTLLALVATE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  768 EAFERAGYNPETY--PEPVGVYAGSSLSTYllnnigSALGIITEQPFIETDMEQFQAKIGNDRSYLATRISYKLNLKGPS 845
Cdd:cd00828     82 EALADAGITDPYEvhPSEVGVVVGSGMGGL------RFLRRGGKLDARAVNPYVSPKWMLSPNTVAGWVNILLLSSHGPI 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  846 VNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKGGYLYEEGMV----RSQDGHCRAFDAEAQGTIFGNGGGL 921
Cdd:cd00828    156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALstaeEEPEEMSRPFDETRDGFVEAEGAGV 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  922 VLLKRLQDALDDNDNIMAVIKATAINNDGAlKMGYTAPsVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGDPIEVA 1001
Cdd:cd00828    236 LVLERAELALARGAPIYGRVAGTASTTDGA-GRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESR 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1002 GLARAFQRSTDSVlgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPffvnTELRe 1081
Cdd:cd00828    314 AIAEVAGALGAPL------PVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVV----GLSR- 382

                          410       420
                   ....*....|....*....|....*.
gi 1331970929 1082 wSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00828    383 -DLNLKVRAALVNAFGFGGSNAALVL 407

Firefly_Luc_like

cd05911

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...

41-556

1.51e-46

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.

Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 176.25 E-value: 1.51e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   41 ALIDGE--QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRD 118
Cdd:cd05911      1 AQIDADtgKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  119 SDARILLTSTDVAKKLaltIPALQECQTVY----LDQEIFEYdfhfLAIAKLLHNQYLRLLHFYFytliqqcqatsvsqg 194
Cdd:cd05911     81 SKPKVIFTDPDGLEKV---KEAAKELGPKDkiivLDDKPDGV----LSIEDLLSPTLGEEDEDLP--------------- 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  195 IQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFD-----FSCHeiFSTLClGG 269
Cdd:cd05911    139 PPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiyglFTTL--ASLLN-GA 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  270 ILVLVPeavRQNPFALAEFISQQKIEKLFL--PVIALLQLAEAVNGNKSTSLalcEVITTG-----EQMQitPAVANLFQ 342
Cdd:cd05911    216 TVIIMP---KFDSELFLDLIEKYKITFLYLvpPIAAALAKSPLLDKYDLSSL---RVILSGgaplsKELQ--ELLAKRFP 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  343 KtgAMLHNHYGATEFQDATTHtlkgNPEGWPTLVPVGRPLHNVQVYILDEA-QQPVPLGGEGEFCIGGIGLARGYHNLPD 421
Cdd:cd05911    288 N--ATIKQGYGMTETGGILTV----NPDGDDKPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPE 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  422 LTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGH 501
Cdd:cd05911    362 ATKETFDEDGW---------LHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVS 432

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  502 TQL-VGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYmipTRFIN----ISNMPLTPSGKL 556
Cdd:cd05911    433 GELpRAYVVRKPGEKLTEKE----VKDYVAKKVASY---KQLRGgvvfVDEIPKSASGKI 485

BCL_4HBCL

cd05959

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...

36-561

6.14e-45

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.

Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 172.17 E-value: 6.14e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   36 RPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYM 115
Cdd:cd05959     17 RGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYY 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  116 LRDSDARILLTSTDVAKKLALTIPALQECQTVYLDQEIFEYDFHFLAIAKLLhnqylrllhfyfytliqqcqATSVSQGI 195
Cdd:cd05959     97 LEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELV--------------------AAEAEQLK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  196 QTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQtrpSVQGVRTLQFCavsfdFSCHEIF-------STLC-- 266
Cdd:cd05959    157 PAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVC-----FSAAKLFfayglgnSLTFpl 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  267 -LGGILVLVPEavRQNPFALAEFISQQKIEKLF-LPVI--ALLQLAEAVNGNKStSLALCevITTGEQMqitPA-VANLF 341
Cdd:cd05959    229 sVGATTVLMPE--RPTPAAVFKRIRRYRPTVFFgVPTLyaAMLAAPNLPSRDLS-SLRLC--VSAGEAL---PAeVGERW 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  342 QK-TGAMLHNHYGATE----FQDATTHTLKGNPEGWPtlVPvgrplhNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGY 416
Cdd:cd05959    301 KArFGLDILDGIGSTEmlhiFLSNRPGRVRYGTTGKP--VP------GYEVELRDEDGGDVADGEPGELYVRGPSSATMY 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  417 HNLPDLTNEKFIpnpfganenaKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR 496
Cdd:cd05959    373 WNNRDKTRDTFQ----------GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGV 442

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929  497 EIA-GHTQLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05959    443 EDEdGLTKPKAFVVLRPGYEDS-EALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507

ligase_PEP_1

TIGR03098

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...

25-561

9.74e-45

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.

Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 171.89 E-value: 9.74e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:TIGR03098    2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  105 VGYPGDRIEYMLRDSDARILLTStdvAKKLALTIPALQECqtvyldqeifeYDFHFLAIAKLLHNqyLRLLHFYFYTLIQ 184
Cdd:TIGR03098   82 PLLKAEQVAHILADCNVRLLVTS---SERLDLLHPALPGC-----------HDLRTLIIVGDPAH--ASEGHPGEEPASW 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  185 QCQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVN---MLWWHQQTRPsvqGVRTLQFCAVSFDFSCHEI 261
Cdd:TIGR03098  146 PKLLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAgaqSVATYLENRP---DDRLLAVLPLSFDYGFNQL 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  262 FSTLCLGGILVLVPEAVrqnPFALAEFISQQKIEKLF-LPVIaLLQLAEaVNGNKSTSLALCEVITTGEQM--QITPAVA 338
Cdd:TIGR03098  223 TTAFYVGATVVLHDYLL---PRDVLKALEKHGITGLAaVPPL-WAQLAQ-LDWPESAAPSLRYLTNSGGAMprATLSRLR 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  339 NLFQKtgAMLHNHYGATEFQDATTHTlkgnpegwPTLV-----PVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLA 413
Cdd:TIGR03098  298 SFLPN--ARLFLMYGLTEAFRSTYLP--------PEEVdrrpdSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVA 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  414 RGYHNLPDLTNEKFIPNPfgANENAKKLYRT----GDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVR 489
Cdd:TIGR03098  368 MGYWNDPEKTAERFRPLP--PFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVA 445

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331970929  490 ECAV--VAREIAGHtQLVGYIIAKDTLNLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:TIGR03098  446 EAVAfgVPDPTLGQ-AIVLVVTPPGGEELDRAALLAECRAR----LPNYMVPALIHVRQALPRNANGKIDRKAL 514

FACL_FadD13-like

cd17631

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...

33-558

1.76e-44

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.

Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 168.94 E-value: 1.76e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRI 112
Cdd:cd17631      5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  113 EYMLRDSDARILLtstdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvs 192
Cdd:cd17631     85 AYILADSGAKVLF------------------------------------------------------------------- 97

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  193 qgiqtqvlpNNLAYCIYTSGSTGNPKGILMEHRSLVnmlwWHQQTRPSVQGVRTLQFCAVSFD-FSCHE----IFSTLCL 267
Cdd:cd17631     98 ---------DDLALLMYTSGTTGRPKGAMLTHRNLL----WNAVNALAALDLGPDDVLLVVAPlFHIGGlgvfTLPTLLR 164

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  268 GGILVLVPEAvrqNPFALAEFISQQKIEKLFLP---VIALLQLAEAVNGNKSTslaLCEVITTGEQMQitPAVANLFQKT 344
Cdd:cd17631    165 GGTVVILRKF---DPETVLDLIERHRVTSFFLVptmIQALLQHPRFATTDLSS---LRAVIYGGAPMP--ERLLRALQAR 236

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  345 GAMLHNHYGATE------FQDATTHTLKgnpegwptLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHN 418
Cdd:cd17631    237 GVKFVQGYGMTEtspgvtFLSPEDHRRK--------LGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWN 308

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  419 LPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR-- 496
Cdd:cd17631    309 RPEATAAAF----------RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVpd 378

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929  497 ----EIAghtqlVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd17631    379 ekwgEAV-----VAVVVPRPGAELD----EDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435

KR_1_FAS_SDR_x

cd08954

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...

2537-2735

1.61e-41

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187657 [Multi-domain] Cd Length: 452 Bit Score: 160.69 E-value: 1.61e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2537 ARFLVTNGA-KYLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLA----QALSAVTYPPLRGVIHAAGTLND 2611
Cdd:cd08954    235 LKWLVKRGAvENIIILSRSGMKWELELLIREWKSQNIKFHFVSVDVSDVSSLEkainLILNAPKIGPIGGIFHLAFVLID 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2612 GILQQQSWQAFKEVMNPKVAGAWNLHILT--KNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLASYRRHLGLPSLS 2689
Cdd:cd08954    315 KVLEIDTESLFISVNKAKVMGAINLHNQSikRCWKLDYFVLFSSVSSIRGSAGQCNYVCANSVLDSLSRYRKSIGLPSIA 394

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1331970929 2690 INWGTWSEVGIAARLE-LDKLSSKQGEGTITLGQGLQILEQLLKDEN 2735
Cdd:cd08954    395 INWGAIGDVGFVSRNEsVDTLLGGQGLLPQSINSCLGTLDLFLQNPS 441

FACL_fum10p_like

cd05926

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...

37-563

4.53e-41

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.

Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 160.17 E-value: 4.53e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALI--DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEY 114
Cdd:cd05926      1 PDAPALVvpGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  115 MLRDSDARILLTSTDV-------AKKLALTIpalqecQTVYLDQEIFEydfhflaiaklLHNQYLRLlhfyfytliQQCQ 187
Cdd:cd05926     81 YLADLGSKLVLTPKGElgpasraASKLGLAI------LELALDVGVLI-----------RAPSAESL---------SNLL 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  188 ATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNmlwwhqqtrpSVQGV----------RTLqfcAVSFDFS 257
Cdd:cd05926    135 ADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAA----------SATNItntykltpddRTL---VVMPLFH 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  258 CHEI----FSTLCLGGILVLVPEavrqnpFALAEFISQqkIEKL------FLPVI--ALLQLAEAVNGNK--------ST 317
Cdd:cd05926    202 VHGLvaslLSTLAAGGSVVLPPR------FSASTFWPD--VRDYnatwytAVPTIhqILLNRPEPNPESPppklrfirSC 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  318 SLALcevittgeqmqiTPAVANLFQKT-GAMLHNHYGATEfqdaTTHTLKGNPegWPTLVP----VGRPlHNVQVYILDE 392
Cdd:cd05926    274 SASL------------PPAVLEALEATfGAPVLEAYGMTE----AAHQMTSNP--LPPGPRkpgsVGKP-VGVEVRILDE 334

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  393 AQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFR 472
Cdd:cd05926    335 DGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW---------FRTGDLGYLDADGYLFLTGRIKELINRGGEK 405

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  473 VELGEIESVLASHQAVRECAVVA--REIAGhtQLVG-YIIAKdtLNLSFDKLEpiLRQYSEAVLPEYMIPTRFINISNMP 549
Cdd:cd05926    406 ISPLEVDGVLLSHPAVLEAVAFGvpDEKYG--EEVAaAVVLR--EGASVTEEE--LRAFCRKHLAAFKVPKKVYFVDELP 479

                          570
                   ....*....|....
gi 1331970929  550 LTPSGKLDRRALPD 563
Cdd:cd05926    480 KTATGKIQRRKVAE 493

PRK07656

long-chain-fatty-acid--CoA ligase; Validated

31-561

5.72e-40

long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 157.37 E-value: 5.72e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   31 DQAAKR-PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPG 109
Cdd:PRK07656    12 ARAARRfGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTA 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  110 DRIEYMLRDSDARILLTSTD---VAKKLALTIPALqECQTVYLDQEIFEYDFHFLAIAKLLhnqylrllhfyfytliqqc 186
Cdd:PRK07656    92 DEAAYILARGDAKALFVLGLflgVDYSATTRLPAL-EHVVICETEEDDPHTEKMKTFTDFL------------------- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  187 qATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSL-------VNMLwwhqQTRPsvqGVRTLqfCAVSFdfsch 259
Cdd:PRK07656   152 -AAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLlsnaadwAEYL----GLTE---GDRYL--AANPF----- 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  260 eiFSTLCL----------GGILVLVPeavRQNPFALAEFISQQKIEKLF-LPVI--ALLQLAEAVNGNKStSLALCevIT 326
Cdd:PRK07656   217 --FHVFGYkagvnaplmrGATILPLP---VFDPDEVFRLIETERITVLPgPPTMynSLLQHPDRSAEDLS-SLRLA--VT 288

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  327 TGEQMqitpAVANL--FQK--------TGamlhnhYGATEFQDATTHTlkgNPEGWPTLVP--VGRPLHNVQVYILDEAQ 394
Cdd:PRK07656   289 GAASM----PVALLerFESelgvdivlTG------YGLSEASGVTTFN---RLDDDRKTVAgtIGTAIAGVENKIVNELG 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  395 QPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakkLYrTGDLARYLPDGTIEHLGRIDHQVKIRGFRVE 474
Cdd:PRK07656   356 EEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW--------LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVY 426

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  475 LGEIESVLASHQAVRECAVV----AR--EiAGHtqlvGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNM 548
Cdd:PRK07656   427 PAEVEEVLYEHPAVAEAAVIgvpdERlgE-VGK----AYVVLKPGAELT----EEELIAYCREHLAKYKVPRSIEFLDEL 497

                          570
                   ....*....|...
gi 1331970929  549 PLTPSGKLDRRAL 561
Cdd:PRK07656   498 PKNATGKVLKRAL 510

MCS

cd05941

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...

38-561

7.20e-40

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.

Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 155.53 E-value: 7.20e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   38 DAIALIDGEQSLTYGELNVRANHLAQHLLSLGC-QPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYML 116
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  117 RDSDARILLtstdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiq 196
Cdd:cd05941     81 TDSEPSLVL----------------------------------------------------------------------- 89

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  197 tqvlpnNLAYCIYTSGSTGNPKGILMEHRSLVNML------W-------------WHQqtrpsVQGVRTLQFCAV----- 252
Cdd:cd05941     90 ------DPALILYTSGTTGRPKGVVLTHANLAANVralvdaWrwteddvllhvlpLHH-----VHGLVNALLCPLfagas 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  253 ---SFDFSCHEIFSTLCLGGILVL--VP-------EAVRQNpFALAEFISQQKIEKLFLPViallqlaeavngnkSTSLA 320
Cdd:cd05941    159 vefLPKFDPKEVAISRLMPSITVFmgVPtiytrllQYYEAH-FTDPQFARAAAAERLRLMV--------------SGSAA 223

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  321 LcevittgeqmqITPAVANLFQKTGAMLHNHYGATEFQDATTHTLKGNPE-GWptlvpVGRPLHNVQVYILD-EAQQPVP 398
Cdd:cd05941    224 L-----------PVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRpGT-----VGMPLPGVQARIVDeETGEPLP 287

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  399 LGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRI-DHQVKIRGFRVELGE 477
Cdd:cd05941    288 RGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW---------FKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALE 358

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  478 IESVLASHQAVRECAVVAREIAGHTQLVGYIIA--KDTLNLSFDKLEPILRQyseaVLPEYMIPTRFINISNMPLTPSGK 555
Cdd:cd05941    359 IERVLLAHPGVSECAVIGVPDPDWGERVVAVVVlrAGAAALSLEELKEWAKQ----RLAPYKRPRRLILVDELPRNAMGK 434


                   ....*.
gi 1331970929  556 LDRRAL 561
Cdd:cd05941    435 VNKKEL 440

MACS_like_3

cd05971

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...

50-561

6.72e-39

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.

Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 152.59 E-value: 6.72e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   50 TYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTStd 129
Cdd:cd05971      8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD-- 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  130 vakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvLPNNLAYCIY 209
Cdd:cd05971     86 ----------------------------------------------------------------------GSDDPALIIY 95

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  210 TSGSTGNPKGILMEHRSLVNMLwwhqqtrPSVQgvrtlqfcavsfdfSCHEIFSTL-----------CLGGIL-VLVPE- 276
Cdd:cd05971     96 TSGTTGPPKGALHAHRVLLGHL-------PGVQ--------------FPFNLFPRDgdlywtpadwaWIGGLLdVLLPSl 154

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  277 -------AVRQNPF---ALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEqmqitPAVANLFQ---- 342
Cdd:cd05971    155 yfgvpvlAHRMTKFdpkAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGE-----SLGEELLGware 229

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  343 KTGAMLHNHYGATEfqdatTHTLKGNPEGWPTLVP--VGRPLHNVQVYILDEAQQPVPLGGEGEfciggIGLAR------ 414
Cdd:cd05971    230 QFGVEVNEFYGQTE-----CNLVIGNCSALFPIKPgsMGKPIPGHRVAIVDDNGTPLPPGEVGE-----IAVELpdpvaf 299

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  415 -GYHNLPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV 493
Cdd:cd05971    300 lGYWNNPSATEKKM----------AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAV 369

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331970929  494 VAREIAGHTQLV-GYIIakdtLNLSFDKLEPI---LRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05971    370 VGIPDPIRGEIVkAFVV----LNPGETPSDALareIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437

BCL_like

cd05919

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...

41-561

3.49e-38

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.

Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 150.30 E-value: 3.49e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   41 ALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSD 120
Cdd:cd05919      3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  121 ARILLTSTDvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvl 200
Cdd:cd05919     83 ARLVVTSAD----------------------------------------------------------------------- 91

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  201 pnNLAYCIYTSGSTGNPKGILMEHRslvNMLWWHQQTRPSVQGV----RTLQFCAVSFDFSC-HEIFSTLCLGGILVLVP 275
Cdd:cd05919     92 --DIAYLLYSSGTTGPPKGVMHAHR---DPLLFADAMAREALGLtpgdRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNP 166

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  276 EAVrqNPFALAEFISQQKIEKLF-LPVIALLQLAEAVNGNKS-TSLALCevITTGEQMQitpavANLFQK----TGAMLH 349
Cdd:cd05919    167 GWP--TAERVLATLARFRPTVLYgVPTFYANLLDSCAGSPDAlRSLRLC--VSAGEALP-----RGLGERwmehFGGPIL 237

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  350 NHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFip 429
Cdd:cd05919    238 DGIGATE----VGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-- 311

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  430 npfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA-REIAGHTQLVGYI 508
Cdd:cd05919    312 --------NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAvPESTGLSRLTAFV 383

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1331970929  509 IAKDTLNLSFDKLEPILRQYSEAvLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05919    384 VLKSPAAPQESLARDIHRHLLER-LSAHKVPRRIAFVDELPRTATGKLQRFKL 435

A_NRPS_acs4

cd17654

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...

37-561

1.45e-37

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 148.77 E-value: 1.45e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQ----SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRI 112
Cdd:cd17654      1 PDRPALIIDQTtsdtTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  113 EYMLRDSDarilltstdvakklaltipalqecqtvyldqeifeyDFHFLAiAKLLHNQYLRLLHFYFYTLIQQcqatsvs 192
Cdd:cd17654     81 LTVMKKCH------------------------------------VSYLLQ-NKELDNAPLSFTPEHRHFNIRT------- 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  193 qgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSVQgvRTLQFCAV-SFDFSCHEIFSTLCLGGI 270
Cdd:cd17654    117 --------DECLAYVIHTSGTTGTPKIVAVPHKCILpNIQHFRSLFNITSE--DILFLTSPlTFDPSVVEIFLSLSSGAT 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  271 LVLVPEAVRQNPFALAEFI-SQQKIEKLFLPViALL-----QLAEAVNGNKSTSLalcEVITTGEQMQITPAVANLFQKT 344
Cdd:cd17654    187 LLIVPTSVKVLPSKLADILfKRHRITVLQATP-TLFrrfgsQSIKSTVLSATSSL---RVLALGGEPFPSLVILSSWRGK 262

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  345 GAMLH--NHYGATEFQD-ATTHTLKGNPEGwptlVPVGRPLHNVQVYILDEAQQPvplgGEGEFCIGGI---GLARGYHN 418
Cdd:cd17654    263 GNRTRifNIYGITEVSCwALAYKVPEEDSP----VQLGSPLLGTVIEVRDQNGSE----GTGQVFLGGLnrvCILDDEVT 334

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  419 LPDLTNekfipnpfganenakklYRTGDLARyLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVareI 498
Cdd:cd17654    335 VPKGTM-----------------RATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT---L 393

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331970929  499 AGHTQLVGYIIAKDTLNLSFDKLEPILrqyseavLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17654    394 SDQQRLIAFIVGESSSSRIHKELQLTL-------LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449

PKS_DH

smart00826

Dehydratase domain in polyketide synthase (PKS) enzymes;

1590-1753

2.05e-37

Dehydratase domain in polyketide synthase (PKS) enzymes;

Pssm-ID: 214837 Cd Length: 167 Bit Score: 139.28 E-value: 2.05e-37

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  1590 HPLLGQRLHLSRTQEIYFQTFIHSDFPIWVADHKVFGNVIIPGVAYFEMALAAGKALKPDSIFWLEDVSIAQALIIPDEG 1669
Cdd:smart00826    1 HPLLGARVELADGGGVVLTGRLSLRTHPWLADHRVGGTVVLPGAAYVELALAAADEVGGGAPARLEELTLEAPLVLPEDG 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  1670 -QTVQIVLS-PQEESAYFFEILSL-EKENSWVLHASGKLVAQEQVLETEPIDLIALQAHCSEEVSVDVLYQEEMARRLDM 1746
Cdd:smart00826   81 aVRVQVVVGaPDEDGRRTFTVYSRpDGDGPWTRHATGTLRPAAAAPAAPAADLAAWPPAGAEPVDVDDLYERLAARGLEY 160


                    ....*..
gi 1331970929  1747 GPMMRGV 1753
Cdd:smart00826  161 GPAFQGL 167

MACS_like

cd05972

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...

49-563

2.22e-37

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.

Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 147.87 E-value: 2.22e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   49 LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTST 128
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  129 DvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlpnNLAYCI 208
Cdd:cd05972     81 E-------------------------------------------------------------------------DPALIY 87

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  209 YTSGSTGNPKGILMEHRSLVNmlwwHQQTRPSVQGVRT--LQFC--------AVSFDFscheiFSTLCLGgILVLVPEAV 278
Cdd:cd05972     88 FTSGTTGLPKGVLHTHSYPLG----HIPTAAYWLGLRPddIHWNiadpgwakGAWSSF-----FGPWLLG-ATVFVYEGP 157

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  279 RQNPFALAEFISQQKIEKLFLPVIALLQLAEA--VNGNKSTslaLCEVITTGEQMqiTPAVANLFQ-KTGAMLHNHYGAT 355
Cdd:cd05972    158 RFDAERILELLERYGVTSFCGPPTAYRMLIKQdlSSYKFSH---LRLVVSAGEPL--NPEVIEWWRaATGLPIRDGYGQT 232

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  356 E--FQDATTHTLKGNPEGwptlvpVGRPLHNVQVYILDEAQQPVPLGGEGEFCI--GGIGLARGYHNLPDLTNEKFIPNp 431
Cdd:cd05972    233 EtgLTVGNFPDMPVKPGS------MGRPTPGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD- 305

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  432 fganenakkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLV-GYIIA 510
Cdd:cd05972    306 ---------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVkAFVVL 376

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1331970929  511 KDTLNLSfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:cd05972    377 TSGYEPS-EELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428

PLN02752

[acyl-carrier protein] S-malonyltransferase

1206-1494

1.07e-36

[acyl-carrier protein] S-malonyltransferase

Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 143.36 E-value: 1.07e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1206 PTIAFLFTGQGSQYINMGRTLYDTEstfrAALDRCETILQNLGIEsILSV-IFGSSEhglSLDDTAYTQPALFAIEYALY 1284
Cdd:PLN02752    38 PTTAFLFPGQGAQAVGMGKEAAEVP----AAKALFDKASEILGYD-LLDVcVNGPKE---KLDSTVVSQPAIYVASLAAV 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1285 QLWKSWGIQPSVV------IGHSVGEYVSACVAGVFSLEDGLKLIAERGRLIQAL--PRDGSMVSV--MASEKrIADIIL 1354
Cdd:PLN02752   110 EKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAadAGPSGMVSVigLDSDK-VQELCA 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1355 PYGGQVG------IAAINGPQSVVISGQQQAIDAICAILETEG-IKSKKLNVSHAFHSPLVEAMLDSFLQVAQEVTYSQP 1427
Cdd:PLN02752   189 AANEEVGeddvvqIANYLCPGNYAVSGGKKGIDAVEAKAKSFKaRMTVRLAVAGAFHTSFMEPAVDALEAALAAVEIRTP 268

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331970929 1428 QIKLISNVTGtlASHeSCPDELPITTAeywvRHVRQPVRFAAGMESLEGQGVNVFIEIGPKPVLLGM 1494
Cdd:PLN02752   269 RIPVISNVDA--QPH-SDPATIKKILA----RQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGI 328

EntE

COG1021

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...

25-561

4.52e-36

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 146.06 E-value: 4.52e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCayVPLD 104
Cdd:COG1021     27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVF 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  105 VgYPGDR---IEYMLRDSDARILLTSTDVAKklaltipalqecqtvyldqeifeydFHFLAIAKLLHNQYLRLLHF---- 177
Cdd:COG1021    105 A-LPAHRraeISHFAEQSEAVAYIIPDRHRG-------------------------FDYRALARELQAEVPSLRHVlvvg 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  178 ---YFYTLiQQCQATSVSqGIQTQVLPNNLAYCIYTSGSTGNPKGILMEH-------RSLVNMLWWHQQTRpsvqgvrtl 247
Cdd:COG1021    159 dagEFTSL-DALLAAPAD-LSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHddylysvRASAEICGLDADTV--------- 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  248 QFCAV----SFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALaefISQQKIEKLFL-PVIALLQLaEAVNGNKST--SLa 320
Cdd:COG1021    228 YLAALpaahNFPLSSPGVLGVLYAGGTVVLAPDPSPDTAFPL---IERERVTVTALvPPLALLWL-DAAERSRYDlsSL- 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  321 lcEVITTGEQmQITPAVANLFQKT-GAMLHNHYGATEF----------QDATTHTlkgnpegwptlvpVGRPL--HNvQV 387
Cdd:COG1021    303 --RVLQVGGA-KLSPELARRVRPAlGCTLQQVFGMAEGlvnytrlddpEEVILTT-------------QGRPIspDD-EV 365

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  388 YILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVk 467
Cdd:COG1021    366 RIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF---------YRTGDLVRRTPDGYLVVEGRAKDQI- 435

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  468 IRGfrvelGE------IESVLASHQAVRECAVVAREiaghTQLVG-----YIIAKDTlNLSFDKLEPILRqysEAVLPEY 536
Cdd:COG1021    436 NRG-----GEkiaaeeVENLLLAHPAVHDAAVVAMP----DEYLGerscaFVVPRGE-PLTLAELRRFLR---ERGLAAF 502

                          570       580
                   ....*....|....*....|....*
gi 1331970929  537 MIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:COG1021    503 KLPDRLEFVDALPLTAVGKIDKKAL 527

23DHB-AMP_lg

cd05920

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...

27-561

4.68e-34

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.

Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 139.00 E-value: 4.68e-34

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   27 HLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVpldVG 106
Cdd:cd05920     19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV---LA 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  107 YPGDRieymLRDSDARIlltstDVAKKLALTIPalqecqtvyldQEIFEYDFHFLAIaKLLHNQylrllhfyfytliqqc 186
Cdd:cd05920     96 LPSHR----RSELSAFC-----AHAEAVAYIVP-----------DRHAGFDHRALAR-ELAESI---------------- 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  187 qatsvsqgiqtqvlpNNLAYCIYTSGSTGNPKGILMEHRSLVNMLwwhqqtRPSVQ----GVRTLQFCAVS----FDFSC 258
Cdd:cd05920    139 ---------------PEVALFLLSGGTTGTPKLIPRTHNDYAYNV------RASAEvcglDQDTVYLAVLPaahnFPLAC 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  259 HEIFSTLCLGGILVLVPEAVRQNPFALaefISQQKIEKLFL-PVIALLQLAEAVNGNKS-TSLALCEVitTGEQMQITPA 336
Cdd:cd05920    198 PGVLGTLLAGGRVVLAPDPSPDAAFPL---IEREGVTVTALvPALVSLWLDAAASRRADlSSLRLLQV--GGARLSPALA 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  337 vANLFQKTGAMLHNHYGATEfqDATTHTLKGNPEGwPTLVPVGRPLH-NVQVYILDEAQQPVPLGGEGEFCIGGIGLARG 415
Cdd:cd05920    273 -RRVPPVLGCTLQQVFGMAE--GLLNYTRLDDPDE-VIIHTQGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRG 348

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  416 YHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA 495
Cdd:cd05920    349 YYRAPEHNARAFTPDGF---------YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVA 419

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929  496 --REIAGHTQLVgYIIAKDTlNLSFDKLEPILRqysEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05920    420 mpDELLGERSCA-FVVLRDP-PPSAAQLRRFLR---ERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482

PRK07314

beta-ketoacyl-ACP synthase II;

687-1107

2.64e-33

beta-ketoacyl-ACP synthase II;

Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 135.30 E-value: 2.64e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  687 PGAETIEQFWHNLC---NGVESITLFSDDELEqtlpelfnnpayVKAGAVLEGvelFDATFFgYSPKEAAVTDPQQRILL 763
Cdd:PRK07314    14 PLGNDVESTWKNLLagkSGIGPITHFDTSDLA------------VKIAGEVKD---FNPDDY-MSRKEARRMDRFIQYGI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  764 ECAWEAFERAGYNPETY-PEPVGVYAGSSlstyllnnIGsALGIITEQ-------------PFietdmeqF-QAKIGNdr 828
Cdd:PRK07314    78 AAAKQAVEDAGLEITEEnADRIGVIIGSG--------IG-GLETIEEQhitllekgprrvsPF-------FvPMAIIN-- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  829 sYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGG-------ISVvvpqkGGYLYEEGMVRSQD- 900
Cdd:PRK07314   140 -MAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGaeaaitpLGI-----AGFAAARALSTRNDd 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  901 --GHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgALKMgyTAPSVDGQ--ADVISEAIAIAD 976
Cdd:PRK07314   214 peRASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGD-AYHM--TAPAPDGEgaARAMKLALKDAG 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  977 IDASTIGYVEAHGTATQLGDPIEVAGLARAFQRSTDSVlgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPS 1056
Cdd:PRK07314   291 INPEDIDYINAHGTSTPAGDKAETQAIKRVFGEHAYKV------AVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPT 364

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929 1057 LHYANPNPRIDFDATPffvntelrewsrnGYPRRAGV-----SSFGVGGTNSHIVL 1107
Cdd:PRK07314   365 INLDNPDEECDLDYVP-------------NEARERKIdyalsNSFGFGGTNASLVF 407

FACL_DitJ_like

cd05934

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

50-562

6.14e-33

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.

Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 134.34 E-value: 6.14e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   50 TYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTStd 129
Cdd:cd05934      5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  130 vakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlpnnLAYCIY 209
Cdd:cd05934     83 --------------------------------------------------------------------------PASILY 88

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  210 TSGSTGNPKGILMEHRslvNMLWWHQQTRpSVQGVRTLQFCAVSFDFS-----CHEIFSTLCLGGILVLVPEavrqnpFA 284
Cdd:cd05934     89 TSGTTGPPKGVVITHA---NLTFAGYYSA-RRFGLGEDDVYLTVLPLFhinaqAVSVLAALSVGATLVLLPR------FS 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  285 LAEFISQqkIEKL------FLPVIALLQLAEAVNGNKSTS---LALCEVITTGEqmqitpaVANLFQKTGAMLHNHYGAT 355
Cdd:cd05934    159 ASRFWSD--VRRYgatvtnYLGAMLSYLLAQPPSPDDRAHrlrAAYGAPNPPEL-------HEEFEERFGVRLLEGYGMT 229

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  356 EfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCI---GGIGLARGYHNLPDLTNEKFiPNPF 432
Cdd:cd05934    230 E----TIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RNGW 304

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  433 ganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA-REIAGHTQLVGYIIAK 511
Cdd:cd05934    305 ---------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAvPDEVGEDEVKAVVVLR 375

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1331970929  512 DTLNLSFDKlepiLRQYSEAVLPEYMIPtRFINI-SNMPLTPSGKLDRRALP 562
Cdd:cd05934    376 PGETLDPEE----LFAFCEGQLAYFKVP-RYIRFvDDLPKTPTEKVAKAQLR 422

cond_enzymes

cd00327

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...

758-1107

1.02e-32

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.

Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 129.10 E-value: 1.02e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  758 QQRILLECAWEAFERAGYnpeTYPEPVGVYAGSSLSTYLLnnigsalgiiteqpfietdmeqfqakigndrSYLATRISY 837
Cdd:cd00327      7 ASELGFEAAEQAIADAGL---SKGPIVGVIVGTTGGSGEF-------------------------------SGAAGQLAY 52

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  838 KLNLK-GPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVpqkggylyeegmvrsqdghcrafdaeaqgtiFG 916
Cdd:cd00327     53 HLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEFV-------------------------------FG 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  917 NGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAlkMGYTAPSVDGQADVISEAIAIADIDASTIGYVEAHGTATQLGD 996
Cdd:cd00327    102 DGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGA--SMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGD 179

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  997 PIEVAGLarafqrstDSVLGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPslhyanpnpridfdatpffvn 1076
Cdd:cd00327    180 AVELALG--------LDPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPP--------------------- 230

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1331970929 1077 telrewsRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00327    231 -------TPREPRTVLLLGFGLGGTNAAVVL 254

PTZ00050

3-oxoacyl-acyl carrier protein synthase; Provisional

691-1103

1.94e-32

3-oxoacyl-acyl carrier protein synthase; Provisional

Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 132.89 E-value: 1.94e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  691 TIEQFWHNLCNGVESITLFS--DDELEQTLPELFNNPAYVkaGAVLEGV------ELFDATFFGYSPKEaavtDPQQRIL 762
Cdd:PTZ00050     8 GAESTWEALIAGKSGIRKLTefPKFLPDCIPEQKALENLV--AAMPCQIaaevdqSEFDPSDFAPTKRE----SRATHFA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  763 LECAWEAFERAG--YNPETYPEPVGVyagsslstyllnNIGSALGIITEqpfIETDMEQFQAK-------------IGND 827
Cdd:PTZ00050    82 MAAAREALADAKldILSEKDQERIGV------------NIGSGIGSLAD---LTDEMKTLYEKghsrvspyfipkiLGNM 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  828 RSYLatrISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGG-------ISVV--------------VPQK 886
Cdd:PTZ00050   147 AAGL---VAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGteasitpVSFAgfsrmralctkyndDPQR 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  887 GgylyeegmvrsqdghCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGalkMGYTAPSVDGQAD 966
Cdd:PTZ00050   224 A---------------SRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDA---HHITAPHPDGRGA 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  967 VISEAIAI---ADIDASTIGYVEAHGTATQLGDPIEVAGLARAFQRSTDsvlgkQQCAIGSVKTNIGHLDEAAGIAGLIK 1043
Cdd:PTZ00050   286 RRCMENALkdgANININDVDYVNAHATSTPIGDKIELKAIKKVFGDSGA-----PKLYVSSTKGGLGHLLGAAGAVESIV 360

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331970929 1044 AALALQYGQIPPSLHYANPNPRIDFDATPFFVNTELRewsrngyPRRAGVS-SFGVGGTNS 1103
Cdd:PTZ00050   361 TILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPLQ-------SIDAVLStSFGFGGVNT 414

PRK06178

acyl-CoA synthetase; Validated

33-561

2.85e-32

acyl-CoA synthetase; Validated

Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 135.17 E-value: 2.85e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRI 112
Cdd:PRK06178    43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  113 EYMLRDSDARILLTSTDVAKklaLTIPALQECQTvyldQEIFEYDFH-------------FLAIAKLLHNQYLRLLhfyf 179
Cdd:PRK06178   123 SYELNDAGAEVLLALDQLAP---VVEQVRAETSL----RHVIVTSLAdvlpaeptlplpdSLRAPRLAAAGAIDLL---- 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  180 ytliqQCQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNM-----LWWHQQTRPSVQGVRTLQFCAVSF 254
Cdd:PRK06178   192 -----PALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTaaaayAVAVVGGEDSVFLSFLPEFWIAGE 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  255 DFSCheIFSTLClGGILVLVpeaVRQNPFALAEFISQQKIEKLFLPV---IALLQLAEAVNGNKSTslaLCEVITTGEQM 331
Cdd:PRK06178   267 NFGL--LFPLFS-GATLVLL---ARWDAVAFMAAVERYRVTRTVMLVdnaVELMDHPRFAEYDLSS---LRQVRVVSFVK 337

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  332 QITPAVANLFQK-TGAML-HNHYGATEFQDATTHT---------LKGNPegwptlVPVGRPLHNVQVYILD-EAQQPVPL 399
Cdd:PRK06178   338 KLNPDYRQRWRAlTGSVLaEAAWGMTETHTCDTFTagfqdddfdLLSQP------VFVGLPVPGTEFKICDfETGELLPL 411

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  400 GGEGEFCIGGIGLARGYHNLPDLTNEKFIPNpfganenakkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIE 479
Cdd:PRK06178   412 GAEGEIVVRTPSLLKGYWNKPEATAEALRDG----------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVE 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  480 SVLASHQAVRECAVVAREIAGHTQL-VGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFInISNMPLTPSGKLDR 558
Cdd:PRK06178   482 ALLGQHPAVLGSAVVGRPDPDKGQVpVAFVQLKPGADLT----AAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRK 556


                   ...
gi 1331970929  559 RAL 561
Cdd:PRK06178   557 QDL 559

PRK06333

beta-ketoacyl-ACP synthase;

692-1107

3.25e-32

beta-ketoacyl-ACP synthase;

Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 132.43 E-value: 3.25e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  692 IEQFWHNLCNGVESITLFSDDELEQTlpelfnnPAYVkAGAVLEGVELFDAtffGYSPkEAAVTDPQQR-----IL--LE 764
Cdd:PRK06333    21 VETFWQRLLAGQSGIRTLTDFPVGDL-------ATKI-GGQVPDLAEDAEA---GFDP-DRYLDPKDQRkmdrfILfaMA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  765 CAWEAFERAGYNPETYPEPV--GVYAGSSlstyllnnIGsALGIITEQpfIETDMEQfqakiGNDR-------SYL---- 831
Cdd:PRK06333    89 AAKEALAQAGWDPDTLEDRErtATIIGSG--------VG-GFPAIAEA--VRTLDSR-----GPRRlspftipSFLtnma 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  832 ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQ--KGGYL----YEEGMVRSQDGHCRA 905
Cdd:PRK06333   153 AGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRvsLAGFAaaraLSTRFNDAPEQASRP 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  906 FDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgALKMgyTAPSVDGQ--ADVISEAIAIADIDASTIG 983
Cdd:PRK06333   233 FDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSAD-AYHM--TAGPEDGEgaRRAMLIALRQAGIPPEEVQ 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  984 YVEAHGTATQLGDPIEVAGLARAFqrSTDSVLgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPN 1063
Cdd:PRK06333   310 HLNAHATSTPVGDLGEVAAIKKVF--GHVSGL-----AVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPD 382

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1331970929 1064 PRID-FDatpfFVNTELREWSRngypRRAGVSSFGVGGTNSHIVL 1107
Cdd:PRK06333   383 PAAEgLD----VVANKARPMDM----DYALSNGFGFGGVNASILF 419

PRK07798

acyl-CoA synthetase; Validated

28-559

9.36e-32

acyl-CoA synthetase; Validated

Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 133.09 E-value: 9.36e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:PRK07798     8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  108 PGDRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQtvyldqeifeydfHFLAIAKLLHNQYLRLLHFYfytliqqcq 187
Cdd:PRK07798    88 VEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLR-------------TLVVVEDGSGNDLLPGAVDY--------- 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  188 ATSVSQGIQTQVL----PNNLaYCIYTSGSTGNPKGILMEH----RSLVNMLWW---------HQQTRPSVQGVRTLQFC 250
Cdd:PRK07798   146 EDALAAGSPERDFgersPDDL-YLLYTGGTTGMPKGVMWRQedifRVLLGGRDFatgepiedeEELAKRAAAGPGMRRFP 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  251 AVSFdfsCH-----EIFSTLCLGGILVLVPEaVRQNPFALAEFISQQKIEKLFL-------PVIALLQLAEAVNGnksTS 318
Cdd:PRK07798   225 APPL---MHgagqwAAFAALFSGQTVVLLPD-VRFDADEVWRTIEREKVNVITIvgdamarPLLDALEARGPYDL---SS 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  319 LALceVITTGEQMqiTPAVANLFQ--KTGAMLHNHYGATE--FQdATTHTLKGNPEGWPTLVPVGRplhnvQVYILDEAQ 394
Cdd:PRK07798   298 LFA--IASGGALF--SPSVKEALLelLPNVVLTDSIGSSEtgFG-GSGTVAKGAVHTGGPRFTIGP-----RTVVLDEDG 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  395 QPVPLGGegefciGGIG-LAR------GYHNLPDLTNEKF---------IPnpfganenakklyrtGDLARYLPDGTIEH 458
Cdd:PRK07798   368 NPVEPGS------GEIGwIARrghiplGYYKDPEKTAETFptidgvryaIP---------------GDRARVEADGTITL 426

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  459 LGRiDHQV------KIrgFrVElgEIESVLASHQAVRECAVVAR--EIAGhtQLVGYIIAKDTlNLSFDKLEpiLRQYSE 530
Cdd:PRK07798   427 LGR-GSVCintggeKV--F-PE--EVEEALKAHPDVADALVVGVpdERWG--QEVVAVVQLRE-GARPDLAE--LRAHCR 495

                          570       580
                   ....*....|....*....|....*....
gi 1331970929  531 AVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:PRK07798   496 SSLAGYKVPRAIWFVDEVQRSPAGKADYR 524

PRK08316

acyl-CoA synthetase; Validated

33-561

1.39e-31

acyl-CoA synthetase; Validated

Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 132.36 E-value: 1.39e-31

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRI 112
Cdd:PRK08316    21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  113 EYMLRDSDARILLTSTDVAkklALTIPALQECQTVYLDQEIF----EYDFHFLAIAKLLhnqylrllhfyfytliqqcQA 188
Cdd:PRK08316   101 AYILDHSGARAFLVDPALA---PTAEAALALLPVDTLILSLVlggrEAPGGWLDFADWA-------------------EA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  189 TSVSQGiQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVnmlwwHQQTRpsvqgvrtlqfCAVSFDFSCHEIF------ 262
Cdd:PRK08316   159 GSVAEP-DVELADDDLAQILYTSGTESLPKGAMLTHRALI-----AEYVS-----------CIVAGDMSADDIPlhalpl 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  263 -----------STLCLGGILVLVPEAVRQNPFALaefISQQKIEKLFLP--V-IALLQLAEaVNGNKSTSLALC------ 322
Cdd:PRK08316   222 yhcaqldvflgPYLYVGATNVILDAPDPELILRT---IEAERITSFFAPptVwISLLRHPD-FDTRDLSSLRKGyygasi 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  323 ---EVITtgEQMQITPAVAnlfqktgamLHNHYGATEFqdATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPL 399
Cdd:PRK08316   298 mpvEVLK--ELRERLPGLR---------FYNCYGQTEI--APLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAP 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  400 GGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIE 479
Cdd:PRK08316   365 GEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF----------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVE 434

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  480 SVLASHQAVRECAVVA----REIAGHTQLVgyiIAKDTLNLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGK 555
Cdd:PRK08316   435 EALYTHPAVAEVAVIGlpdpKWIEAVTAVV---VPKAGATVTEDELIAHCRAR----LAGFKVPKRVIFVDELPRNPSGK 507


                   ....*.
gi 1331970929  556 LDRRAL 561
Cdd:PRK08316   508 ILKREL 513

PRK06188

acyl-CoA synthetase; Validated

34-561

4.29e-31

acyl-CoA synthetase; Validated

Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 130.88 E-value: 4.29e-31

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   34 AKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD-VGYPGDRI 112
Cdd:PRK06188    23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHpLGSLDDHA 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  113 eYMLRDSDARILLTS----TDVAKKLALTIPALQECQTVyldqEIFEYDFHFLAIAkllhnqylrllhfyfytliqqcqA 188
Cdd:PRK06188   103 -YVLEDAGISTLIVDpapfVERALALLARVPSLKHVLTL----GPVPDGVDLLAAA-----------------------A 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  189 TSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNML------W-WHQQTRPSVqgVRTLQFCAVSFdfscheI 261
Cdd:PRK06188   155 KFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAqiqlaeWeWPADPRFLM--CTPLSHAGGAF------F 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  262 FSTLCLGGILVLVPEAvrqNPFALAEFISQQKIEKLFL-P--VIALLQLAEAVNGNKStSLalcEVITTGEQmQITPA-V 337
Cdd:PRK06188   227 LPTLLRGGTVIVLAKF---DPAEVLRAIEEQRITATFLvPtmIYALLDHPDLRTRDLS-SL---ETVYYGAS-PMSPVrL 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  338 ANLFQKTGAMLHNHYGATEFQDATTHTLKG-----NPEgwpTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGL 412
Cdd:PRK06188   299 AEAIERFGPIFAQYYGQTEAPMVITYLRKRdhdpdDPK---RLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLV 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  413 ARGYHNLPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECA 492
Cdd:PRK06188   376 MDGYWNRPEETAEAF----------RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVA 445

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331970929  493 V--VAREIAGHTqLVGYIIAKDTLNLSFDKLEPILRQYSEAVlpeyMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK06188   446 VigVPDEKWGEA-VTAVVVLRPGAAVDAAELQAHVKERKGSV----HAPKQVDFVDSLPLTALGKPDKKAL 511

LC_FACS_like

cd05935

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...

48-561

1.28e-30

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.

Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 127.98 E-value: 1.28e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   48 SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTS 127
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  128 TDVakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlpNNLAYC 207
Cdd:cd05935     81 SEL-----------------------------------------------------------------------DDLALI 89

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  208 IYTSGSTGNPKGILMEHRSL----VNMLWWHQQTrPSVQGVRTLQFCAVSfDFScHEIFSTLCLGGILVLVpeaVRQNPF 283
Cdd:cd05935     90 PYTSGTTGLPKGCMHTHFSAaanaLQSAVWTGLT-PSDVILACLPLFHVT-GFV-GSLNTAVYVGGTYVLM---ARWDRE 163

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  284 ALAEFISQQKIEKLFLPVIALLQLAEAVNgNKSTSLALCEVITTGeQMQITPAVANLFQKTGAMLHNH-YGATEFQdATT 362
Cdd:cd05935    164 TALELIEKYKVTFWTNIPTMLVDLLATPE-FKTRDLSSLKVLTGG-GAPMPPAVAEKLLKLTGLRFVEgYGLTETM-SQT 240

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  363 HTlkgNPEGWPTLVPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIpnpfgaNENAKKL 441
Cdd:cd05935    241 HT---NPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI------EIKGRRF 311

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  442 YRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR--EIAGHTqLVGYIIAKDTLNLSFD 519
Cdd:cd05935    312 FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVpdERVGEE-VKAFIVLRPEYRGKVT 390

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1331970929  520 KLEPIlrQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05935    391 EEDII--EWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430

PRK06087

medium-chain fatty-acid--CoA ligase;

31-561

3.97e-30

medium-chain fatty-acid--CoA ligase;

Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 128.33 E-value: 3.97e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   31 DQAAKRPDAIALIDGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPG 109
Cdd:PRK06087    31 QTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  110 DRIEYMLRDSDARILLTSTDVAK----KLALTI----PALQecQTVYLDQEIFEYDfhFLAIAKLLHNqylrllhfyFYT 181
Cdd:PRK06087   111 AELVWVLNKCQAKMFFAPTLFKQtrpvDLILPLqnqlPQLQ--QIVGVDKLAPATS--SLSLSQIIAD---------YEP 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  182 LIQQCQATSvsqgiqtqvlpNNLAYCIYTSGSTGNPKGILMEHRSLV----------NMLWWHQQTRPSVQGVRTLQFca 251
Cdd:PRK06087   178 LTTAITTHG-----------DELAAVLFTSGTEGLPKGVMLTHNNILaseraycarlNLTWQDVFMMPAPLGHATGFL-- 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  252 vsfdfscHEIFSTLCLGGILVLVPeavRQNPFALAEFISQQKIEKLF--LPVIA-LLQLAEAVNGNKST-SLALCEVITt 327
Cdd:PRK06087   245 -------HGVTAPFLIGARSVLLD---IFTPDACLALLEQQRCTCMLgaTPFIYdLLNLLEKQPADLSAlRFFLCGGTT- 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  328 geqmqITPAVANLFQKTGAMLHNHYGATEfqdATTHTL--KGNPEGWpTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEF 405
Cdd:PRK06087   314 -----IPKKVARECQQRGIKLLSVYGSTE---SSPHAVvnLDDPLSR-FMHTDGYAAAGVEIKVVDEARKTLPPGCEGEE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  406 CIGGIGLARGYHNLPDLTNEKFipnpfganeNAKKLYRTGDLARYLPDGTIEHLGRiDHQVKIRGFR-VELGEIESVLAS 484
Cdd:PRK06087   385 ASRGPNVFMGYLDEPELTARAL---------DEEGWYYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQ 454

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331970929  485 HQAVRECAVVAR--EIAGHtQLVGYIIAKDTLNLSfdKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK06087   455 HPKIHDACVVAMpdERLGE-RSCAYVVLKAPHHSL--TLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530

FAA1

COG1022

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];

25-494

4.00e-29

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];

Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 125.98 E-value: 4.00e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALI----DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAY 100
Cdd:COG1022     13 LPDLLRRRAARFPDRVALRekedGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  101 VPLDVGYPGDRIEYMLRDSDARILLTST----DVAKKLALTIPALQecQTVYLDQEIFEYDFHFLAIAKLLHNQYLRLLH 176
Cdd:COG1022     93 VPIYPTSSAEEVAYILNDSGAKVLFVEDqeqlDKLLEVRDELPSLR--HIVVLDPRGLRDDPRLLSLDELLALGREVADP 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  177 FYFYTLIQQCQatsvsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLqfcavSFDF 256
Cdd:COG1022    171 AELEARRAAVK-------------PDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL-----SFLP 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  257 SCH--E-IFSTLCL-GGILVLVPEAVRQNPFALAE-----FIS------------QQKIE-------KLFLPVIAL-LQL 307
Cdd:COG1022    233 LAHvfErTVSYYALaAGATVAFAESPDTLAEDLREvkptfMLAvprvwekvyagiQAKAEeagglkrKLFRWALAVgRRY 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  308 AEAVNGNKSTSLAL----------------------CEV-ITTGEQMQitPAVANLFQKTGAMLHNHYGATEfqdaTTHT 364
Cdd:COG1022    313 ARARLAGKSPSLLLrlkhaladklvfsklrealggrLRFaVSGGAALG--PELARFFRALGIPVLEGYGLTE----TSPV 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  365 LKGNPEGWPTLVPVGRPLHNVQVYIldeaqqpvplGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRT 444
Cdd:COG1022    387 ITVNRPGDNRIGTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW---------LHT 447

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1331970929  445 GDLARYLPDGTIEHLGRIDHQVKIR-GFRVELGEIESVLASHQAVRECAVV 494
Cdd:COG1022    448 GDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498

PRK07910

beta-ketoacyl-ACP synthase;

676-1107

1.11e-28

beta-ketoacyl-ACP synthase;

Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 121.76 E-value: 1.11e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  676 DIAIISVAGRFPGAETIEQFWHNLCNGVESITLFSDDELEQtlpelFNNPayVKAGAVLegVELFDAtffGYSPKEAAVT 755
Cdd:PRK07910    13 NVVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEE-----FDLP--VRIGGHL--LEEFDH---QLTRVELRRM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  756 DPQQRILLECAWEAFERAGyNPETYPEPVGVyagsslstyllnNIGSALGIITEQPFIETDMEQFQAKIGNDRS---YL- 831
Cdd:PRK07910    81 SYLQRMSTVLGRRVWENAG-SPEVDTNRLMV------------SIGTGLGSAEELVFAYDDMRARGLRAVSPLAvqmYMp 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  832 ---ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISV---VVPQKGGYLYEEGMVRSQD---GH 902
Cdd:PRK07910   148 ngpAAAVGLERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETrieAVPIAGFAQMRIVMSTNNDdpaGA 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  903 CRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGalkMGYTAPSVDGQ--ADVISEAIAIADIDAS 980
Cdd:PRK07910   228 CRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDG---FHMVAPDPNGEraGHAMTRAIELAGLTPG 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  981 TIGYVEAHGTATQLGDPIEvaglARAFQRStdsvLGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYA 1060
Cdd:PRK07910   305 DIDHVNAHATGTSVGDVAE----GKAINNA----LGGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLE 376

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1331970929 1061 NPNPRIDFDAtpffVNTElrewSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:PRK07910   377 NLDPEIDLDV----VAGE----PRPGNYRYAINNSFGFGGHNVALAF 415

MACS_like_2

cd05973

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...

49-561

2.56e-28

Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 121.09 E-value: 2.56e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   49 LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTst 128
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  129 DVAKKlaltipalqecqtvyldqeifeydfHFLAIAKLLHnqylrllhfyfytliqqcqatsvsqgiqtqvlpnnlaycI 208
Cdd:cd05973     79 DAANR-------------------------HKLDSDPFVM---------------------------------------M 94

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  209 YTSGSTGNPKGILMEHRSLvnmLWWHQQTRPSVqGVR--TLQFCAVSFDFSC---HEIFSTLCLGgilvlVPEAVRQNPF 283
Cdd:cd05973     95 FTSGTTGLPKGVPVPLRAL---AAFGAYLRDAV-DLRpeDSFWNAADPGWAYglyYAITGPLALG-----HPTILLEGGF 165

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  284 ALAefISQQKIEKLFL------PVIALLQLAEAVNGNKSTSLALCEVITTGEQMqiTPAVANLFQKT-GAMLHNHYGATE 356
Cdd:cd05973    166 SVE--STWRVIERLGVtnlagsPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPL--TPEVIRWFDAAlGVPIHDHYGQTE 241

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  357 F------QDATTHTLKgnpEGwptlvPVGRPLHNVQVYILDEAQQPVplgGEGEFCIGGIGLAR-------GYHNLPDlt 423
Cdd:cd05973    242 LgmvlanHHALEHPVH---AG-----SAGRAMPGWRVAVLDDDGDEL---GPGEPGRLAIDIANsplmwfrGYQLPDT-- 308

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  424 nekfiPNPFGanenakKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQ 503
Cdd:cd05973    309 -----PAIDG------GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTE 377

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1331970929  504 LV-GYIIAKDTLNLSFDkLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05973    378 VVkAFVVLRGGHEGTPA-LADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435

FACL_like_6

cd05922

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

57-561

3.17e-28

Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 121.01 E-value: 3.17e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   57 RANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCA----YVPLDVGYPGDRIEYMLRDSDARILLTSTDVAK 132
Cdd:cd05922      2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  133 KLALTIPALQECQTVYLDQEIfeydfhflaiaklLHNQYLRLLHfyfytliqqcqatsvsqgiqtQVLPNNLAYCIYTSG 212
Cdd:cd05922     82 RLRDALPASPDPGTVLDADGI-------------RAARASAPAH---------------------EVSHEDLALLLYTSG 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  213 STGNPKGILMEHRSLVnmlwWHQQTRPSVQGV----RTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEAVRqnPFALAEF 288
Cdd:cd05922    128 STGSPKLVRLSHQNLL----ANARSIAEYLGItaddRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL--DDAFWED 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  289 ISQQKIEKlFLPVIALLQLAEAVnGNKSTSLALCEVIT-TGEQMqitPAV-----ANLFQktGAMLHNHYGATE-FQDAT 361
Cdd:cd05922    202 LREHGATG-LAGVPSTYAMLTRL-GFDPAKLPSLRYLTqAGGRL---PQEtiarlRELLP--GAQVYVMYGQTEaTRRMT 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  362 T---HTLKGNPEGwptlvpVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPdltnekfiPNPFGANENA 438
Cdd:cd05922    275 YlppERILEKPGS------IGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDP--------PYRRKEGRGG 340

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  439 KKLYrTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSf 518
Cdd:cd05922    341 GVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKIDPK- 418

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1331970929  519 dklePILRQYSEaVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05922    419 ----DVLRSLAE-RLPPYKVPATVRVVDELPLTASGKVDYAAL 456

PRK06839

o-succinylbenzoate--CoA ligase;

25-568

9.52e-28

o-succinylbenzoate--CoA ligase;

Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 120.35 E-value: 9.52e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLL-SLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPL 103
Cdd:PRK06839     4 IAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  104 DVGYPGDRIEYMLRDSDARILLtstdVAKKLALTIPALQECQTVYldqeifeydfHFLAIAKLlhnqylrllhfyfytli 183
Cdd:PRK06839    84 NIRLTENELIFQLKDSGTTVLF----VEKTFQNMALSMQKVSYVQ----------RVISITSL----------------- 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  184 qqcqATSVSQGIQTQVLPNNLAYCI--YTSGSTGNPKGILMEHrslVNMLWwhqqtrPSVQGVRTLqfcavsfDFSCHEI 261
Cdd:PRK06839   133 ----KEIEDRKIDNFVEKNESASFIicYTSGTTGKPKGAVLTQ---ENMFW------NALNNTFAI-------DLTMHDR 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  262 -----------------FSTLCLGGILVlVPEavRQNPFALAEFISQQKIEKLF-LPVI--ALLQLAEAVngnkSTSLAL 321
Cdd:PRK06839   193 sivllplfhiggiglfaFPTLFAGGVII-VPR--KFEPTKALSMIEKHKVTVVMgVPTIhqALINCSKFE----TTNLQS 265

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  322 CEVITTGEQMQITPAVANlFQKTGAMLHNHYGATEFQDATTHTLKGNPEGWPTlvPVGRPLHNVQVYILDEAQQPVPLGG 401
Cdd:PRK06839   266 VRWFYNGGAPCPEELMRE-FIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVG--SIGKPVLFCDYELIDENKNKVEVGE 342

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  402 EGEFCIGGIGLARGYHNLPDLTNEKfIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESV 481
Cdd:PRK06839   343 VGELLIRGPNVMKEYWNRPDATEET-IQDGW---------LCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQV 412

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  482 LASHQAVRECAVVAR------EIAghtqlVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGK 555
Cdd:PRK06839   413 INKLSDVYEVAVVGRqhvkwgEIP-----IAFIVKKSSSVLI----EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGK 483

                          570
                   ....*....|...
gi 1331970929  556 LDRRALPDPKGDR 568
Cdd:PRK06839   484 IQKAQLVNQLKSR 496

PRK06164

acyl-CoA synthetase; Validated

28-554

1.57e-27

acyl-CoA synthetase; Validated

Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 120.23 E-value: 1.57e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:PRK06164    15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  108 PGDRIEYMLRDSDARILLT-----STDVAKKLALTIPAlqECQTVyldQEIFEYDFHFLAIAKllhnqylRLLHFYFYTL 182
Cdd:PRK06164    95 RSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVPPD--ALPPL---RAIAVVDDAADATPA-------PAPGARVQLF 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  183 IQQCQATSVSQGIQTQVlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTL---QFCAVsFDFSch 259
Cdd:PRK06164   163 ALPDPAPPAAAGERAAD-PDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLaalPFCGV-FGFS-- 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  260 EIFSTLCLGGILVLVP--EAVRQnpfalAEFISQQKIEKLFLPVIALLQLAEAVNGNKS-TSLALCEVITtgeqmqITPA 336
Cdd:PRK06164   239 TLLGALAGGAPLVCEPvfDAART-----ARALRRHRVTHTFGNDEMLRRILDTAGERADfPSARLFGFAS------FAPA 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  337 VANLFQKT---GAMLHNHYGATEFQDATThtlkgnpeGWPTLVPV-------GRPLH-NVQVYILDEAQQPV-PLGGEGE 404
Cdd:PRK06164   308 LGELAALArarGVPLTGLYGSSEVQALVA--------LQPATDPVsvrieggGRPASpEARVRARDPQDGALlPDGESGE 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  405 FCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLAS 484
Cdd:PRK06164   380 IEIRAPSLMRGYLDNPDATARALTDDGY---------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEA 450

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  485 HQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSG 554
Cdd:PRK06164   451 LPGVAAAQVVGATRDGKTVPVAFVIPTDGASPD----EAGLMAACREALAGFKVPARVQVVEAFPVTESA 516

4CL

cd05904

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...

33-500

3.14e-27

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.

Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 118.88 E-value: 3.14e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALIDGE--QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGD 110
Cdd:cd05904     15 ASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  111 RIEYMLRDSDARILLTSTDVAKKLA-LTIPalqecqTVYLDqeifEYDFHFLAiakllhnqylrllhfyFYTLIQQCQAT 189
Cdd:cd05904     95 EIAKQVKDSGAKLAFTTAELAEKLAsLALP------VVLLD----SAEFDSLS----------------FSDLLFEADEA 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  190 SVSQgiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLwwhQQTRPSVQGVRTLQ---FCAVSFdfsCHeIFS--- 263
Cdd:cd05904    149 EPPV---VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMV---AQFVAGEGSNSDSEdvfLCVLPM---FH-IYGlss 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  264 ----TLCLGGILVLVPEavrqnpFALAEFISQ-QKIEKLFLPVIA--LLQLAEAVNGNKSTSLALcEVITTGE---QMQI 333
Cdd:cd05904    219 falgLLRLGATVVVMPR------FDLEELLAAiERYKVTHLPVVPpiVLALVKSPIVDKYDLSSL-RQIMSGAaplGKEL 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  334 TPAVANLFQKtgAMLHNHYGATEFQDATTHTLkgNPEGWPT-LVPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIG 411
Cdd:cd05904    292 IEAFRAKFPN--VDLGQGYGMTESTGVVAMCF--APEKDRAkYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPS 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  412 LARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVREC 491
Cdd:cd05904    368 IMKGYLNNPEATAATIDKEGW---------LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDA 438

                          490
                   ....*....|.
gi 1331970929  492 AVVAR--EIAG 500
Cdd:cd05904    439 AVIPYpdEEAG 449

PRK07103

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated

829-1108

3.89e-27

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated

Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 117.05 E-value: 3.89e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  829 SYLATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALA-GGISVVVPQKGGYLYEEGMVRSQ------DG 901
Cdd:PRK07103   144 TDLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAvGALMDLSYWECQALRSLGAMGSDrfadepEA 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  902 HCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGALKmgyTAPSVDGQADVISEAIAIADIDAST 981
Cdd:PRK07103   224 ACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRG---PDPSLEGEMRVIRAALRRAGLGPED 300

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  982 IGYVEAHGTATQLGDPIEVAGLARAfqrstdsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYAN 1061
Cdd:PRK07103   301 IDYVNPHGTGSPLGDETELAALFAS---------GLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDE 371

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1331970929 1062 P-NPRIDFdatpffvnteLREWSRNGYPRRAGVSSFGVGGTNSHIVLE 1108
Cdd:PRK07103   372 PiDERFRW----------VGSTAESARIRYALSLSFGFGGINTALVLE 409

PRK08314

long-chain-fatty-acid--CoA ligase; Validated

21-495

4.01e-27

long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 119.29 E-value: 4.01e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   21 PDSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLS-LGCQPDDLLAICIERSAELFIGLLGILKAGCA 99
Cdd:PRK08314     8 PETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  100 YVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLAltiPALQECQ---------TVYLDQEiFEYDFH-FLAIAKLLHN 169
Cdd:PRK08314    88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVA---PAVGNLRlrhvivaqySDYLPAE-PEIAVPaWLRAEPPLQA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  170 QYLRLLHFYFYTLIQQCQATSVSQGiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSL----VNMLWWHQQTRPSVqGVR 245
Cdd:PRK08314   164 LAPGGVVAWKEALAAGLAPPPHTAG------PDDLAVLPYTSGTTGVPKGCMHTHRTVmanaVGSVLWSNSTPESV-VLA 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  246 TLQFCAVS-FDFSCHeifSTLCLGGILVLVPEAVRQnpfALAEFISQQK-----------IEKLFLPVIALLQLAeavng 313
Cdd:PRK08314   237 VLPLFHVTgMVHSMN---APIYAGATVVLMPRWDRE---AAARLIERYRvthwtniptmvVDFLASPGLAERDLS----- 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  314 nkstSLALceviTTGEQMQITPAVAN-LFQKTGAMLHNHYGATEfQDATTHTlkgNPEGWPTLVPVGRPLHNVQVYILD- 391
Cdd:PRK08314   306 ----SLRY----IGGGGAAMPEAVAErLKELTGLDYVEGYGLTE-TMAQTHS---NPPDRPKLQCLGIPTFGVDARVIDp 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  392 EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIpnpfganE-NAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRG 470
Cdd:PRK08314   374 ETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI-------EiDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASG 446

                          490       500
                   ....*....|....*....|....*
gi 1331970929  471 FRVELGEIESVLASHQAVRECAVVA 495
Cdd:PRK08314   447 FKVWPAEVENLLYKHPAIQEACVIA 471

AAS_C

cd05909

C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...

48-561

5.51e-27

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.

Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 117.82 E-value: 5.51e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   48 SLTYGELNVRANHLAQhLLSLGCQPDDLLAICIERSAELFIGLLGILKAGcaYVPLDVGYPG--DRIEYMLRDSDARILL 125
Cdd:cd05909      7 SLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAglRELRACIKLAGIKTVL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  126 TSTDVAKKLALT--IPALQECQTVYLDQ---EIFEYDFHFLAIAKLLHNQYLRLLHFyfytliqqcqatsvsqgiQTQVL 200
Cdd:cd05909     84 TSKQFIEKLKLHhlFDVEYDARIVYLEDlraKISKADKCKAFLAGKFPPKWLLRIFG------------------VAPVQ 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  201 PNNLAYCIYTSGSTGNPKGILMEHRSLVNMLwwhQQTRPSVQGVRTLQFCAV-----SFDF-SCheIFSTLCLGGILVLV 274
Cdd:cd05909    146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANV---EQITAIFDPNPEDVVFGAlpffhSFGLtGC--LWLPLLSGIKVVFH 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  275 PEAVrqNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALceVITTGEQMQitPAVANLFQKT-GAMLHNHYG 353
Cdd:cd05909    221 PNPL--DYKKIPELIYDKKATILLGTPTFLRGYARAAHPEDFSSLRL--VVAGAEKLK--DTLRQEFQEKfGIRILEGYG 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  354 ATEFQDATTHTLK--GNPEGwptlvPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipn 430
Cdd:cd05909    295 TTECSPVISVNTPqsPNKEG-----TVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF--- 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  431 pfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAV-RECAVVAREIAGHTQLVgyII 509
Cdd:cd05909    367 -------GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKI--VL 437

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1331970929  510 AKDTLNLSFDKLEPILRqysEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05909    438 LTTTTDTDPSSLNDILK---NAGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486

CHC_CoA_lg

cd05903

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...

48-556

8.26e-27

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.

Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 116.33 E-value: 8.26e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   48 SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTs 127
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  128 tdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqaTSVSQGIQTQVLPNNLAYC 207
Cdd:cd05903     80 -------------------------------------------------------------PERFRQFDPAAMPDAVALL 98

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  208 IYTSGSTGNPKGILMEHRSLVNMLwwHQQTRPSVQGVRTLQFCAVS---FDFSCHEIFSTLCLGGILVLVPeavRQNPFA 284
Cdd:cd05903     99 LFTSGTTGEPKGVMHSHNTLSASI--RQYAERLGLGPGDVFLVASPmahQTGFVYGFTLPLLLGAPVVLQD---IWDPDK 173

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  285 LAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQmqITPAVA-NLFQKTGAMLHNHYGATEFQDATTH 363
Cdd:cd05903    174 ALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGAT--VPRSLArRAAELLGAKVCSAYGSTECPGAVTS 251

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  364 TLKGNPEgwPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipnPFGanenakkLYR 443
Cdd:cd05903    252 ITPAPED--RRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA---PEG-------WFR 319

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  444 TGDLARYLPDGTIEHLGRiDHQVKIR-GFRVELGEIESVLASHQAVRECAVVA--REIAGHtQLVGYIIAKDTLNLSFDK 520
Cdd:cd05903    320 TGDLARLDEDGYLRITGR-SKDIIIRgGENIPVLEVEDLLLGHPGVIEAAVVAlpDERLGE-RACAVVVTKSGALLTFDE 397

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1331970929  521 lepiLRQYSEAV-LPEYMIPTRFINISNMPLTPSGKL 556
Cdd:cd05903    398 ----LVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKV 430

MACS_like_4

cd05969

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...

49-561

1.31e-26

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.

Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 116.06 E-value: 1.31e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   49 LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTST 128
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  129 DVAKKLAltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlPNNLAYCI 208
Cdd:cd05969     81 ELYERTD-----------------------------------------------------------------PEDPTLLH 95

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  209 YTSGSTGNPKGILMEHRSLVNmlwwHQQTRPSVQGVRT--LQFCAVSFDF---SCHEIFSTLcLGGILVLVPEAvRQNPF 283
Cdd:cd05969     96 YTSGTTGTPKGVLHVHDAMIF----YYFTGKYVLDLHPddIYWCTADPGWvtgTVYGIWAPW-LNGVTNVVYEG-RFDAE 169

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  284 ALAEFISQQKIEKLFLPVIALLQL----AEAVNGNKSTSLALceVITTGEQMQiTPAVANLFQKTGAMLHNHYGATEfqd 359
Cdd:cd05969    170 SWYGIIERVKVTVWYTAPTAIRMLmkegDELARKYDLSSLRF--IHSVGEPLN-PEAIRWGMEVFGVPIHDTWWQTE--- 243

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  360 aTTHTLKGNPEGWPTLV-PVGRPLHNVQVYILDEAQQPVPLGGEGEFCI--GGIGLARGYHNLPDLTNEKFIPNpfgane 436
Cdd:cd05969    244 -TGSIMIANYPCMPIKPgSMGKPLPGVKAAVVDENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFIDG------ 316

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  437 nakkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREiaghTQLVGYII-AKDTLN 515
Cdd:cd05969    317 ----WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKP----DPLRGEIIkAFISLK 388

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1331970929  516 LSF---DKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05969    389 EGFepsDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437

PRK07059

Long-chain-fatty-acid--CoA ligase; Validated

27-565

1.71e-26

Long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 117.43 E-value: 1.71e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   27 HLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:PRK07059    27 DLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  107 YPGDRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYLDQEifeydfHFLAIAKLLHNQYLRLL----------- 175
Cdd:PRK07059   107 YTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMG------DLLGFKGHIVNFVVRRVkkmvpawslpg 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  176 HFYFYTLIQQCQATSVSQgiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLW---WHQ---QTRPSVQGVRTLq 248
Cdd:PRK07059   181 HVRFNDALAEGARQTFKP---VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQmeaWLQpafEKKPRPDQLNFV- 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  249 fCAVSFdfscHEIFS-TLC------LGGILVLVPeavrqNPFALAEFISQQKIEKlFLPVIALLQLAEAV-NGNKSTSLA 320
Cdd:PRK07059   257 -CALPL----YHIFAlTVCgllgmrTGGRNILIP-----NPRDIPGFIKELKKYQ-VHIFPAVNTLYNALlNNPDFDKLD 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  321 LCEVITT-GEQMQITPAVAN-LFQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLV-PVGRPLHNVQVYILDEAQQPV 397
Cdd:PRK07059   326 FSKLIVAnGGGMAVQRPVAErWLEMTGCPITEGYGLSE----TSPVATCNPVDATEFSgTIGLPLPSTEVSIRDDDGNDL 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  398 PLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGE 477
Cdd:PRK07059   402 PLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF---------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNE 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  478 IESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPtRFINISN-MPLTPSGKL 556
Cdd:PRK07059   473 IEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALT----EEDVKAFCKERLTNYKRP-KFVEFRTeLPKTNVGKI 547


                   ....*....
gi 1331970929  557 DRRALPDPK 565
Cdd:PRK07059   548 LRRELRDGK 556

VL_LC_FACS_like

cd05907

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...

44-561

2.61e-26

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.

Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 115.39 E-value: 2.61e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   44 DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLdvgYP---GDRIEYMLRDSD 120
Cdd:cd05907      1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPI---YPtssAEQIAYILNDSE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  121 ARILLTSTdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvl 200
Cdd:cd05907     78 AKALFVED------------------------------------------------------------------------ 85

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  201 PNNLAYCIYTSGSTGNPKGILMEHRslvNMLWwhqQTRPSVQGVRTLQFCA-VSFDFSCH--E----IFSTLCLGGILVL 273
Cdd:cd05907     86 PDDLATIIYTSGTTGRPKGVMLSHR---NILS---NALALAERLPATEGDRhLSFLPLAHvfErragLYVPLLAGARIYF 159

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  274 VP--EAVRQNpfaLAEFISQQKI------EKLFLPViallqLAEAVNGNKSTSLAL-----CEVITTGEQmQITPAVANL 340
Cdd:cd05907    160 ASsaETLLDD---LSEVRPTVFLavprvwEKVYAAI-----KVKAVPGLKRKLFDLavggrLRFAASGGA-PLPAELLHF 230

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  341 FQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEaqqpvplggeGEFCIGGIGLARGYHNLP 420
Cdd:cd05907    231 FRALGIPVYEGYGLTE----TSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNP 296

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  421 DLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRI-DHQVKIRGFRVELGEIESVLASHQAVRECAVVAR--- 496
Cdd:cd05907    297 EATAEALDADGW---------LHTGDLGEIDEDGFLHITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVIGDgrp 367

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  497 ----------EIAGHTQLVGYIIAKDTLNLSFDK-LEPILRQYSEAV---LPEYMIPTRFI------NISNMPLTPSGKL 556
Cdd:cd05907    368 flvalivpdpEALEAWAEEHGIAYTDVAELAANPaVRAEIEAAVEAAnarLSRYEQIKKFLllpepfTIENGELTPTLKL 447


                   ....*
gi 1331970929  557 DRRAL 561
Cdd:cd05907    448 KRPVI 452

PRK05677

long-chain-fatty-acid--CoA ligase; Validated

19-563

3.05e-26

long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 116.79 E-value: 3.05e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   19 EFPDscIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSL-GCQPDDLLAICIERSAELFIGLLGILKAG 97
Cdd:PRK05677    22 EYPN--IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAG 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   98 CAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYldQEIfeYDFHfLAIAKLLHNQYLRLLHF 177
Cdd:PRK05677   100 LIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIV--TEV--ADML-PPLKRLLINAVVKHVKK 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  178 YF--YTLIQQCQATSV-SQGIQTQVLP-----NNLAYCIYTSGSTGNPKGILMEHRSLV-NMLwwhqQTRPSVqGVRTLQ 248
Cdd:PRK05677   175 MVpaYHLPQAVKFNDAlAKGAGQPVTEanpqaDDVAVLQYTGGTTGVAKGAMLTHRNLVaNML----QCRALM-GSNLNE 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  249 FCAV-----------SFDFSCheiFSTLCLGGILVLVPeavrqNPFALAEFISQQKIEKlFLPVIALLQLAEAVNGNKS- 316
Cdd:PRK05677   250 GCEIliaplplyhiyAFTFHC---MAMMLIGNHNILIS-----NPRDLPAMVKELGKWK-FSGFVGLNTLFVALCNNEAf 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  317 -----TSLALceviTTGEQMQITPAVANLFQK-TGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYIL 390
Cdd:PRK05677   321 rkldfSALKL----TLSGGMALQLATAERWKEvTGCAICEGYGMTE----TSPVVSVNPSQAIQVGTIGIPVPSTLCKVI 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  391 DEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipnpfganeNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRG 470
Cdd:PRK05677   393 DDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL---------DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSG 463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  471 FRVELGEIESVLASHQAVRECAV--VAREIAGHTQLVgYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNM 548
Cdd:PRK05677   464 FNVYPNELEDVLAALPGVLQCAAigVPDEKSGEAIKV-FVVVKPGETLTKEQ----VMEHMRANLTGYKVPKAVEFRDEL 538

                          570
                   ....*....|....*
gi 1331970929  549 PLTPSGKLDRRALPD 563
Cdd:PRK05677   539 PTTNVGKILRRELRD 553

CBAL

cd05923

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...

33-561

4.36e-26

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.

Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 115.30 E-value: 4.36e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALIDGEQS--LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGD 110
Cdd:cd05923     11 ASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  111 RIEYMLRDSDARILLTSTDvakklALTIPALqecqtvyldqeifeydfhFLAIAKLLhnqylrllhfYFYTLIQQCQATS 190
Cdd:cd05923     91 ELAELIERGEMTAAVIAVD-----AQVMDAI------------------FQSGVRVL----------ALSDLVGLGEPES 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  191 VSQGIQT-QVLPNNLAYCIYTSGSTGNPKGILMEHRslvnmlwwHQQTR----PSVQGVR---------------TLQFC 250
Cdd:cd05923    138 AGPLIEDpPREPEQPAFVFYTSGTTGLPKGAVIPQR--------AAESRvlfmSTQAGLRhgrhnvvlglmplyhVIGFF 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  251 AVsfdfscheIFSTLCLGGILVLVPEAVRQNPFALaefISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQ 330
Cdd:cd05923    210 AV--------LVAALALDGTYVVVEEFDPADALKL---IEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGAT 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  331 MQiTPAVANLFQKTGAMLHNHYGATEfqdATTHTLKGNP-EGwptlvPVGRPLHNVQVY---ILDEAQQPVPLGGEGEFC 406
Cdd:cd05923    279 MP-DAVLERVNQHLPGEKVNIYGTTE---AMNSLYMRDArTG-----TEMRPGFFSEVRivrIGGSPDEALANGEEGELI 349

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  407 IGGIGLA--RGYHNLPDLTnekfipnpfganenAKKL----YRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIES 480
Cdd:cd05923    350 VAAAADAafTGYLNQPEAT--------------AKKLqdgwYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIER 415

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  481 VLASHQAVRECAV--VAREIAGhtQLVGYIIAKDTLNLSFDKLEPILRQySEavLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd05923    416 VLSRHPGVTEVVVigVADERWG--QSVTACVVPREGTLSADELDQFCRA-SE--LADFKRPRRYFFLDELPKNAMNKVLR 490


                   ...
gi 1331970929  559 RAL 561
Cdd:cd05923    491 RQL 493

FAAL

cd05931

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...

31-560

5.84e-26

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.

Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 115.41 E-value: 5.84e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   31 DQAAKRPDAIALI------DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICiERSAELFIGLLGILKAGCAYVPLD 104
Cdd:cd05931      1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVGKPGDRVLLLA-PPGLDFVAAFLGCLYAGAIAVPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  105 VGYPG---DRIEYMLRDSDARILLTSTDVAKKLAltipalqecqtvyldqEIFEYDFHFLAIAKLLHNQYLrllhfyfyt 181
Cdd:cd05931     80 PPTPGrhaERLAAILADAGPRVVLTTAAALAAVR----------------AFAASRPAAGTPRLLVVDLLP--------- 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  182 liqqcqATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWwhqqtrpsvQGVRTLQFCA----VSF--- 254
Cdd:cd05931    135 ------DTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVR---------QIRRAYGLDPgdvvVSWlpl 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  255 --DFSCHE-IFSTLCLGGILVLV-PEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLAL--CEVITTG 328
Cdd:cd05931    200 yhDMGLIGgLLTPLYSGGPSVLMsPAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRDEDLEGLDLssWRVALNG 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  329 EQMqITPAVANLFQKTGA-------MLHNHYG---ATEF-------QDATTHTL------------KGNPEGWPTLVPVG 379
Cdd:cd05931    280 AEP-VRPATLRRFAEAFApfgfrpeAFRPSYGlaeATLFvsggppgTGPVVLRVdrdalagravavAADDPAARELVSCG 358

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  380 RPLHNVQVYILDEA-QQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipNPFGANENAKKLyRTGDLArYLPDGTIEH 458
Cdd:cd05931    359 RPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASGYWGRPEATAETF--GALAATDEGGWL-RTGDLG-FLHDGELYI 434

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  459 LGRIDHQVKIRGFRVELGEIE-SVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYSEAVLPEYM 537
Cdd:cd05931    435 TGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHG 514

                          570       580
                   ....*....|....*....|....*.
gi 1331970929  538 IPTR---FINISNMPLTPSGKLDRRA 560
Cdd:cd05931    515 VAPAdvvLVRPGSIPRTSSGKIQRRA 540

PRK08722

beta-ketoacyl-ACP synthase II;

831-1109

1.06e-25

beta-ketoacyl-ACP synthase II;

Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 112.79 E-value: 1.06e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  831 LATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQKG--GYLYEEGMVRSQD---GHCRA 905
Cdd:PRK08722   143 IAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGmaGFGAAKALSTRNDepqKASRP 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  906 FDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgALKMgyTAPSVDGQADVISEAIAIAD--IDASTIG 983
Cdd:PRK08722   223 WDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGD-AYHM--TSPSEDGSGGALAMEAAMRDagVTGEQIG 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  984 YVEAHGTATQLGDPIEVAGLARAFQRStdsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPN 1063
Cdd:PRK08722   300 YVNAHGTSTPAGDVAEIKGIKRALGEA-----GSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPE 374

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1331970929 1064 PRIDFDATPFfvntELREWSRNGYprrAGVSSFGVGGTNSHIVLEE 1109
Cdd:PRK08722   375 EGLDIDLVPH----TARKVESMEY---AICNSFGFGGTNGSLIFKK 413

PLN02836

3-oxoacyl-[acyl-carrier-protein] synthase

832-1111

1.84e-25

3-oxoacyl-[acyl-carrier-protein] synthase

Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 112.58 E-value: 1.84e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  832 ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQkggyLYEEGMVRSQ----------DG 901
Cdd:PLN02836   164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDA----LSIAGFSRSRalstkfnscpTE 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  902 HCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGalkMGYTAPSVDGQADV--ISEAIAIADIDA 979
Cdd:PLN02836   240 ASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDA---HHITQPHEDGRGAVlaMTRALQQSGLHP 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  980 STIGYVEAHGTATQLGDPIEVAGLARAF-QRSTDSVLgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLH 1058
Cdd:PLN02836   317 NQVDYVNAHATSTPLGDAVEARAIKTVFsEHATSGGL-----AFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLN 391

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1331970929 1059 YANPNPRIDFDATPFfvnTELREwsrngYPRRAGVS-SFGVGGTNSHIVLEESP 1111
Cdd:PLN02836   392 LERPDPIFDDGFVPL---TASKA-----MLIRAALSnSFGFGGTNASLLFTSPP 437

PRK12583

acyl-CoA synthetase; Provisional

22-558

1.92e-25

acyl-CoA synthetase; Provisional

Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 114.10 E-value: 1.92e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   22 DSCIHHLFEDQAAKRPDAIALIDGEQSL--TYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCA 99
Cdd:PRK12583    17 TQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  100 YVPLDVGYPGDRIEYMLRDSDARILLT-----STDVAKKLALTIPALQECQTVYLdqeifeydfhflAIAKLLHNQYLRL 174
Cdd:PRK12583    97 LVNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEGQPGAL------------ACERLPELRGVVS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  175 L------HFYFYTLIQQcQATSVSQG----IQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQtrpSVQGV 244
Cdd:PRK12583   165 LapapppGFLAWHELQA-RGETVSREalaeRQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAE---SLGLT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  245 RTLQFCA-VSFdFSCH-EIFSTL-CL--GGILVLVPEAVrqNPFALAEFISQQKIEKLF-LPVIALLQLAEAVNGNKSTS 318
Cdd:PRK12583   241 EHDRLCVpVPL-YHCFgMVLANLgCMtvGACLVYPNEAF--DPLATLQAVEEERCTALYgVPTMFIAELDHPQRGNFDLS 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  319 lalceVITTGeQMQITPAVANLFQKTGAMLHNH-----YGATE-----FQDATTHTLKGNPEgwptlvPVGRPLHNVQVY 388
Cdd:PRK12583   318 -----SLRTG-IMAGAPCPIEVMRRVMDEMHMAevqiaYGMTEtspvsLQTTAADDLERRVE------TVGRTQPHLEVK 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  389 ILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipnpfganeNAKKLYRTGDLARYLPDGTIEHLGRIDHQVkI 468
Cdd:PRK12583   386 VVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESI---------DEDGWMHTGDLATMDEQGYVRIVGRSKDMI-I 455

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  469 RGFR-VELGEIESVLASHQAVRECAV--VAREIAGHtQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINI 545
Cdd:PRK12583   456 RGGEnIYPREIEEFLFTHPAVADVQVfgVPDEKYGE-EIVAWVRLHPGHAASEEE----LREFCKARIAHFKVPRYFRFV 530

                          570
                   ....*....|...
gi 1331970929  546 SNMPLTPSGKLDR 558
Cdd:PRK12583   531 DEFPMTVTGKVQK 543

PRK08439

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed

732-1106

2.44e-25

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed

Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 111.36 E-value: 2.44e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  732 AVLEG------VELFDATFF---------GYSPKEaaVTDPQQ--------RILLECAWEAFERAGYNPETY-PEPVGVY 787
Cdd:PRK08439    25 AICNGecgikkITLFDASDFpvqiageitDFDPTE--VMDPKEvkkadrfiQLGLKAAREAMKDAGFLPEELdAERFGVS 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  788 AGSSLSTylLNNIGSALGIITEQ------PFIetdmeqFQAKIGNdrsYLATRISYKLNLKGPSVNVQTACSTSLVAVHM 861
Cdd:PRK08439   103 SASGIGG--LPNIEKNSIICFEKgprkisPFF------IPSALVN---MLGGFISIEHGLKGPNLSSVTACAAGTHAIIE 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  862 ACQSLISGEC-QMALAGGISVVVPQK-GGYLYEEGM-VRSQDGH--CRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDN 936
Cdd:PRK08439   172 AVKTIMLGGAdKMLVVGAESAICPVGiGGFAAMKALsTRNDDPKkaSRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAK 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  937 IMAVIKATAINNDGAlkmGYTAPSVDGQADVISEAIAIADIDasTIGYVEAHGTATQLGDPIEVAGLARAFQrstdsvlG 1016
Cdd:PRK08439   252 IYAEIIGFGESGDAN---HITSPAPEGPLRAMKAALEMAGNP--KIDYINAHGTSTPYNDKNETAALKELFG-------S 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1017 KQQCA-IGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATPffvNTelrewsrngyPRRAGV-- 1093
Cdd:PRK08439   320 KEKVPpVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIP---NV----------ARKAELnv 386

                          410
                   ....*....|....*.
gi 1331970929 1094 ---SSFGVGGTNSHIV 1106
Cdd:PRK08439   387 vmsNSFGFGGTNGVVI 402

PRK08276

long-chain-fatty-acid--CoA ligase; Validated

39-564

3.56e-25

long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 112.69 E-value: 3.56e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   39 AIALIDGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLR 117
Cdd:PRK08276     1 PAVIMAPSgEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  118 DSDARILLTST---DVAKKLALTIPA-LQECQTVYLDQEIFE-YDfhflaiakllhnqylrllhfyfytliqQCQATSVS 192
Cdd:PRK08276    81 DSGAKVLIVSAalaDTAAELAAELPAgVPLLLVVAGPVPGFRsYE---------------------------EALAAQPD 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  193 QGIQTQVLPNNLAyciYTSGSTGNPKGILME------HRSLVNMLWWHQQTRPSVQGVRTL-----------QFCAvsfd 255
Cdd:PRK08276   134 TPIADETAGADML---YSSGTTGRPKGIKRPlpgldpDEAPGMMLALLGFGMYGGPDSVYLspaplyhtaplRFGM---- 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  256 fscheifSTLCLGGILVLVPeavRQNPFALAEFISQQKIEKL-FLPV--IALLQLAEAVNGNKSTSlALCEVITTG---- 328
Cdd:PRK08276   207 -------SALALGGTVVVME---KFDAEEALALIERYRVTHSqLVPTmfVRMLKLPEEVRARYDVS-SLRVAIHAAapcp 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  329 ----EQMqitpavanlFQKTGAMLHNHYGATEFQDATTHTlkgnPEGWPTLvP--VGRPLHNVqVYILDEAQQPVPLGGE 402
Cdd:PRK08276   276 vevkRAM---------IDWWGPIIHEYYASSEGGGVTVIT----SEDWLAH-PgsVGKAVLGE-VRILDEDGNELPPGEI 340

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  403 GE--FCIGGIGLArgYHNLPDLTNekfipnpfgANENAKKLYRTGDLArYL-PDGTIEHLGRIDHQVKIRGFRVELGEIE 479
Cdd:PRK08276   341 GTvyFEMDGYPFE--YHNDPEKTA---------AARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMIISGGVNIYPQEIE 408

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  480 SVLASHQAVRECAV--VAREIAGHtQLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:PRK08276   409 NLLVTHPKVADVAVfgVPDEEMGE-RVKAVVQPADGADAG-DALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLY 486


                   ....*..
gi 1331970929  558 RRALPDP 564
Cdd:PRK08276   487 KRRLRDR 493

Methyltransf_12

pfam08242

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

2113-2213

7.00e-25

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 100.91 E-value: 7.00e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2113 LEIGAGTGGTTAYLLPHLPGdqTKYVFTDISAFFLAKAEERFKDYPFVRYQVLDIEQAPQAQGFEPQiYDLIVAADVLHA 2192
Cdd:pfam08242    1 LEIGCGTGTLLRALLEALPG--LEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGS-FDVVVASNVLHH 77

                           90       100
                   ....*....|....*....|.
gi 1331970929 2193 TSDLRQTLVHIRQLLAPGGML 2213
Cdd:pfam08242   78 LADPRAVLRNIRRLLKPGGVL 98

PKS_PP

smart00823

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...

2795-2881

9.49e-25

Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 100.02 E-value: 9.49e-25

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  2795 LENAPPKEGLTLLQAHVREQVSQVLGIDTKTLLaEQDVGFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQALV 2874
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAI-DPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79


                    ....*..
gi 1331970929  2875 NYLANEL 2881
Cdd:smart00823   80 EHLAAEL 86

ABCL

cd05958

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...

209-561

1.33e-24

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.

Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 109.88 E-value: 1.33e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  209 YTSGSTGNPKGILMEHRSLVNM--LWWHQQTRPSVQGVrtlqFCAVSfdfschEIFSTLCLGGIL----------VLVPE 276
Cdd:cd05958    104 FTSGTTGAPKATMHFHRDPLASadRYAVNVLRLREDDR----FVGSP------PLAFTFGLGGVLlfpfgvgasgVLLEE 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  277 AVRQNPFALaefISQQKIEKLF-LPVI--ALLQLAEAvNGNKSTSLALCevITTGEQMqiTPAVANLFQK-TGAMLHNHY 352
Cdd:cd05958    174 ATPDLLLSA---IARYKPTVLFtAPTAyrAMLAHPDA-AGPDLSSLRKC--VSAGEAL--PAALHRAWKEaTGIPIIDGI 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  353 GATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGiglARGYHNLPDLTNEKFipnpF 432
Cdd:cd05958    246 GSTE----MFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTY----V 314

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  433 GANENAkklyrTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLV-GYIIAK 511
Cdd:cd05958    315 QGGWNI-----TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVkAFVVLR 389

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1331970929  512 DTLNLSFDKLEPiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05958    390 PGVIPGPVLARE-LQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438

ttLC_FACS_AlkK_like

cd12119

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...

50-561

2.31e-24

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.

Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 110.41 E-value: 2.31e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   50 TYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTD 129
Cdd:cd12119     27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  130 VAKKLAltiPALQECQTVYLDQEIFEYDFHFLAIAKLLHNqYLRLLHfyfytliqqcqatSVSQGIQTQVLPNNLAYCI- 208
Cdd:cd12119    107 FLPLLE---AIAPRLPTVEHVVVMTDDAAMPEPAGVGVLA-YEELLA-------------AESPEYDWPDFDENTAAAIc 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  209 YTSGSTGNPKGILMEHRSLVnmlwwhqqtrpsvqgVRTLQFCAVSFdFSCHEI------------------FSTLCLGGI 270
Cdd:cd12119    170 YTSGTTGNPKGVVYSHRSLV---------------LHAMAALLTDG-LGLSESdvvlpvvpmfhvnawglpYAAAMVGAK 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  271 LVLvPeAVRQNPFALAEFISQQKIE-KLFLPVIaLLQLAEAVNGNKSTSLALCEVITTGEQMqiTPAVANLFQKTGAMLH 349
Cdd:cd12119    234 LVL-P-GPYLDPASLAELIEREGVTfAAGVPTV-WQGLLDHLEANGRDLSSLRRVVIGGSAV--PRSLIEAFEERGVRVI 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  350 NHYGATE------FQDATTHTLKGNP-EGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGE--GEFCIGGIGLARGYHNLP 420
Cdd:cd12119    309 HAWGMTEtsplgtVARPPSEHSNLSEdEQLALRAKQGRPVPGVELRIVDDDGRELPWDGKavGELQVRGPWVTKSYYKND 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  421 DlTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA----- 495
Cdd:cd12119    389 E-ESEALTEDGW---------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGvphpk 458

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331970929  496 ---REIAghtqlvgYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd12119    459 wgeRPLA-------VVVLKEGATVTAEE----LLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516

PRK05605

long-chain-fatty-acid--CoA ligase; Validated

19-563

3.24e-24

long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 110.47 E-value: 3.24e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   19 EFPDSCIHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGC 98
Cdd:PRK05605    28 DYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   99 AYV---PLdvgYPGDRIEYMLRDSDARILL---TSTDVAKKLALTIPAlqecqtvyldQEIFEYDfhfLAIAKLLHNQY- 171
Cdd:PRK05605   108 VVVehnPL---YTAHELEHPFEDHGARVAIvwdKVAPTVERLRRTTPL----------ETIVSVN---MIAAMPLLQRLa 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  172 LRL-----------LH------FYFYTLIQqcqATSVSQGIQTQ---VLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NM 230
Cdd:PRK05605   172 LRLpipalrkaraaLTgpapgtVPWETLVD---AAIGGDGSDVShprPTPDDVALILYTSGTTGKPKGAQLTHRNLFaNA 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  231 LwwhqQTRPSVQGVRTLQ--FCAVSFDFscHEIFSTLCL------GGILVLVP--------EAVRQNPfalaefisqqki 294
Cdd:PRK05605   249 A----QGKAWVPGLGDGPerVLAALPMF--HAYGLTLCLtlavsiGGELVLLPapdidlilDAMKKHP------------ 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  295 eKLFLPVI-----ALLQLAEAvngnKSTSLALCEVITTGeQMQITPAVANLFQK-TGAMLHNHYGATEfqdaTTHTLKGN 368
Cdd:PRK05605   311 -PTWLPGVpplyeKIAEAAEE----RGVDLSGVRNAFSG-AMALPVSTVELWEKlTGGLLVEGYGLTE----TSPIIVGN 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  369 PEGwPTLVP--VGRPLHNVQVYILD--EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNpfganenakkLYRT 444
Cdd:PRK05605   381 PMS-DDRRPgyVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG----------WFRT 449

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  445 GDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVV--AREiAGHTQLVGYIIAKDTLNLSFDKle 522
Cdd:PRK05605   450 GDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVglPRE-DGSEEVVAAVVLEPGAALDPEG-- 526

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1331970929  523 piLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:PRK05605   527 --LRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565

UbiE

COG2226

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...

2100-2224

1.06e-23

Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 99.30 E-value: 1.06e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2100 ALEQLPPERGWRILEIGAGTGGTTAYLLPHlpgdQTKYVFTDISAFFLAKAEERFKDYPF-VRYQVLDIEQAPqaqgFEP 2178
Cdd:COG2226     14 LLAALGLRPGARVLDLGCGTGRLALALAER----GARVTGVDISPEMLELARERAAEAGLnVEFVVGDAEDLP----FPD 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1331970929 2179 QIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILMEDSEPARW 2224
Cdd:COG2226     86 GSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLA 131

PRK12492

long-chain-fatty-acid--CoA ligase; Provisional

28-564

1.98e-23

long-chain-fatty-acid--CoA ligase; Provisional

Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 107.99 E-value: 1.98e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAKRPDAIALIDGEQSLTYGELN----VRANHLAQHLlslGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPL 103
Cdd:PRK12492    29 VFERSCKKFADRPAFSNLGVTLSYAELErhsaAFAAYLQQHT---DLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNT 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  104 DVGYPGDRIEYMLRDSDARILLTSTDVAKKLaltipalqecQTVYLDQEIfEYDFH-----FLAIAK-LLHNQYLRLLHF 177
Cdd:PRK12492   106 NPLYTAREMRHQFKDSGARALVYLNMFGKLV----------QEVLPDTGI-EYLIEakmgdLLPAAKgWLVNTVVDKVKK 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  178 YF--YTLIQQC---QATSVSQGIQTQVLPNNL---AYCIYTSGSTGNPKGILMEHRSLV-NMLWWH---QQTRPSVQGV- 244
Cdd:PRK12492   175 MVpaYHLPQAVpfkQALRQGRGLSLKPVPVGLddiAVLQYTGGTTGLAKGAMLTHGNLVaNMLQVRaclSQLGPDGQPLm 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  245 RTLQFCAVS---------FDFSCheifstLCL---GGILVLVpeavrQNPFALAEFISQQKIEKlFLPVIALLQLAEAVN 312
Cdd:PRK12492   255 KEGQEVMIAplplyhiyaFTANC------MCMmvsGNHNVLI-----TNPRDIPGFIKELGKWR-FSALLGLNTLFVALM 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  313 GN---KSTSLALCEVITTGEQMQITPAVANLFQKTGAMLHNHYGATEfqdaTTHTLKGNPEG-WPTLVPVGRPLHNVQVY 388
Cdd:PRK12492   323 DHpgfKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTE----TSPVASTNPYGeLARLGTVGIPVPGTALK 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  389 ILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipnpfganeNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKI 468
Cdd:PRK12492   399 VIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL---------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIV 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  469 RGFRVELGEIESVLASHQAVRECAV--VAREIAGHTQLVgYIIAKDTlNLSFDKlepiLRQYSEAVLPEYMIPTRFINIS 546
Cdd:PRK12492   470 SGFNVYPNEIEDVVMAHPKVANCAAigVPDERSGEAVKL-FVVARDP-GLSVEE----LKAYCKENFTGYKVPKHIVLRD 543

                          570
                   ....*....|....*...
gi 1331970929  547 NMPLTPSGKLDRRALPDP 564
Cdd:PRK12492   544 SLPMTPVGKILRRELRDI 561

ACS-like

cd17634

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...

20-556

1.99e-23

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.

Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 108.05 E-value: 1.99e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   20 FPDSCI---HHLFEDQAAKRPDAIALI----DGEQS--LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGL 90
Cdd:cd17634     47 FEDATLnlaANALDRHLRENGDRTAIIyegdDTSQSrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   91 LGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTD-------------VAKKLALTIPALQecQTVYLDQEIFEYD 157
Cdd:cd17634    127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGgvragrsvplkknVDDALNPNVTSVE--HVIVLKRTGSDID 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  158 FHFLAiakllhnqylrllHFYFYTLIQQCQATSVSQgiqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQT 237
Cdd:cd17634    205 WQEGR-------------DLWWRDLIAKASPEHQPE----AMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKY 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  238 RPSVqGVRTLQFCAVSFDF-SCHE--IFSTLCLGGILVLVPEA-VRQNPFALAEFISQQKIEKLFLPVIALLQLA----E 309
Cdd:cd17634    268 VFDY-GPGDIYWCTADVGWvTGHSylLYGPLACGATTLLYEGVpNWPTPARMWQVVDKHGVNILYTAPTAIRALMaagdD 346

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  310 AVNGNKSTSLALceVITTGEQMQITP---AVANLFQKTGAMLhNHYGATEFQDATTHTLKGNPE---GWPTlvpvgRPLH 383
Cdd:cd17634    347 AIEGTDRSSLRI--LGSVGEPINPEAyewYWKKIGKEKCPVV-DTWWQTETGGFMITPLPGAIElkaGSAT-----RPVF 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  384 NVQVYILDEAQQPVPLGGEGEFCIGGI--GLARGYHNLPDltneKFIPNPFGANENakkLYRTGDLARYLPDGTIEHLGR 461
Cdd:cd17634    419 GVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKG---MYFSGDGARRDEDGYYWITGR 491

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  462 IDHQVKIRGFRVELGEIESVLASHQAVRECAVVA--REIAGhTQLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIP 539
Cdd:cd17634    492 SDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGipHAIKG-QAPYAYVVLNHGVEPS-PELYAELRNWVRKEIGPLATP 569

                          570
                   ....*....|....*..
gi 1331970929  540 TRFINISNMPLTPSGKL 556
Cdd:cd17634    570 DVVHWVDSLPKTRSGKI 586

PRK07638

acyl-CoA synthetase; Validated

25-561

2.42e-23

acyl-CoA synthetase; Validated

Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 106.79 E-value: 2.42e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLlAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:PRK07638     3 ITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTI-AILLENRIEFLQLFAGAAMAGWTCVPLD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  105 VGYPGDRIEYMLRDSDARILLTSTDVAKKLALtipalQECQTVYLDQeifeydfhflaiakllhnqYLRLLHFYfytliq 184
Cdd:PRK07638    82 IKWKQDELKERLAISNADMIVTERYKLNDLPD-----EEGRVIEIDE-------------------WKRMIEKY------ 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  185 qcqATSVSQGIQTQVLPnnlAYCIYTSGSTGNPKGILMEHRSLV-----NMLWWHQQTRPSVQGVRTLqfcavsfdFSCH 259
Cdd:PRK07638   132 ---LPTYAPIENVQNAP---FYMGFTSGSTGKPKAFLRAQQSWLhsfdcNVHDFHMKREDSVLIAGTL--------VHSL 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  260 EIF---STLCLGGILVLVPeavRQNPFALAEFISQQKIEKLF-LPVI--ALLQlAEAVNGNKSTslalceVITTGEQMQI 333
Cdd:PRK07638   198 FLYgaiSTLYVGQTVHLMR---KFIPNQVLDKLETENISVMYtVPTMleSLYK-ENRVIENKMK------IISSGAKWEA 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  334 TP--AVANLFQKtgAMLHNHYGATE--FQDATTH---TLKGNPegwptlvpVGRPLHNVQVYILDEAQQPVPLGGEGEFC 406
Cdd:PRK07638   268 EAkeKIKNIFPY--AKLYEFYGASElsFVTALVDeesERRPNS--------VGRPFHNVQVRICNEAGEEVQKGEIGTVY 337

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  407 IGGIGLARGYHNLPDLTNEKfipnpfganeNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQ 486
Cdd:PRK07638   338 VKSPQFFMGYIIGGVLAREL----------NADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHP 407

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331970929  487 AVRECAVV--AREIAGhTQLVGYIIAKDTlnlsfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK07638   408 AVDEIVVIgvPDSYWG-EKPVAIIKGSAT--------KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475

entE

PRK10946

(2,3-dihydroxybenzoyl)adenylate synthase;

27-561

4.86e-23

(2,3-dihydroxybenzoyl)adenylate synthase;

Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 106.23 E-value: 4.86e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   27 HLFEDQAAkrPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAyvPLDVG 106
Cdd:PRK10946    29 DILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNAL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  107 YPGDRIE---Y-------MLRDSDARILLTSTDVAKKLALTIPALQecqtvyldqeifeydfhflaIAKLLHNQYLRLLH 176
Cdd:PRK10946   105 FSHQRSElnaYasqiepaLLIADRQHALFSDDDFLNTLVAEHSSLR--------------------VVLLLNDDGEHSLD 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  177 fyfyTLIQQCQATSVSqgiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSlvnmlwWHQQTRPSVQ----GVRTLQFCAV 252
Cdd:PRK10946   165 ----DAINHPAEDFTA----TPSPADEVAFFQLSGGSTGTPKLIPRTHND------YYYSVRRSVEicgfTPQTRYLCAL 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  253 ----SFDFSCHEIFSTLCLGGILVLVPeavrqNPFALAEF--ISQQKIE--KLFLPVIAL-LQLAEAVNGNKS-TSLALC 322
Cdd:PRK10946   231 paahNYPMSSPGALGVFLAGGTVVLAP-----DPSATLCFplIEKHQVNvtALVPPAVSLwLQAIAEGGSRAQlASLKLL 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  323 EV--ITTGEQM--QITPAVANLFQKTGAM---LHNHygaTEFQDATTHTLKGNpegwptlvpvGRPLH-NVQVYILDEAQ 394
Cdd:PRK10946   306 QVggARLSETLarRIPAELGCQLQQVFGMaegLVNY---TRLDDSDERIFTTQ----------GRPMSpDDEVWVADADG 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  395 QPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVE 474
Cdd:PRK10946   373 NPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF---------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIA 443

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  475 LGEIESVLASHQAVRECAVVAREiaghTQLVG-----YIIAKDTLNlsfdklEPILRQY-SEAVLPEYMIPTRFINISNM 548
Cdd:PRK10946   444 AEEIENLLLRHPAVIHAALVSME----DELMGekscaFLVVKEPLK------AVQLRRFlREQGIAEFKLPDRVECVDSL 513

                          570
                   ....*....|...
gi 1331970929  549 PLTPSGKLDRRAL 561
Cdd:PRK10946   514 PLTAVGKVDKKQL 526

PRK06710

long-chain-fatty-acid--CoA ligase; Validated

25-561

7.32e-23

long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 105.89 E-value: 7.32e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLD 104
Cdd:PRK06710    26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  105 VGYPGDRIEYMLRDSDARILLTstdvakkLALTIPALQECQ-TVYLDQEIFEYDFHFLAIAKLLHNQYLRLLHFYFYTLI 183
Cdd:PRK06710   106 PLYTERELEYQLHDSGAKVILC-------LDLVFPRVTNVQsATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNLVVKV 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  184 QQCQA----TSVSQGIQTQV-LP----NNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSVQGVRTLqFCAVS 253
Cdd:PRK06710   179 SESETihlwNSVEKEVNTGVeVPcdpeNDLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVV-LGVLP 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  254 FdFSCHEIFSTLCL----GGILVLVPEAVRQNPFalaEFISQQKIeKLF--LPV--IALLQlAEAVNGNKSTSLALCevI 325
Cdd:PRK06710   258 F-FHVYGMTAVMNLsimqGYKMVLIPKFDMKMVF---EAIKKHKV-TLFpgAPTiyIALLN-SPLLKEYDISSIRAC--I 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  326 TTGEQMQItpAVANLFQK-TGAMLHNHYGATEFQDATTHTLKgnpegWPTLVP--VGRPLHNVQVYILD-EAQQPVPLGG 401
Cdd:PRK06710   330 SGSAPLPV--EVQEKFETvTGGKLVEGYGLTESSPVTHSNFL-----WEKRVPgsIGVPWPDTEAMIMSlETGEALPPGE 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  402 EGEFCIGGIGLARGYHNLPDLTnekfipnpfgANENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESV 481
Cdd:PRK06710   403 IGEIVVKGPQIMKGYWNKPEET----------AAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEV 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  482 LASHQAVRECAVVAREIAGHTQLV-GYIIAKDTLNLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGKLDRRA 560
Cdd:PRK06710   473 LYEHEKVQEVVTIGVPDPYRGETVkAFVVLKEGTECSEEELNQFARKY----LAAYKVPKVYEFRDELPKTTVGKILRRV 548


                   .
gi 1331970929  561 L 561
Cdd:PRK06710   549 L 549

PRK07788

acyl-CoA synthetase; Validated

33-563

1.21e-22

acyl-CoA synthetase; Validated

Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 105.39 E-value: 1.21e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGcayvpldvgypgdri 112
Cdd:PRK07788    59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVG--------------- 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  113 eymlrdsdARILLTSTDVAKklaltiPALQEC------QTVYLDQEifeydfhFLAIAKLLHNQYLRLLHFYFYTLIQQC 186
Cdd:PRK07788   124 --------ARIILLNTGFSG------PQLAEVaaregvKALVYDDE-------FTDLLSALPPDLGRLRAWGGNPDDDEP 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  187 QATSVS------QGIQTQVLP---NNLAYCIYTSGSTGNPKGILMEH----RSLVNMLwwhqqTRPSVQGVRTLQFCAVS 253
Cdd:PRK07788   183 SGSTDEtlddliAGSSTAPLPkppKPGGIVILTSGTTGTPKGAPRPEpsplAPLAGLL-----SRVPFRAGETTLLPAPM 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  254 FD---FSCHEIfsTLCLGGILVLvpeAVRQNPFALAEFISQQKIEKLFL-PVI--ALLQLAEAVNGNKSTSlALCEVITT 327
Cdd:PRK07788   258 FHatgWAHLTL--AMALGSTVVL---RRRFDPEATLEDIAKHKATALVVvPVMlsRILDLGPEVLAKYDTS-SLKIIFVS 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  328 GEQMqiTPAVANLFQKT-GAMLHNHYGATEFQDATTHTlkgnPEGW---PTLVpvGRPLHNVQVYILDEAQQPVPLGGEG 403
Cdd:PRK07788   332 GSAL--SPELATRALEAfGPVLYNLYGSTEVAFATIAT----PEDLaeaPGTV--GRPPKGVTVKILDENGNEVPRGVVG 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  404 E-FCIGGIGLaRGYHNLPDltnekfipnpfgaNENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVL 482
Cdd:PRK07788   404 RiFVGNGFPF-EGYTDGRD-------------KQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLL 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  483 ASHQAVRECAVVAREIA--GHtQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRA 560
Cdd:PRK07788   470 AGHPDVVEAAVIGVDDEefGQ-RLRAFVVKAPGAALDEDA----IKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRE 544


                   ...
gi 1331970929  561 LPD 563
Cdd:PRK07788   545 LRE 547

Firefly_Luc

cd17642

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...

31-561

1.22e-22

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.

Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 104.92 E-value: 1.22e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   31 DQAAKRPDAIALIDG--EQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYP 108
Cdd:cd17642     25 KRYASVPGTIAFTDAhtGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYN 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  109 GDRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYLDQEIFEYDfHFLAIAKLLHNQYLRLLHFYFYTliqqcqa 188
Cdd:cd17642    105 ERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYK-GYQCLYTFITQNLPPGFNEYDFK------- 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  189 tSVSQGIQTQVlpnnlAYCIYTSGSTGNPKGILMEHRSLVNMLwwHQQTRPSV-----QGVRTLQFCAVSFDFSCHEIFS 263
Cdd:cd17642    177 -PPSFDRDEQV-----ALIMNSSGSTGLPKGVQLTHKNIVARF--SHARDPIFgnqiiPDTAILTVIPFHHGFGMFTTLG 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  264 TLCLGGILVLVPEavrqnpFALAEFIS---QQKIEKLFL--PVIALLQLAEAVNGNKSTSLAlcEVITTGEQM--QITPA 336
Cdd:cd17642    249 YLICGFRVVLMYK------FEEELFLRslqDYKVQSALLvpTLFAFFAKSTLVDKYDLSNLH--EIASGGAPLskEVGEA 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  337 VANLFQKTGamLHNHYGATEfqdaTTHTLKGNPEGW--PTLVPVGRPLHNVQVYILDEAQQpvpLGGE--GEFCIGGIGL 412
Cdd:cd17642    321 VAKRFKLPG--IRQGYGLTE----TTSAILITPEGDdkPGAVGKVVPFFYAKVVDLDTGKT---LGPNerGELCVKGPMI 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  413 ARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECA 492
Cdd:cd17642    392 MKGYVNNPEATKALIDKDGW---------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAG 462

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331970929  493 VVAR--EIAGHTQLVGYII-AKDTLNlsfdklEPILRQY-SEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17642    463 VAGIpdEDAGELPAAVVVLeAGKTMT------EKEVMDYvASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529

PRK06155

crotonobetaine/carnitine-CoA ligase; Provisional

28-561

1.36e-22

crotonobetaine/carnitine-CoA ligase; Provisional

Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 104.84 E-value: 1.36e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:PRK06155    26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTAL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  108 PGDRIEYMLRDSDARILLTSTDVAKKLALTIPALqecqtvyldqeifeydfhfLAIAKLLhnqylrllhfyfytLIQQCQ 187
Cdd:PRK06155   106 RGPQLEHILRNSGARLLVVEAALLAALEAADPGD-------------------LPLPAVW--------------LLDAPA 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  188 ATSVSQGIQT-------------QVLPNNLAYCIYTSGSTGNPKGILMEHrslVNMLWWhqqtrpSVQGVRTLQFCAVSF 254
Cdd:PRK06155   153 SVSVPAGWSTaplppldapapaaAVQPGDTAAILYTSGTTGPSKGVCCPH---AQFYWW------GRNSAEDLEIGADDV 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  255 DFSCHEIFST---------LCLGGILVLVP--------EAVRQN----PFALAEFISqqkieklflpvIALLQLAEAVNG 313
Cdd:PRK06155   224 LYTTLPLFHTnalnaffqaLLAGATYVLEPrfsasgfwPAVRRHgatvTYLLGAMVS-----------ILLSQPARESDR 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  314 NKSTSLALcevittgeqmqiTPAV-----ANLFQKTGAMLHNHYGATEFQDATTHTLKGNPEGWptlvpVGRPLHNVQVY 388
Cdd:PRK06155   293 AHRVRVAL------------GPGVpaalhAAFRERFGVDLLDGYGSTETNFVIAVTHGSQRPGS-----MGRLAPGFEAR 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  389 ILDEAQQPVPLGGEGEFCIGG---IGLARGYHNLPDLTNEKFipnpfganenaKKL-YRTGDLARYLPDGTIEHLGRIDH 464
Cdd:PRK06155   356 VVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTVEAW-----------RNLwFHTGDRVVRDADGWFRFVDRIKD 424

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  465 QVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAGHTQLVGyIIAKDTLNLSFDKLEpilrQYSEAVLPEYMIPtRF 542
Cdd:PRK06155   425 AIRRRGENISSFEVEQVLLSHPAVAAAAVfpVPSELGEDEVMAA-VVLRDGTALEPVALV----RHCEPRLAYFAVP-RY 498

                          570       580
                   ....*....|....*....|
gi 1331970929  543 INI-SNMPLTPSGKLDRRAL 561
Cdd:PRK06155   499 VEFvAALPKTENGKVQKFVL 518

PRK07529

AMP-binding domain protein; Validated

21-561

2.79e-22

AMP-binding domain protein; Validated

Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 104.65 E-value: 2.79e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   21 PDScIHHLFEDQAAKRPDAIALI--------DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLG 92
Cdd:PRK07529    24 PAS-TYELLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   93 ILKAGCAyVPLDVGYPGDRIEYMLRDSDARILLT-----STDVAKKLALTIPALQECQTVYL----DQEIFEYDFHFLAI 163
Cdd:PRK07529   103 GEAAGIA-NPINPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVLAALPELRTVVEvdlaRYLPGPKRLAVPLI 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  164 AKLLHNQYLRllhfyFYTLIQQCQATSVSQGiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQG 243
Cdd:PRK07529   182 RRKAHARILD-----FDAELARQPGDRLFSG--RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPG 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  244 vRTLqFCAVS-FD-FSCHEI-FSTLCLGGILVLVPEAVRQNPFALAEF---ISQQKIEKLF-LPVI--ALLQLaeAVNGN 314
Cdd:PRK07529   255 -DTV-FCGLPlFHvNALLVTgLAPLARGAHVVLATPQGYRGPGVIANFwkiVERYRINFLSgVPTVyaALLQV--PVDGH 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  315 KSTSLALceVITTGEQMqiTPAVANLFQ-KTGAMLHNHYGATEfqdATTHTLKGNPEGWPTLVPVGRPL--HNVQVYILD 391
Cdd:PRK07529   331 DISSLRY--ALCGAAPL--PVEVFRRFEaATGVRIVEGYGLTE---ATCVSSVNPPDGERRIGSVGLRLpyQRVRVVILD 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  392 EA---QQPVPLGGEGEFCIGGIGLARGYhnlpdlTNEkfipnpfganENAKKLY------RTGDLARYLPDGTIEHLGRi 462
Cdd:PRK07529   404 DAgryLRDCAVDEVGVLCIAGPNVFSGY------LEA----------AHNKGLWledgwlNTGDLGRIDADGYFWLTGR- 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  463 dhqVK---IR-GFRVELGEIESVLASHQAVRECAVVAREIAGHTQL-VGYIIAKDTLNLSfdklEPILRQYSEAVLPE-Y 536
Cdd:PRK07529   467 ---AKdliIRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELpVAYVQLKPGASAT----EAELLAFARDHIAErA 539

                          570       580
                   ....*....|....*....|....*
gi 1331970929  537 MIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK07529   540 AVPKHVRILDALPKTAVGKIFKPAL 564

PRK13295

cyclohexanecarboxylate-CoA ligase; Reviewed

21-561

6.21e-22

cyclohexanecarboxylate-CoA ligase; Reviewed

Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 102.82 E-value: 6.21e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   21 PDSCIHHLFEDQAAKRPDAIALID-----GE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGIL 94
Cdd:PRK13295    22 HDRTINDDLDACVASCPDKTAVTAvrlgtGApRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACS 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   95 KAGCAYVPLDVGYPGDRIEYMLRDSDARILLtstdvakklaltIPALqecqtvyldqeiFEyDFHFLAIAKLLHNQYLRL 174
Cdd:PRK13295   102 RIGAVLNPLMPIFRERELSFMLKHAESKVLV------------VPKT------------FR-GFDHAAMARRLRPELPAL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  175 LHFY---------FYTLI------QQCQATSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLwwhqqtRP 239
Cdd:PRK13295   157 RHVVvvggdgadsFEALLitpaweQEPDAPAILARLRPG--PDDVTQLIYTSGTTGEPKGVMHTANTLMANI------VP 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  240 SVQGVRtlqfcaVSFDFSCHeIFSTLC-LGGIL--VLVP-----EAVRQ---NPFALAEFISQQKIEKLFLPVIALLQLA 308
Cdd:PRK13295   229 YAERLG------LGADDVIL-MASPMAhQTGFMygLMMPvmlgaTAVLQdiwDPARAAELIRTEGVTFTMASTPFLTDLT 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  309 EAVNGNKSTSLALCEVITTGEQmqITPAVANLFQKT-GAMLHNHYGATEFQDATTHTLKGNPEgwPTLVPVGRPLHNVQV 387
Cdd:PRK13295   302 RAVKESGRPVSSLRTFLCAGAP--IPGALVERARAAlGAKIVSAWGMTENGAVTLTKLDDPDE--RASTTDGCPLPGVEV 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  388 YILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTnekfipnpfgaNENAKKLYRTGDLARYLPDGTIEHLGRiDHQVK 467
Cdd:PRK13295   378 RVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN-----------GTDADGWFDTGDLARIDADGYIRISGR-SKDVI 445

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  468 IRGFR-VELGEIESVLASHQAVRECAVVA--------REIAghtqlvgYIIAKDTLNLSFDKLEPILRqySEAVLPEYmI 538
Cdd:PRK13295   446 IRGGEnIPVVEIEALLYRHPAIAQVAIVAypderlgeRACA-------FVVPRPGQSLDFEEMVEFLK--AQKVAKQY-I 515

                          570       580
                   ....*....|....*....|...
gi 1331970929  539 PTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK13295   516 PERLVVRDALPRTPSGKIQKFRL 538

OSB_MenE-like

cd17630

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...

204-561

8.32e-22

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.

Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 99.33 E-value: 8.32e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  204 LAYCIYTSGSTGNPKGILMEHRSLVNmlwwhqqtrpSVQGVRTLqfcaVSFDFSCHEIfstLCL-----GGILVLV---- 274
Cdd:cd17630      2 LATVILTSGSTGTPKAVVHTAANLLA----------SAAGLHSR----LGFGGGDSWL---LSLplyhvGGLAILVrsll 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  275 ---PEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEavNGNKSTSLALCEVITTGEQmQITPAVANLFQKTGAMLHNH 351
Cdd:cd17630     65 agaELVLLERNQALAEDLAPPGVTHVSLVPTQLQRLLD--SGQGPAALKSLRAVLLGGA-PIPPELLERAADRGIPLYTT 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  352 YGATEFQDATThtlkgnpeGWPTLVP----VGRPLHNVQVYILDEaqqpvplggeGEFCIGGIGLARGYHNLPdltnekf 427
Cdd:cd17630    142 YGMTETASQVA--------TKRPDGFgrggVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ------- 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  428 IPNPFganeNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVV--AREIAGHtQLV 505
Cdd:cd17630    197 LVPEF----NEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVgvPDEELGQ-RPV 271

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929  506 GYIIAKDTLNLSfdklepILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd17630    272 AVIVGRGPADPA------ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321

PRK08751

long-chain fatty acid--CoA ligase;

25-563

1.55e-21

long-chain fatty acid--CoA ligase;

Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 101.88 E-value: 1.55e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLS-LGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPL 103
Cdd:PRK08751    27 VAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNV 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  104 DVGYPGDRIEYMLRDSDARILLT----STDVAKKLALTiPALQECQTVYLDQEIFE----YDFHFLAIAKLLHNQYL-RL 174
Cdd:PRK08751   107 NPLYTPRELKHQLIDSGASVLVVidnfGTTVQQVIADT-PVKQVITTGLGDMLGFPkaalVNFVVKYVKKLVPEYRInGA 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  175 LHFyfytliQQCQATSVSQGIQT-QVLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQ--QTRPSVQGVRTLQFC 250
Cdd:PRK08751   186 IRF------REALALGRKHSMPTlQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVaNMQQAHQwlAGTGKLEEGCEVVIT 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  251 AVSFdfscHEIFSTLCLGGILVLVP--EAVRQNPFALAEFISQQKIeklfLPVIALLQLAEAVNGNKST----SLALCEV 324
Cdd:PRK08751   260 ALPL----YHIFALTANGLVFMKIGgcNHLISNPRDMPGFVKELKK----TRFTAFTGVNTLFNGLLNTpgfdQIDFSSL 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  325 -ITTGEQMQITPAVANLFQK-TGAMLHNHYGATEFQDATTHtlkgNPEGWPTLV-PVGRPLHNVQVYILDEAQQPVPLGG 401
Cdd:PRK08751   332 kMTLGGGMAVQRSVAERWKQvTGLTLVEAYGLTETSPAACI----NPLTLKEYNgSIGLPIPSTDACIKDDAGTVLAIGE 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  402 EGEFCIGGIGLARGYHNLPDLTNEKFipnpfganeNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESV 481
Cdd:PRK08751   408 IGELCIKGPQVMKGYWKRPEETAKVM---------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDV 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  482 LASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPtRFINI-SNMPLTPSGKLDRRA 560
Cdd:PRK08751   479 IAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAED----VKAHARANLTGYKQP-RIIEFrKELPKTNVGKILRRE 553


                   ...
gi 1331970929  561 LPD 563
Cdd:PRK08751   554 LRD 556

KAsynt_C_assoc

pfam16197

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...

1062-1175

2.19e-21

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.

Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 91.45 E-value: 2.19e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1062 PNPRID-FDATPFFVNTELREWSRNgyprRAGVSSFGVGGTNSHIVLEESPVKQPTlfSSLPERSHHLLTLSAHTQEALH 1140
Cdd:pfam16197    1 PNPDIPaLLDGRLKVVTEPTPWPGG----IVGVNSFGFGGANAHVILKSNPKPKIP--PESPDNLPRLVLLSGRTEEAVK 74

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1331970929 1141 ELVQRYIQHNETHLDINLGDLCFTANtgRKHFEHR 1175
Cdd:pfam16197   75 ALLEKLENHLDDAEFLSLLNDIHSLP--ISGHPYR 107

A_NRPS_TubE_like

cd05906

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...

32-561

3.77e-21

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 100.43 E-value: 3.77e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   32 QAAKRPDAIALI----DG-EQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:cd05906     18 RAAERGPTKGITyidaDGsEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVP 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  107 yPGDRIEymlRDSDARILLTSTDVAKKLALTIPALQEcqtvyldqeifeydfHFLAIAKLLHNQYLRLLhfyfyTLIQQC 186
Cdd:cd05906     98 -PTYDEP---NARLRKLRHIWQLLGSPVVLTDAELVA---------------EFAGLETLSGLPGIRVL-----SIEELL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  187 QATSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLW---WHQQTRPsvqgvRTLQFCAVSFD-----FSC 258
Cdd:cd05906    154 DTAADHDLPQSR--PDDLALLMLTSGSTGFPKAVPLTHRNILARSAgkiQHNGLTP-----QDVFLNWVPLDhvgglVEL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  259 HeIFStLCLGGILVLVP-EAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEV---ITTGEQMqIT 334
Cdd:cd05906    227 H-LRA-VYLGCQQVHVPtEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLrylVNAGEAV-VA 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  335 PAVANLFQ---KTGA---MLHNHYGATEFQDATT---HTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEF 405
Cdd:cd05906    304 KTIRRLLRllePYGLppdAIRPAFGMTETCSGVIysrSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRL 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  406 CIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLArYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASH 485
Cdd:cd05906    384 QVRGPVVTKGYYNNPEANAEAFTEDGW---------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEV 453

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  486 QAVRE---CAVVAREIAGHT-QLVgyIIAKDTLNLSfDKLEPILRQYSEAVL------PEYMIPtrfINISNMPLTPSGK 555
Cdd:cd05906    454 PGVEPsftAAFAVRDPGAETeELA--IFFVPEYDLQ-DALSETLRAIRSVVSrevgvsPAYLIP---LPKEEIPKTSLGK 527


                   ....*.
gi 1331970929  556 LDRRAL 561
Cdd:cd05906    528 IQRSKL 533

MACS_AAE_MA_like

cd05970

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...

33-558

5.81e-21

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.

Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 99.88 E-value: 5.81e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALI-----DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY 107
Cdd:cd05970     27 AKEYPDKLALVwcddaGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  108 PGDRIEYMLRDSDARILLTS-----TDVAKKlaltipALQECQTVYL-------DQEIFEyDFHflaiaKLLHNQYlrll 175
Cdd:cd05970    107 TAKDIVYRIESADIKMIVAIaedniPEEIEK------AAPECPSKPKlvwvgdpVPEGWI-DFR-----KLIKNAS---- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  176 hfyfyTLIQQCQATSVSQGiqtqvlpNNLAYCIYTSGSTGNPKgiLMEHR------SLVNMLWWHQqTRPsvqGVRTLQF 249
Cdd:cd05970    171 -----PDFERPTANSYPCG-------EDILLVYFSSGTTGMPK--MVEHDftyplgHIVTAKYWQN-VRE---GGLHLTV 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  250 CAVSFDFSCHEIFSTLCLGGILVLVPEAVRQNPFALAEFISQQKIEKLFLP-VIALLQLAEAVNGNKSTSLALCevITTG 328
Cdd:cd05970    233 ADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPpTIYRFLIREDLSRYDLSSLRYC--TTAG 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  329 EQMqiTPAVANLF-QKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCI 407
Cdd:cd05970    311 EAL--NPEVFNTFkEKTGIKLMEGFGQTE----TTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVI 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  408 G-----GIGLARGYHNLPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVL 482
Cdd:cd05970    385 RtskgkPVGLFGGYYKDAEKTAEVW----------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESAL 454

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929  483 ASHQAVRECAV--VAREIAGHTQLVGYIIAKDTlnLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd05970    455 IQHPAVLECAVtgVPDPIRGQVVKATIVLAKGY--EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530

PLN02787

3-oxoacyl-[acyl-carrier-protein] synthase II

800-1107

7.32e-21

3-oxoacyl-[acyl-carrier-protein] synthase II

Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 99.67 E-value: 7.32e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  800 IGSALGIIteqpfietdmeqfqaKIGNDrSYLATRISYK----------------------LNLKGPSVNVQTACSTSLV 857
Cdd:PLN02787   233 IGSAMGGM---------------KVFND-AIEALRISYRkmnpfcvpfattnmgsamlamdLGWMGPNYSISTACATSNF 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  858 AVHMACQSLISGECQMALAGGI-SVVVP-QKGGYLYEEGMVRSQDGHCRA---FDAEAQGTIFGNGGGLVLLKRLQDALD 932
Cdd:PLN02787   297 CILNAANHIIRGEADVMLCGGSdAAIIPiGLGGFVACRALSQRNDDPTKAsrpWDMNRDGFVMGEGAGVLLLEELEHAKK 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  933 DNDNIMAVIKATAINNDgALKMgyTAPSVDGQADV--ISEAIAIADIDASTIGYVEAHGTATQLGDPIEVAGLARAFQRS 1010
Cdd:PLN02787   377 RGANIYAEFLGGSFTCD-AYHM--TEPHPEGAGVIlcIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQN 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1011 TdsvlgkqQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDfdaTPFFVNTELREWSrngyPRR 1090
Cdd:PLN02787   454 P-------ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVD---TKVLVGPKKERLD----IKV 519

                          330
                   ....*....|....*..
gi 1331970929 1091 AGVSSFGVGGTNSHIVL 1107
Cdd:PLN02787   520 ALSNSFGFGGHNSSILF 536

ttLC_FACS_AEE21_like

cd12118

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...

28-555

8.86e-21

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.

Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 98.91 E-value: 8.86e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAK-RPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVG 106
Cdd:cd12118      8 SFLERAAAvYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  107 YPGDRIEYMLRDSDARILLTstdvakklaltipalqecqtvylDQEiFEYDfHFLAIAKllhnqylrllhfYFYTLIQ-- 184
Cdd:cd12118     88 LDAEEIAFILRHSEAKVLFV-----------------------DRE-FEYE-DLLAEGD------------PDFEWIPpa 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  185 -QCQATSVSqgiqtqvlpnnlayciYTSGSTGNPKGILMEHR-----SLVNMLWWHQQTRPSVqgVRTLQfcavsfDFSC 258
Cdd:cd12118    131 dEWDPIALN----------------YTSGTTGRPKGVVYHHRgaylnALANILEWEMKQHPVY--LWTLP------MFHC 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  259 HE---IFSTLCLGGILVLVPEAvrqNPFALAEFISQQKIEKLFLPVIALLQLAeavNGNKSTSLAL---CEVITTGEqmq 332
Cdd:cd12118    187 NGwcfPWTVAAVGGTNVCLRKV---DAKAIYDLIEKHKVTHFCGAPTVLNMLA---NAPPSDARPLphrVHVMTAGA--- 257

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  333 iTPAVANLFQKTGAMLH-NH-YGATE-FQDATTHTLKgnPEgWPTLVP-----------VGRPLHNvQVYILD-EAQQPV 397
Cdd:cd12118    258 -PPPAAVLAKMEELGFDvTHvYGLTEtYGPATVCAWK--PE-WDELPTeerarlkarqgVRYVGLE-EVDVLDpETMKPV 332

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  398 PLGGE--GEFCIGGIGLARGYHNLPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVEL 475
Cdd:cd12118    333 PRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF----------RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISS 402

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  476 GEIESVLASHQAVRECAVVAR--EIAGHTqLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPtRFINISNMPLTPS 553
Cdd:cd12118    403 VEVEGVLYKHPAVLEAAVVARpdEKWGEV-PCAFVELKEGAKVTEEE----IIAFCREHLAGFMVP-KTVVFGELPKTST 476


                   ..
gi 1331970929  554 GK 555
Cdd:cd12118    477 GK 478

PRK06501

beta-ketoacyl-ACP synthase;

832-1112

1.69e-20

beta-ketoacyl-ACP synthase;

Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 97.01 E-value: 1.69e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  832 ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISvvvpqkgGYLYEEGMVR--------SQD--- 900
Cdd:PRK06501   155 ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATD-------GSVSAEALIRfsllsalsTQNdpp 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  901 -GHCRAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGALKmgyTAPSVDGQADV--ISEAIAIADI 977
Cdd:PRK06501   228 eKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHR---TRSSPDGSPAIgaIRAALADAGL 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  978 DASTIGYVEAHGTATQLGDPIEVAGLArafqrstdSVLGKQ--QCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPP 1055
Cdd:PRK06501   305 TPEQIDYINAHGTSTPENDKMEYLGLS--------AVFGERlaSIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPP 376

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1331970929 1056 SLHYANPNPRIDFDATPffvNTelrewSRNGYPRRAGVSSFGVGGTNSHIVLEESPV 1112
Cdd:PRK06501   377 TINYDNPDPAIPLDVVP---NV-----ARDARVTAVLSNSFGFGGQNASLVLTAEPA 425

ACS

cd05966

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...

32-561

1.91e-20

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.

Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 98.79 E-value: 1.91e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   32 QAAKRPDAIALI----DGEQS--LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGcayVPLDV 105
Cdd:cd05966     62 HLKERGDKVAIIwegdEPDQSrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIG---AVHSV 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  106 GYPG-------DRIEymlrDSDARILLTsTDVAKKLALTIP-------ALQECQTVYldqeifeydfHFLaIAKLLHNQ- 170
Cdd:cd05966    139 VFAGfsaeslaDRIN----DAQCKLVIT-ADGGYRGGKVIPlkeivdeALEKCPSVE----------KVL-VVKRTGGEv 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  171 -YLRLLHFYFYTLIQQ----CQATSVSqgiqtqvlPNNLAYCIYTSGSTGNPKGILmeHRSLVNMLWWHqqtrpsvqgvR 245
Cdd:cd05966    203 pMTEGRDLWWHDLMAKqspeCEPEWMD--------SEDPLFILYTSGSTGKPKGVV--HTTGGYLLYAA----------T 262

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  246 TLQFcavSFDFSCHEIF------------STLCLG----GILVLVPEAVRQNPFA--LAEFISQQKIEKLFL-P-VIALL 305
Cdd:cd05966    263 TFKY---VFDYHPDDIYwctadigwitghSYIVYGplanGATTVMFEGTPTYPDPgrYWDIVEKHKVTIFYTaPtAIRAL 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  306 QLA--EAVNGNKSTSLalcEVITT-GEQmqITPAVANLFqktgamlHNHYGA-------TEFQDAT-THTLKGNPEGWPT 374
Cdd:cd05966    340 MKFgdEWVKKHDLSSL---RVLGSvGEP--INPEAWMWY-------YEVIGKercpivdTWWQTETgGIMITPLPGATPL 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  375 lVP--VGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGI--GLARGYHNLPdltnEKFIP---NPFganenaKKLYRTGDL 447
Cdd:cd05966    408 -KPgsATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDtyfSKF------PGYYFTGDG 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  448 ARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR--EIAGHTqLVGYIIAKDTLNLSfDKLEPIL 525
Cdd:cd05966    477 ARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRphDIKGEA-IYAFVTLKDGEEPS-DELRKEL 554

                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1331970929  526 RQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05966    555 RKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590

PRK05952

beta-ketoacyl-ACP synthase;

842-1107

2.56e-20

beta-ketoacyl-ACP synthase;

Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 95.89 E-value: 2.56e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  842 KGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGI-SVVVP------QKGGYLYEEGmvrsqdghCRAFDAEAQGTI 914
Cdd:PRK05952   136 QGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVeAPITPltlagfQQMGALAKTG--------AYPFDRQREGLV 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  915 FGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgALKMgyTAPSVDGQADV--ISEAIAIADIDASTIGYVEAHGTAT 992
Cdd:PRK05952   208 LGEGGAILVLESAELAQKRGAKIYGQILGFGLTCD-AYHM--SAPEPDGKSAIaaIQQCLARSGLTPEDIDYIHAHGTAT 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  993 QLGDPIEVAGLARAFqrstdsvlgKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPRIDFDATP 1072
Cdd:PRK05952   285 RLNDQREANLIQALF---------PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNFVRQA 355

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1331970929 1073 ffVNTELREwsrngyprrAGVSSFGVGGTNSHIVL 1107
Cdd:PRK05952   356 --QQSPLQN---------VLCLSFGFGGQNAAIAL 379

PRK07786

long-chain-fatty-acid--CoA ligase; Validated

33-556

2.70e-20

long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 97.93 E-value: 2.70e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRI 112
Cdd:PRK07786    27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  113 EYMLRDSDARILLTS---TDVAKKLALTIPALQECQTV--YLDQEIFEYDfhflaiakllhnqylrllhfyfyTLIQQCQ 187
Cdd:PRK07786   107 AFLVSDCGAHVVVTEaalAPVATAVRDIVPLLSTVVVAggSSDDSVLGYE-----------------------DLLAEAG 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  188 ATSVSQGIqtqvlPNNLAYCI-YTSGSTGNPKGILMEHRSLVN-----MLWWHQQTRPSVqgvrtlQFCAVSFdFSCHEI 261
Cdd:PRK07786   164 PAHAPVDI-----PNDSPALImYTSGTTGRPKGAVLTHANLTGqamtcLRTNGADINSDV------GFVGVPL-FHIAGI 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  262 FST---LCLGGILVLVPEAVRqNPFALAEFISQQKIEKLFLpVIALLQLAEAVNGNKSTSLALcEVITTGEqmqiTPAVA 338
Cdd:PRK07786   232 GSMlpgLLLGAPTVIYPLGAF-DPGQLLDVLEAEKVTGIFL-VPAQWQAVCAEQQARPRDLAL-RVLSWGA----APASD 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  339 NLFQKTGAMLHNH-----YGATEFQDATThTLKGNpEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLA 413
Cdd:PRK07786   305 TLLRQMAATFPEAqilaaFGQTEMSPVTC-MLLGE-DAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLM 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  414 RGYHNLPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV 493
Cdd:PRK07786   383 SGYWNNPEATAEAF----------AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAV 452

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331970929  494 VAR--EIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGKL 556
Cdd:PRK07786   453 IGRadEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDR----LARYKHPKALEIVDALPRNPAGKV 513

PRK07470

acyl-CoA synthetase; Validated

32-574

3.25e-20

acyl-CoA synthetase; Validated

Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 97.42 E-value: 3.25e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   32 QAAKR-PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGD 110
Cdd:PRK07470    15 QAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  111 RIEYMLRDSDARILLTSTDVAKKL-ALTIPALQECQTVYLDQEIFEYDFHflaiakllhnqylrllhfyfyTLIQQCQAT 189
Cdd:PRK07470    95 EVAYLAEASGARAMICHADFPEHAaAVRAASPDLTHVVAIGGARAGLDYE---------------------ALVARHLGA 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  190 SVSQgiqTQVLPNNLAYCIYTSGSTGNPKGILMEH----------------------RSLVnmlwwhqqTRPSVQGVRTL 247
Cdd:PRK07470   154 RVAN---AAVDHDDPCWFFFTSGTTGRPKAAVLTHgqmafvitnhladlmpgtteqdASLV--------VAPLSHGAGIH 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  248 QFCAVSfdfscheifstlcLGGILVLVPeavrQNPFALAEF---ISQQKIEKLF-LPVI-ALLQLAEAVNGNKSTSLAlc 322
Cdd:PRK07470   223 QLCQVA-------------RGAATVLLP----SERFDPAEVwalVERHRVTNLFtVPTIlKMLVEHPAVDRYDHSSLR-- 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  323 EVITTGEQMQITPAVANLfQKTGAMLHNHYGATEFQDATT------HTLKGNPEgwPTLVPVGRPLHNVQVYILDEAQQP 396
Cdd:PRK07470   284 YVIYAGAPMYRADQKRAL-AKLGKVLVQYFGLGEVTGNITvlppalHDAEDGPD--ARIGTCGFERTGMEVQIQDDEGRE 360

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  397 VPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELG 476
Cdd:PRK07470   361 LPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF----------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPR 430

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  477 EIESVLASHQAVRECAVVA------REIAghtqlVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPL 550
Cdd:PRK07470   431 EIEEKLLTHPAVSEVAVLGvpdpvwGEVG-----VAVCVARDGAPVD----EAELLAWLDGKVARYKLPKRFFFWDALPK 501

                          570       580
                   ....*....|....*....|....*..
gi 1331970929  551 TPSGKLDRRALPDP---KGDRPALSTP 574
Cdd:PRK07470   502 SGYGKITKKMVREEleeRGLLDLERAP 528

PRK12406

long-chain-fatty-acid--CoA ligase; Provisional

41-564

8.84e-20

long-chain-fatty-acid--CoA ligase; Provisional

Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 95.92 E-value: 8.84e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   41 ALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSD 120
Cdd:PRK12406     4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  121 ARILLTSTDVAKKLALTIPALQECQTVYLDQEIfeydfhfLAIAKL-LHNQYLRLLHFYFYTLIQQCQATSVSQGIQTQV 199
Cdd:PRK12406    84 ARVLIAHADLLHGLASALPAGVTVLSVPTPPEI-------AAAYRIsPALLTPPAGAIDWEGWLAQQEPYDGPPVPQPQS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  200 LpnnlaycIYTSGSTGNPKGI-----LMEH------------------RSLVNMLWWHqqTRPSVQGVRTLQfcavsfdf 256
Cdd:PRK12406   157 M-------IYTSGTTGHPKGVrraapTPEQaaaaeqmraliyglkpgiRALLTGPLYH--SAPNAYGLRAGR-------- 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  257 scheifstlcLGGILVLVPeavRQNPFALAEFISQQKIEKLFL-PV--IALLQLAEAVNGNKSTSlALCEVITTGeqmqi 333
Cdd:PRK12406   220 ----------LGGVLVLQP---RFDPEELLQLIERHRITHMHMvPTmfIRLLKLPEEVRAKYDVS-SLRHVIHAA----- 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  334 TPAVANLFQKT----GAMLHNHYGATEFQDATTHTlkgnPEGW---PTlvPVGRPLHNVQVYILDEAQQPVPLGGEGEFC 406
Cdd:PRK12406   281 APCPADVKRAMiewwGPVIYEYYGSTESGAVTFAT----SEDAlshPG--TVGKAAPGAELRFVDEDGRPLPQGEIGEIY 354

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  407 IGGIGLAR-GYHNLPD----LTNEKFIPnpfganenakklyrTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESV 481
Cdd:PRK12406   355 SRIAGNPDfTYHNKPEkraeIDRGGFIT--------------SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAV 420

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  482 LASHQAVRECAV--VAREIAGHTqLVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:PRK12406   421 LHAVPGVHDCAVfgIPDAEFGEA-LMAVVEPQPGATLD----EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKR 495


                   ....*
gi 1331970929  560 ALPDP 564
Cdd:PRK12406   496 RLRDP 500

PRK13391

acyl-CoA synthetase; Provisional

33-564

1.00e-19

acyl-CoA synthetase; Provisional

Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 95.91 E-value: 1.00e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALI---DGEqSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPG 109
Cdd:PRK13391     7 AQTTPDKPAVImasTGE-VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  110 DRIEYMLRDSDARILLTST---DVAKKLALTIPALQECQTVYLDQEIFEYDFHFLAIAkllhnqylrllhfyfytliqQC 186
Cdd:PRK13391    86 AEAAYIVDDSGARALITSAaklDVARALLKQCPGVRHRLVLDGDGELEGFVGYAEAVA--------------------GL 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  187 QATSvsqgIQTQVLPNNLaycIYTSGSTGNPKGILMEHRSLvnmlwwhqqtrPSVQGVRTLQFCAVSFDFSCHEIF---- 262
Cdd:PRK13391   146 PATP----IADESLGTDM---LYSSGTTGRPKGIKRPLPEQ-----------PPDTPLPLTAFLQRLWGFRSDMVYlspa 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  263 ------------STLCLGGILVLVPeavRQNPFALAEFISQQKI-EKLFLPV--IALLQLAEAVNGNKSTS--------L 319
Cdd:PRK13391   208 plyhsapqravmLVIRLGGTVIVME---HFDAEQYLALIEEYGVtHTQLVPTmfSRMLKLPEEVRDKYDLSslevaihaA 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  320 ALCEViTTGEQMqitpavanlFQKTGAMLHNHYGATEFQDATThtlkGNPEGWptLV---PVGRPLHNVqVYILDEAQQP 396
Cdd:PRK13391   285 APCPP-QVKEQM---------IDWWGPIIHEYYAATEGLGFTA----CDSEEW--LAhpgTVGRAMFGD-LHILDDDGAE 347

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  397 VPLGGEGEFCIGGiGLARGYHNLPDLTNEKFIPNPfganenakKLYRTGDLArYLPDGTIEHL-GRIDHQVKIRGFRVEL 475
Cdd:PRK13391   348 LPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG--------TWSTVGDIG-YVDEDGYLYLtDRAAFMIISGGVNIYP 417

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  476 GEIESVLASHQAVRECAVV-------AREIAGHTQLVGYIIAKdtlnlsfDKLEPILRQYSEAVLPEYMIPTRFINISNM 548
Cdd:PRK13391   418 QEAENLLITHPKVADAAVFgvpnedlGEEVKAVVQPVDGVDPG-------PALAAELIAFCRQRLSRQKCPRSIDFEDEL 490

                          570
                   ....*....|....*.
gi 1331970929  549 PLTPSGKLDRRALPDP 564
Cdd:PRK13391   491 PRLPTGKLYKRLLRDR 506

AACS_like

cd05968

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...

25-574

1.21e-19

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.

Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 96.02 E-value: 1.21e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALI----DGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCA 99
Cdd:cd05968     63 VEQLLDKWLADTRTRPALRwegeDGTsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  100 YVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKK------LALTIPALQECQTVYldqeifeydfHFLAIAKLLHNQYLR 173
Cdd:cd05968    143 VVPIFSGFGKEAAATRLQDAEAKALITADGFTRRgrevnlKEEADKACAQCPTVE----------KVVVVRHLGNDFTPA 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  174 LLHFYFYTLIQQCQATSVSQgiqtqVLPNNLAYCIYTSGSTGNPKGILMEH-----RSLVNMlwWHQ-QTRPsvqGVRTL 247
Cdd:cd05968    213 KGRDLSYDEEKETAGDGAER-----TESEDPLMIIYTSGTTGKPKGTVHVHagfplKAAQDM--YFQfDLKP---GDLLT 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  248 QFCAVSFDFSCHEIFSTLCLGGILVLVpEAVRQNPFA--LAEFISQQKIEKLFLP---VIALLQLAEA-VNGNKSTSLal 321
Cdd:cd05968    283 WFTDLGWMMGPWLIFGGLILGATMVLY-DGAPDHPKAdrLWRMVEDHEITHLGLSptlIRALKPRGDApVNAHDLSSL-- 359

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  322 cEVI-TTGEQmqITPAVANLFQKTGAMLH----NHYGATEFQDAtthtLKGN-------PEGWPTLVPvgrplhNVQVYI 389
Cdd:cd05968    360 -RVLgSTGEP--WNPEPWNWLFETVGKGRnpiiNYSGGTEISGG----ILGNvlikpikPSSFNGPVP------GMKADV 426

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  390 LDEAQQPVPlGGEGEFCIGG--IGLARGYHNLPDLTNEKFipnpFGANENakkLYRTGDLARYLPDGTIEHLGRIDHQVK 467
Cdd:cd05968    427 LDESGKPAR-PEVGELVLLApwPGMTRGFWRDEDRYLETY----WSRFDN---VWVHGDFAYYDEEGYFYILGRSDDTIN 498

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  468 IRGFRVELGEIESVLASHQAVRECAV--VAREIAGhTQLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIPTRFINI 545
Cdd:cd05968    499 VAGKRVGPAEIESVLNAHPAVLESAAigVPHPVKG-EAIVCFVVLKPGVTPT-EALAEELMERVADELGKPLSPERILFV 576

                          570       580       590
                   ....*....|....*....|....*....|....
gi 1331970929  546 SNMPLTPSGKLDRRA-----LPDPKGDRPALSTP 574
Cdd:cd05968    577 KDLPKTRNAKVMRRViraayLGKELGDLSSLENP 610

caiC

PRK08008

putative crotonobetaine/carnitine-CoA ligase; Validated

28-561

1.42e-19

putative crotonobetaine/carnitine-CoA ligase; Validated

Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 95.52 E-value: 1.42e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAKRPDAIALI----DGE-QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVP 102
Cdd:PRK08008    12 MWDDLADVYGHKTALIfessGGVvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVP 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  103 LDVGYPGDRIEYMLRDSDARILLTStdvAKKLALTIPALQECQTVYldQEIFEYDFHFLAIAKLLHnqylrllhfyFYTL 182
Cdd:PRK08008    92 INARLLREESAWILQNSQASLLVTS---AQFYPMYRQIQQEDATPL--RHICLTRVALPADDGVSS----------FTQL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  183 IQQcQATSVSQgiQTQVLPNNLAYCIYTSGSTGNPKGILMEHrslVNMLW------WHQQTRPSVQGVRTLQFCAVsfDF 256
Cdd:PRK08008   157 KAQ-QPATLCY--APPLSTDDTAEILFTSGTTSRPKGVVITH---YNLRFagyysaWQCALRDDDVYLTVMPAFHI--DC 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  257 SCHEIFSTLCLGGILVLVPEavrqnpFALAEFISQQKIEKLFL----PVIA---LLQLAEAVNGNKstslALCEVITTge 329
Cdd:PRK08008   229 QCTAAMAAFSAGATFVLLEK------YSARAFWGQVCKYRATIteciPMMIrtlMVQPPSANDRQH----CLREVMFY-- 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  330 qMQITPAVANLF-QKTGAMLHNHYGATEfqdaTTHTLKGNPEG----WPTlvpVGRPLHNVQVYILDEAQQPVPLGGEGE 404
Cdd:PRK08008   297 -LNLSDQEKDAFeERFGVRLLTSYGMTE----TIVGIIGDRPGdkrrWPS---IGRPGFCYEAEIRDDHNRPLPAGEIGE 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  405 FCIGGI---GLARGYHNLPDLTNEKFIPNPFganenakkLYrTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESV 481
Cdd:PRK08008   369 ICIKGVpgkTIFKEYYLDPKATAKVLEADGW--------LH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENI 439

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  482 LASHQAVRECAVVAREIAGHTQLV-GYIIAKDTLNLSfdkLEPILrQYSEAVLPEYMIPTrFINI-SNMPLTPSGKLDRR 559
Cdd:PRK08008   440 IATHPKIQDIVVVGIKDSIRDEAIkAFVVLNEGETLS---EEEFF-AFCEQNMAKFKVPS-YLEIrKDLPRNCSGKIIKK 514


                   ..
gi 1331970929  560 AL 561
Cdd:PRK08008   515 NL 516

YqjQ

COG0300

Short-chain dehydrogenase [General function prediction only];

2536-2693

1.66e-19

Short-chain dehydrogenase [General function prediction only];

Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 90.70 E-value: 1.66e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGAKyLVLVGRRGAREEQQAQlsELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:COG0300     21 LARALAARGAR-VVLVARDAERLEALAA--ELRAAGARVEVVALDVTDPDAVAALAEAVlaRFGPIDVLVNNAGVGGGGP 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2614 LQQQSWQAFKEVMNPKVAGAWNLHILT----KNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA-SYR---RHLGL 2685
Cdd:COG0300     98 FEELDLEDLRRVFEVNVFGPVRLTRALlplmRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSeSLRaelAPTGV 177


                   ....*...
gi 1331970929 2686 PSLSINWG 2693
Cdd:COG0300    178 RVTAVCPG 185

PRK07787

acyl-CoA synthetase; Validated

33-494

2.20e-19

acyl-CoA synthetase; Validated

Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 94.29 E-value: 2.20e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALidGEQSLTYGELNVRANHLAQHLLSLgcqpdDLLAICIERSAELFIGLLGILKAGCAYVPL--DVGyPGD 110
Cdd:PRK07787    12 AADIADAVRI--GGRVLSRSDLAGAATAVAERVAGA-----RRVAVLATPTLATVLAVVGALIAGVPVVPVppDSG-VAE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  111 RiEYMLRDSDARILLTSTDvakklaltiPALQECQTVYLDqeifeydfhflaiaklLHNqylRLLHFYfytliqqcqats 190
Cdd:PRK07787    84 R-RHILADSGAQAWLGPAP---------DDPAGLPHVPVR----------------LHA---RSWHRY------------ 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  191 vsqgiqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNML------WwhQQTRPSVQgVRTLQFcavsfdFSCHE---- 260
Cdd:PRK07787   123 ------PEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLdalaeaW--QWTADDVL-VHGLPL------FHVHGlvlg 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  261 IFSTLCLGGILVLVpeaVRQNPFALAEFISQQKIEKLFLP-----VIALLQLAEAVNGNK---STSLALCevittgeqmq 332
Cdd:PRK07787   188 VLGPLRIGNRFVHT---GRPTPEAYAQALSEGGTLYFGVPtvwsrIAADPEAARALRGARllvSGSAALP---------- 254

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  333 iTPAVANLFQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGE--GEFCIGGI 410
Cdd:PRK07787   255 -VPVFDRLAALTGHRPVERYGMTE----TLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGP 329

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  411 GLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGR--IDhQVKIRGFRVELGEIESVLASHQAV 488
Cdd:PRK07787   330 TLFDGYLNRPDATAAAFTADGW---------FRTGDVAVVDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGV 399


                   ....*.
gi 1331970929  489 RECAVV 494
Cdd:PRK07787   400 REAAVV 405

LC_FACS_like

cd17640

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...

44-482

2.35e-19

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.

Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 94.35 E-value: 2.35e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   44 DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARI 123
Cdd:cd17640      1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  124 LLTSTDvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlPNN 203
Cdd:cd17640     81 LVVEND-----------------------------------------------------------------------SDD 89

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  204 LAYCIYTSGSTGNPKGILMEHRSL---VNMLWWHQQTRPsvqGVRTLQFCAV--SFDFSChEIFSTLCLGGI-------- 270
Cdd:cd17640     90 LATIIYTSGTTGNPKGVMLTHANLlhqIRSLSDIVPPQP---GDRFLSILPIwhSYERSA-EYFIFACGCSQaytsirtl 165

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  271 -----------LVLVP---EAVRQN---PFALAEFISQqkieKLFLPVIALLQLAEAVNGNKStslalcevittgeqmqI 333
Cdd:cd17640    166 kddlkrvkphyIVSVPrlwESLYSGiqkQVSKSSPIKQ----FLFLFFLSGGIFKFGISGGGA----------------L 225

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  334 TPAVANLFQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIGL 412
Cdd:cd17640    226 PPHVDTFFEAIGIEVLNGYGLTE----TSPVVSARRLKCNVRGSVGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQV 301

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331970929  413 ARGYHNLPDLTnEKFIpnpfganeNAKKLYRTGDLARYLPDGTIEHLGRI-DHQVKIRGFRVELGEIESVL 482
Cdd:cd17640    302 MKGYYKNPEAT-SKVL--------DSDGWFNTGDLGWLTCGGELVLTGRAkDTIVLSNGENVEPQPIEEAL 363

AFD_YhfT-like

cd17633

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...

203-558

2.57e-19

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain

Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 91.70 E-value: 2.57e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  203 NLAYCIYTSGSTGNPKGILMEHRSL-------VNMLWWHQQTRPSVQGvrtlqfcAVSFDFSCHEIFSTLCLGGILVLVP 275
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWiesfvcnEDLFNISGEDAILAPG-------PLSHSLFLYGAISALYLGGTFIGQR 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  276 EAvrqNPFALAEFISQQKIEKLFLpVIALLQLAEAVNGNKSTslalCEVITTGEQM---QITPAVANLFQKtgAMLHNHY 352
Cdd:cd17633     74 KF---NPKSWIRKINQYNATVIYL-VPTMLQALARTLEPESK----IKSIFSSGQKlfeSTKKKLKNIFPK--ANLIEFY 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  353 GATEfqdATTHTLKGNPEGWPTLvPVGRPLHNVQVYILDEAQqpvplGGEGEFCIGgiglargyhnlpdlTNEKFIPNPF 432
Cdd:cd17633    144 GTSE---LSFITYNFNQESRPPN-SVGRPFPNVEIEIRNADG-----GEIGKIFVK--------------SEMVFSGYVR 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  433 GANENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKD 512
Cdd:cd17633    201 GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD 280

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1331970929  513 TLNlsfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd17633    281 KLT------YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320

PRK05852

fatty acid--CoA ligase family protein;

28-561

3.26e-19

fatty acid--CoA ligase family protein;

Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 94.18 E-value: 3.26e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAKRPDAIALIDGEQ--SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDV 105
Cdd:PRK05852    21 LVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  106 GYPGDRIEYMLRDSDAR-ILLTSTDVAKKLALTIPALQECQTVYLDQEIFE--YDFHFLAIAKLLHnqylrllhfyfytl 182
Cdd:PRK05852   101 ALPIAEQRVRSQAAGARvVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGgtLSVHLDAATEPTP-------------- 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  183 iqqcqATSVSQGiqtqvLPNNLAYCIYTSGSTGNPKgilmehrslvnML-WWHQQTRPSVQGVRTL-------QFCAVSF 254
Cdd:PRK05852   167 -----ATSTPEG-----LRPDDAMIMFTGGTTGLPK-----------MVpWTHANIASSVRAIITGyrlsprdATVAVMP 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  255 DFSCH----EIFSTLCLGGIlVLVPEAVRqnpFALAEFISQQKIEK----LFLPVI--ALLQLA-EAVNGNKSTSLALCE 323
Cdd:PRK05852   226 LYHGHgliaALLATLASGGA-VLLPARGR---FSAHTFWDDIKAVGatwyTAVPTIhqILLERAaTEPSGRKPAALRFIR 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  324 VITTgeqmQITPAVANLFQKT-GAMLHNHYGATE--FQDATTHTLKGNPEGWPTLV--PVGRPLhNVQVYILDEAQQPVP 398
Cdd:PRK05852   302 SCSA----PLTAETAQALQTEfAAPVVCAFGMTEatHQVTTTQIEGIGQTENPVVStgLVGRST-GAQIRIVGSDGLPLP 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  399 LGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEI 478
Cdd:PRK05852   377 AGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL----------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERV 446

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  479 ESVLASHQAVRECAVVAREIAGHTQLVG-YIIAKDTLNLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:PRK05852   447 EGVLASHPNVMEAAVFGVPDQLYGEAVAaVIVPRESAPPTAEELVQFCRER----LAAFEIPASFQEASGLPHTAKGSLD 522


                   ....
gi 1331970929  558 RRAL 561
Cdd:PRK05852   523 RRAV 526

PRK06145

acyl-CoA synthetase; Validated

33-563

3.72e-19

acyl-CoA synthetase; Validated

Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 93.80 E-value: 3.72e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRI 112
Cdd:PRK06145    12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  113 EYMLRDSDARILLtstdvakklaltipalqecqtvyLDQEifeydfhFLAIAKLLHNQYLRLLHfyfytliQQCQATSVS 192
Cdd:PRK06145    92 AYILGDAGAKLLL-----------------------VDEE-------FDAIVALETPKIVIDAA-------AQADSRRLA 134

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  193 QG-----IQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLvnmlWWHQQTRPSVQGVRTLQFCAV--------SFDFSCh 259
Cdd:PRK06145   135 QGgleipPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNL----HWKSIDHVIALGLTASERLLVvgplyhvgAFDLPG- 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  260 eiFSTLCLGGILVLVPEAvrqNPFALAEFISQQKIE-KLFLPVI--ALLQLAEAVNGNKSTslaLCEVITTGEQmqiTP- 335
Cdd:PRK06145   210 --IAVLWVGGTLRIHREF---DPEAVLAAIERHRLTcAWMAPVMlsRVLTVPDRDRFDLDS---LAWCIGGGEK---TPe 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  336 ----AVANLFqkTGAMLHNHYGATEFQDATTHTLKGNPegWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIG 411
Cdd:PRK06145   279 srirDFTRVF--TRARYIDAYGLTETCSGDTLMEAGRE--IEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPK 354

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  412 LARGYHNLPDLTNEKFIPNPFganenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVREC 491
Cdd:PRK06145   355 VTKGYWKDPEKTAEAFYGDWF----------RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEA 424

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331970929  492 AVV-AREIAGHTQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:PRK06145   425 AVIgVHDDRWGERITAVVVLNPGATLTLEA----LDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493

Tam

COG4106

Trans-aconitate methyltransferase [Energy production and conversion];

2108-2215

4.02e-19

Trans-aconitate methyltransferase [Energy production and conversion];

Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 84.49 E-value: 4.02e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2108 RGWRILEIGAGTGGTTAYLLPHLPGDQtkYVFTDISAFFLAKAEERFKDypfVRYQVLDIEQAPqaqgFEPQiYDLIVAA 2187
Cdd:COG4106      1 PPRRVLDLGCGTGRLTALLAERFPGAR--VTGVDLSPEMLARARARLPN---VRFVVADLRDLD----PPEP-FDLVVSN 70

                           90       100
                   ....*....|....*....|....*...
gi 1331970929 2188 DVLHATSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:COG4106     71 AALHWLPDHAALLARLAAALAPGGVLAV 98

FACL_like_2

cd05917

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

209-558

4.18e-19

Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 91.57 E-value: 4.18e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  209 YTSGSTGNPKGILMEHRSLVN-------MLWWHQQTRPSvqgvrtlqfCAVSFdFSCH----EIFSTLCLGGILVLVPEA 277
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNIVNngyfigeRLGLTEQDRLC---------IPVPL-FHCFgsvlGVLACLTHGATMVFPSPS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  278 VrqNPFALAEFISQQKIEKLF-LPV--IALLQLAEAVNGNKSTslaLCEVITTG-----EQMQitpavaNLFQKTGAM-L 348
Cdd:cd05917     79 F--DPLAVLEAIEKEKCTALHgVPTmfIAELEHPDFDKFDLSS---LRTGIMAGapcppELMK------RVIEVMNMKdV 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  349 HNHYGATEFQDATTHTLKGNPEGwPTLVPVGRPLHNVQVYILDEAQQPVP-LGGEGEFCIGGIGLARGYHNLPDLTNEKf 427
Cdd:cd05917    148 TIAYGMTETSPVSTQTRTDDSIE-KRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEA- 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  428 ipnpfganENAKKLYRTGDLARYLPDGTIEHLGRIDHQVkIRGfrvelG------EIESVLASHQAVRECAVVAreIAGH 501
Cdd:cd05917    226 --------IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRG-----GeniyprEIEEFLHTHPKVSDVQVVG--VPDE 289

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  502 T---QLVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd05917    290 RygeEVCAWIRLKEGAELT----EEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345

COG4976

Predicted methyltransferase, contains TPR repeat [General function prediction only];

2094-2221

4.57e-19

Predicted methyltransferase, contains TPR repeat [General function prediction only];

Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 87.36 E-value: 4.57e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2094 QEALLSALEQLPPERGWRILEIGAGTGGTTAYLLPHlpGDqtKYVFTDISAFFLAKAEERFKDypfVRYQVLDIEQAPQa 2173
Cdd:COG4976     32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR--GY--RLTGVDLSEEMLAKAREKGVY---DRLLVADLADLAE- 103

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1331970929 2174 qgfEPQIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLIL-MEDSEP 2221
Cdd:COG4976    104 ---PDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFsVEDADG 149

PrpE

cd05967

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...

199-561

5.44e-19

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.

Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 93.92 E-value: 5.44e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  199 VLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLqFCA------VSFDFSCheiFSTLCLG---- 268
Cdd:cd05967    227 VAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVW-WAAsdvgwvVGHSYIV---YGPLLHGattv 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  269 ---GILVLVPEavrqnPFALAEFISQQKIEKLFLPVIALLQL----AEAVNGNKSTSLALCEVITTGEQMQItPAVANLF 341
Cdd:cd05967    303 lyeGKPVGTPD-----PGAFWRVIEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLSSLRTLFLAGERLDP-PTLEWAE 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  342 QKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVP----VGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGiGLARGyh 417
Cdd:cd05967    377 NTLGVPVIDHWWQTE----TGWPITANPVGLEPLPIkagsPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPG-- 449

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  418 NLPDL--TNEKFIPNPFGaneNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA 495
Cdd:cd05967    450 CLLTLwkNDERFKKLYLS---KFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVG 526

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929  496 R--EIAGHTQLvGYIIAKDTLNLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05967    527 VrdELKGQVPL-GLVVLKEGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593

PRK08974

long-chain-fatty-acid--CoA ligase FadD;

27-563

5.70e-19

long-chain-fatty-acid--CoA ligase FadD;

Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 93.58 E-value: 5.70e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   27 HLFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLS-LGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDV 105
Cdd:PRK08974    27 DMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNP 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  106 GYPGDRIEYMLRDSDAR-ILLTS------------TDVaKKLALT-----IPA----LQECQTVYLDQEIFEYDF-HFLA 162
Cdd:PRK08974   107 LYTPRELEHQLNDSGAKaIVIVSnfahtlekvvfkTPV-KHVILTrmgdqLSTakgtLVNFVVKYIKRLVPKYHLpDAIS 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  163 IAKLLHNQYLRllhfyfytliqqcqatsvsQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSV 241
Cdd:PRK08974   186 FRSALHKGRRM-------------------QYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLaNLEQAKAAYGPLL 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  242 QGVRTLQFCAVSFdfscHEIF--STLCL-----GGILVLVpeavrQNPFALAEFISQQKIEKlFLPVIALLQLAEAVNGN 314
Cdd:PRK08974   247 HPGKELVVTALPL----YHIFalTVNCLlfielGGQNLLI-----TNPRDIPGFVKELKKYP-FTAITGVNTLFNALLNN 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  315 KS------TSLALceviTTGEQMQITPAVANLFQK-TGAMLHNHYGATE---FQDATTHTLKGNpEGwptlvPVGRPLHN 384
Cdd:PRK08974   317 EEfqeldfSSLKL----SVGGGMAVQQAVAERWVKlTGQYLLEGYGLTEcspLVSVNPYDLDYY-SG-----SIGLPVPS 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  385 VQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEkFIPNPFGAnenakklyrTGDLARYLPDGTIEHLGRIDH 464
Cdd:PRK08974   387 TEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGWLA---------TGDIAVMDEEGFLRIVDRKKD 456

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  465 QVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAGHTQLVgYIIAKDTlNLSFDKLEPILRQYseavLPEYMIPtRF 542
Cdd:PRK08974   457 MILVSGFNVYPNEIEDVVMLHPKVLEVAAvgVPSEVSGEAVKI-FVVKKDP-SLTEEELITHCRRH----LTGYKVP-KL 529

                          570       580
                   ....*....|....*....|..
gi 1331970929  543 INISN-MPLTPSGKLDRRALPD 563
Cdd:PRK08974   530 VEFRDeLPKSNVGKILRRELRD 551

LC_FACL_like

cd05914

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...

42-558

6.11e-19

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.

Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 92.89 E-value: 6.11e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   42 LIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDA 121
Cdd:cd05914      1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  122 RILLTSTdvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlP 201
Cdd:cd05914     81 KAIFVSD------------------------------------------------------------------------E 88

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  202 NNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFSCheifstlCLGGILVLVPEA---- 277
Cdd:cd05914     89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPL-------TFTLLLPLLNGAhvvf 161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  278 VRQNPFALAEFISQQK------------IEKLF----LPVIAL----LQLAEAVNGNKSTSLA-----------LCEVIT 326
Cdd:cd05914    162 LDKIPSAKIIALAFAQvtptlgvpvplvIEKIFkmdiIPKLTLkkfkFKLAKKINNRKIRKLAfkkvheafggnIKEFVI 241

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  327 TGEQMQitPAVANLFQKTGAMLHNHYGATEfqdaTTHTLKGNPEGWPTLVPVGRPLHNVQVYILDeaqqPVPLGGEGEFC 406
Cdd:cd05914    242 GGAKIN--PDVEEFLRTIGFPYTIGYGMTE----TAPIISYSPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEII 311

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  407 IGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQ-VKIRGFRVELGEIESVLASH 485
Cdd:cd05914    312 VRGPNVMKGYYKNPEATAEAFDKDGW---------FHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNM 382

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  486 QAVRECAVVAREiaGHTQLVGYIIAkDTLNLSFDKLEPILRQYSEAV-------LPEY-------MIPTRFinisnmPLT 551
Cdd:cd05914    383 PFVLESLVVVQE--KKLVALAYIDP-DFLDVKALKQRNIIDAIKWEVrdkvnqkVPNYkkiskvkIVKEEF------EKT 453


                   ....*..
gi 1331970929  552 PSGKLDR 558
Cdd:cd05914    454 PKGKIKR 460

UbiG

COG2227

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...

2095-2216

7.87e-19

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis

Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 84.68 E-value: 7.87e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2095 EALLSALEQLPPeRGWRILEIGAGTGGTTAYLLPHlpGDQtkYVFTDISAFFLAKAEERFKDYPfVRYQVLDIEQAPqaq 2174
Cdd:COG2227     12 RRLAALLARLLP-AGGRVLDVGCGTGRLALALARR--GAD--VTGVDISPEALEIARERAAELN-VDFVQGDLEDLP--- 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1331970929 2175 gFEPQIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILM 2216
Cdd:COG2227     83 -LEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLS 123

FADD10

cd17635

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...

208-558

1.23e-18

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.

Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 90.01 E-value: 1.23e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  208 IYTSGSTGNPKGILMEHRSLV---NMLWWHQQTrpSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGILVLVPEavRQNPFA 284
Cdd:cd17635      7 IFTSGTTGEPKAVLLANKTFFavpDILQKEGLN--WVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE--NTTYKS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  285 LAEFISQQKIEKLFLPVIALLQLaeaVNGNKSTsLALCE---VITTGEQMQITPAVANLFQKTGAMLHNHYGATEfqdAT 361
Cdd:cd17635     83 LFKILTTNAVTTTCLVPTLLSKL---VSELKSA-NATVPslrLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSE---TG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  362 THTLKGNPEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakkl 441
Cdd:cd17635    156 TALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--------- 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  442 yRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAK---DTLNLSF 518
Cdd:cd17635    227 -NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeLDENAIR 305

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1331970929  519 DKLEPILRQyseavLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:cd17635    306 ALKHTIRRE-----LEPYARPSTIVIVTDIPRTQSGKVKR 340

PtmA

cd17636

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...

208-494

1.45e-18

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.

Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 89.67 E-value: 1.45e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  208 IYTSGSTGNPKGILMEHRSL----VNMLWWHQQTRPSV---QG----VRTLQFCavsfdfscheiFSTLCLGGILVLVPe 276
Cdd:cd17636      6 IYTAAFSGRPNGALLSHQALlaqaLVLAVLQAIDEGTVflnSGplfhIGTLMFT-----------LATFHAGGTNVFVR- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  277 avRQNPFALAEFISQQKIEKLFLPVIALLQLAEAvNGNKSTSLALCEVITT--GEQMQITPAVANLFQKTGAmlhnhYGA 354
Cdd:cd17636     74 --RVDAEEVLELIEAERCTHAFLLPPTIDQIVEL-NADGLYDLSSLRSSPAapEWNDMATVDTSPWGRKPGG-----YGQ 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  355 TE-FQDATTHTLKGNPEGwptlvPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFipnpfg 433
Cdd:cd17636    146 TEvMGLATFAALGGGAIG-----GAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT------ 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331970929  434 anenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVV 494
Cdd:cd17636    215 ----RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271

PRK03640

o-succinylbenzoate--CoA ligase;

32-561

1.52e-18

o-succinylbenzoate--CoA ligase;

Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 91.95 E-value: 1.52e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   32 QAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDR 111
Cdd:PRK03640    11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  112 IEYMLRDSDARILLTSTDVAKKLALTIPAL-QECQTVYLDQEIFEYDFHFLAIAKLlhnqylrllhfyfytliqqcqats 190
Cdd:PRK03640    91 LLWQLDDAEVKCLITDDDFEAKLIPGISVKfAELMNGPKEEAEIQEEFDLDEVATI------------------------ 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  191 vsqgiqtqvlpnnlaycIYTSGSTGNPKGILM---EHrslvnmlWWHqqtrpsvqgvrtlqfcAVS--FDFSCHEIFSTL 265
Cdd:PRK03640   147 -----------------MYTSGTTGKPKGVIQtygNH-------WWS----------------AVGsaLNLGLTEDDCWL 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  266 C------LGGILVLVPEAVRQNPFALAEFISQQKIEKLFLP--------VIALLQ--LAEAVNGNKSTSLAlCEVITTGe 329
Cdd:PRK03640   187 AavpifhISGLSILMRSVIYGMRVVLVEKFDAEKINKLLQTggvtiisvVSTMLQrlLERLGEGTYPSSFR-CMLLGGG- 264

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  330 qmqitPAVANLFQKtgAMLHN-----HYGATE---------FQDATThtlkgnpegwpTLVPVGRPLHNVQVYILDEAQq 395
Cdd:PRK03640   265 -----PAPKPLLEQ--CKEKGipvyqSYGMTEtasqivtlsPEDALT-----------KLGSAGKPLFPCELKIEKDGV- 325

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  396 PVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklyRTGDLArYL-PDGTIEHLGRIDHQVKIRGFRVE 474
Cdd:PRK03640   326 VVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF----------KTGDIG-YLdEEGFLYVLDRRSDLIISGGENIY 394

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  475 LGEIESVLASHQAVRECAVVAREIAGHTQL-VGYIIAKDTLNlsfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPS 553
Cdd:PRK03640   395 PAEIEEVLLSHPGVAEAGVVGVPDDKWGQVpVAFVVKSGEVT------EEELRHFCEEKLAKYKVPKRFYFVEELPRNAS 468


                   ....*...
gi 1331970929  554 GKLDRRAL 561
Cdd:PRK03640   469 GKLLRHEL 476

PLN02330

4-coumarate--CoA ligase-like 1

38-563

2.35e-18

4-coumarate--CoA ligase-like 1

Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 91.58 E-value: 2.35e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   38 DAIALIDGE--QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYM 115
Cdd:PLN02330    43 DKVAFVEAVtgKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQ 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  116 LRDSDARILLTS-TDVAKKLALTIPalqecqTVYLDQEIFEYDFHFlaiAKLLHNQylrllhfyfytliQQCQATSVSQg 194
Cdd:PLN02330   123 AEAAGAKLIVTNdTNYGKVKGLGLP------VIVLGEEKIEGAVNW---KELLEAA-------------DRAGDTSDNE- 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  195 iqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSVQG-VRTLQFcaVSFdFSCHEI----FSTLCLG 268
Cdd:PLN02330   180 ---EILQTDLCALPFSSGTTGISKGVMLTHRNLVaNLCSSLFSVGPEMIGqVVTLGL--IPF-FHIYGItgicCATLRNK 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  269 GILVLVpeavrqNPFALAEF----ISQQ-KIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQMqiTPAVANLFQK 343
Cdd:PLN02330   254 GKVVVM------SRFELRTFlnalITQEvSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPL--APELLTAFEA 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  344 T--GAMLHNHYGATEFQDAT-THtlkGNPE---GWPTLVPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIGLARGY 416
Cdd:PLN02330   326 KfpGVQVQEAYGLTEHSCITlTH---GDPEkghGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGY 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  417 HNLPDLTNEKFipnpfganeNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVV-- 494
Cdd:PLN02330   403 YNNKEETDRTI---------DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVpl 473

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  495 AREIAGHTQLVGYIIAKDtlnlSFDKLEPILrQYSEAVLPEYMiPTRFIN-ISNMPLTPSGKLDRRALPD 563
Cdd:PLN02330   474 PDEEAGEIPAACVVINPK----AKESEEDIL-NFVAANVAHYK-KVRVVQfVDSIPKSLSGKIMRRLLKE 537

PRK04319

acetyl-CoA synthetase; Provisional

36-573

3.69e-18

acetyl-CoA synthetase; Provisional

Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 91.11 E-value: 3.69e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   36 RPDAIALI----DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGY-PG- 109
Cdd:PRK04319    57 RKDKVALRyldaSRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFmEEa 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  110 --DRIEymlrDSDARILLTSTDV-AKKLALTIPALqecQTVYLDQEIFEYDFHFLAIAKLLhnqylrllhfyfytliqqc 186
Cdd:PRK04319   137 vrDRLE----DSEAKVLITTPALlERKPADDLPSL---KHVLLVGEDVEEGPGTLDFNALM------------------- 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  187 QATSVSQGIqTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNmlwwHQQTRPSVQgvrtlqfcavsfDFscHE------ 260
Cdd:PRK04319   191 EQASDEFDI-EWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ----HYQTGKYVL------------DL--HEddvywc 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  261 -------------IFSTLCLGGILVLVpeAVRQNPFALAEFISQQKIEKLFLPVIALLQL----AEAVNGNKSTSLALC- 322
Cdd:PRK04319   252 tadpgwvtgtsygIFAPWLNGATNVID--GGRFSPERWYRILEDYKVTVWYTAPTAIRMLmgagDDLVKKYDLSSLRHIl 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  323 --------EVITTGEQMQITPAVANLFQ-KTGAMLHNHYGATEFQDATthtlkgnpegwptlvpVGRPLHNVQVYILDEA 393
Cdd:PRK04319   330 svgeplnpEVVRWGMKVFGLPIHDNWWMtETGGIMIANYPAMDIKPGS----------------MGKPLPGIEAAIVDDQ 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  394 QQPVPLGGEGEFCI--GGIGLARGYHNLPDLTNEKFIPNpfganenakkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGF 471
Cdd:PRK04319   394 GNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAGD----------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGE 463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  472 RVELGEIESVLASHQAVRECAVvareIAGHTQLVGYII-AKDTLNLSF---DKLEPILRQYSEAVLPEYMIPTRFINISN 547
Cdd:PRK04319   464 RVGPFEVESKLMEHPAVAEAGV----IGKPDPVRGEIIkAFVALRPGYepsEELKEEIRGFVKKGLGAHAAPREIEFKDK 539

                          570       580       590
                   ....*....|....*....|....*....|.
gi 1331970929  548 MPLTPSGKLDRRALPD-----PKGDrpaLST 573
Cdd:PRK04319   540 LPKTRSGKIMRRVLKAwelglPEGD---LST 567

PRK09185

beta-ketoacyl-ACP synthase;

839-1107

7.59e-18

beta-ketoacyl-ACP synthase;

Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 88.75 E-value: 7.59e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  839 LNLKGPSVNVQTACSTSlVAVHMACQSLI-SGECQMALAGGI---------------SVvvpqkggylyeegmvrsQDGH 902
Cdd:PRK09185   147 LGLSGPAYTISTACSSS-AKVFASARRLLeAGLCDAAIVGGVdslcrltlngfnsleSL-----------------SPQP 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  903 CRAFDAEAQGTIFGNGGGLVLLKRLQDAlddndnimAVIKATAINNDGALKMGYTAPSVDGQADVISEAIAIADIDASTI 982
Cdd:PRK09185   209 CRPFSANRDGINIGEAAAFFLLEREDDA--------AVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADI 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  983 GYVEAHGTATQLGDPIEVAGLARAFQRSTdsvlgkqqcAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANP 1062
Cdd:PRK09185   281 GYINLHGTATPLNDAMESRAVAAVFGDGV---------PCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQP 351

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1331970929 1063 NPriDFDATPFFVNTELREwsrngyPRRAGVSSFGVGGTNSHIVL 1107
Cdd:PRK09185   352 DP--ALPPLYLVENAQALA------IRYVLSNSFAFGGNNCSLIF 388

Methyltransf_25

pfam13649

Methyltransferase domain; This family appears to be a methyltransferase domain.

2112-2211

1.38e-17

Methyltransferase domain; This family appears to be a methyltransferase domain.

Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 80.30 E-value: 1.38e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2112 ILEIGAGTGGTTAYLLPHLPGdqtKYVFTDISAFFLAKAEERFKDYPF-VRYQVLDIEQAPqaqgFEPQIYDLIVAADVL 2190
Cdd:pfam13649    1 VLDLGCGTGRLTLALARRGGA---RVTGVDLSPEMLERARERAAEAGLnVEFVQGDAEDLP----FPDGSFDLVVSSGVL 73

                           90       100
                   ....*....|....*....|...
gi 1331970929 2191 HATS--DLRQTLVHIRQLLAPGG 2211
Cdd:pfam13649   74 HHLPdpDLEAALREIARVLKPGG 96

OSB_CoA_lg

cd05912

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...

48-561

1.61e-17

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.

Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 87.79 E-value: 1.61e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   48 SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDarillts 127
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  128 tdVAKKLALTIpalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlpnnlayc 207
Cdd:cd05912     74 --VKLDDIATI--------------------------------------------------------------------- 82

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  208 IYTSGSTGNPKGILMEHRslvnMLWWHqqtrpSVQGVRTLQF-------CAVS-FDFSCHEI-FSTLCLGGILVLVPeav 278
Cdd:cd05912     83 MYTSGTTGKPKGVQQTFG----NHWWS-----AIGSALNLGLteddnwlCALPlFHISGLSIlMRSVIYGMTVYLVD--- 150

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  279 RQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALceVITTGEqmqitPAVANLF---QKTGAMLHNHYGAT 355
Cdd:cd05912    151 KFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRC--ILLGGG-----PAPKPLLeqcKEKGIPVYQSYGMT 223

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  356 EfqdATTHTLKGNPEGWPT-LVPVGRPLHNVQVYILDEAQQPvplGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFga 434
Cdd:cd05912    224 E---TCSQIVTLSPEDALNkIGSAGKPLFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFENGWF-- 295

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  435 nenakklyRTGDLArYL-PDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQL-VGYIIAKD 512
Cdd:cd05912    296 --------KTGDIG-YLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVpVAFVVSER 366

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1331970929  513 TlnLSFDKLEPILRQYseavLPEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05912    367 P--ISEEELIAYCSEK----LAKYKVPKKIYFVDELPRTASGKLLRHEL 409

PRK09274

peptide synthase; Provisional

26-505

1.66e-17

peptide synthase; Provisional

Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 89.19 E-value: 1.66e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   26 HHLfEDQAAKRPDAIALIDGE----------QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILK 95
Cdd:PRK09274    10 RHL-PRAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFK 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   96 AGCAYVPLDvgyPGdrieyMLRDSDARILltsTDVAKKLALTIPALQecqtvyLDQEIFEYDF----HFLAIAKllhnqy 171
Cdd:PRK09274    89 AGAVPVLVD---PG-----MGIKNLKQCL---AEAQPDAFIGIPKAH------LARRLFGWGKpsvrRLVTVGG------ 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  172 lRLLHF-YFYTLIQQCQATSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRtlqfc 250
Cdd:PRK09274   146 -RLLWGgTTLATLLRDGAAAPFPMADLA--PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEI----- 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  251 avsfDFSCHEIFS--TLCLGGILVlVPEA-----VRQNPFALAEFISQQKIEKLFL-PviALLQ-LAEAVNGNKSTSLAL 321
Cdd:PRK09274   218 ----DLPTFPLFAlfGPALGMTSV-IPDMdptrpATVDPAKLFAAIERYGVTNLFGsP--ALLErLGRYGEANGIKLPSL 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  322 CEVITTGEqmQITPAVANLFQKT---GAMLHNHYGATE------------FQDATTHTLKGnpEGwptlVPVGRPLHNVQ 386
Cdd:PRK09274   291 RRVISAGA--PVPIAVIERFRAMlppDAEILTPYGATEalpissiesreiLFATRAATDNG--AG----ICVGRPVDGVE 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  387 VYILD---------EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPfganeNAKKLYRTGDLARYLPDGTIE 457
Cdd:PRK09274   363 VRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDG-----QGDVWHRMGDLGYLDAQGRLW 437

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1331970929  458 HLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLV 505
Cdd:PRK09274   438 FCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPGAQRPV 485

PRK08279

long-chain-acyl-CoA synthetase; Validated

29-233

2.16e-17

long-chain-acyl-CoA synthetase; Validated

Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 88.78 E-value: 2.16e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   29 FEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYP 108
Cdd:PRK08279    43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  109 GDRIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYLDQEIFEYDFH-FLAIAKLLHNqylrllhfyfytliqQCQ 187
Cdd:PRK08279   123 GAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEgYEDLAAAAAG---------------APT 187

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1331970929  188 ATSVSQGiqtQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWW 233
Cdd:PRK08279   188 TNPASRS---GVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGG 230

AcpA

COG3433

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...

369-656

2.16e-17

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 85.57 E-value: 2.16e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  369 PEGWPTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEfcIGGIGLARGYHNLPDLTNEKFIPNPFGANENAKKLYRTGDLA 448
Cdd:COG3433     11 PTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGE--GGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  449 RYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFdklepILRQY 528
Cdd:COG3433     89 LRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAA-----AAALA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  529 SEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPDPKGDRPALSTPLVKPRT---QTEKRLAEIWGSYLAVDI--VGTHD 603
Cdd:COG3433    164 ALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALetaLTEEELRADVAELLGVDPeeIDPDD 243

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929  604 NFFDLGGTSLLLTQahkfLCETFN---INLSAVSLFQYPTIQTLAQYIDCQGDTTS 656
Cdd:COG3433    244 NLFDLGLDSIRLMQ----LVERWRkagLDVSFADLAEHPTLAAWWALLAAAQAAAA 295

PRK09088

acyl-CoA synthetase; Validated

32-563

1.32e-16

acyl-CoA synthetase; Validated

Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 85.63 E-value: 1.32e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   32 QAAKRPDAIALID--GEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPG 109
Cdd:PRK09088     4 HARLQPQRLAAVDlaLGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  110 DRIEYMLRDSDARILLTSTDVAkklALTipalqeCQTVYLDQEIFEYDFHFLAIAKLLHnqylrllhfyfytliqqcqat 189
Cdd:PRK09088    84 SELDALLQDAEPRLLLGDDAVA---AGR------TDVEDLAAFIASADALEPADTPSIP--------------------- 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  190 svsqgiqtqvlPNNLAYCIYTSGSTGNPKGILMEHRSL----VNMLWWHQQTRPSVQGVRTLQFCAVSFDFScheIFSTL 265
Cdd:PRK09088   134 -----------PERVSLILFTSGTSGQPKGVMLSERNLqqtaHNFGVLGRVDAHSSFLCDAPMFHIIGLITS---VRPVL 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  266 CLGGILVLVP--EAVRqnpfALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLA-LCEVITTGEQMQITPAVANLFQ 342
Cdd:PRK09088   200 AVGGSILVSNgfEPKR----TLGRLGDPALGITHYFCVPQMAQAFRAQPGFDAAALRhLTALFTGGAPHAAEDILGWLDD 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  343 ktGAMLHNHYGATE----FQDATTHTLKGNPEGwptlvPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHN 418
Cdd:PRK09088   276 --GIPMVDGFGMSEagtvFGMSVDCDVIRAKAG-----AAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWR 348

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  419 LPDLTNEKFipnpfganeNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREI 498
Cdd:PRK09088   349 RPQATARAF---------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMAD 419

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331970929  499 AGHTQlVGYIIAKDTLNLSFDkLEPIlRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:PRK09088   420 AQWGE-VGYLAIVPADGAPLD-LERI-RSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481

PLN02574

4-coumarate--CoA ligase-like

23-563

1.38e-16

4-coumarate--CoA ligase-like

Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 86.05 E-value: 1.38e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   23 SCIHHLFedQAAKRPDAIALIDGEQ--SLTYGELNVRANHLAQHLL-SLGCQPDDLLAICIERSAELFIGLLGILKAGCA 99
Cdd:PLN02574    41 DAVSFIF--SHHNHNGDTALIDSSTgfSISYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGI 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  100 YVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKL-ALTIPALQECQTVYLDQEIFEYDfhflaiakllhnqylrllhfY 178
Cdd:PLN02574   119 VTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLsPLGVPVIGVPENYDFDSKRIEFP--------------------K 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  179 FYTLIQQ----CQATSVSQgiqtqvlpNNLAYCIYTSGSTGNPKGILMEHRSLVNMlwwhqqtrpsvqgVRT-LQFCAVS 253
Cdd:PLN02574   179 FYELIKEdfdfVPKPVIKQ--------DDVAAIMYSSGTTGASKGVVLTHRNLIAM-------------VELfVRFEASQ 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  254 FDFS------------CHEIFSTLCLGGILVLVPEAVRQNPFALAEFIsqQKIEKL---FLPVI-----ALLQLAEAVNG 313
Cdd:PLN02574   238 YEYPgsdnvylaalpmFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMV--KVIDRFkvtHFPVVppilmALTKKAKGVCG 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  314 NKSTSLAlcevittgeqmQITPAVANLFQKT-----GAMLH----NHYGATEFQDATTHTLkgNPEGWPTLVPVGRPLHN 384
Cdd:PLN02574   316 EVLKSLK-----------QVSCGAAPLSGKFiqdfvQTLPHvdfiQGYGMTESTAVGTRGF--NTEKLSKYSSVGLLAPN 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  385 VQVYILD-EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRID 463
Cdd:PLN02574   383 MQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW---------LRTGDIAYFDEDGYLYIVDRLK 453

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  464 HQVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAGHTQlVGYIIAKDTLNLSfdkLEPILRQYSEAVLPeYMIPTR 541
Cdd:PLN02574   454 EIIKYKGFQIAPADLEAVLISHPEIIDAAVtaVPDKECGEIP-VAFVVRRQGSTLS---QEAVINYVAKQVAP-YKKVRK 528

                          570       580
                   ....*....|....*....|..
gi 1331970929  542 FINISNMPLTPSGKLDRRALPD 563
Cdd:PLN02574   529 VVFVQSIPKSPAGKILRRELKR 550

MACS_like_1

cd05974

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...

209-561

1.97e-16

Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 84.93 E-value: 1.97e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  209 YTSGSTGNPKGILMEHRS-----LVNMLWWHQQTRPSVQGVRTLQFCAVSFdfSCheIFSTLCLGGILVLVPEAvRQNPF 283
Cdd:cd05974     92 FTSGTTSKPKLVEHTHRSypvghLSTMYWIGLKPGDVHWNISSPGWAKHAW--SC--FFAPWNAGATVFLFNYA-RFDAK 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  284 ALAEFISQQKIEKLFLPVIALLQLAEAvnGNKSTSLALCEVITTGEQMQitPAVANLFQKT-GAMLHNHYGATEfqdatT 362
Cdd:cd05974    167 RVLAALVRYGVTTLCAPPTVWRMLIQQ--DLASFDVKLREVVGAGEPLN--PEVIEQVRRAwGLTIRDGYGQTE-----T 237

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  363 HTLKGNPEGWPTLV-PVGRPLHNVQVYILDEAQQPVplgGEGEFCIG-----GIGLARGYHNLPDLTNekfipnpfGANE 436
Cdd:cd05974    238 TALVGNSPGQPVKAgSMGRPLPGYRVALLDPDGAPA---TEGEVALDlgdtrPVGLMKGYAGDPDKTA--------HAMR 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  437 NAkkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAreiaghtqlvgyiiAKDTLNL 516
Cdd:cd05974    307 GG--YYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVP--------------SPDPVRL 370

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929  517 SFDKLEPILRQYSEAV----------LPEYMIP---TRFINISNMPLTPSGKLDRRAL 561
Cdd:cd05974    371 SVPKAFIVLRAGYEPSpetaleifrfSRERLAPykrIRRLEFAELPKTISGKIRRVEL 428

PRK14691

3-oxoacyl-(acyl carrier protein) synthase II; Provisional

832-1108

2.52e-16

3-oxoacyl-(acyl carrier protein) synthase II; Provisional

Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 83.24 E-value: 2.52e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  832 ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVP--QKGGYLYEEGMV----RSQDGHCRA 905
Cdd:PRK14691    71 AGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDtvSLAGFAAARALSthfnSTPEKASRP 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  906 FDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDgALKMGYTAPSVDGQADVISEAIAIADIDASTIGYV 985
Cdd:PRK14691   151 FDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSAD-AYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHL 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  986 EAHGTATQLGDPIEVAGLARAFQRStdsvlgkQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPNPR 1065
Cdd:PRK14691   230 NAHATSTPVGDLGEINAIKHLFGES-------NALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPA 302

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1331970929 1066 ------IDFDATPFFVNTELrewsRNGyprragvssFGVGGTNSHIVLE 1108
Cdd:PRK14691   303 akglniIAGNAQPHDMTYAL----SNG---------FGFAGVNASILLK 338

FACL_like_5

cd05924

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

206-559

1.01e-15

Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 81.66 E-value: 1.01e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  206 YCIYTSGSTGNPKGILMEHRSLVNML--------------WWHQQTRPSVQGVRTLQFCAVSFDFSCHEIFSTLCLGGIL 271
Cdd:cd05924      7 YILYTGGTTGMPKGVMWRQEDIFRMLmggadfgtgeftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  272 VLVpeAVRQNPFALAEFISQQKIEKLFLPVIALLQ-LAEAVNGNKSTSL-ALCEVITTGEQMqiTPAVANLFQ--KTGAM 347
Cdd:cd05924     87 VLP--DDRFDPEEVWRTIEKHKVTSMTIVGDAMARpLIDALRDAGPYDLsSLFAISSGGALL--SPEVKQGLLelVPNIT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  348 LHNHYGATEFQDATTHTLKGNPEGWPTLVPVGrplHNVQVyiLDEAQQPVPLGGEGEFCIGGIGL-ARGYHNLPDLTNEK 426
Cdd:cd05924    163 LVDAFGSSETGFTGSGHSAGSGPETGPFTRAN---PDTVV--LDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAET 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  427 FIpnpfgaNENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVG 506
Cdd:cd05924    238 FP------EVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1331970929  507 YIIAKDT-LNLSFDKLEPILRQyseaVLPEYMIPTRFINISNMPLTPSGKLDRR 559
Cdd:cd05924    312 AVVQLREgAGVDLEELREHCRT----RIARYKLPKQVVFVDEIERSPAGKADYR 361

PRK13383

acyl-CoA synthetase; Provisional

33-562

3.11e-15

acyl-CoA synthetase; Provisional

Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 81.58 E-value: 3.11e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   33 AAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRI 112
Cdd:PRK13383    45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  113 EYMLRDSDARILLTSTDVAKKLALTIPALqecqtvyldqeifeydfhflaiakllhnqylrllhfyfyTLIQQCQATSVS 192
Cdd:PRK13383   125 AAALRAHHISTVVADNEFAERIAGADDAV---------------------------------------AVIDPATAGAEE 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  193 QGIQTQVLPNNlAYCIYTSGSTGNPKGILMEHRSLVNMLWW---HQQTR---PSVQGVRTLQFCAVSFDFscheIFSTLC 266
Cdd:PRK13383   166 SGGRPAVAAPG-RIVLLTSGTTGKPKGVPRAPQLRSAVGVWvtiLDRTRlrtGSRISVAMPMFHGLGLGM----LMLTIA 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  267 LGGILVLVPEAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSlALCEVITTGEQMQitPAVANLFQKT-G 345
Cdd:PRK13383   241 LGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLP-QLRVVMSSGDRLD--PTLGQRFMDTyG 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  346 AMLHNHYGATEF---QDATTHTLKGNPEgwptlvPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNlpdl 422
Cdd:PRK13383   318 DILYNGYGSTEVgigALATPADLRDAPE------TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD---- 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  423 tnekfipnpFGANENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAG 500
Cdd:PRK13383   388 ---------GGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVigVPDERFG 458

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331970929  501 HtQLVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPtRFINI-SNMPLTPSGKLDRRALP 562
Cdd:PRK13383   459 H-RLAAFVVLHPGSGVDAAQ----LRDYLKDRVSRFEQP-RDINIvSSIPRNPTGKVLRKELP 515

FabG

COG1028

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...

2536-2677

3.40e-15

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 440651 [Multi-domain] Cd Length: 249 Bit Score: 77.90 E-value: 3.40e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGAKyLVLVGRRGAREEQQAQlsELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:COG1028     22 IARALAAEGAR-VVITDRDAEALEAAAA--ELRAAGGRALAVAADVTDEAAVEALVAAAvaAFGRLDILVNNAGITPPGP 98

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2614 LQQQSWQAFKEVMNPKVAGAWNL------HILTKNQPLdfFVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:COG1028     99 LEELTEEDWDRVLDVNLKGPFLLtraalpHMRERGGGR--IVNISSIAGLRGSPGQAAYAASKAAVVGLT 166

PRK08315

AMP-binding domain protein; Validated

16-555

5.13e-15

AMP-binding domain protein; Validated

Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 81.01 E-value: 5.13e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   16 TQSEFPDSCIHHLFEDQAAKRPDAIALIDGEQSL--TYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGI 93
Cdd:PRK08315     9 TDVPLLEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFAT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   94 LKAGCAYVPLDVGYPGDRIEYMLRDSDARILLT-----STDVAKKLALTIPALQECQ--------------TVYLDQEIF 154
Cdd:PRK08315    89 AKIGAILVTINPAYRLSELEYALNQSGCKALIAadgfkDSDYVAMLYELAPELATCEpgqlqsarlpelrrVIFLGDEKH 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  155 EYDFHFLAIAKLLHNQYLRLLhfyfytliQQCQAT-SVSQGIQTQvlpnnlayciYTSGSTGNPKGILMEHRSLVNMLWW 233
Cdd:PRK08315   169 PGMLNFDELLALGRAVDDAEL--------AARQATlDPDDPINIQ----------YTSGTTGFPKGATLTHRNILNNGYF 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  234 hqqtrpsvqgV-RTLQF-------CAVSFdFSCheiF----STL-CL--GGILVLVPEAVrqNPFALAEFISQQKIEKLF 298
Cdd:PRK08315   231 ----------IgEAMKLteedrlcIPVPL-YHC---FgmvlGNLaCVthGATMVYPGEGF--DPLATLAAVEEERCTALY 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  299 -LPV--IALLQLAEAVNGNKStSL-------ALC------EVIttgEQM---QITPAvanlfqktgamlhnhYGATE--- 356
Cdd:PRK08315   295 gVPTmfIAELDHPDFARFDLS-SLrtgimagSPCpievmkRVI---DKMhmsEVTIA---------------YGMTEtsp 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  357 --FQDATTHTLKGNPEgwpTlvpVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFg 433
Cdd:PRK08315   356 vsTQTRTDDPLEKRVT---T---VGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW- 428

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  434 anenakklYRTGDLARYLPDGTIEHLGRIDHQVkIRGfrvelG------EIESVLASHQAVRECAV--VAREIAGHtQLV 505
Cdd:PRK08315   429 --------MHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEFLYTHPKIQDVQVvgVPDEKYGE-EVC 493

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|
gi 1331970929  506 GYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPLTPSGK 555
Cdd:PRK08315   494 AWIILRPGATLTEED----VRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539

PRK07967

beta-ketoacyl-ACP synthase I;

904-1107

8.34e-15

beta-ketoacyl-ACP synthase I;

Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 79.33 E-value: 8.34e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  904 RAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAlKMgyTAPSvdGQADVISEAIAIADIDAStIG 983
Cdd:PRK07967   219 RAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGY-DM--VAPS--GEGAVRCMQMALATVDTP-ID 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  984 YVEAHGTATQLGDPIEVAGLARAFqrstdsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLHYANPN 1063
Cdd:PRK07967   293 YINTHGTSTPVGDVKELGAIREVF--------GDKSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELD 364

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1331970929 1064 PriDFDATPFfvnteLREWSRNGYPRRAGVSSFGVGGTNSHIVL 1107
Cdd:PRK07967   365 P--QAAGMPI-----VTETTDNAELTTVMSNSFGFGGTNATLVF 401

PRK09116

beta-ketoacyl-ACP synthase;

832-1065

1.31e-14

beta-ketoacyl-ACP synthase;

Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 78.88 E-value: 1.31e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  832 ATRISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMALAGGISVVVPQkggylyeEGMV---------RSQDGH 902
Cdd:PRK09116   144 AVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPT-------EAAVfdtlfatstRNDAPE 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  903 C--RAFDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGAlkmGYTAPSVDGQADVISEAIAIADIDAS 980
Cdd:PRK09116   217 LtpRPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGA---HVTQPQAETMQIAMELALKDAGLAPE 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  981 TIGYVEAHGTATQLGDPIEvaglarafQRSTDSVLGKQQcAIGSVKTNIGHldeAAGIAGLIKAALALQY---GQIPPSL 1057
Cdd:PRK09116   294 DIGYVNAHGTATDRGDIAE--------SQATAAVFGARM-PISSLKSYFGH---TLGACGALEAWMSIEMmneGWFAPTL 361


                   ....*...
gi 1331970929 1058 HYANPNPR 1065
Cdd:PRK09116   362 NLTQVDPA 369

SmtA

COG0500

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...

2094-2215

2.26e-14

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];

Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 74.18 E-value: 2.26e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2094 QEALLSALEQLPPERgwRILEIGAGTGGTTAYLLPHLPGdqtKYVFTDISAFFLAKAEERFKDYPF--VRYQVLDIEQAP 2171
Cdd:COG0500     14 LAALLALLERLPKGG--RVLDLGCGTGRNLLALAARFGG---RVIGIDLSPEAIALARARAAKAGLgnVEFLVADLAELD 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1331970929 2172 QaqgFEPQIYDLIVAADVLHATS--DLRQTLVHIRQLLAPGGMLIL 2215
Cdd:COG0500     89 P---LPAESFDLVVAFGVLHHLPpeEREALLRELARALKPGGVLLL 131

FACL_like_1

cd05910

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

205-531

2.29e-14

Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 78.66 E-value: 2.29e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  205 AYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRtlqfcavsfDFSCHEIFSTL-CLGGILVLVPE-----AV 278
Cdd:cd05910     88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV---------DLATFPLFALFgPALGLTSVIPDmdptrPA 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  279 RQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGeqmqiTPAVANLFQKTGAMLH------NHY 352
Cdd:cd05910    159 RADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAG-----APVPIALAARLRKMLSdeaeilTPY 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  353 GATEFQD----------ATTHTLKGNPEGwptlVPVGRPLHNVQVYILDEAQQP---------VPLGGEGEFCIGGIGLA 413
Cdd:cd05910    234 GATEALPvssigsrellATTTAATSGGAG----TCVGRPIPGVRVRIIEIDDEPiaewddtleLPRGEIGEITVTGPTVT 309

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  414 RGYHNLPDLTNEKFIPNPFGanenaKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV 493
Cdd:cd05910    310 PTYVNRPVATALAKIDDNSE-----GFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAL 384

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1331970929  494 VAREIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYSEA 531
Cdd:cd05910    385 VGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALAKD 422

MACS_euk

cd05928

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...

31-563

4.30e-14

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.

Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 77.89 E-value: 4.30e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   31 DQAAKRPDAIAL--IDG---EQSLTYGELNVRANHLAqHLLSLGC--QPDDLLAICIERSAELFIGLLGILKAGCAYVPL 103
Cdd:cd05928     19 EKAGKRPPNPALwwVNGkgdEVKWSFRELGSLSRKAA-NVLSGACglQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPG 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  104 DVGYPGDRIEYMLRDSDARILLTSTDVAKKL---ALTIPALQecqtvyldqeifeydfhflaiAKLLHNQYLRLLHFYFY 180
Cdd:cd05928     98 TIQLTAKDILYRLQASKAKCIVTSDELAPEVdsvASECPSLK---------------------TKLLVSEKSRDGWLNFK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  181 TLIQQcqATSVSQGIQTQVLPNNLAYciYTSGSTGNPKGILMEHRSL-----VNMLWWHQQTRPSVQGVRTLQFCAVSFD 255
Cdd:cd05928    157 ELLNE--ASTEHHCVETGSQEPMAIY--FTSGTTGSPKMAEHSHSSLglglkVNGRYWLDLTASDIMWNTSDTGWIKSAW 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  256 FScheIFSTLCLGGIlVLVPEAVRQNPFALAEFISQQKIEKLF-LPVIALLQLAEAVNGNKSTSLALCevITTGEQmqIT 334
Cdd:cd05928    233 SS---LFEPWIQGAC-VFVHHLPRFDPLVILKTLSSYPITTFCgAPTVYRMLVQQDLSSYKFPSLQHC--VTGGEP--LN 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  335 PAVANLFQ-KTGAMLHNHYGATEfqdatTHTLKGNPEGW---PTLVPVGRPLHNVQvyILDEAQQPVPLGGEGEFCI--- 407
Cdd:cd05928    305 PEVLEKWKaQTGLDIYEGYGQTE-----TGLICANFKGMkikPGSMGKASPPYDVQ--IIDDNGNVLPPGTEGDIGIrvk 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  408 --GGIGLARGYHNLPDLTNEKFIPNpfganenakkLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASH 485
Cdd:cd05928    378 piRPFGLFSGYVDNPEKTAATIRGD----------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEH 447

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  486 QAVRECAVVAR--EIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:cd05928    448 PAVVESAVVSSpdPIRGEVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527

PRK07514

malonyl-CoA synthase; Validated

26-494

5.35e-14

malonyl-CoA synthase; Validated

Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 77.61 E-value: 5.35e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   26 HHLFE--DQAAKRPDAIAL-IDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVP 102
Cdd:PRK07514     3 NNLFDalRAAFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  103 LDVGYPGDRIEYMLRDSDARILLTST---DVAKKLALTIPAlqecQTVY-LDQEifeydfhflAIAKLLHnqylrllhfy 178
Cdd:PRK07514    83 LNTAYTLAELDYFIGDAEPALVVCDPanfAWLSKIAAAAGA----PHVEtLDAD---------GTGSLLE---------- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  179 fytliqqcQATSVSQGIQT-QVLPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSVQGV--RTLQFcavsf 254
Cdd:PRK07514   140 --------AAAAAPDDFETvPRGADDLAAILYTSGTTGRSKGAMLSHGNLLsNALTLVDYWRFTPDDVliHALPI----- 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  255 dFSCHEIF----STLCLGGILVLVPEavrqnpFALAEFISQQKIEKLFLPV----IALLQLA----EAVNGNK---STSL 319
Cdd:PRK07514   207 -FHTHGLFvatnVALLAGASMIFLPK------FDPDAVLALMPRATVMMGVptfyTRLLQEPrltrEAAAHMRlfiSGSA 279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  320 ALceVITTGEQMQitpavanlfQKTGAMLHNHYGATEfqdatTHTLKGNP-EGwpTLVP--VGRPLHNVQVYILD-EAQQ 395
Cdd:PRK07514   280 PL--LAETHREFQ---------ERTGHAILERYGMTE-----TNMNTSNPyDG--ERRAgtVGFPLPGVSLRVTDpETGA 341

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  396 PVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVEL 475
Cdd:PRK07514   342 ELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF---------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYP 412

                          490
                   ....*....|....*....
gi 1331970929  476 GEIESVLASHQAVRECAVV 494
Cdd:PRK07514   413 KEVEGEIDELPGVVESAVI 431

PRK08633

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated

201-561

1.02e-13

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated

Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 77.66 E-value: 1.02e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  201 PNNLAYCIYTSGSTGNPKGILMEHRslvNMLWWHQQTRPSVQGVRTLQFCAV-----SFDFSChEIFSTLCLGGILVLVP 275
Cdd:PRK08633   781 PDDTATIIFSSGSEGEPKGVMLSHH---NILSNIEQISDVFNLRNDDVILSSlpffhSFGLTV-TLWLPLLEGIKVVYHP 856

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  276 eavrqNP---FALAEFISQQKIEKLF-----------LPVIALLQLAeavngnkstSLALceVITTGEQMqiTPAVANLF 341
Cdd:PRK08633   857 -----DPtdaLGIAKLVAKHRATILLgtptflrlylrNKKLHPLMFA---------SLRL--VVAGAEKL--KPEVADAF 918

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  342 Q-KTGAMLHNHYGATE-----------FQDATTHTLKGNPEGwptlvPVGRPLHNVQVYILD-EAQQPVPLGGEGEFCIG 408
Cdd:PRK08633   919 EeKFGIRILEGYGATEtspvasvnlpdVLAADFKRQTGSKEG-----SVGMPLPGVAVRIVDpETFEELPPGEDGLILIG 993

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  409 GIGLARGYHNLPDLTNEKFipnpfgANENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLA--SHQ 486
Cdd:PRK08633   994 GPQVMKGYLGDPEKTAEVI------KDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAkaLGG 1067

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  487 AVRECAVVA--------REIAGHTQLvgyiiAKDTlnlsfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:PRK08633  1068 EEVVFAVTAvpdekkgeKLVVLHTCG-----AEDV--------EELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDL 1134


                   ...
gi 1331970929  559 RAL 561
Cdd:PRK08633  1135 KGL 1137

PRK12582

acyl-CoA synthetase; Provisional

25-495

1.09e-13

acyl-CoA synthetase; Provisional

Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 77.01 E-value: 1.09e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   25 IHHLFEDQAAKRPDAIALIDGEQ------SLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGC 98
Cdd:PRK12582    51 IPHLLAKWAAEAPDRPWLAQREPghgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGV 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   99 AYVPLDVGY---PGD--RIEYMLRDSDARILLTSTDVAKKLALTIPALQECQTVYLDQEIfeYDFHFLAIAKLLhnqylr 173
Cdd:PRK12582   131 PAAPVSPAYslmSHDhaKLKHLFDLVKPRVVFAQSGAPFARALAALDLLDVTVVHVTGPG--EGIASIAFADLA------ 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  174 llhfyfytliqqcqATSVSQGIQ---TQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTlqfc 250
Cdd:PRK12582   203 --------------ATPPTAAVAaaiAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPP---- 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  251 AVSFDF-SCHEIFS-------TLCLGGILVL-----VPEAVRQNPFALAEfISqqkieklflPV------IALLQLAEAV 311
Cdd:PRK12582   265 PVSLDWmPWNHTMGgnanfngLLWGGGTLYIddgkpLPGMFEETIRNLRE-IS---------PTvygnvpAGYAMLAEAM 334

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  312 NGNKstslALCE----------------------------VITTGEQMQITpavanlfqkTGamlhnhYGATEFQDATTH 363
Cdd:PRK12582   335 EKDD----ALRRsffknlrlmayggatlsddlyermqalaVRTTGHRIPFY---------TG------YGATETAPTTTG 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  364 TlkgnpeGWPTLVP--VGRPLHNVQVYIldeaqqpVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakkl 441
Cdd:PRK12582   396 T------HWDTERVglIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF--------- 453

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  442 YRTGDLARYL-PDGTIEHL---GRIDHQVKI-RGFRVELGEIE-SVLASHQAVRECAVVA 495
Cdd:PRK12582   454 YRLGDAARFVdPDDPEKGLifdGRVAEDFKLsTGTWVSVGTLRpDAVAACSPVIHDAVVA 513

BioC

TIGR02072

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...

2097-2215

1.81e-13

Pssm-ID: 273953 [Multi-domain] Cd Length: 240 Bit Score: 72.70 E-value: 1.81e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2097 LLSALEQLPPERGWRILEIGAGTGGTTAYLLPHLPgdQTKYVFTDISAFFLAKAEERFKdyPFVRYQVLDIEQAPqaqgF 2176
Cdd:TIGR02072   23 LLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFP--QAEFIALDISAGMLAQAKTKLS--ENVQFICGDAEKLP----L 94

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1331970929 2177 EPQIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:TIGR02072   95 EDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAF 133

PRK07824

o-succinylbenzoate--CoA ligase;

379-561

1.82e-13

o-succinylbenzoate--CoA ligase;

Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 74.70 E-value: 1.82e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  379 GRPLHNVQVYILDeaqqpvplggeGEFCIGGIGLARGYHNLPDltnekfiPNPFgANENakkLYRTGDLARyLPDGTIEH 458
Cdd:PRK07824   195 GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPF-AEPG---WFRTDDLGA-LDDGVLTV 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  459 LGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAGH---TQLVGYIIAKDTLNlsfdklepILRQYSEAVL 533
Cdd:PRK07824   252 LGRADDAISTGGLTVLPQVVEAALATHPAVADCAVfgLPDDRLGQrvvAAVVGDGGPAPTLE--------ALRAHVARTL 323

                          170       180
                   ....*....|....*....|....*...
gi 1331970929  534 PEYMIPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PRK07824   324 DRTAAPRELHVVDELPRRGIGKVDRRAL 351

AcpP

COG0236

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...

2805-2881

2.07e-13

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 67.57 E-value: 2.07e-13

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929 2805 TLLQAHVREQVSQVLGIDTKTLLAEQDvgFFT-LGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQALVNYLANEL 2881
Cdd:COG0236      4 EELEERLAEIIAEVLGVDPEEITPDDS--FFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79

PRK13382

bile acid CoA ligase;

28-564

4.91e-13

bile acid CoA ligase;

Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 74.79 E-value: 4.91e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAKRPDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAIcIERSAELFIGLLgilkagCAYvpldvgy 107
Cdd:PRK13382    48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGI-MCRNHRGFVEAL------LAA------- 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  108 pgDRIeymlrdsDARILLTSTDVAKKLALTIPALQECQTVYLDQEifeydfhFLA-IAKLLHN--QYLRLLHF---YFYT 181
Cdd:PRK13382   114 --NRI-------GADILLLNTSFAGPALAEVVTREGVDTVIYDEE-------FSAtVDRALADcpQATRIVAWtdeDHDL 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  182 LIQQCQATSVSQGIQTQvlPNNLAYCIYTSGSTGNPKGI-------LMEHRSLVNMLWWHQQtRPSV--------QGVRT 246
Cdd:PRK13382   178 TVEVLIAAHAGQRPEPT--GRKGRVILLTSGTTGTPKGArrsgpggIGTLKAILDRTPWRAE-EPTVivapmfhaWGFSQ 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  247 LQFCAVsfdFSCHEI----FStlclggilvlvPEAV-----RQNPFALAefisqqkieklFLPVI--ALLQLAEAVNgNK 315
Cdd:PRK13382   255 LVLAAS---LACTIVtrrrFD-----------PEATldlidRHRATGLA-----------VVPVMfdRIMDLPAEVR-NR 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  316 STSLALCEVITTGEQMQitPAVANLFQ-KTGAMLHNHYGATEFQDATTHT---LKGNPEgwptlvPVGRPLHNVQVYILD 391
Cdd:PRK13382   309 YSGRSLRFAAASGSRMR--PDVVIAFMdQFGDVIYNNYNATEAGMIATATpadLRAAPD------TAGRPAEGTEIRILD 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  392 EAQQPVPLGGEGEFCIGGIGLARGYhnlpdltnekfipNPFGANENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGF 471
Cdd:PRK13382   381 QDFREVPTGEVGTIFVRNDTQFDGY-------------TSGSTKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGE 447

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  472 RVELGEIESVLASHQAVRECAVVAREIAGHTQ-LVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYMIPTRFINISNMPL 550
Cdd:PRK13382   448 NVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQrLAAFVVLKPGASATPET----LKQHVRDNLANYKVPRDIVVLDELPR 523

                          570
                   ....*....|....
gi 1331970929  551 TPSGKLDRRALPDP 564
Cdd:PRK13382   524 GATGKILRRELQAR 537

ACLS-CaiC

cd17637

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...

205-494

5.79e-13

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.

Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 72.69 E-value: 5.79e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  205 AYCI-YTSGSTGNPKGILMEHRSLV--NMlwwhqqtrpsvQGVRTLQFCAVSFDFSCHEIF---------STLCLGGILV 272
Cdd:cd17637      2 PFVIiHTAAVAGRPRGAVLSHGNLIaaNL-----------QLIHAMGLTEADVYLNMLPLFhiaglnlalATFHAGGANV 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  273 LVPeavRQNPFALAEFISQQKIEKL--FLPVIALLQLAEAVNGNKSTSLalcEVITTGEqmqiTPAVANLFQK-TGAMLH 349
Cdd:cd17637     71 VME---KFDPAEALELIEEEKVTLMgsFPPILSNLLDAAEKSGVDLSSL---RHVLGLD----APETIQRFEEtTGATFW 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  350 NHYGATEfqdatTHtlkgnpeGWPTLVP-------VGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDL 422
Cdd:cd17637    141 SLYGQTE-----TS-------GLVTLSPyrerpgsAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPEL 208

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331970929  423 TNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQ--VKIRGFRVELGEIESVLASHQAVRECAVV 494
Cdd:cd17637    209 TAYTF----------RNGWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVI 272

PLN03102

acyl-activating enzyme; Provisional

37-563

1.25e-12

acyl-activating enzyme; Provisional

Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 73.51 E-value: 1.25e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYML 116
Cdd:PLN03102    28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  117 RDSDARILLTSTDVAkklaltiPALQECQTVYLDQE---------IFEYDFHFLAIAKLLHnqylrllhfyFYTLIQQCQ 187
Cdd:PLN03102   108 RHAKPKILFVDRSFE-------PLAREVLHLLSSEDsnlnlpvifIHEIDFPKRPSSEELD----------YECLIQRGE 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  188 ATSVSQG----IQTQVLPNNLAYciyTSGSTGNPKGILMEHR-----SLVNMLWWHQQTRPSVqgVRTLQFcavsfdFSC 258
Cdd:PLN03102   171 PTPSLVArmfrIQDEHDPISLNY---TSGTTADPKGVVISHRgaylsTLSAIIGWEMGTCPVY--LWTLPM------FHC 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  259 H---EIFSTLCLGGILVLV-----PEAVRQnpfalaefISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEQ 330
Cdd:PLN03102   240 NgwtFTWGTAARGGTSVCMrhvtaPEIYKN--------IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSP 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  331 mqiTPAV-ANLFQKTGAMLHNHYGATE---------FQDATTHTlkgnPEGWPTLVPVGRPLHNVQVYILD----EAQQP 396
Cdd:PLN03102   312 ---PPAAlVKKVQRLGFQVMHAYGLTEatgpvlfceWQDEWNRL----PENQQMELKARQGVSILGLADVDvknkETQES 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  397 VPLGGE--GEFCIGGIGLARGYHNLPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVE 474
Cdd:PLN03102   385 VPRDGKtmGEIVIKGSSIMKGYLKNPKATSEAF----------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENIS 454

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  475 LGEIESVLASHQAVRECAVVA--REIAGHTQLVGYIIAK--DTLNLSFDKL---EPILRQYSEAVLPEYMIPTRFINISN 547
Cdd:PLN03102   455 SVEVENVLYKYPKVLETAVVAmpHPTWGETPCAFVVLEKgeTTKEDRVDKLvtrERDLIEYCRENLPHFMCPRKVVFLQE 534

                          570
                   ....*....|....*.
gi 1331970929  548 MPLTPSGKLDRRALPD 563
Cdd:PLN03102   535 LPKNGNGKILKPKLRD 550

Methyltransf_11

pfam08241

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

2113-2215

1.60e-12

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.

Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 65.76 E-value: 1.60e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2113 LEIGAGTGGTTAYLLPHLPgdqtKYVFTDISAFFLAKAEERFKDYPfVRYQVLDIEQAPqaqgFEPQIYDLIVAADVLHA 2192
Cdd:pfam08241    1 LDVGCGTGLLTELLARLGA----RVTGVDISPEMLELAREKAPREG-LTFVVGDAEDLP----FPDNSFDLVLSSEVLHH 71

                           90       100
                   ....*....|....*....|...
gi 1331970929 2193 TSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:pfam08241   72 VEDPERALREIARVLKPGGILII 94

PRK05691

peptide synthase; Validated

19-645

1.68e-12

peptide synthase; Validated

Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.05 E-value: 1.68e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   19 EFPDSCIHHLfEDQAAKRPDAIALI----DGEQS--LTYGELNVRANHLAQHLLSLGcQPDDLLAICIERSAELFIGLLG 92
Cdd:PRK05691     6 ELPLTLVQAL-QRRAAQTPDRLALRfladDPGEGvvLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   93 ILKAGCAYVPldvGYPGdriEYMLRDSDARILLTSTDVAKKLALTIPALQECqtvyldqeifeydfhFLAIAKLLHNQYL 172
Cdd:PRK05691    84 CLYAGVIAVP---AYPP---ESARRHHQERLLSIIADAEPRLLLTVADLRDS---------------LLQMEELAAANAP 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  173 RLLhfyfytLIQQCQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWwhqqtrpsvqgvrtLQFCAV 252
Cdd:PRK05691   143 ELL------CVDTLDPALAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQ--------------LIRHGF 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  253 SFDFSCHE-IFSTLCL-------GGIL----------VLVPEAVRQNPFALAEFISQ-----------------QKIEKL 297
Cdd:PRK05691   203 GIDLNPDDvIVSWLPLyhdmgliGGLLqpifsgvpcvLMSPAYFLERPLRWLEAISEyggtisggpdfayrlcsERVSES 282

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  298 FLPVIALLQLAEAVNGnkSTSLALCEVITTGEQMQ---ITP---------AVANLFQkTGAMLHNHYGATEFQDATTHTL 365
Cdd:PRK05691   283 ALERLDLSRWRVAYSG--SEPIRQDSLERFAEKFAacgFDPdsffasyglAEATLFV-SGGRRGQGIPALELDAEALARN 359

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  366 KGNPEGWPTLVPVGRPLHNVQVYILDEAQQPV-PLGGEGEFCIGGIGLARGYHNLPDLTNEKFIpnpfgaNENAKKLYRT 444
Cdd:PRK05691   360 RAEPGTGSVLMSCGRSQPGHAVLIVDPQSLEVlGDNRVGEIWASGPSIAHGYWRNPEASAKTFV------EHDGRTWLRT 433

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  445 GDLArYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAV---------------RECAVVAREIAGHTQLVgyii 509
Cdd:PRK05691   434 GDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVvrkgrvaafavnhqgEEGIGIAAEISRSVQKI---- 508

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  510 akdtlnLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRA----LPDPKGDRPAL--STPLVKPRTQT- 582
Cdd:PRK05691   509 ------LPPQALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSAcrlrLADGSLDSYALfpALQAVEAAQTAa 582

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929  583 -----EKRLAEIWGSYLAVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQTLA 645
Cdd:PRK05691   583 sgdelQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFS 650

Methyltransf_31

pfam13847

Methyltransferase domain; This family appears to have methyltransferase activity.

2111-2227

1.94e-12

Methyltransferase domain; This family appears to have methyltransferase activity.

Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 67.44 E-value: 1.94e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2111 RILEIGAGTGgTTAYLLPHLPGDQTKYVFTDISAFFLAKAEERFKDYPF--VRYQVLDIEQAPQAqgFEPQIYDLIVAAD 2188
Cdd:pfam13847    6 RVLDLGCGTG-HLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFdnVEFEQGDIEELPEL--LEDDKFDVVISNC 82

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1331970929 2189 VLHATSDLRQTLVHIRQLLAPGGMLILmedSEPARWADL 2227
Cdd:pfam13847   83 VLNHIPDPDKVLQEILRVLKPGGRLII---SDPDSLAEL 118

Methyltransf_23

pfam13489

Methyltransferase domain; This family appears to be a methyltransferase domain.

2093-2264

2.55e-12

Methyltransferase domain; This family appears to be a methyltransferase domain.

Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 67.45 E-value: 2.55e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2093 VQEALLSALEQLPP--ERGWRILEIGAGTGgttaYLLPHLPGDQTKYVFTDISAfflakaEERFKDYPFVRYQVLDIEQA 2170
Cdd:pfam13489    5 RERLLADLLLRLLPklPSPGRVLDFGCGTG----IFLRLLRAQGFSVTGVDPSP------IAIERALLNVRFDQFDEQEA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2171 PQAQGfepqIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILMEDSEPARWADLtfgLTEGWWKFTDHDLrpnHPLL 2250
Cdd:pfam13489   75 AVPAG----KFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRL---LLEWPYLRPRNGH---ISLF 144

                          170
                   ....*....|....
gi 1331970929 2251 SPEQWQILLSEMGF 2264
Cdd:pfam13489  145 SARSLKRLLEEAGF 158

AMP-binding_C

pfam13193

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...

477-555

2.92e-12

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.

Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 64.10 E-value: 2.92e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  477 EIESVLASHQAVRECAVVAR--EIAGHTqLVGYIIAKDtlnlSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSG 554
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVpdELKGEA-PVAFVVLKP----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75


                   .
gi 1331970929  555 K 555
Cdd:pfam13193   76 K 76

BACL_like

cd05929

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...

208-563

2.94e-12

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.

Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 72.02 E-value: 2.94e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  208 IYTSGSTGNPKGILMEH----------RSLVNMLWWHQqtrpsvqGVRTLQ----FCAVSFDFScheiFSTLCLGGILVL 273
Cdd:cd05929    131 LYSGGTTGRPKGIKRGLpggppdndtlMAAALGFGPGA-------DSVYLSpaplYHAAPFRWS----MTALFMGGTLVL 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  274 VPeavRQNPFALAEFISQQKIEKL-FLPVI--ALLQLAEAVNGNKSTSlALCEVITTGEQMqiTPAV-ANLFQKTGAMLH 349
Cdd:cd05929    200 ME---KFDPEEFLRLIERYRVTFAqFVPTMfvRLLKLPEAVRNAYDLS-SLKRVIHAAAPC--PPWVkEQWIDWGGPIIW 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  350 NHYGATEFQDAT--------THtlKGNpegwptlvpVGRPLHNVqVYILDEAQQPVPLGGEGEFCIGGiGLARGYHNLPD 421
Cdd:cd05929    274 EYYGGTEGQGLTiingeewlTH--PGS---------VGRAVLGK-VHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPE 340

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  422 LTNEKFipnpfganeNAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGH 501
Cdd:cd05929    341 KTAAAR---------NEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEEL 411

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331970929  502 TQLVGYIIAKDTLNLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALPD 563
Cdd:cd05929    412 GQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473

PLN02479

acetate-CoA ligase

209-561

8.58e-12

acetate-CoA ligase

Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 70.64 E-value: 8.58e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  209 YTSGSTGNPKGILMEHR-----SLVNMLWWHQQtrpsvQGVRTLQFCAVsfdFSCHE-----IFSTLCLGGIlvlvpeAV 278
Cdd:PLN02479   202 YTSGTTASPKGVVLHHRgaylmALSNALIWGMN-----EGAVYLWTLPM---FHCNGwcftwTLAALCGTNI------CL 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  279 RQ-NPFALAEFISQQKIEKLF-LPVIallqLAEAVNGNKS-TSLAL---CEVITTGEQMqiTPAVANLFQKTGAMLHNHY 352
Cdd:PLN02479   268 RQvTAKAIYSAIANYGVTHFCaAPVV----LNTIVNAPKSeTILPLprvVHVMTAGAAP--PPSVLFAMSEKGFRVTHTY 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  353 GATE-FQDATTHTLKgnPEgWPTLVPVGRP-LHNVQ--VYI----LD----EAQQPVPLGGE--GEFCIGGIGLARGYHN 418
Cdd:PLN02479   342 GLSEtYGPSTVCAWK--PE-WDSLPPEEQArLNARQgvRYIglegLDvvdtKTMKPVPADGKtmGEIVMRGNMVMKGYLK 418

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  419 LPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR-- 496
Cdd:PLN02479   419 NPKANEEAF----------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARpd 488

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929  497 EIAGHTQlVGYIIAKDTLNLSFD-KLEPILRQYSEAVLPEYMIPtRFINISNMPLTPSGKLDRRAL 561
Cdd:PLN02479   489 ERWGESP-CAFVTLKPGVDKSDEaALAEDIMKFCRERLPAYWVP-KSVVFGPLPKTATGKIQKHVL 552

PRK12476

putative fatty-acid--CoA ligase; Provisional

49-560

1.49e-11

putative fatty-acid--CoA ligase; Provisional

Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 70.16 E-value: 1.49e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   49 LTYGELNVRANHLAQHLLSLgCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDV-GYPG--DRIEYMLRDSDARILL 125
Cdd:PRK12476    69 LTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFApELPGhaERLDTALRDAEPTVVL 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  126 TSTDVAkklaltiPALQEcqtvyldqeifeydfhFLAiaKLLHNQYLRLLhfyfytLIQQCQATSVSQGIQTQVLPNNLA 205
Cdd:PRK12476   148 TTTAAA-------EAVEG----------------FLR--NLPRLRRPRVI------AIDAIPDSAGESFVPVELDTDDVS 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  206 YCIYTSGSTGNPKGILMEHRS----LVNMLWWHQQTRPSVQGVRTLqfcAVSFDFSCHEI-FSTLCLGGILVLVPEAVRQ 280
Cdd:PRK12476   197 HLQYTSGSTRPPVGVEITHRAvgtnLVQMILSIDLLDRNTHGVSWL---PLYHDMGLSMIgFPAVYGGHSTLMSPTAFVR 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  281 NPFalaEFISQQKIEKLFLPVIAL--------------------LQLAEAV--NGNKSTSLALCEVITTG------EQMQ 332
Cdd:PRK12476   274 RPQ---RWIKALSEGSRTGRVVTAapnfayewaaqrglpaegddIDLSNVVliIGSEPVSIDAVTTFNKAfapyglPRTA 350

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  333 ITP----AVANLFQKTGAMlHNHYGATEF---QDATTHTLKgNPEGWPTLVP---VGRPLHNVQVYILDE-AQQPVPLGG 401
Cdd:PRK12476   351 FKPsygiAEATLFVATIAP-DAEPSVVYLdreQLGAGRAVR-VAADAPNAVAhvsCGQVARSQWAVIVDPdTGAELPDGE 428

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  402 EGEFCIGGIGLARGYHNLPDLTNEKF-------IP---NPFGANENAKKLyRTGDLARYLpDGTIEHLGRIDHQVKIRGF 471
Cdd:PRK12476   429 VGEIWLHGDNIGRGYWGRPEETERTFgaklqsrLAegsHADGAADDGTWL-RTGDLGVYL-DGELYITGRIADLIVIDGR 506

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  472 RVELGEIE-SVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTLNLSFDKLEPILRQYSEAVLPEYMIPT---RFINISN 547
Cdd:PRK12476   507 NHYPQDIEaTVAEASPMVRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVadvRLVPAGA 586

                          570
                   ....*....|...
gi 1331970929  548 MPLTPSGKLDRRA 560
Cdd:PRK12476   587 IPRTTSGKLARRA 599

AcpP

COG0236

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...

578-649

1.68e-11

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 62.18 E-value: 1.68e-11

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331970929  578 PRTQTEKRLAEIWGSYLAVDI--VGTHDNFF-DLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQTLAQYID 649
Cdd:COG0236      2 PREELEERLAEIIAEVLGVDPeeITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLE 76

fabG

PRK12825

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

2540-2677

2.16e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

Pssm-ID: 237218 [Multi-domain] Cd Length: 249 Bit Score: 66.82 E-value: 2.16e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2540 LVTNGAK--------------YLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVI 2603
Cdd:PRK12825    10 LVTGAARglgraialrlaragADVVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAveRFGRIDILV 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2604 HAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNL-----HILTKNQpldF--FVLFSSATSLLGNAGQANHAAANAFLDGL 2676
Cdd:PRK12825    90 NNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLlravvPPMRKQR---GgrIVNISSVAGLPGWPGRSNYAAAKAGLVGL 166


                   .
gi 1331970929 2677 A 2677
Cdd:PRK12825   167 T 167

PRK05850

acyl-CoA synthetase; Validated

28-228

6.42e-11

acyl-CoA synthetase; Validated

Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 68.05 E-value: 6.42e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   28 LFEDQAAKRPDAIAL--IDGEQ-------SLTYGELNVRANHLAQHLLSLGcQPDDLLAICIERSAELFIGLLGILKAGC 98
Cdd:PRK05850     6 LLRERASLQPDDAAFtfIDYEQdpagvaeTLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   99 AYVPLDVGYPG---DRIEYMLRDSDARILLTS----TDVAKKLAL----TIPALQECQTVYLDQEifeydfhflaiakll 167
Cdd:PRK05850    85 IAVPLSVPQGGahdERVSAVLRDTSPSVVLTTsavvDDVTEYVAPqpgqSAPPVIEVDLLDLDSP--------------- 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331970929  168 hnqylrllhfyfytliQQCQATSVSqgiqtqvLPnNLAYCIYTSGSTGNPKGILMEHRSLV 228
Cdd:PRK05850   150 ----------------RGSDARPRD-------LP-STAYLQYTSGSTRTPAGVMVSHRNVI 186

Cfa

COG2230

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...

2094-2215

7.60e-11

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];

Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 63.02 E-value: 7.60e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2094 QEALLSA-LEQLPPERGWRILEIGAGTGGTTAYLLPHLpgdQTKYVFTDISAFFLAKAEERFKDYPF---VRYQVLDIEQ 2169
Cdd:COG2230     36 QEAKLDLiLRKLGLKPGMRVLDIGCGWGGLALYLARRY---GVRVTGVTLSPEQLEYARERAAEAGLadrVEVRLADYRD 112

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1331970929 2170 APQAQGFepqiyDLIVAADVLHA--TSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:COG2230    113 LPADGQF-----DAIVSIGMFEHvgPENYPAYFAKVARLLKPGGRLLL 155

SDR

cd02266

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...

2602-2722

1.73e-10

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187535 [Multi-domain] Cd Length: 186 Bit Score: 62.53 E-value: 1.73e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2602 VIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNLHILTKNQ----PLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:cd02266     35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELmkakRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2678 SYRRHL----GLPSLSINWGTWSEVGIAARLELD-KLSSKQGEGTITLGQ 2722
Cdd:cd02266    115 QQWASEgwgnGLPATAVACGTWAGSGMAKGPVAPeEILGNRRHGVRTMPP 164

fabG

PRK05557

3-ketoacyl-(acyl-carrier-protein) reductase; Validated

2536-2676

2.47e-10

3-ketoacyl-(acyl-carrier-protein) reductase; Validated

Pssm-ID: 235500 [Multi-domain] Cd Length: 248 Bit Score: 63.67 E-value: 2.47e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGAKylVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:PRK05557    21 IAERLAAQGAN--VVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAkaEFGGVDILVNNAGITRDNL 98

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929 2614 LQQQSWQAFKEVMNPKVAGAWNL-----HILTKnQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGL 2676
Cdd:PRK05557    99 LMRMKEEDWDRVIDTNLTGVFNLtkavaRPMMK-QRSGRIINISSVVGLMGNPGQANYAASKAGVIGF 165

PRK00174

acetyl-CoA synthetase; Provisional

379-561

2.89e-10

acetyl-CoA synthetase; Provisional

Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 65.93 E-value: 2.89e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  379 GRPLHNVQVYILDEAQQPVPLGGEGEFCIGGI--GLARGYHNLPdltnEKFIPNPFGAnenAKKLYRTGDLARYLPDGTI 456
Cdd:PRK00174   427 TRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFST---FKGMYFTGDGARRDEDGYY 499

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  457 EHLGRIDHQVKIRGFRveLG--EIESVLASHQAVRECAVVAR--EIAGHtQLVGYIIAKDTLNLSfDKLEPILRQY-SEA 531
Cdd:PRK00174   500 WITGRVDDVLNVSGHR--LGtaEIESALVAHPKVAEAAVVGRpdDIKGQ-GIYAFVTLKGGEEPS-DELRKELRNWvRKE 575

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1331970929  532 VLPeymIPT----RFinISNMPLTPSGKLDRRAL 561
Cdd:PRK00174   576 IGP---IAKpdviQF--APGLPKTRSGKIMRRIL 604

PLN02246

4-coumarate--CoA ligase

18-561

2.93e-10

4-coumarate--CoA ligase

Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 65.77 E-value: 2.93e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   18 SEFPDSCI-HHL------FEdQAAKRPDAIALIDGE--QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFI 88
Cdd:PLN02246    12 SKLPDIYIpNHLplhdycFE-RLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVL 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   89 GLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTSTDVAKKLAltipALQECQTVYldqeIFEYDFHFlaiAKLLH 168
Cdd:PLN02246    91 AFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLK----GLAEDDGVT----VVTIDDPP---EGCLH 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  169 nqylrllhfyFYTLIQQCQATSVSQGIQtqvlPNNLAYCIYTSGSTGNPKGILMEHRSLVNMLwwHQQtrpsVQG-VRTL 247
Cdd:PLN02246   160 ----------FSELTQADENELPEVEIS----PDDVVALPYSSGTTGLPKGVMLTHKGLVTSV--AQQ----VDGeNPNL 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  248 QF-------CAVS-FD-FSCHEIFstLC---LGGILVLVPEavrqnpF---ALAEFISQQKIE-KLFLPVIaLLQLAE-- 309
Cdd:PLN02246   220 YFhsddvilCVLPmFHiYSLNSVL--LCglrVGAAILIMPK------FeigALLELIQRHKVTiAPFVPPI-VLAIAKsp 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  310 AVNGNKSTSLALceVITTGEQM--QITPAVANLFqkTGAMLHNHYGATEFQDATTHTLKGNPEGWP-------TLVpvgr 380
Cdd:PLN02246   291 VVEKYDLSSIRM--VLSGAAPLgkELEDAFRAKL--PNAVLGQGYGMTEAGPVLAMCLAFAKEPFPvksgscgTVV---- 362

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  381 plHNVQVYILD-EAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTnEKFIpnpfganeNAKKLYRTGDLARYLPDGTIEHL 459
Cdd:PLN02246   363 --RNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEAT-ANTI--------DKDGWLHTGDIGYIDDDDELFIV 431

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  460 GRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR--EIAGHTQlVGYIIAKDTLNLSFDKlepiLRQYSEAVLPEYM 537
Cdd:PLN02246   432 DRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMkdEVAGEVP-VAFVVRSNGSEITEDE----IKQFVAKQVVFYK 506

                          570       580
                   ....*....|....*....|....
gi 1331970929  538 IPTRFINISNMPLTPSGKLDRRAL 561
Cdd:PLN02246   507 RIHKVFFVDSIPKAPSGKILRKDL 530

fabG

PRK05653

3-oxoacyl-ACP reductase FabG;

2536-2671

3.54e-10

3-oxoacyl-ACP reductase FabG;

Pssm-ID: 235546 [Multi-domain] Cd Length: 246 Bit Score: 62.87 E-value: 3.54e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGAKylVLVGRRGaREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:PRK05653    21 IALRLAADGAK--VVIYDSN-EEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAveAFGALDILVNNAGITRDAL 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929 2614 LQQQSWQAFKEVMNPKVAGAWN-----LHILTKNQpldfF---VLFSSATSLLGNAGQANHAAANA 2671
Cdd:PRK05653    98 LPRMSEEDWDRVIDVNLTGTFNvvraaLPPMIKAR----YgriVNISSVSGVTGNPGQTNYSAAKA 159

SDR_c

cd05233

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...

2530-2684

6.23e-10

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 212491 [Multi-domain] Cd Length: 234 Bit Score: 61.92 E-value: 6.23e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2530 GGLGLVVARFLVTNGAKyLVLVGRrgaREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAG 2607
Cdd:cd05233      8 SGIGRAIARRLAREGAK-VVLADR---NEEALAELAAIEALGGNAVAVQADVSDEEDVEALVEEAleEFGRLDILVNNAG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2608 TLNDGILQQQSWQAFKEVMNPKVAGAWNL------HILTKNQPLdfFVLFSSATSLLGNAGQANHAAANAFLDGLA-SYR 2680
Cdd:cd05233     84 IARPGPLEELTDEDWDRVLDVNLTGVFLLtraalpHMKKQGGGR--IVNISSVAGLRPLPGQAAYAASKAALEGLTrSLA 161


                   ....
gi 1331970929 2681 RHLG 2684
Cdd:cd05233    162 LELA 165

A_NRPS_MycA_like

cd05908

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...

200-558

8.78e-10

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 64.05 E-value: 8.78e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  200 LPNNLAYCIYTSGSTGNPKGILMEHRSLV-NMLWWHQQTRPSVQGvRTLQFCAVSFDF---SCHeifstlclggiLVLVP 275
Cdd:cd05908    104 LADELAFIQFSSGSTGDPKGVMLTHENLVhNMFAILNSTEWKTKD-RILSWMPLTHDMgliAFH-----------LAPLI 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  276 EAVRQNPFALAEFI----------SQQKIE---------KLFL----PVIA----LLQLAEAVNGNKSTSLALCEVITTg 328
Cdd:cd05908    172 AGMNQYLMPTRLFIrrpilwlkkaSEHKATivsspnfgyKYFLktlkPEKAndwdLSSIRMILNGAEPIDYELCHEFLD- 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  329 eQMqitpAVANLfqKTGAMLhNHYGATE------FQDATTHTL-------------------KGNPEGWpTLVPVGRPLH 383
Cdd:cd05908    251 -HM----SKYGL--KRNAIL-PVYGLAEasvgasLPKAQSPFKtitlgrrhvthgepepevdKKDSECL-TFVEVGKPID 321

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  384 NVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLArYLPDGTIEHLGRID 463
Cdd:cd05908    322 ETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW---------LKTGDLG-FIRNGRLVITGREK 391

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  464 HQVKIRGFRVELGEIESVLASHQAVRECAVVA----REIAGHTQLVGYIIAKDTLN----LSfDKLEPILRQYS----EA 531
Cdd:cd05908    392 DIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvnNSNTRNEEIFCFIEHRKSEDdfypLG-KKIKKHLNKRGgwqiNE 470

                          410       420
                   ....*....|....*....|....*..
gi 1331970929  532 VLPeymiptrfinISNMPLTPSGKLDR 558
Cdd:cd05908    471 VLP----------IRRIPKTTSGKVKR 487

PP-binding

pfam00550

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...

2811-2869

1.58e-09

Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 56.03 E-value: 1.58e-09

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1331970929 2811 VREQVSQVLGIDTKTLLAEQDvgFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPT 2869
Cdd:pfam00550    3 LRELLAEVLGVPAEEIDPDTD--LFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPT 59

LC-FACS_euk

cd05927

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...

49-493

2.35e-09

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.

Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 63.00 E-value: 2.35e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   49 LTYGELNVRANHLAQHLLSLGC--QPDDLLAICIERSAELFIGLLGILKAGCAYVPLdvgYP---GDRIEYMLRDSDARI 123
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPL---YDtlgPEAIEYILNHAEISI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  124 LLTSTDVakklaltipalqecqTVYLDQEifeydfhFLAIAKllhnqylrllhfyfytliqqcqatsvsQGIQTQVL--P 201
Cdd:cd05927     83 VFCDAGV---------------KVYSLEE-------FEKLGK---------------------------KNKVPPPPpkP 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  202 NNLAYCIYTSGSTGNPKGILMEHRSLVN----MLWWHQQTRPsvqgvRTLQFCAVSFDFSCHeIF------STLCLGG-- 269
Cdd:cd05927    114 EDLATICYTSGTTGNPKGVMLTHGNIVSnvagVFKILEILNK-----INPTDVYISYLPLAH-IFervveaLFLYHGAki 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  270 --------------------ILVLVP------------EAVRQNPFA--LAEFISQQKIEKL---------FLPVIALLQ 306
Cdd:cd05927    188 gfysgdirlllddikalkptVFPGVPrvlnriydkifnKVQAKGPLKrkLFNFALNYKLAELrsgvvraspFWDKLVFNK 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  307 LAEAVNGNkstslalCEVITTGEQmQITPAVANLFQKT-GAMLHNHYGATEFQDATTHTLKGNpegwPTLVPVGRPLHNV 385
Cdd:cd05927    268 IKQALGGN-------VRLMLTGSA-PLSPEVLEFLRVAlGCPVLEGYGQTECTAGATLTLPGD----TSVGHVGGPLPCA 335

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  386 QVYILDeaqqpVP-LG-------GEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGDLARYLPDGTIE 457
Cdd:cd05927    336 EVKLVD-----VPeMNydakdpnPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGW---------LHTGDIGEWLPNGTLK 401

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1331970929  458 HLGRIDHQVKI-RGFRVELGEIESVLASHQAVRECAV 493
Cdd:cd05927    402 IIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFV 438

AFD_CAR-like

cd17632

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...

48-556

2.75e-09

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.

Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 62.86 E-value: 2.75e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   48 SLTYGELNVRANHLA-QHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLT 126
Cdd:cd17632     67 TITYAELWERVGAVAaAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  127 ST---DVAKKLALTIPALQecQTVYLDQEIfEYDFHFLAiaklLHNQYLRLLHF-----YFYTLIQQCQATSVSQGIQTQ 198
Cdd:cd17632    147 SAehlDLAVEAVLEGGTPP--RLVVFDHRP-EVDAHRAA----LESARERLAAVgipvtTLTLIAVRGRDLPPAPLFRPE 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  199 VLPNNLAYCIYTSGSTGNPKGILMEHRsLVNMLWwhqQTRPSVQGVR-----TLQFCAVSFDFSCHEIFSTLCLGGI--- 270
Cdd:cd17632    220 PDDDPLALLIYTSGSTGTPKGAMYTER-LVATFW---LKVSSIQDIRppasiTLNFMPMSHIAGRISLYGTLARGGTayf 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  271 --------------------LVLVP---EAVRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSlALCEVITT 327
Cdd:cd17632    296 aaasdmstlfddlalvrpteLFLVPrvcDMLFQRYQAELDRRSVAGADAETLAERVKAELRERVLGGRLLA-AVCGSAPL 374

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  328 GEQMQitpavANLFQKTGAMLHNHYGATEfqdATTHTLKGNpegwptlvpVGRPlhnvqvYILDEAQQPVP-LG------ 400
Cdd:cd17632    375 SAEMK-----AFMESLLDLDLHDGYGSTE---AGAVILDGV---------IVRP------PVLDYKLVDVPeLGyfrtdr 431

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  401 --GEGEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklYRTGD-LARYLPDgTIEHLGRIDHQVKI-RGFRVELG 476
Cdd:cd17632    432 phPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGF---------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVA 501

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  477 EIESVLASHQAVRECAVVAReiAGHTQLVGYII-------AKDTLNLSFDKLEPILRQYSEAVLPEYMIPTRFInISNMP 549
Cdd:cd17632    502 RLEAVFAASPLVRQIFVYGN--SERAYLLAVVVptqdalaGEDTARLRAALAESLQRIAREAGLQSYEIPRDFL-IETEP 578


                   ....*..
gi 1331970929  550 LTPSGKL 556
Cdd:cd17632    579 FTIANGL 585

PRK07769

long-chain-fatty-acid--CoA ligase; Validated

11-560

2.97e-09

long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 62.82 E-value: 2.97e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   11 FDGNGTQSEFPDSCIHHLFEDQAAKRPDAIAL--------IDGE-QSLTYGELNVRANHLAQHLLSLGcQPDDLLAICIE 81
Cdd:PRK07769     9 FDVNGKIRFPPNTNLVRHVERWAKVRGDKLAYrfldfsteRDGVaRDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAP 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   82 RSAELFIGLLGILKAGCAYVPL-DVGYPG--DRIEYMLRDSDARILLTSTDVA---KKLALTIPALQECQTVYLDqeife 155
Cdd:PRK07769    88 QNLDYLIAFFGALYAGRIAVPLfDPAEPGhvGRLHAVLDDCTPSAILTTTDSAegvRKFFRARPAKERPRVIAVD----- 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  156 ydfhflAIAkllhnqylrllhfyfytliQQCQATSVSQGIQTqvlpNNLAYCIYTSGSTGNPKGILMEHRSL-VNMLwwh 234
Cdd:PRK07769   163 ------AVP-------------------DEVGATWVPPEANE----DTIAYLQYTSGSTRIPAGVQITHLNLpTNVL--- 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  235 qQTRPSVQ---GVRTLQFCAVSFDFS-CHEIFSTLCLGGILVLVPEAVRQNP-----------------FALA-----EF 288
Cdd:PRK07769   211 -QVIDALEgqeGDRGVSWLPFFHDMGlITVLLPALLGHYITFMSPAAFVRRPgrwirelarkpggtggtFSAApnfafEH 289

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  289 ISQQKIEKLFLPVIALLQLAEAVNGNkstslalcEVITTGEQMQITPAVANL-FQKTGamLHNHYG---ATEFQDATTHt 364
Cdd:PRK07769   290 AAARGLPKDGEPPLDLSNVKGLLNGS--------EPVSPASMRKFNEAFAPYgLPPTA--IKPSYGmaeATLFVSTTPM- 358

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  365 lkgnpEGWPTLVPVGRPLHN----VQV----------------------YILD-EAQQPVPLGGEGEFCIGGIGLARGYH 417
Cdd:PRK07769   359 -----DEEPTVIYVDRDELNagrfVEVpadapnavaqvsagkvgvsewaVIVDpETASELPDGQIGEIWLHGNNIGTGYW 433

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  418 NLPDLTNEKF-------IPNPF--GANENAKKLyRTGDLARYLpDGTIEHLGRIDHQVKIRGFRVELGEIE-SVLASHQA 487
Cdd:PRK07769   434 GKPEETAATFqnilksrLSESHaeGAPDDALWV-RTGDYGVYF-DGELYITGRVKDLVIIDGRNHYPQDLEyTAQEATKA 511

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  488 VRECAVVAREIAGHtQLVGYIIAKDTLNLSFDK---------------------LEPILRQYSEAVLPEYMIPTRFINI- 545
Cdd:PRK07769   512 LRTGYVAAFSVPAN-QLPQVVFDDSHAGLKFDPedtseqlvivaerapgahkldPQPIADDIRAAIAVRHGVTVRDVLLv 590

                          650
                   ....*....|....*..
gi 1331970929  546 --SNMPLTPSGKLDRRA 560
Cdd:PRK07769   591 paGSIPRTSSGKIARRA 607

AdoMet_MTases

cd02440

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...

2111-2216

4.87e-09

Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 56.28 E-value: 4.87e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2111 RILEIGAGTGGTTAYLLPHLPGdqtKYVFTDISAFFLAKAEERFKDYPFVRYQVL--DIEQAPQaqgFEPQIYDLIVAAD 2188
Cdd:cd02440      1 RVLDLGCGTGALALALASGPGA---RVTGVDISPVALELARKAAAALLADNVEVLkgDAEELPP---EADESFDVIISDP 74

                           90       100
                   ....*....|....*....|....*....
gi 1331970929 2189 VLHATSDLRQTLVH-IRQLLAPGGMLILM 2216
Cdd:cd02440     75 PLHHLVEDLARFLEeARRLLKPGGVLVLT 103

CLF

cd00832

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...

755-1107

5.79e-09

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.

Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 61.22 E-value: 5.79e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  755 TDPQQRILLECAWEAFERAGYNPETYPE-PVGVYAGSSLStyllnniGSALGiiteQPFIETDMEQFQAKIGNDRS---- 829
Cdd:cd00832     68 TDRMTRLALAAADWALADAGVDPAALPPyDMGVVTASAAG-------GFEFG----QRELQKLWSKGPRHVSAYQSfawf 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  830 YLAT--RISYKLNLKGPSVNVQTACSTSLVAVHMACQSLISGECQMaLAGGISV------VVPQKGGylyeeGMVRSQDG 901
Cdd:cd00832    137 YAVNtgQISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRGTPLV-VSGGVDSalcpwgWVAQLSS-----GRLSTSDD 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  902 HCRA---FDAEAQGTIFGNGGGLVLLKRLQDALDDNDNIMAVIKATAINNDGALKMGYTApsvdGQADVISEAIAIADID 978
Cdd:cd00832    211 PARAylpFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPP----GLARAIRLALADAGLT 286

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  979 ASTIGYVEAHGTATQLGDPIEVAGLARAFqrstdsvlGKQQCAIGSVKTNIGHLDEAAGIAGLIKAALALQYGQIPPSLH 1058
Cdd:cd00832    287 PEDVDVVFADAAGVPELDRAEAAALAAVF--------GPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVN 358

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1331970929 1059 YANPNPRIDFDAtpffVNTELREWSrngyPRRAGVSSFGVGGTNSHIVL 1107
Cdd:cd00832    359 VTDVPPAYGLDL----VTGRPRPAA----LRTALVLARGRGGFNSALVV 399

PRK06060

p-hydroxybenzoic acid--AMP ligase FadD22;

205-586

6.36e-09

p-hydroxybenzoic acid--AMP ligase FadD22;

Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 61.59 E-value: 6.36e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  205 AYCIYTSGSTGNPKGILmeHRSLVNMLWWHQQTRPSVQGV-RTLQFCAVSFDFSC---HEIFSTLCLGGILVLVPEAVRQ 280
Cdd:PRK06060   148 AYATYTSGTTGPPKAAI--HRHADPLTFVDAMCRKALRLTpEDTGLCSARMYFAYglgNSVWFPLATGGSAVINSAPVTP 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  281 NPFALaefisqqkIEKLFLPVIA------LLQLAEAVNGNKSTSLAlCeVITTGEQMQitPAVANLFQK--TGAMLHNHY 352
Cdd:PRK06060   226 EAAAI--------LSARFGPSVLygvpnfFARVIDSCSPDSFRSLR-C-VVSAGEALE--LGLAERLMEffGGIPILDGI 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  353 GATEF-QDATTHTLkgnpEGWpTLVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYHNLPD--LTNEKFIp 429
Cdd:PRK06060   294 GSTEVgQTFVSNRV----DEW-RLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWL- 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  430 npfganenakklyRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVA-REIAGHTQLVGYI 508
Cdd:PRK06060   368 -------------DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAvRESTGASTLQAFL 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  509 IAKDTLNLSfdklEPILRQYSEAVLPE---YMIPTRFINISNMPLTPSGKLDRRALPDPKGDRPALSTPLVKPRTQTEKR 585
Cdd:PRK06060   435 VATSGATID----GSVMRDLHRGLLNRlsaFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSGVRAQ 510


                   .
gi 1331970929  586 L 586
Cdd:PRK06060   511 R 511

LC_FACS_euk1

cd17639

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...

49-488

8.59e-09

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.

Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 61.08 E-value: 8.59e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   49 LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGcayVPLDVGYP---GDRIEYMLRDSDARILL 125
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSAIF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  126 TSTDvakklaltipalqecqtvyldqeifeydfhflaiakllhnqylrllhfyfytliqqcqatsvsqgiqtqvlPNNLA 205
Cdd:cd17639     83 TDGK-----------------------------------------------------------------------PDDLA 91

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  206 YCIYTSGSTGNPKGILMEHRSLVNMLwwHQQTRPSVQGVRT-------------LQFCA--VSFDFSCHEIFS---TL-- 265
Cdd:cd17639     92 CIMYTSGSTGNPKGVMLTHGNLVAGI--AGLGDRVPELLGPddrylaylplahiFELAAenVCLYRGGTIGYGsprTLtd 169

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  266 -----CLGGILVL-------VPE-----------------AVRQNPFALAEFISQQKI----------EKLFLPVIALL- 305
Cdd:cd17639    170 kskrgCKGDLTEFkptlmvgVPAiwdtirkgvlaklnpmgGLKRTLFWTAYQSKLKALkegpgtplldELVFKKVRAALg 249

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  306 -QLAEAVNG----NKST----SLALCEVITtgeqmqitpavanlfqktGamlhnhYGATEFQDATTHTlkgNPEGWPTLV 376
Cdd:cd17639    250 gRLRYMLSGgaplSADTqeflNIVLCPVIQ------------------G------YGLTETCAGGTVQ---DPGDLETGR 302

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  377 pVGRPLHNVQVYILDeaqqpVPLGG--------EGEFCIGGIGLARGYHNLPDLTNEKFipnpfganeNAKKLYRTGDLA 448
Cdd:cd17639    303 -VGPPLPCCEIKLVD-----WEEGGystdkpppRGEILIRGPNVFKGYYKNPEKTKEAF---------DGDGWFHTGDIG 367

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1331970929  449 RYLPDGTIEHLGRIDHQVKIR-GFRVELGEIESVLASHQAV 488
Cdd:cd17639    368 EFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLV 408

PRK08162

acyl-CoA synthetase; Validated

37-572

1.21e-08

acyl-CoA synthetase; Validated

Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 60.73 E-value: 1.21e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   37 PDAIALIDGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYML 116
Cdd:PRK08162    32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  117 RDSDARILLTST---DVAKKLALTIPALQECQTVYLDQEIFEYDFhflaIAKLLHNQYLRLLHFYF-YTLIQ-QCQATSV 191
Cdd:PRK08162   112 RHGEAKVLIVDTefaEVAREALALLPGPKPLVIDVDDPEYPGGRF----IGALDYEAFLASGDPDFaWTLPAdEWDAIAL 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  192 SqgiqtqvlpnnlayciYTSGSTGNPKGILMEHR-----SLVNMLWWHQQTRPSVqgVRTLQFcavsfdFSCHE---IFS 263
Cdd:PRK08162   188 N----------------YTSGTTGNPKGVVYHHRgaylnALSNILAWGMPKHPVY--LWTLPM------FHCNGwcfPWT 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  264 TLCLGGILVLVPeavRQNPFALAEFISQQKIEKLFLPVIALLQLAEAVNGNKSTSLALCEVITTGEqmqiTPAVANLfQK 343
Cdd:PRK08162   244 VAARAGTNVCLR---KVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGA----APPAAVI-AK 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  344 TGAM---LHNHYGATEFQDATTHTLKgnPEGWPTLVPVGRPLHNV----------QVYILD-EAQQPVPLGGE--GEFCI 407
Cdd:PRK08162   316 MEEIgfdLTHVYGLTETYGPATVCAW--QPEWDALPLDERAQLKArqgvryplqeGVTVLDpDTMQPVPADGEtiGEIMF 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  408 GGIGLARGYHNLPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIehlgridhQVKIR--------GFRVELGEIE 479
Cdd:PRK08162   394 RGNIVMKGYLKNPKATEEAF----------AGGWFHTGDLAVLHPDGYI--------KIKDRskdiiisgGENISSIEVE 455

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  480 SVLASHQAVRECAVVAR--EIAGHTQlVGYIIAKDTLNLSfdklEPILRQYSEAVLPEYMIPTRFInISNMPLTPSGKLD 557
Cdd:PRK08162   456 DVLYRHPAVLVAAVVAKpdPKWGEVP-CAFVELKDGASAT----EEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQ 529

                          570
                   ....*....|....*
gi 1331970929  558 RRALPDPKGDRPALS 572
Cdd:PRK08162   530 KFVLREQAKSLKAID 544

PRK08308

acyl-CoA synthetase; Validated

436-562

1.26e-08

acyl-CoA synthetase; Validated

Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 60.05 E-value: 1.26e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  436 ENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVREcAVVAReiaGHTQLVGYIIAkdTLN 515
Cdd:PRK08308   287 KMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQE-AVVYR---GKDPVAGERVK--AKV 360

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1331970929  516 LSFDKLEPI-LRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP 562
Cdd:PRK08308   361 ISHEEIDPVqLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408

FACL_like_4

cd05944

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...

201-561

2.33e-08

Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 59.03 E-value: 2.33e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  201 PNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQqtRPSVQGVRTLQFCAVSFdFSCHEIFSTLCL----GGILVLVPE 276
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLA--LNSLFDPDDVLLCGLPL-FHVNGSVVTLLTplasGAHVVLAGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  277 AVRQNPFALAEF---ISQQKIEKLF-LPVI--ALLQlaeaVNGNKSTSlALCEVITTGEQMQItpAVANLFQ-KTGAMLH 349
Cdd:cd05944     78 AGYRNPGLFDNFwklVERYRITSLStVPTVyaALLQ----VPVNADIS-SLRFAMSGAAPLPV--ELRARFEdATGLPVV 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  350 NHYGATEfqdATTHTLKGNPEGWPTLVPVGRPLHNVQVYILDE-----AQQPVPLGGEGEFCIGGIGLARGYhnlpdlTN 424
Cdd:cd05944    151 EGYGLTE---ATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLdgvgrLLRDCAPDEVGEICVAGPGVFGGY------LY 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  425 EKFIPNPFGANenakKLYRTGDLARYLPDGTIEHLGRIDHQVkIR-GFRVELGEIESVLASHQAVRECAVVAREIAGHTQ 503
Cdd:cd05944    222 TEGNKNAFVAD----GWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGE 296

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331970929  504 L-VGYIIAKDTLNLSFDKLEPILRQY--SEAVLPEYMIPtrfinISNMPLTPSGKLDRRAL 561
Cdd:cd05944    297 LpVAYVQLKPGAVVEEEELLAWARDHvpERAAVPKHIEV-----LEELPVTAVGKVFKPAL 352

FadD3

cd17638

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...

208-556

2.53e-08

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.

Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 58.67 E-value: 2.53e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  208 IYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVSFDFScheiFSTLCLGGIL---VLVPEAVRqNPFA 284
Cdd:cd17638      6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFG----YKAGIVACLLtgaTVVPVAVF-DVDA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  285 LAEFISQQKIEklFLP-VIALLQLAEAVNGNKSTSLALCEVITTGEQMQITPAVANLFQKTGAM-LHNHYGATEfqdATT 362
Cdd:cd17638     81 ILEAIERERIT--VLPgPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTE---AGV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  363 HTLkGNPEGWPTLVP--VGRPLHNVQVYILDEaqqpvplggeGEFCIGGIGLARGYHNLPDLTNEKFipnpfganeNAKK 440
Cdd:cd17638    156 ATM-CRPGDDAETVAttCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI---------DADG 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  441 LYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAV--VAREIAGHtqlVG--YIIAKDTLNL 516
Cdd:cd17638    216 WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVigVPDERMGE---VGkaFVVARPGVTL 292

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1331970929  517 SfdklEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKL 556
Cdd:cd17638    293 T----EEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328

PP-binding

pfam00550

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...

584-642

6.91e-08

Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 51.41 E-value: 6.91e-08

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331970929  584 KRLAEIWGSYLAVDI--VGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQ 642
Cdd:pfam00550    1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61

DUF938

pfam06080

Protein of unknown function (DUF938); This family consists of several hypothetical proteins ...

2095-2215

1.19e-07

Protein of unknown function (DUF938); This family consists of several hypothetical proteins from both prokaryotes and eukaryotes. The function of this family is unknown.

Pssm-ID: 253548 Cd Length: 201 Bit Score: 54.77 E-value: 1.19e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2095 EALLSALEQLPPERGWRILEIGAGTGGTTAYLLPHLP------GDQTKYVFTDISAFFLAKAEERFKdYPFvryqVLDIE 2168
Cdd:pfam06080   12 EPILSVLQSYFAKTTERVLEIASGTGQHAVFFAPLLPnltwqpSDPDPNLRGSIAAWADQQGLRNLR-PPL----HLDVT 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1331970929 2169 QAP-QAQGFEPQIYDLIVAADVLHaTSDLRQTLVHIR---QLLAPGGMLIL 2215
Cdd:pfam06080   87 RPPwPVEAPAPASYDAIFSINMIH-ISPWSCVEGLFRgagRLLPPGGVLYI 136

prpE

PRK10524

propionyl-CoA synthetase; Provisional

439-574

1.46e-07

propionyl-CoA synthetase; Provisional

Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 57.27 E-value: 1.46e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  439 KKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVV--AREIAGhtQL-VGYIIAKDTLN 515
Cdd:PRK10524   472 RQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVgvKDALKG--QVaVAFVVPKDSDS 549

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331970929  516 LS----FDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDRRALP------DPkGDRPALSTP 574
Cdd:PRK10524   550 LAdreaRLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQaiaegrDP-GDLTTIEDP 617

PLN02387

long-chain-fatty-acid-CoA ligase family protein

49-488

1.53e-07

long-chain-fatty-acid-CoA ligase family protein

Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 57.05 E-value: 1.53e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   49 LTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILLTST 128
Cdd:PLN02387   107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  129 DVAKKLALTIPALQECQTV-YLDQEIFEYDFhflaiaKLLHNQYLRLLHFyfyTLIQQCQATSVSQGIQTqvLPNNLAYC 207
Cdd:PLN02387   187 KQLKKLIDISSQLETVKRViYMDDEGVDSDS------SLSGSSNWTVSSF---SEVEKLGKENPVDPDLP--SPNDIAVI 255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  208 IYTSGSTGNPKGILMEHRSLVnmlwwhqqtrPSVQGVRTlqfcaVSFDFSCHEIF-STLCLGGILVLVPEAVRQ------ 280
Cdd:PLN02387   256 MYTSGSTGLPKGVMMTHGNIV----------ATVAGVMT-----VVPKLGKNDVYlAYLPLAHILELAAESVMAavgaai 320

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  281 ---NPFALAEfiSQQKIEK------------LFLPVIALL----------------------QLA-----EAVNGNKSTS 318
Cdd:PLN02387   321 gygSPLTLTD--TSNKIKKgtkgdasalkptLMTAVPAILdrvrdgvrkkvdakgglakklfDIAykrrlAAIEGSWFGA 398

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  319 LALcevittgEQMQITPAVanlFQKTGAMLHNH------------------------------YGATEFQDATTHTlkgn 368
Cdd:PLN02387   399 WGL-------EKLLWDALV---FKKIRAVLGGRirfmlsggaplsgdtqrfiniclgapigqgYGLTETCAGATFS---- 464

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  369 peGW--PTLVPVGRPLHNVQVYILD-------EAQQPVPlggEGEFCIGGIGLARGYHNLPDLTNEKFipnpfGANENAK 439
Cdd:PLN02387   465 --EWddTSVGRVGPPLPCCYVKLVSweeggylISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVY-----KVDERGM 534

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1331970929  440 KLYRTGDLARYLPDGTIEHLGRIDHQVKIR-GFRVELGEIESVLASHQAV 488
Cdd:PLN02387   535 RWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYV 584

HSD10-like_SDR_c

cd05371

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...

2536-2668

2.09e-07

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187629 [Multi-domain] Cd Length: 252 Bit Score: 54.99 E-value: 2.09e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGAKyLVLVGRRGAREEQQAqlseleQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAG------ 2607
Cdd:cd05371     18 TVERLLAQGAK-VVILDLPNSPGETVA------KLGDNCRFVPVDVTSEKDVKAALALAkaKFGRLDIVVNCAGiavaak 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331970929 2608 TLNDGILQQQSWQAFKEVMNPKVAGAWNL-----HILTKNQPLDF-----FVLFSSATSLLGNAGQANHAA 2668
Cdd:cd05371     91 TYNKKGQQPHSLELFQRVINVNLIGTFNVirlaaGAMGKNEPDQGgergvIINTASVAAFEGQIGQAAYSA 161

FATP_FACS

cd05940

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...

46-546

2.20e-07

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.

Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 56.21 E-value: 2.20e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   46 EQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCayvpldvgyPGDRIEYMLRdsdARILL 125
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA---------VAALINYNLR---GESLA 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  126 TSTDVAKKLALTIPALqecqtvyldqeifeydfhflaiakllhnqylrllhFYfytliqqcqatsvsqgiqtqvlpnnla 205
Cdd:cd05940     69 HCLNVSSAKHLVVDAA-----------------------------------LY--------------------------- 86

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  206 ycIYTSGSTGNPKGILMEHRSLVNMLWWHQQtrpSVQGVRTLQFcavsfdFSC----HEIFSTLCLGGILVLVPEAVRQN 281
Cdd:cd05940     87 --IYTSGTTGLPKAAIISHRRAWRGGAFFAG---SGGALPSDVL------YTClplyHSTALIVGWSACLASGATLVIRK 155

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  282 PFALAEFISQ-QKIEKLFLPVIA-----LLQLAEAVNGNKSTSLALCevittGEQMQitPAVANLFQKTGAMLH--NHYG 353
Cdd:cd05940    156 KFSASNFWDDiRKYQATIFQYIGelcryLLNQPPKPTERKHKVRMIF-----GNGLR--PDIWEEFKERFGVPRiaEFYA 228

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  354 ATEFQDATTHtLKGNPEGW---PTLVPVGRPLHNVQVYIldEAQQP----------VPLGGEGEfCIGGIG-LAR--GYH 417
Cdd:cd05940    229 ATEGNSGFIN-FFGKPGAIgrnPSLLRKVAPLALVKYDL--ESGEPirdaegrcikVPRGEPGL-LISRINpLEPfdGYT 304

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  418 NlPDLTNEKFIPNPFganENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVARE 497
Cdd:cd05940    305 D-PAATEKKILRDVF---KKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQ 380

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1331970929  498 IAGHTQLVGYIIAKDTLNLSFDkLEPiLRQYSEAVLPEYMIPtRFINIS 546
Cdd:cd05940    381 VPGTDGRAGMAAIVLQPNEEFD-LSA-LAAHLEKNLPGYARP-LFLRLQ 426

Gcd14

COG2519

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...

2109-2214

2.75e-07

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification

Pssm-ID: 442009 [Multi-domain] Cd Length: 249 Bit Score: 54.40 E-value: 2.75e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2109 GWRILEIGAGTGGTTAYLLPHLpGDQTKYVFTDISAFFLAKAE---ERFKDYPFVRYQVLDIEqapqaQGFEPQIYDLIV 2185
Cdd:COG2519     92 GARVLEAGTGSGALTLALARAV-GPEGKVYSYERREDFAEIARknlERFGLPDNVELKLGDIR-----EGIDEGDVDAVF 165

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1331970929 2186 AadvlhatsDLRQ---TLVHIRQLLAPGGMLI 2214
Cdd:COG2519    166 L--------DMPDpweALEAVAKALKPGGVLV 189

HTH_51

pfam18558

Helix-turn-helix domain; This is helix turn helix domain found in polyketide synthases (PKSs) ...

1928-2011

3.38e-07

Helix-turn-helix domain; This is helix turn helix domain found in polyketide synthases (PKSs) in fungi. They are multidomain enzymes that biosynthesize a wide range of natural products. Family members include citrinin polyketide synthases which contain a C-methyltransferase (CMeT) domain pfam08242 that adds one or more S-adenosylmethionine (SAM)-derived methyl groups to the carbon framework.

Pssm-ID: 465801 Cd Length: 90 Bit Score: 50.16 E-value: 3.38e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 1928 ETKLAT--LIIEANLATYA-IAYTQLERLSLAYVVAAFRQMGW---LFQPGerfstaQKVSALGIVDQHRQLFARLLDIL 2001
Cdd:pfam18558    3 ETKKLTdqFIEEYGFAGYWdEVYPRQTRLCLALIVEAFEKLGCdlrSAKPG------QKLPRIPHLPKHQRLVDYLYEIL 76

                           90
                   ....*....|
gi 1331970929 2002 AEADILRSEN 2011
Cdd:pfam18558   77 EDARLVDIDG 86

PRK13388

acyl-CoA synthetase; Provisional

345-561

4.17e-07

acyl-CoA synthetase; Provisional

Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 55.42 E-value: 4.17e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  345 GAMLHNHYGATEFQDATTHTlKGNPEGwptlvPVGRPLHNVQVYILDEAQQ-PVPLGGE------GEFCIG------GIG 411
Cdd:PRK13388   288 GCQVEDGYGSSEGAVIVVRE-PGTPPG-----SIGRGAPGVAIYNPETLTEcAVARFDAhgallnADEAIGelvntaGAG 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  412 LARGYHNLPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVREC 491
Cdd:PRK13388   362 FFEGYYNNPEATAERM----------RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRV 431

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331970929  492 AV--VAREIAGhTQLVGYIIAKDTLNLSFDKLEPILRqySEAVLPEYMIPtRFINIS-NMPLTPSGKLDRRAL 561
Cdd:PRK13388   432 AVyaVPDERVG-DQVMAALVLRDGATFDPDAFAAFLA--AQPDLGTKAWP-RYVRIAaDLPSTATNKVLKREL 500

hsFATP2a_ACSVL_like

cd05938

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...

45-230

5.12e-07

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.

Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 55.38 E-value: 5.12e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   45 GEQSLTYGELNVRANHLAQHLLS-LGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARI 123
Cdd:cd05938      2 EGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  124 LLTSTDVAKKLALTIPALQecqtvyldqeifEYDFHFLAIAKLLHNQYLRllhfyfyTLIQQCQATS---VSQGIQTQVL 200
Cdd:cd05938     82 LVVAPELQEAVEEVLPALR------------ADGVSVWYLSHTSNTEGVI-------SLLDKVDAASdepVPASLRAHVT 142

                          170       180       190
                   ....*....|....*....|....*....|
gi 1331970929  201 PNNLAYCIYTSGSTGNPKGILMEHRSLVNM 230
Cdd:cd05938    143 IKSPALYIYTSGTTGLPKAARISHLRVLQC 172

PRK06060

p-hydroxybenzoic acid--AMP ligase FadD22;

2801-2893

1.35e-06

p-hydroxybenzoic acid--AMP ligase FadD22;

Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.27 E-value: 1.35e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2801 KEGLTLLQAHVREQVSQVLGIDTKTLLAE-------QDVGFFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPTQQAL 2873
Cdd:PRK06060   532 RERLVALRQERQRLVVDAVCAEAAKMLGEpdpwsvdQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGL 611

                           90       100
                   ....*....|....*....|
gi 1331970929 2874 VNYLANELLGTPEQLQEPES 2893
Cdd:PRK06060   612 AQYLEAELAGGHGRLKSAGP 631

PRK08180

feruloyl-CoA synthase; Reviewed

24-227

2.05e-06

feruloyl-CoA synthase; Reviewed

Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 53.34 E-value: 2.05e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   24 CIHHLFEDQAAKRPDAIALI-----DGEQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGC 98
Cdd:PRK08180    40 RLTDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGV 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   99 AYVPLDVGY---PGD--RIEYMLRdsdariLLTSTDV-AKKLALTIPALQECqtVYLDQEIFeydfhflaiakLLHNQYL 172
Cdd:PRK08180   120 PYAPVSPAYslvSQDfgKLRHVLE------LLTPGLVfADDGAAFARALAAV--VPADVEVV-----------AVRGAVP 180

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1331970929  173 RLLHFYFYTLIQQCQATSVSQGIQtQVLPNNLAYCIYTSGSTGNPKGILMEHRSL 227
Cdd:PRK08180   181 GRAATPFAALLATPPTAAVDAAHA-AVGPDTIAKFLFTSGSTGLPKAVINTHRML 234

PRK07768

long-chain-fatty-acid--CoA ligase; Validated

375-560

2.62e-06

long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.08 E-value: 2.62e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  375 LVPVGRPLHNVQVYILDEAQQPVPLGGEGEFCIGGIGLARGYhnlpdLTNEKFIPnpfgaNENAKKLYRTGDLARYLPDG 454
Cdd:PRK07768   359 LATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIP-----AQDADGWLDTGDLGYLTEEG 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  455 TIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRE-CAVVAREIAGHTQlVGYIIAKDTlNLSFD--KLEPILRQYSEA 531
Cdd:PRK07768   429 EVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPgNAVAVRLDAGHSR-EGFAVAVES-NAFEDpaEVRRIRHQVAHE 506

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1331970929  532 VLPEYMIPTRFINI---SNMPLTPSGKLDRRA 560
Cdd:PRK07768   507 VVAEVGVRPRNVVVlgpGSIPKTPSGKLRRAN 538

PRK12827

short chain dehydrogenase; Provisional

2536-2676

2.79e-06

short chain dehydrogenase; Provisional

Pssm-ID: 237219 [Multi-domain] Cd Length: 249 Bit Score: 51.26 E-value: 2.79e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGAKYLVLVG--RRGaREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAVT--YPPLRGVIHAAGTLND 2611
Cdd:PRK12827    22 IAVRLAADGADVIVLDIhpMRG-RAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVeeFGRLDILVNNAGIATD 100

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2612 GILQQQSWQAFKEVMNPKVAGAWNL-HILT----KNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGL 2676
Cdd:PRK12827   101 AAFAELSIEEWDDVIDVNLDGFFNVtQAALppmiRARRGGRIVNIASVAGVRGNRGQVNYAASKAGLIGL 170

PRK06198

short chain dehydrogenase; Provisional

2536-2627

2.84e-06

short chain dehydrogenase; Provisional

Pssm-ID: 180462 [Multi-domain] Cd Length: 260 Bit Score: 51.54 E-value: 2.84e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGAKYLVLVGRRGAREEQQAqlSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:PRK06198    22 IARAFAERGAAGLVICGRNAEKGEAQA--AELEALGAKAVFVQADLSDVEDCRRVVAAAdeAFGRLDALVNAAGLTDRGT 99

                           90
                   ....*....|....
gi 1331970929 2614 LQQQSWQAFKEVMN 2627
Cdd:PRK06198   100 ILDTSPELFDRHFA 113

PKS_PP

smart00823

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...

595-648

6.46e-06

Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 46.47 E-value: 6.46e-06

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1331970929   595 AVDIVGTHDNFFDLGGTSLLLTQAHKFLCETFNINLSAVSLFQYPTIQTLAQYI 648
Cdd:smart00823   29 AAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82

adh_short

pfam00106

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.

2530-2677

9.10e-06

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.

Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 49.15 E-value: 9.10e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2530 GGLGLVVARFLVTNGAKyLVLVGRRGAREEQQAQlsELEQLGASVKVLQADIADAEQLAQALSAVT--YPPLRGVIHAAG 2607
Cdd:pfam00106   10 SGIGRAIAKRLAKEGAK-VVLVDRSEEKLEAVAK--ELGALGGKALFIQGDVTDRAQVKALVEQAVerLGRLDILVNNAG 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929 2608 TLNDGILQQQSWQAFKEVMNPKVAGAWNL------HILTKNQPLDFFVlfSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:pfam00106   87 ITGLGPFSELSDEDWERVIDVNLTGVFNLtravlpAMIKGSGGRIVNI--SSVAGLVPYPGGSAYSASKAAVIGFT 160

FATP_chFAT1_like

cd05937

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...

45-545

9.56e-06

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.

Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 50.89 E-value: 9.56e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   45 GEQSLTYGELNVRANHLAQHLLS-LGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARI 123
Cdd:cd05937      2 EGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  124 LLTSTDvakklaltipalqecqtvyldqeifeydfhflaiakllhnqYLRLLhfyfytliqqcqatsvsqgiqtqvlpnn 203
Cdd:cd05937     82 VIVDPD-----------------------------------------DPAIL---------------------------- 92

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  204 laycIYTSGSTGNPKGILMEHRslvnMLWWHQQTRPSVQGVR---TLQFCAVSFDFSCHEIFSTLCL--GGILVLVPEav 278
Cdd:cd05937     93 ----IYTSGTTGLPKAAAISWR----RTLVTSNLLSHDLNLKngdRTYTCMPLYHGTAAFLGACNCLmsGGTLALSRK-- 162

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  279 rqnpFALAEFISQQKIEK--LFLPVIALLQLAEAVNGNKSTSLALCEVITtGEQMQitPAVANLFQKTGAM--LHNHYGA 354
Cdd:cd05937    163 ----FSASQFWKDVRDSGatIIQYVGELCRYLLSTPPSPYDRDHKVRVAW-GNGLR--PDIWERFRERFNVpeIGEFYAA 235

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  355 TEfqdATTHTLKGNPEGWpTLVPVGR-------PLHNVQVYI-LD-EAQQP-----------VPLGGEGEFcIGGI---- 410
Cdd:cd05937    236 TE---GVFALTNHNVGDF-GAGAIGHhglirrwKFENQVVLVkMDpETDDPirdpktgfcvrAPVGEPGEM-LGRVpfkn 310

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  411 -GLARGYHNLPDLTNEKFIPNPFganENAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVR 489
Cdd:cd05937    311 rEAFQGYLHNEDATESKLVRDVF---RKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIA 387

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1331970929  490 ECAVVAREIAGHTQLVGY--IIAKDTLNLSFDKLEPILRQYSEAVLPEYMIPtRFINI 545
Cdd:cd05937    388 EANVYGVKVPGHDGRAGCaaITLEESSAVPTEFTKSLLASLARKNLPSYAVP-LFLRL 444

PRK12826

SDR family oxidoreductase;

2524-2684

1.05e-05

SDR family oxidoreductase;

Pssm-ID: 183775 [Multi-domain] Cd Length: 251 Bit Score: 49.53 E-value: 1.05e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2524 LIAGGLGGLGLVVARFLVTNGAKYLVlVGRRGAREEQQAQLseLEQLGASVKVLQADIADAEQLAQALSAVT--YPPLRG 2601
Cdd:PRK12826    10 LVTGAARGIGRAIAVRLAADGAEVIV-VDICGDDAAATAEL--VEAAGGKARARQVDVRDRAALKAAVAAGVedFGRLDI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2602 VIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNL------HILTKNQPLdfFVLFSSATSL-LGNAGQANHAAANAFLD 2674
Cdd:PRK12826    87 LVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLtqaalpALIRAGGGR--IVLTSSVAGPrVGYPGLAHYAASKAGLV 164

                          170
                   ....*....|.
gi 1331970929 2675 GLA-SYRRHLG 2684
Cdd:PRK12826   165 GFTrALALELA 175

AACS

cd05943

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...

27-555

1.51e-05

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.

Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 50.73 E-value: 1.51e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   27 HLFEDQAAkrPDAIALIDGE----QSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLL-----GILKAG 97
Cdd:cd05943     75 NLLRHADA--DDPAAIYAAEdgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLatasiGAIWSS 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   98 CAyvPlDVGYPG--DRieymLRDSDARILLT---------STDVAKKLALTIPALQEC-QTVYLDQEIFEYDFHFLAIAK 165
Cdd:cd05943    153 CS--P-DFGVPGvlDR----FGQIEPKVLFAvdaytyngkRHDVREKVAELVKGLPSLlAVVVVPYTVAAGQPDLSKIAK 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  166 LlhnqylrllHFYFYTLiqqcQATSVSQGIQTQVLPNNLAYCIYTSGSTGNPK-------GILMEHRSLVnMLwwHQQTR 238
Cdd:cd05943    226 A---------LTLEDFL----ATGAAGELEFEPLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEH-IL--HCDLR 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  239 PsvqGVRtlqFCAVSfdfSC-----HEIFSTLCLGGILVLVPEavrqNPF-----ALAEFISQQKIEklFLPVIA--LLQ 306
Cdd:cd05943    290 P---GDR---LFYYT---TCgwmmwNWLVSGLAVGATIVLYDG----SPFypdtnALWDLADEEGIT--VFGTSAkyLDA 354

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  307 LAEA-VNGNKSTSL-ALCEVITTGeqmqiTPAVANLFQ------KTGAMLHNHYGATefqDATTHTLKGNPegwptLVPV 378
Cdd:cd05943    355 LEKAgLKPAETHDLsSLRTILSTG-----SPLKPESFDyvydhiKPDVLLASISGGT---DIISCFVGGNP-----LLPV 421

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  379 GR-----PLHNVQVYILDEAQQPVPlGGEGEF-CIGGI-GLARGYHNLPDltNEKFIPNPFGANENakkLYRTGDLARYL 451
Cdd:cd05943    422 YRgeiqcRGLGMAVEAFDEEGKPVW-GEKGELvCTKPFpSMPVGFWNDPD--GSRYRAAYFAKYPG---VWAHGDWIEIT 495

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  452 PDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREI-AGHTQLVGYIIAKDTLNLSFDKLEPILRQYSE 530
Cdd:cd05943    496 PRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWkDGDERVILFVKLREGVELDDELRKRIRSTIRS 575

                          570       580
                   ....*....|....*....|....*
gi 1331970929  531 AVLPEYmIPTRFINISNMPLTPSGK 555
Cdd:cd05943    576 ALSPRH-VPAKIIAVPDIPRTLSGK 599

YdfG

COG4221

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...

2530-2684

1.96e-05

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation

Pssm-ID: 443365 [Multi-domain] Cd Length: 240 Bit Score: 48.64 E-value: 1.96e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2530 GGLGLVVARFLVTNGAKyLVLVGRRGAReeqqaqLSEL-EQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAA 2606
Cdd:COG4221     15 SGIGAATARALAAAGAR-VVLAARRAER------LEALaAELGGRALAVPLDVTDEAAVEAAVAAAvaEFGRLDVLVNNA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2607 GTLNDGILQQQSWQAFKEVMNPKVAGAWNL--------------HILTknqpldffvlFSSATSLLGNAGQANHAAANAF 2672
Cdd:COG4221     88 GVALLGPLEELDPEDWDRMIDVNVKGVLYVtraalpamrargsgHIVN----------ISSIAGLRPYPGGAVYAATKAA 157

                          170
                   ....*....|...
gi 1331970929 2673 LDGLA-SYRRHLG 2684
Cdd:COG4221    158 VRGLSeSLRAELR 170

PTZ00237

acetyl-CoA synthetase; Provisional

206-558

3.30e-05

acetyl-CoA synthetase; Provisional

Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 49.35 E-value: 3.30e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  206 YCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRpSVQGVRTLQFCAVSFDF-SCHE-IFSTLCLGGILVLVPEAVRQNPF 283
Cdd:PTZ00237   258 YILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSI-IEKDIPTVVFSHSSIGWvSFHGfLYGSLSLGNTFVMFEGGIIKNKH 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  284 A---LAEFISQQKIEKLFLPVIALLQL------AEAVNGNKSTSlALCEVITTGEQmqITPAVANLF-QKTGAMLHNHYG 353
Cdd:PTZ00237   337 IeddLWNTIEKHKVTHTLTLPKTIRYLiktdpeATIIRSKYDLS-NLKEIWCGGEV--IEESIPEYIeNKLKIKSSRGYG 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  354 ATE-----FQDATTHTLKGNPEGWPTlvPVGRPLhnvqvyILDEAQQPVPLGGEGEFCIggiglargyhNLPdltnekfI 428
Cdd:PTZ00237   414 QTEigityLYCYGHINIPYNATGVPS--IFIKPS------ILSEDGKELNVNEIGEVAF----------KLP-------M 468

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  429 PNPFGA-----NENAKKL-------YRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR 496
Cdd:PTZ00237   469 PPSFATtfyknDEKFKQLfskfpgyYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGI 548

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929  497 E-IAGHTQLVGYIIAK---DTLNLSFDKLEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLDR 558
Cdd:PTZ00237   549 YdPDCYNVPIGLLVLKqdqSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614

KDSR-like_SDR_c

cd08939

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...

2524-2740

5.27e-05

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187643 [Multi-domain] Cd Length: 239 Bit Score: 47.25 E-value: 5.27e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2524 LIAGGLGGLGLVVARFLVTNGAKyLVLVGRRGAREEQQAQLSELEQLGASVKVL--QADIADAEQLAQALSAVTYP--PL 2599
Cdd:cd08939      5 LITGGSSGIGKALAKELVKEGAN-VIIVARSESKLEEAVEEIEAEANASGQKVSyiSADLSDYEEVEQAFAQAVEKggPP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2600 RGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAGAWNL-H---ILTKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDG 2675
Cdd:cd08939     84 DLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVaHavlPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFALRG 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331970929 2676 LA----------SYRRHLGLPSlsinwGTWSEvGIAARLELDKLSSKQGEGTITLGQGLQILEQLLKD-ENGVYQV 2740
Cdd:cd08939    164 LAeslrqelkpyNIRVSVVYPP-----DTDTP-GFEEENKTKPEETKAIEGSSGPITPEEAARIIVKGlDRGYDDV 233

PRK05851

long-chain-fatty acid--ACP ligase MbtM;

378-558

5.67e-05

long-chain-fatty acid--ACP ligase MbtM;

Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.61 E-value: 5.67e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  378 VGRPLHNVQVYIlDEAQQPVPLGGE--GEFCIGGIGLARGYHNLPDLTNEKFIPnpfganenakklyrTGDLArYLPDGT 455
Cdd:PRK05851   347 LGNPIPGMEVRI-SPGDGAAGVAGReiGEIEIRGASMMSGYLGQAPIDPDDWFP--------------TGDLG-YLVDGG 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  456 IEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGHTQLVGYIIAKDTL--NLSFDKLEPILRQYSE-AV 532
Cdd:PRK05851   411 LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEFRgpDEAGARSEVVQRVASEcGV 490

                          170       180
                   ....*....|....*....|....*.
gi 1331970929  533 LPEYMIptrFINISNMPLTPSGKLDR 558
Cdd:PRK05851   491 VPSDVV---FVAPGSLPRTSSGKLRR 513

PRK08317

hypothetical protein; Provisional

2100-2217

6.03e-05

hypothetical protein; Provisional

Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 47.24 E-value: 6.03e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2100 ALEQLPPERGWRILEIGAGTGGTTAYlLPHLPGDQTKYVFTDISAFFLAKAEERFK-DYPFVRYQVLDIEQAPqaqgFEP 2178
Cdd:PRK08317    11 TFELLAVQPGDRVLDVGCGPGNDARE-LARRVGPEGRVVGIDRSEAMLALAKERAAgLGPNVEFVRGDADGLP----FPD 85

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1331970929 2179 QIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILME 2217
Cdd:PRK08317    86 GSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLD 124

PRK05620

long-chain fatty-acid--CoA ligase;

44-227

7.87e-05

long-chain fatty-acid--CoA ligase;

Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 48.24 E-value: 7.87e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   44 DGEQSLTYGELNVRANHLAqHLL--SLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDA 121
Cdd:PRK05620    34 AEQEQTTFAAIGARAAALA-HALhdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAED 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  122 RILLTSTDVAKKLAltiPALQECQTVYLDQEIFEYDFHFLAIAKLLHnqylrlLHFYFYTLIQQCQATSVSQgiqtQVLP 201
Cdd:PRK05620   113 EVIVADPRLAEQLG---EILKECPCVRAVVFIGPSDADSAAAHMPEG------IKVYSYEALLDGRSTVYDW----PELD 179

                          170       180
                   ....*....|....*....|....*..
gi 1331970929  202 NNLAYCI-YTSGSTGNPKGILMEHRSL 227
Cdd:PRK05620   180 ETTAAAIcYSTGTTGAPKGVVYSHRSL 206

SCP-x_thiolase

cd00829

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...

761-879

9.09e-05

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.

Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 47.64 E-value: 9.09e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  761 ILLECAWEAFERAGynpETYPEPVGVYAGSSLStyllnnigsalgiiteqpfietdmeqfqakiGNDRSYLATRISYKLN 840
Cdd:cd00829     19 LAAEAARAALDDAG---LEPADIDAVVVGNAAG-------------------------------GRFQSFPGALIAEYLG 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1331970929  841 LKG-PSVNVQTACSTSLVAVHMACQSLISGECQMALAGGI 879
Cdd:cd00829     65 LLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGA 104

COG3963

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];

2101-2214

9.23e-05

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];

Pssm-ID: 443163 Cd Length: 193 Bit Score: 45.97 E-value: 9.23e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2101 LEQLPPERGWRILEIGAGTGGTTAYLLPHLPGDQTKYVFtDISAFFLAKAEERFKDYPFVRYQVLDIEQAPQAQGFEPqi 2180
Cdd:COG3963     38 ASEVDWSGAGPVVELGPGTGVFTRAILARGVPDARLLAV-EINPEFAEHLRRRFPRVTVVNGDAEDLAELLAEHGIGK-- 114

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1331970929 2181 YDLIVaadvlhatS---------DLRQTLVH-IRQLLAPGGMLI 2214
Cdd:COG3963    115 VDAVV--------SglpllsfppELRRAILDaAFRVLAPGGVFV 150

PLN02654

acetate-CoA ligase

46-576

1.06e-04

acetate-CoA ligase

Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 47.97 E-value: 1.06e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   46 EQSLTYGELNVRANHLAQHLLSLGCQPDDLLAICIERSAELFIGLLGILKAGCAYVPLDVGYPGDRIEYMLRDSDARILL 125
Cdd:PLN02654   118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  126 TSTDVaKKLALTIPaLQECQTVYLDQEifEYDFHFLAIAKLLHNQylrllhfyfytLIQQCQATSVSQGIQT---QVLPN 202
Cdd:PLN02654   198 TCNAV-KRGPKTIN-LKDIVDAALDES--AKNGVSVGICLTYENQ-----------LAMKREDTKWQEGRDVwwqDVVPN 262

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  203 NLAYC-------------IYTSGSTGNPKGILmehrslvnmlwwHQQTRPSVQGVRTLQFcavSFDFSCHEIF--STLC- 266
Cdd:PLN02654   263 YPTKCevewvdaedplflLYTSGSTGKPKGVL------------HTTGGYMVYTATTFKY---AFDYKPTDVYwcTADCg 327

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  267 -------------LGGILVLVPEAVRQNPFA--LAEFISQQKIEKLFLPVIALLQLA----EAVNGNKSTSLALceVITT 327
Cdd:PLN02654   328 witghsyvtygpmLNGATVLVFEGAPNYPDSgrCWDIVDKYKVTIFYTAPTLVRSLMrdgdEYVTRHSRKSLRV--LGSV 405

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  328 GEQmqITPAVANLFqktgamlHNHYGATE--FQDATTHTLKGN------PEGWPtLVP--VGRPLHNVQVYILDEAQQPV 397
Cdd:PLN02654   406 GEP--INPSAWRWF-------FNVVGDSRcpISDTWWQTETGGfmitplPGAWP-QKPgsATFPFFGVQPVIVDEKGKEI 475

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  398 PLGGEGEFCI-----GGIGLARGYHNLPDLTNEKfipnPFganenaKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFR 472
Cdd:PLN02654   476 EGECSGYLCVkkswpGAFRTLYGDHERYETTYFK----PF------AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHR 545

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  473 VELGEIESVLASHQAVRECAVVA--REIAGHTqLVGYIIAKDTLNLSfDKLEPILRQYSEAVLPEYMIPTRFINISNMPL 550
Cdd:PLN02654   546 IGTAEVESALVSHPQCAEAAVVGieHEVKGQG-IYAFVTLVEGVPYS-EELRKSLILTVRNQIGAFAAPDKIHWAPGLPK 623

                          570       580       590
                   ....*....|....*....|....*....|...
gi 1331970929  551 TPSGKLDRRALP-------DPKGDRPALSTPLV 576
Cdd:PLN02654   624 TRSGKIMRRILRkiasrqlDELGDTSTLADPGV 656

BKR_SDR_c

cd05333

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...

2530-2677

1.60e-04

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187594 [Multi-domain] Cd Length: 240 Bit Score: 46.00 E-value: 1.60e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2530 GGLGLVVARFLVTNGAKyLVLVGRRgaREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAVT--YPPLRGVIHAAG 2607
Cdd:cd05333     10 RGIGRAIALRLAAEGAK-VAVTDRS--EEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEaeFGPVDILVNNAG 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331970929 2608 TLNDGILQQQSWQAFKEVMNPKVAGAWNL-----HILTKNQPLDfFVLFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:cd05333     87 ITRDNLLMRMSEEDWDAVINVNLTGVFNVtqaviRAMIKRRSGR-IINISSVVGLIGNPGQANYAASKAGVIGFT 160

PLN02614

long-chain acyl-CoA synthetase

201-488

1.86e-04

long-chain acyl-CoA synthetase

Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 46.94 E-value: 1.86e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  201 PNNLAYCIYTSGSTGNPKGILMEHRSLVNMLWWHQQTRPSVQGVRTLQFCAVS-------FDFSCHEIF----------- 262
Cdd:PLN02614   222 KSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAALTVKDVYLSylplahiFDRVIEECFiqhgaaigfwr 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  263 --STLCLGGILVLVPEAVRQNPFALAEFIS--QQKI------EKLFLPVIALLQLAEAVNGNKSTSLA-LCEVITTGEQM 331
Cdd:PLN02614   302 gdVKLLIEDLGELKPTIFCAVPRVLDRVYSglQKKLsdggflKKFVFDSAFSYKFGNMKKGQSHVEASpLCDKLVFNKVK 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  332 QITPAVANLFQKTGAMLHNH----------------YGATEFQDATTHTLkgnPEGWPTLVPVGRPLHNVQVYIldeaqQ 395
Cdd:PLN02614   382 QGLGGNVRIILSGAAPLASHvesflrvvacchvlqgYGLTESCAGTFVSL---PDELDMLGTVGPPVPNVDIRL-----E 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  396 PVP------LGG--EGEFCIGGIGLARGYHNLPDLTNEKFIPNpfganenakkLYRTGDLARYLPDGTIEHLGRIDHQVK 467
Cdd:PLN02614   454 SVPemeydaLAStpRGEICIRGKTLFSGYYKREDLTKEVLIDG----------WLHTGDVGEWQPNGSMKIIDRKKNIFK 523

                          330       340
                   ....*....|....*....|..
gi 1331970929  468 I-RGFRVELGEIESVLASHQAV 488
Cdd:PLN02614   524 LsQGEYVAVENIENIYGEVQAV 545

PLN03052

acetate--CoA ligase; Provisional

387-561

4.10e-04

acetate--CoA ligase; Provisional

Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 45.84 E-value: 4.10e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  387 VYILDEAQQPVPlggEGEFCIGGIGLArgyhnlpdltnekfiPNPFGANE------------------NAKKLYRTGDLA 448
Cdd:PLN03052   536 LFILDDSGNPYP---DDAPCTGELALF---------------PLMFGASStllnadhykvyfkgmpvfNGKILRRHGDIF 597

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  449 RYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVL-ASHQAVRECAVVAREIA--GHTQLV---------GYIIAKDTLNL 516
Cdd:PLN03052   598 ERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPggGPEQLViaavlkdppGSNPDLNELKK 677

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1331970929  517 SF-----DKLEPILRQYSEAVLPEYmiptrfinisnmPLTPSGKLDRRAL 561
Cdd:PLN03052   678 IFnsaiqKKLNPLFKVSAVVIVPSF------------PRTASNKVMRRVL 715

PRK07867

acyl-CoA synthetase; Validated

352-564

4.34e-04

acyl-CoA synthetase; Validated

Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 45.83 E-value: 4.34e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  352 YGATEFQDATTHTlKGNPEGwptlvPVGRPLHNVQvyILD-EAQQPVPLG-------GEGEFCIG------GIGLARGYH 417
Cdd:PRK07867   297 FGSTEGGVAITRT-PDTPPG-----ALGPLPPGVA--IVDpDTGTECPPAedadgrlLNADEAIGelvntaGPGGFEGYY 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  418 NLPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAR- 496
Cdd:PRK07867   369 NDPEADAERM----------RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVp 438

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331970929  497 -EIAGhTQLVGYIIAKDTLNLSFDKLEPILRQYSEavLPEYMIPtRFINISN-MPLTPSGKLDRRAL-------PDP 564
Cdd:PRK07867   439 dPVVG-DQVMAALVLAPGAKFDPDAFAEFLAAQPD--LGPKQWP-SYVRVCAeLPRTATFKVLKRQLsaegvdcADP 511

Thiolase_N

pfam00108

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...

844-878

4.35e-04

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.

Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 44.60 E-value: 4.35e-04

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1331970929  844 PSVNVQTACSTSLVAVHMACQSLISGECQMALAGG 878
Cdd:pfam00108   77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGG 111

PRK07008

long-chain-fatty-acid--CoA ligase; Validated

50-228

7.75e-04

long-chain-fatty-acid--CoA ligase; Validated

Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 45.08 E-value: 7.75e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929   50 TYGELNVRANHLAQHLLSLGCQPDD---LLAICIERSAELFIGLLGiLKAGCAYVPLDVgYPgDRIEYMLRDSDARILLt 126
Cdd:PRK07008    41 TYRDCERRAKQLAQALAALGVEPGDrvgTLAWNGYRHLEAYYGVSG-SGAVCHTINPRL-FP-EQIAYIVNHAEDRYVL- 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  127 stdvakklaltipalqecqtvyldqeifeYDFHFLAIAKLLHNQYLRLLHFYFYTLIQQCQATSV------------SQG 194
Cdd:PRK07008   117 -----------------------------FDLTFLPLVDALAPQCPNVKGWVAMTDAAHLPAGSTpllcyetlvgaqDGD 167

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1331970929  195 IQTQVLPNNLA-YCIYTSGSTGNPKGILMEHRSLV 228
Cdd:PRK07008   168 YDWPRFDENQAsSLCYTSGTTGNPKGALYSHRSTV 202

AcpA

COG3433

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...

2751-2878

8.44e-04

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 44.36 E-value: 8.44e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2751 LARQLTPQPFFSDAMKSIDTSVGKLTLQERDSCPQGYGHNIREQLENAPPKEGL--TLLQAHVREQVSQVLGIDTKTLLA 2828
Cdd:COG3433    162 LAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALetALTEEELRADVAELLGVDPEEIDP 241

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2829 EQDvgFFTLGMDSLTSVELRNRLQAsLGCSLSSTLAFDYPTQQALVNYLA 2878
Cdd:COG3433    242 DDN--LFDLGLDSIRLMQLVERWRK-AGLDVSFADLAEHPTLAAWWALLA 288

PaaJ

COG0183

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...

844-878

9.04e-04

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis

Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 44.29 E-value: 9.04e-04

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1331970929  844 PSVNVQTACSTSLVAVHMACQSLISGECQMALAGG 878
Cdd:COG0183     80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGG 114

ubiE

PRK00216

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...

2100-2221

9.16e-04

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;

Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 43.60 E-value: 9.16e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2100 ALEQLPPERGWRILEIGAGTgGTTAYLLPHLPGDQTKYVFTDISAFFLAKAEERFKDY---PFVRYQVLDIEQAPqaqgF 2176
Cdd:PRK00216    43 TIKWLGVRPGDKVLDLACGT-GDLAIALAKAVGKTGEVVGLDFSEGMLAVGREKLRDLglsGNVEFVQGDAEALP----F 117

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1331970929 2177 EPQIYDLIVAADVLHATSDLRQTLVHIRQLLAPGGMLILMEDSEP 2221
Cdd:PRK00216   118 PDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFSKP 162

PRK12939

short chain dehydrogenase; Provisional

2536-2691

9.28e-04

short chain dehydrogenase; Provisional

Pssm-ID: 183833 [Multi-domain] Cd Length: 250 Bit Score: 43.81 E-value: 9.28e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGAKylVLVGrRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIHAAGTLNDGI 2613
Cdd:PRK12939    23 FAEALAEAGAT--VAFN-DGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAaaALGGLDGLVNNAGITNSKS 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2614 LQQQSWQAFKEVMNPKVAGAWNL------HIltKNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGL-ASYRRHLGLP 2686
Cdd:PRK12939   100 ATELDIDTWDAVMNVNVRGTFLMlraalpHL--RDSGRGRIVNLASDTALWGAPKLGAYVASKGAVIGMtRSLARELGGR 177


                   ....*
gi 1331970929 2687 SLSIN 2691
Cdd:PRK12939   178 GITVN 182

Pcm

COG2518

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...

2101-2214

9.47e-04

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 43.15 E-value: 9.47e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2101 LEQLPPERGWRILEIGAGTGGTTAyLLPHLpgdqTKYVFT-DISAFFLAKAEERFKD--YPFVRYQVLD-----IEQAPq 2172
Cdd:COG2518     59 LEALDLKPGDRVLEIGTGSGYQAA-VLARL----AGRVYSvERDPELAERARERLAAlgYDNVTVRVGDgalgwPEHAP- 132

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1331970929 2173 aqgfepqiYDLI-VAAdvlhATSDLRQTLVhirQLLAPGGMLI 2214
Cdd:COG2518    133 --------FDRIiVTA----AAPEVPEALL---EQLAPGGRLV 160

PRK12936

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed

2536-2716

9.86e-04

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed

Pssm-ID: 171820 [Multi-domain] Cd Length: 245 Bit Score: 43.75 E-value: 9.86e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGAkylvLVGRRGAREEQQAQLSEleQLGASVKVLQADIADAEQLaQALSAVTYPPLRGV---IHAAGTLNDG 2612
Cdd:PRK12936    22 IARLLHAQGA----IVGLHGTRVEKLEALAA--ELGERVKIFPANLSDRDEV-KALGQKAEADLEGVdilVNNAGITKDG 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2613 ILQQQSWQAFKEVMNPKVAGAWNL-----HILTKNQpLDFFVLFSSATSLLGNAGQANHAAANAFLDGLA-SYRRHLGLP 2686
Cdd:PRK12936    95 LFVRMSDEDWDSVLEVNLTATFRLtreltHPMMRRR-YGRIINITSVVGVTGNPGQANYCASKAGMIGFSkSLAQEIATR 173

                          170       180       190
                   ....*....|....*....|....*....|
gi 1331970929 2687 SLSINwgtWSEVGIAARLELDKLSSKQGEG 2716
Cdd:PRK12936   174 NVTVN---CVAPGFIESAMTGKLNDKQKEA 200

thiolase

cd00751

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...

844-879

1.14e-03

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.

Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 44.01 E-value: 1.14e-03

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1331970929  844 PSVNVQTACSTSLVAVHMACQSLISGECQMALAGGI 879
Cdd:cd00751     76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGV 111

hydroxyacyl-CoA-like_DH_SDR_c-like

cd05353

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...

2578-2677

1.37e-03

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187611 [Multi-domain] Cd Length: 250 Bit Score: 43.08 E-value: 1.37e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2578 QADIADAEQLAQ-ALSAvtYPPLRGVIHAAGTLNDGILQQQSWQAFKEVMNPKVAG-------AWNlHIltKNQPLDFFV 2649
Cdd:cd05353     69 YDSVEDGEKIVKtAIDA--FGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGsfkvtraAWP-YM--RKQKFGRII 143

                           90       100
                   ....*....|....*....|....*...
gi 1331970929 2650 LFSSATSLLGNAGQANHAAANAFLDGLA 2677
Cdd:cd05353    144 NTSSAAGLYGNFGQANYSAAKLGLLGLS 171

TrmR

COG4122

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...

2111-2215

1.83e-03

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification

Pssm-ID: 443298 Cd Length: 173 Bit Score: 41.71 E-value: 1.83e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2111 RILEIGAGTGGTTAYLLPHLPGDqTKYVFTDISAFFLAKAEERFKDYPF---VRYQVLD-IEQAPQaqgFEPQIYDLIVA 2186
Cdd:COG4122     19 RILEIGTGTGYSTLWLARALPDD-GRLTTIEIDPERAAIARENFARAGLadrIRLILGDaLEVLPR---LADGPFDLVFI 94

                           90       100       110
                   ....*....|....*....|....*....|
gi 1331970929 2187 -ADVLHATSDLRqtlvHIRQLLAPGGMLIL 2215
Cdd:COG4122     95 dADKSNYPDYLE----LALPLLRPGGLIVA 120

Methyltransf_24

pfam13578

Methyltransferase domain; This family appears to be a methyltransferase domain.

2113-2215

2.45e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.

Pssm-ID: 433324 [Multi-domain] Cd Length: 106 Bit Score: 39.98 E-value: 2.45e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2113 LEIGAGTGGTTAYLLPHLP-GDQTKYVFTDI------SAFFLAKAEERfkdyPFVRYQVLDIEQApqAQGFEPQIYDLIV 2185
Cdd:pfam13578    1 VEIGTYSGVSTLWLAAALRdNGLGRLTAVDPdpgaeeAGALLRKAGLD----DRVRLIVGDSREA--LPSLADGPIDLLF 74

                           90       100       110
                   ....*....|....*....|....*....|
gi 1331970929 2186 AaDVLHATSDLRQTLVHIRQLLAPGGMLIL 2215
Cdd:pfam13578   75 I-DGDHTYEAVLNDLELWLPRLAPGGVILF 103

ChcA_like_SDR_c

cd05359

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...

2536-2679

2.48e-03

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

Pssm-ID: 187617 [Multi-domain] Cd Length: 242 Bit Score: 42.34 E-value: 2.48e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGAKylVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAV--TYPPLRGVIH--AAGTLND 2611
Cdd:cd05359     14 IALRLAERGAD--VVINYRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVkeRFGRLDVLVSnaAAGAFRP 91

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331970929 2612 giLQQQSWQAFKEVMNPKVAGAwnLHILTKNQPL------DFFVLFSSATSLLGNAGQANHAAANAFLDGLASY 2679
Cdd:cd05359     92 --LSELTPAHWDAKMNTNLKAL--VHCAQQAAKLmrerggGRIVAISSLGSIRALPNYLAVGTAKAALEALVRY 161

PLN02430

long-chain-fatty-acid-CoA ligase

398-481

2.77e-03

long-chain-fatty-acid-CoA ligase

Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 43.27 E-value: 2.77e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  398 PLGG--EGEFCIGGIGLARGYHNLPDLTNEKFipnpfganenAKKLYRTGDLARYLPDGTIEHLGRIDHQVKI-RGFRVE 474
Cdd:PLN02430   459 PLGEppRGEICVRGKCLFSGYYKNPELTEEVM----------KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVA 528


                   ....*..
gi 1331970929  475 LGEIESV 481
Cdd:PLN02430   529 LEYLENV 535

PaaK

COG1541

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...

442-497

4.01e-03

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];

Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 42.44 E-value: 4.01e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331970929  442 YRTGDLARYLPD----GT----IE-HLGRIDHQVKIRGFRVELGEIESVLASHQAVREC--AVVARE 497
Cdd:COG1541    297 YRTGDLTRLLPEpcpcGRthprIGrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEyqIVVDRE 363

PLN02861

long-chain-fatty-acid-CoA ligase

403-495

4.30e-03

long-chain-fatty-acid-CoA ligase

Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 42.52 E-value: 4.30e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  403 GEFCIGGIGLARGYHNLPDLTNEKFIPNPFganenakklyRTGDLARYLPDGTIEhlgRIDHQVKIrgFRVELGEIESVL 482
Cdd:PLN02861   466 GEICLRGNTLFSGYHKRQDLTEEVLIDGWF----------HTGDIGEWQPNGAMK---IIDRKKNI--FKLSQGEYVAVE 530

                           90
                   ....*....|...
gi 1331970929  483 ASHQAVRECAVVA 495
Cdd:PLN02861   531 NLENTYSRCPLIA 543

PRK06814

acyl-[ACP]--phospholipid O-acyltransferase;

442-557

5.17e-03

acyl-[ACP]--phospholipid O-acyltransferase;

Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 42.65 E-value: 5.17e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929  442 YRTGDLARYLPDGTIEHLGRIDHQVKIRGFRVELGEIESVLASHQAVRECAVVAREIAGH-TQLVGYIIAKDTlnlsfdK 520
Cdd:PRK06814  1012 YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKgERIILLTTASDA------T 1085

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1331970929  521 LEPILRQYSEAVLPEYMIPTRFINISNMPLTPSGKLD 557
Cdd:PRK06814  1086 RAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122

PRK12316

peptide synthase; Provisional

2798-2905

5.64e-03

peptide synthase; Provisional

Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 42.64 E-value: 5.64e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2798 APPKEGLTLLQ----AHVREQVSQVLGIDTKTLLAEQdVG----FFTLGMDSLTSVELRNRLQASLGCSLSSTLAFDYPT 2869
Cdd:PRK12316  5053 ALPQPDASLLQqayvAPRSELEQQVAAIWAEVLQLER-VGlddnFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPT 5131

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1331970929 2870 QQALVNYLANELLGTPEQLqepeSDEEDQISSMDDI 2905
Cdd:PRK12316  5132 LAAFVELAAAAGSGDDEKF----DDLEELLSELEEI 5163

PRK12824

3-oxoacyl-ACP reductase;

2536-2676

6.25e-03

3-oxoacyl-ACP reductase;

Pssm-ID: 183773 [Multi-domain] Cd Length: 245 Bit Score: 40.90 E-value: 6.25e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2536 VARFLVTNGakYLVLVGRRGAREEQQAQLSELEQLGASVKVLQADIADAEQLAQALSAVT--YPPLRGVIHAAGTLNDGI 2613
Cdd:PRK12824    18 IARELLNDG--YRVIATYFSGNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEeeEGPVDILVNNAGITRDSV 95

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331970929 2614 LQQQSWQAFKEVMNPKVAGAWNLHILT----KNQPLDFFVLFSSATSLLGNAGQANHAAANAFLDGL 2676
Cdd:PRK12824    96 FKRMSHQEWNDVINTNLNSVFNVTQPLfaamCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGF 162

PRK01683

trans-aconitate 2-methyltransferase; Provisional

2101-2263

7.44e-03

trans-aconitate 2-methyltransferase; Provisional

Pssm-ID: 234970 Cd Length: 258 Bit Score: 41.08 E-value: 7.44e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2101 LEQLPPERGWRILEIGAGTGGTTAYLLPHLPGDQTkyVFTDISAFFLAKAEERFKDYPFVRyqvLDIEQ-APqaqgfePQ 2179
Cdd:PRK01683    24 LARVPLENPRYVVDLGCGPGNSTELLVERWPAARI--TGIDSSPAMLAEARSRLPDCQFVE---ADIASwQP------PQ 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331970929 2180 IYDLIVAADVLHATSDLRQTLVHIRQLLAPGGML-------------ILMED-SEPARWADltfgltegwwKFTDHDLRP 2245
Cdd:PRK01683    93 ALDLIFANASLQWLPDHLELFPRLVSLLAPGGVLavqmpdnldepshVLMREvAENGPWEQ----------NLPDRGARR 162

                          170
                   ....*....|....*...
gi 1331970929 2246 NhPLLSPEQWQILLSEMG 2263
Cdd:PRK01683   163 A-PLPPPHAYYDALAPAA 179

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01