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Conserved domains on  [gi|41872631|ref|NP_004095|]
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fatty acid synthase [Homo sapiens]

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 ...
1-1358 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: 682.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1 MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTD-DDRRWKAGLYGLP----------RRSGKLKDLSRFDASFFGVHP 69
Cdd:COG3321    3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEvPADRWDADAYYDPdpdapgktyvRWGGFLDDVDEFDALFFGISP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   70 KQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFD 149
Cdd:COG3321   83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  150 FRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVV 229
Cdd:COG3321  163 LRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  230 AVLLtkKSLAR------RVYATILNAGTNTDGfKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQ 303
Cdd:COG3321  243 VVVL--KRLSDalrdgdRIYAVIRGSAVNQDG-RSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPI 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  304 ELNGITRALCATRQE--PLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPaLLDGRLQVVDQ-- 379
Cdd:COG3321  320 EAAALTAAFGQGRPAdqPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID-FENSPFYVNTElr 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  380 PLPVRGG--NVGINSFGFGGSNVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSmLNDI 457
Cdd:COG3321  399 PWPAGGGprRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLD-LADV 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  458 AAVPAT---AMPFRGyAVLG---------------GERGGPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDR-FRD 518
Cdd:COG3321  478 AYTLATgraHFEHRL-AVVAssreelaaklralaaGEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYETEPvFRA 556
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  519 SILRSDEAVKPF-GLKVSQLLLSTDE-STFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQ 596
Cdd:COG3321  557 ALDECDALLRPHlGWSLREVLFPDEEeSRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSL 636
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  597 EEAVLAAYWRGQCIKEAHlPPGAMAAVGLSWEECKQRCP--PGVVPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKE 674
Cdd:COG3321  637 EDALRLVAARGRLMQALP-GGGAMLAVGLSEEEVEALLAgyDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARR 715
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  675 VRTGGmAFHSYFMEAIAPPLLQELKKVirEPKPRSARWLSTSipEAQWHSSLARTssAEYNVNNLVSPVLFQEALWHVPE 754
Cdd:COG3321  716 LPVSH-AFHSPLMEPALEEFRAALAGV--TPRAPRIPLISNV--TGTWLTGEALD--ADYWVRHLRQPVRFADAVEALLA 788
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  755 --HAVVLEIAPHALLQAVLKRGLK--PSCTIIPLMKKDhRDNLEFFLAGIGRLHLSGIDANPNALFPPvefPAPRGTPLi 830
Cdd:COG3321  789 dgVRVFLEVGPGPVLTGLVRQCLAaaGDAVVLPSLRRG-EDELAQLLTALAQLWVAGVPVDWSALYPG---RGRRRVPL- 863
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  831 sPLIKWDHSLAWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVwkTLARALGLGVEQL 910
Cdd:COG3321  864 -PTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALA--ALLALVALAAAAA 940
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  911 PVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQWDDPDPRLFDHPESPTPNPTEPLFLAQAEV 990
Cdd:COG3321  941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  991 YKELRLRGYDYGPHFQGILEASLEGDSGRLLWKDNWVsfmDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQ 1070
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAA---AAALALALAALLLLAALAELALAAAALALAAALAAAALAL 1097
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1071 DKAQVADVVVSRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQT 1150
Cdd:COG3321 1098 ALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1151 KVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQVLAQERPKLPEDPLLSGLLDSPALKACLDT 1230
Cdd:COG3321 1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1231 AVENMPSLKMKVVEVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSA 1310
Cdd:COG3321 1258 ALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAV 1337
                       1370      1380      1390      1400
                 ....*....|....*....|....*....|....*....|....*...
gi 41872631 1311 DLLVCNCAVAALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVA 1358
Cdd:COG3321 1338 AAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
1564-1854 2.29e-130

Enoylreductase; Enoylreductase in Polyketide synthases.


:

Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 410.63  E-value: 2.29e-130
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1564 CTVYYASLNFRDIMLATGKLSPDAipgkwtsqdsLLGMEFSGRD----------ASGKRVMGLVPAkGLATSVLLSPDFL 1633
Cdd:smart00829    1 IEVRAAGLNFRDVLIALGLYPGEA----------VLGGECAGVVtrvgpgvtglAVGDRVMGLAPG-AFATRVVTDARLV 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1634 WDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLqaRFP 1713
Cdd:smart00829   70 VPIPDGWSFEEAATVPVVFLTAYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFL--RAL 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1714 QLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHG 1793
Cdd:smart00829  148 GIPDDHIFSSRDLSFADEILRATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHA 227
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41872631    1794 VLLDAFFnESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:smart00829  228 VDLDALE-EGPDRIRELLAEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
1876-2112 5.85e-100

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: 330.18  E-value: 5.85e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1876 ISKTFCPA--HKSYIIAGGLGGFGLELAQWLIQRGVQK-LVLTSRSGIRTGyQAKQVRRWRRQ---GVQVQVSTSNISSL 1949
Cdd:cd08954  208 ILKTNYPInlGKSYLITGGSGGLGLEILKWLVKRGAVEnIIILSRSGMKWE-LELLIREWKSQnikFHFVSVDVSDVSSL 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1950 EGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNA 2029
Cdd:cd08954  287 EKAINLILNAPKIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDYFVLFSSVSSIRGSA 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2030 GQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGIlVETMSTNDTIVS--GTLPQRMASCLEVLDLFLN--QPHMV 2105
Cdd:cd08954  367 GQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGF-VSRNESVDTLLGgqGLLPQSINSCLGTLDLFLQnpSPNLV 445

                 ....*..
gi 41872631 2106 LSSFVLA 2112
Cdd:cd08954  446 LSSFNFA 452
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
1316-1522 6.79e-52

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: 191.12  E-value: 6.79e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1316 NCAVAALGDPASalSNMVAALREGGFLLLHTLLRGHPLGDIVAFlTSTEPQYGQGILSQDAWESLFS---RVSLRLVGLK 1392
Cdd:cd08954    5 VCNLVLNGNLQS--ENLYALLKPNGFLLFVEPLKGSTLGDTWWL-TDNDIRKQSCLLSQEQWNQLLKstqEVSIKLSGVK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1393 KSFYGSTLflCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEdSSRPVWLKAINCATSGVVGLVNCLRREPGGNRLRCV 1472
Cdd:cd08954   82 KSFYGSVL--CRIQSPTDKSEFLPVEEQTFEYVEILKSLLATA-SCKPVLLTADGCESSGVIGAVRYFREEPQLKLIRCL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 41872631 1473 LLSNLSSTSHvPEVDPGSAELQKVLQGDLVMNVYRDGAWGAFRHFLLEED 1522
Cdd:cd08954  159 FVSNLNSQKE-PIIRNGKVYYERVKKNSNIKNVYKSGSWGDFRHLLLDLS 207
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
2242-2488 4.91e-47

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


:

Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 169.11  E-value: 4.91e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   2242 RPLFLVHPIEGSTTVFHSLASRLSIPTygLQCTRAAP--------LDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACV 2313
Cdd:pfam00975    1 RPLFCFPPAGGSASSFRSLARRLPPPA--EVLAVQYPgrgrgeppLNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   2314 AFEMCSQLQAQqspAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPgceaeaeteaicfFVQQFTDMEHNrvLEALLP---- 2389
Cdd:pfam00975   79 AFEVARRLERQ---GEAVRSLFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeel 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   2390 LKGLEERVAAAVDLIIKSHQGLDRQelsfaarsfyykLRAAEQYTPKAKYHGNVMLlraktggaygedlgaDYNLSQVCD 2469
Cdd:pfam00975  141 LSMLLPALRADYRALESYSCPPLDA------------QSATLFYGSDDPLHDADDL---------------AEWVRDHTP 193
                          250
                   ....*....|....*....
gi 41872631   2470 GKVSVHVIEGDHRTLLEGS 2488
Cdd:pfam00975  194 GEFDVHVFDGDHFYLIEHL 212
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2111-2179 3.81e-14

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: 69.97  E-value: 3.81e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41872631    2111 LAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREV 2179
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLV 69
 
Name Accession Description Interval E-value
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1-1358 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: 682.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1 MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTD-DDRRWKAGLYGLP----------RRSGKLKDLSRFDASFFGVHP 69
Cdd:COG3321    3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEvPADRWDADAYYDPdpdapgktyvRWGGFLDDVDEFDALFFGISP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   70 KQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFD 149
Cdd:COG3321   83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  150 FRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVV 229
Cdd:COG3321  163 LRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  230 AVLLtkKSLAR------RVYATILNAGTNTDGfKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQ 303
Cdd:COG3321  243 VVVL--KRLSDalrdgdRIYAVIRGSAVNQDG-RSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPI 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  304 ELNGITRALCATRQE--PLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPaLLDGRLQVVDQ-- 379
Cdd:COG3321  320 EAAALTAAFGQGRPAdqPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID-FENSPFYVNTElr 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  380 PLPVRGG--NVGINSFGFGGSNVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSmLNDI 457
Cdd:COG3321  399 PWPAGGGprRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLD-LADV 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  458 AAVPAT---AMPFRGyAVLG---------------GERGGPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDR-FRD 518
Cdd:COG3321  478 AYTLATgraHFEHRL-AVVAssreelaaklralaaGEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYETEPvFRA 556
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  519 SILRSDEAVKPF-GLKVSQLLLSTDE-STFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQ 596
Cdd:COG3321  557 ALDECDALLRPHlGWSLREVLFPDEEeSRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSL 636
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  597 EEAVLAAYWRGQCIKEAHlPPGAMAAVGLSWEECKQRCP--PGVVPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKE 674
Cdd:COG3321  637 EDALRLVAARGRLMQALP-GGGAMLAVGLSEEEVEALLAgyDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARR 715
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  675 VRTGGmAFHSYFMEAIAPPLLQELKKVirEPKPRSARWLSTSipEAQWHSSLARTssAEYNVNNLVSPVLFQEALWHVPE 754
Cdd:COG3321  716 LPVSH-AFHSPLMEPALEEFRAALAGV--TPRAPRIPLISNV--TGTWLTGEALD--ADYWVRHLRQPVRFADAVEALLA 788
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  755 --HAVVLEIAPHALLQAVLKRGLK--PSCTIIPLMKKDhRDNLEFFLAGIGRLHLSGIDANPNALFPPvefPAPRGTPLi 830
Cdd:COG3321  789 dgVRVFLEVGPGPVLTGLVRQCLAaaGDAVVLPSLRRG-EDELAQLLTALAQLWVAGVPVDWSALYPG---RGRRRVPL- 863
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  831 sPLIKWDHSLAWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVwkTLARALGLGVEQL 910
Cdd:COG3321  864 -PTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALA--ALLALVALAAAAA 940
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  911 PVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQWDDPDPRLFDHPESPTPNPTEPLFLAQAEV 990
Cdd:COG3321  941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  991 YKELRLRGYDYGPHFQGILEASLEGDSGRLLWKDNWVsfmDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQ 1070
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAA---AAALALALAALLLLAALAELALAAAALALAAALAAAALAL 1097
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1071 DKAQVADVVVSRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQT 1150
Cdd:COG3321 1098 ALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1151 KVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQVLAQERPKLPEDPLLSGLLDSPALKACLDT 1230
Cdd:COG3321 1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1231 AVENMPSLKMKVVEVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSA 1310
Cdd:COG3321 1258 ALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAV 1337
                       1370      1380      1390      1400
                 ....*....|....*....|....*....|....*....|....*...
gi 41872631 1311 DLLVCNCAVAALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVA 1358
Cdd:COG3321 1338 AAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
2-404 1.01e-174

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: 542.53  E-value: 1.01e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    2 EEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDD-DRRWKAGLY---------GLPRRSGKLKDLSRFDASFFGVHPKQ 71
Cdd:cd00833    1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIpEDRWDADGYypdpgkpgkTYTRRGGFLDDVDAFDAAFFGISPRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   72 AHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFDFR 151
Cdd:cd00833   81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  152 GPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAV 231
Cdd:cd00833  161 GPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  232 LLTKKSLARR----VYATILNAGTNTDGFKeQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNG 307
Cdd:cd00833  241 VLKRLSDALRdgdrIYAVIRGSAVNQDGRT-KGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  308 ITRALCATRQE--PLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPaLLDGRLQVVDQPLP--- 382
Cdd:cd00833  320 LAKVFGGSRSAdqPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKID-FEESPLRVPTEARPwpa 398
                        410       420
                 ....*....|....*....|...
gi 41872631  383 -VRGGNVGINSFGFGGSNVHIIL 404
Cdd:cd00833  399 pAGPRRAGVSSFGFGGTNAHVIL 421
Acyl_transf_1 pfam00698
Acyl transferase domain;
493-810 2.08e-132

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 418.03  E-value: 2.08e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    493 WFICSGMGTQWRGMGLSLMRL-DRFRDSILRSDEAVKP-FGLKVSQLLLSTDESTFDDIVHSFVSLTAIQIGLIDLLSCM 570
Cdd:pfam00698    1 VFVFSGQGSQWAGMGMQLLKTsPAFAAVIDRADEAFKPqYGFSVSDVLRNNPEGTLDGTQFVQPALFAMQIALAALLQSY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    571 GLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEAHlPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVT 650
Cdd:pfam00698   81 GVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLA-GPGGMAAVELSAEEVEQRWPDDVVGAVVNSPRSVV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    651 ISGPQAPVFEFVEQLRKEGVFAkEVRTGGMAFHSYFMEAIAPPLLQELKKvIREPKPRSARWLSTSIPEaqwhsSLARTS 730
Cdd:pfam00698  160 ISGPQEAVRELVERVSKEGVGA-LVENVNYAVHSPQMDAIAPALLSALAD-IAPRTPRVPFISSTSIDP-----SDQRTL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    731 SAEYNVNNLVSPVLFQEALWHV--PEHAVVLEIAPHALLQAVLKRGLK-----PSCTIIPLMKKDHRDNLEFFLAGIGRL 803
Cdd:pfam00698  233 SAEYWVRNLRSPVRFAEAILSAaePGPLVFIEISPHPLLLAALIDTLKsasdgKVATLVGTLIRDQTDFLVTFLYILAVA 312

                   ....*..
gi 41872631    804 HLSGIDA 810
Cdd:pfam00698  313 HLTGSAP 319
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
1564-1854 2.29e-130

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 410.63  E-value: 2.29e-130
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1564 CTVYYASLNFRDIMLATGKLSPDAipgkwtsqdsLLGMEFSGRD----------ASGKRVMGLVPAkGLATSVLLSPDFL 1633
Cdd:smart00829    1 IEVRAAGLNFRDVLIALGLYPGEA----------VLGGECAGVVtrvgpgvtglAVGDRVMGLAPG-AFATRVVTDARLV 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1634 WDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLqaRFP 1713
Cdd:smart00829   70 VPIPDGWSFEEAATVPVVFLTAYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFL--RAL 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1714 QLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHG 1793
Cdd:smart00829  148 GIPDDHIFSSRDLSFADEILRATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHA 227
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41872631    1794 VLLDAFFnESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:smart00829  228 VDLDALE-EGPDRIRELLAEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
4-404 2.76e-118

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: 376.67  E-value: 2.76e-118
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631       4 VVIAGMSGKLPESENLQEFWDNLIGGVDmvtdddrrwkaglyglprrsgklkDLSRFDASFFGVHPKQAHTMDPQLRLLL 83
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAGLD------------------------DVDLFDAAFFGISPREAEAMDPQQRLLL 56
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631      84 EVTYEAIVDGGINPDSLRGTHTGVWVGVSGSEtsealsrdpetlvgYSMvgcqrammanrlsfffdfrgpsiALDTACSS 163
Cdd:smart00825   57 EVAWEALEDAGIDPESLRGSRTGVFVGVSSSD--------------YSV-----------------------TVDTACSS 99
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     164 SLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARR-- 241
Cdd:smart00825  100 SLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRdg 179
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     242 --VYATILNAGTNTDGFKEqGVTFPSGDIQeqlirslyqsagvapesfeyieahgtgtkvgdpqelngitralcatrqep 319
Cdd:smart00825  180 dpILAVIRGSAVNQDGRSN-GITAPSGPAQ-------------------------------------------------- 208
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     320 LLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPaLLDGRLQVVDQPLPVRGGN----VGINSFGF 395
Cdd:smart00825  209 LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHID-LEESPLRVPTELTPWPPPGrprrAGVSSFGF 287

                    ....*....
gi 41872631     396 GGSNVHIIL 404
Cdd:smart00825  288 GGTNAHVIL 296
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
1566-1854 1.62e-112

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 359.96  E-value: 1.62e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1566 VYYASLNFRDIMLATGKLSPDaipgkwtsqDSLLGMEFSGRD----------ASGKRVMGLVPaKGLATSVLLSPDFLWD 1635
Cdd:cd05195    7 VKAAGLNFRDVLVALGLLPGD---------ETPLGLECSGIVtrvgsgvtglKVGDRVMGLAP-GAFATHVRVDARLVVK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1636 VPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPql 1715
Cdd:cd05195   77 IPDSLSFEEAATLPVAYLTAYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGG-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1716 DSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVL 1795
Cdd:cd05195  155 PVDHIFSSRDLSFADGILRATGGRGVDVVLNSLSGELLRASWRCLAPFGRFVEIGKRDILSNSKLGMRPFLRNVSFSSVD 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 41872631 1796 LDAFFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd05195  235 LDQLARERPELLRELLREVLELLEAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
1876-2112 5.85e-100

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: 330.18  E-value: 5.85e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1876 ISKTFCPA--HKSYIIAGGLGGFGLELAQWLIQRGVQK-LVLTSRSGIRTGyQAKQVRRWRRQ---GVQVQVSTSNISSL 1949
Cdd:cd08954  208 ILKTNYPInlGKSYLITGGSGGLGLEILKWLVKRGAVEnIIILSRSGMKWE-LELLIREWKSQnikFHFVSVDVSDVSSL 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1950 EGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNA 2029
Cdd:cd08954  287 EKAINLILNAPKIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDYFVLFSSVSSIRGSA 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2030 GQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGIlVETMSTNDTIVS--GTLPQRMASCLEVLDLFLN--QPHMV 2105
Cdd:cd08954  367 GQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGF-VSRNESVDTLLGgqGLLPQSINSCLGTLDLFLQnpSPNLV 445

                 ....*..
gi 41872631 2106 LSSFVLA 2112
Cdd:cd08954  446 LSSFNFA 452
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
1566-1856 3.23e-67

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 230.80  E-value: 3.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1566 VYYASLNFRDIMLATGKLSPD----AIPGkwtsqdsllgMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPD 1631
Cdd:COG0604   34 VKAAGVNPADLLIRRGLYPLPpglpFIPG----------SDAAGvvvavgegvtGFKVGDRVAGLGRGGGYAEYVVVPAD 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1632 FLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQAr 1711
Cdd:COG0604  104 QLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRA- 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1712 fpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTF 1791
Cdd:COG0604  183 ---LGADHVIDYREEDFAERVRALTGGRGVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTL 259
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41872631 1792 HGVLLDAFFNESS-ADWREVWALVQAgirdGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 1856
Cdd:COG0604  260 TGFTLFARDPAERrAALAELARLLAA----GKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTV 321
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
1897-2065 2.81e-52

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: 182.30  E-value: 2.81e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1897 GLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVL 1975
Cdd:smart00822   13 GRALARWLAERGARRLVLLSRSGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIpAVEGPLTGVIHAAGVL 92
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1976 RDGLLENQTPEFFQDVCKPKYSGTLNLDRVTReaCPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPG 2055
Cdd:smart00822   93 DDGVLASLTPERFAAVLAPKAAGAWNLHELTA--DLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRRARGLPA 170
                           170
                    ....*....|
gi 41872631    2056 LAVQWGAIGD 2065
Cdd:smart00822  171 LSIAWGAWAE 180
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
1316-1522 6.79e-52

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: 191.12  E-value: 6.79e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1316 NCAVAALGDPASalSNMVAALREGGFLLLHTLLRGHPLGDIVAFlTSTEPQYGQGILSQDAWESLFS---RVSLRLVGLK 1392
Cdd:cd08954    5 VCNLVLNGNLQS--ENLYALLKPNGFLLFVEPLKGSTLGDTWWL-TDNDIRKQSCLLSQEQWNQLLKstqEVSIKLSGVK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1393 KSFYGSTLflCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEdSSRPVWLKAINCATSGVVGLVNCLRREPGGNRLRCV 1472
Cdd:cd08954   82 KSFYGSVL--CRIQSPTDKSEFLPVEEQTFEYVEILKSLLATA-SCKPVLLTADGCESSGVIGAVRYFREEPQLKLIRCL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 41872631 1473 LLSNLSSTSHvPEVDPGSAELQKVLQGDLVMNVYRDGAWGAFRHFLLEED 1522
Cdd:cd08954  159 FVSNLNSQKE-PIIRNGKVYYERVKKNSNIKNVYKSGSWGDFRHLLLDLS 207
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
4-835 3.36e-50

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: 197.92  E-value: 3.36e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631      4 VVIAGMSGKLPESENLQEFWDNLIGGVDMVTD-DDRRWKAGLY----------GLPRRSGKLKDLSrFDASFFGVHPKQA 72
Cdd:TIGR02813    9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITDvPSDHWAKDDYydsdkseadkSYCKRGGFLPEVD-FNPMEFGLPPNIL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     73 HTMDPQLRLLLEVTYEAIVDGGInPDSLRGTHTGVWVGVSGSET-SEALS-------------------RDPETL----- 127
Cdd:TIGR02813   88 ELTDISQLLSLVVAKEVLNDAGL-PDGYDRDKIGITLGVGGGQKqSSSLNarlqypvlkkvfkasgvedEDSEMLikkfq 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    128 ---VGY---SMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFL 201
Cdd:TIGR02813  167 dqyIHWeenSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFS 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    202 RLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARR----VYATILNAGTNTDGfKEQGVTFPSGDIQEQLIRSLY 277
Cdd:TIGR02813  247 KTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERdgdrIYAVIKGVGASSDG-KFKSIYAPRPEGQAKALKRAY 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    278 QSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEP--LLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAP 355
Cdd:TIGR02813  326 DDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPP 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    356 NLHFHSPNPEI-----PALLDGR----LQVVDQpLPVRGgnvGINSFGFGGSNVHIIL---RPNTQPPPAPAPHAtLPRL 423
Cdd:TIGR02813  406 TINVDQPNPKLdiensPFYLNTEtrpwMQREDG-TPRRA---GISSFGFGGTNFHMVLeeySPKHQRDDQYRQRA-VAQT 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    424 LRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAV-------PATAMPFRGYAVLGG--------------ERGGPEV 482
Cdd:TIGR02813  481 LLFTAANEKALVSSLKDWKNKLSAKADDQPYAFNALAventlrtIAVALARLGFVAKNAdelitmleqaitqlEAKSCEE 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    483 QQVPAG-----------ERPLWFICSGMGTQWRGMGLSLM-RLDRFRDSILRSDEAVKPFGL-KVSQLLLS----TDEST 545
Cdd:TIGR02813  561 WQLPSGisyrksalvveSGKVAALFAGQGSQYLNMGRELAcNFPEVRQAAADMDSVFTQAGKgALSPVLYPipvfNDESR 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    546 ------FDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKE--AHLPP 617
Cdd:TIGR02813  641 kaqeeaLTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMAAptGEADI 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    618 GAMAAVGLsweecKQRCPPGVVPAC-----------HNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGmAFHSYF 686
Cdd:TIGR02813  721 GFMYAVIL-----AVVGSPTVIANCikdfegvsianYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSG-AFHTPL 794
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    687 MEAIAPPLLQELKKViREPKPRSARWLSTSipeAQWHSSLARTSSAEYNvNNLVSPVLFQEALWHVPEHA--VVLEIAPH 764
Cdd:TIGR02813  795 VAHAQKPFSAAIDKA-KFNTPLVPLYSNGT---GKLHSNDAAAIKKALK-NHMLQSVHFSEQLEAMYAAGarVFVEFGPK 869
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    765 ALLQAVLKRGLKPS----CTII--PLMKKDHRDNLEFF---LAGIGrLHLSGIDANPNALFPPVEfPAP-----RGTPLI 830
Cdd:TIGR02813  870 NILQKLVENTLKDKenelCAISinPNPKGDSDMQLRQAavqLAVLG-LELTEIDPYQAEKRPPAA-TSPmniklNAANYI 947

                   ....*
gi 41872631    831 SPLIK 835
Cdd:TIGR02813  948 SPATR 952
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
1556-1856 2.37e-49

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 179.38  E-value: 2.37e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1556 PTC-PGAQLCTVYYASLNFRDIMLATGK--LSPDAIPgkwtsqdsLLGMEFSG----------RDASGKRVMGLVPAKGL 1622
Cdd:TIGR02824   23 PVPkAGEVLIRVAAAGVNRPDLLQRAGKypPPPGASD--------ILGLEVAGevvavgegvsRWKVGDRVCALVAGGGY 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1623 ATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSA 1702
Cdd:TIGR02824   95 AEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWSNLFQRGGLKAGETVLIHGGASGIGTTAIQLAKAFGARVFTTAGSD 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1703 EKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG-------KFDLs 1775
Cdd:TIGR02824  175 EKCAACEA----LGADIAINYREEDFVEVVKAETGGKGVDVILDIVGGSYLNRNIKALALDGRIVQIGfqggrkaELDL- 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1776 qnhplgMAIFLKNVTFHGVLL----DAFFNESSADWRE-VWALvqagIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIG 1850
Cdd:TIGR02824  250 ------GPLLAKRLTITGSTLrarpVAEKAAIAAELREhVWPL----LASGRVRPVIDKVFPLEDAAQAHALMESGDHIG 319

                   ....*.
gi 41872631   1851 KVVVQV 1856
Cdd:TIGR02824  320 KIVLTV 325
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
2242-2488 4.91e-47

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 169.11  E-value: 4.91e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   2242 RPLFLVHPIEGSTTVFHSLASRLSIPTygLQCTRAAP--------LDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACV 2313
Cdd:pfam00975    1 RPLFCFPPAGGSASSFRSLARRLPPPA--EVLAVQYPgrgrgeppLNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   2314 AFEMCSQLQAQqspAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPgceaeaeteaicfFVQQFTDMEHNrvLEALLP---- 2389
Cdd:pfam00975   79 AFEVARRLERQ---GEAVRSLFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeel 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   2390 LKGLEERVAAAVDLIIKSHQGLDRQelsfaarsfyykLRAAEQYTPKAKYHGNVMLlraktggaygedlgaDYNLSQVCD 2469
Cdd:pfam00975  141 LSMLLPALRADYRALESYSCPPLDA------------QSATLFYGSDDPLHDADDL---------------AEWVRDHTP 193
                          250
                   ....*....|....*....
gi 41872631   2470 GKVSVHVIEGDHRTLLEGS 2488
Cdd:pfam00975  194 GEFDVHVFDGDHFYLIEHL 212
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
1886-2065 7.73e-41

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: 149.63  E-value: 7.73e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1886 SYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGP 1964
Cdd:pfam08659    2 TYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIkAEGPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1965 VGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERI 2044
Cdd:pfam08659   82 IRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDE--PLDFFVLFSSIAGLLGSPGQANYAAANAFLDAL 159
                          170       180
                   ....*....|....*....|.
gi 41872631   2045 CEKRRHEGLPGLAVQWGAIGD 2065
Cdd:pfam08659  160 AEYRRSQGLPATSINWGPWAE 180
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1-406 3.91e-33

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 134.74  E-value: 3.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     1 MEEVVIAGMSGKLPESENLQEFWDNLIGG---VDMVTDDDRRwkaglyGLPRR-SGKLKDLSR-----FDASFFgVHPKQ 71
Cdd:PRK06333    3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGqsgIRTLTDFPVG------DLATKiGGQVPDLAEdaeagFDPDRY-LDPKD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    72 AHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTH-TGVWV--GVSGSET-SEA----LSRDPETL----VGYSMVGcqraM 139
Cdd:PRK06333   76 QRKMDRFILFAMAAAKEALAQAGWDPDTLEDRErTATIIgsGVGGFPAiAEAvrtlDSRGPRRLspftIPSFLTN----M 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   140 MANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLS------PEGTCK 213
Cdd:PRK06333  152 AAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALStrfndaPEQASR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   214 AFDTAGNGYCRSEGvvAVLLTKKSL----AR--RVYATILNAGTNTDGFKeqgVTFP--SGDIQEQLIRSLYQSAGVAPE 285
Cdd:PRK06333  232 PFDRDRDGFVMGEG--AGILVIETLehalARgaPPLAELVGYGTSADAYH---MTAGpeDGEGARRAMLIALRQAGIPPE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   286 SFEYIEAHGTGTKVGDPQELNGITRALCATRQepLLIGSTKSNMGHPEPAS-GLAALAKVlLSLEHGLWAPNLHFHSPNP 364
Cdd:PRK06333  307 EVQHLNAHATSTPVGDLGEVAAIKKVFGHVSG--LAVSSTKSATGHLLGAAgGVEAIFTI-LALRDQIAPPTLNLENPDP 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 41872631   365 EIpallDGrLQVVD---QPLPVRggnVGI-NSFGFGGSNVHIILRP 406
Cdd:PRK06333  384 AA----EG-LDVVAnkaRPMDMD---YALsNGFGFGGVNASILFRR 421
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
2042-2491 1.71e-31

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 135.22  E-value: 1.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2042 ERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKAAAYRDR 2121
Cdd:COG3319  410 LREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLA 489
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2122 DSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELA 2201
Cdd:COG3319  490 ALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLL 569
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2202 CPTPKEDGLAQQQTQLNLRSLLVNPEGPTlmrlnsvqSSERPLFLVHPIEGSTTVFHSLASRLS--IPTYGLQC----TR 2275
Cdd:COG3319  570 APTLAALAAALAAAAAAAALSPLVPLRAG--------GSGPPLFCVHPAGGNVLCYRPLARALGpdRPVYGLQApgldGG 641
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2276 AAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQ-QSPApthnSLFLFDgspTYVLAYTqsyrak 2354
Cdd:COG3319  642 EPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQgEEVA----LLVLLD---SYAPGAL------ 708
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2355 ltpgcEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSH--QGLDRQELSFAARSFYYKLRAAEQ 2432
Cdd:COG3319  709 -----ARLDEAELLAALLRDLARGVDLPLDAEELRALDPEERLARLLERLREAGlpAGLDAERLRRLLRVFRANLRALRR 783
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 41872631 2433 YTPKAkYHGNVMLLRAkTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLE 2491
Cdd:COG3319  784 YRPRP-YDGPVLLFRA-EEDPPGRADDPALGWRPLVAGGLEVHDVPGDHFSMLREPHVA 840
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
1563-1856 2.26e-29

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 121.68  E-value: 2.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1563 LCTVYYASLNFRDIMLATGKLSPDaiPGkwtsQDSLLGMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPDF 1632
Cdd:PTZ00354   32 LIKVSAAGVNRADTLQRQGKYPPP--PG----SSEILGLEVAGyvedvgsdvkRFKEGDRVMALLPGGGYAEYAVAHKGH 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1633 LWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarf 1712
Cdd:PTZ00354  106 VMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDFCK--- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1713 pQLDSTSFANSRD-TSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG--------KFDLsqnhplgMA 1783
Cdd:PTZ00354  183 -KLAAIILIRYPDeEGFAPKVKKLTGEKGVNLVLDCVGGSYLSETAEVLAVDGKWIVYGfmggakveKFNL-------LP 254
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41872631  1784 IFLKNVTFHGVLL----DAFFNESSADW-REVWALvqagIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 1856
Cdd:PTZ00354  255 LLRKRASIIFSTLrsrsDEYKADLVASFeREVLPY----MEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLTV 328
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
1679-1816 6.44e-21

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 90.74  E-value: 6.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1679 GVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASV 1757
Cdd:pfam00107    1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELAK----ELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVgSPATLEQAL 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1758 RCLATHGRFLEIGKFdlSQNHPLGMA-IFLKNVTFHGVLLDaffneSSADWREVWALVQA 1816
Cdd:pfam00107   77 KLLRPGGRVVVVGLP--GGPLPLPLApLLLKELTILGSFLG-----SPEEFPEALDLLAS 129
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2111-2179 3.81e-14

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: 69.97  E-value: 3.81e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41872631    2111 LAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREV 2179
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLV 69
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2126-2409 3.93e-12

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 72.38  E-value: 3.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  2126 DLVEAVAHILGirdLAAVNLDSSLADLGLDSLMSVEVRQTLERELNlvlsvrevRQLTLRKLQELSSKADEASELAcptp 2205
Cdd:PRK10252  982 IIAAAFSSLLG---CDVVDADADFFALGGHSLLAMKLAAQLSRQFA--------RQVTPGQVMVASTVAKLATLLD---- 1046
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  2206 kEDGLAQQQTQLNLRSLLVNPEGPTLmrlnsvqsserplFLVHPIEGSTTVFHSLASRLS--IPTYGLQCTR---AAPL- 2279
Cdd:PRK10252 1047 -AEEDESRRLGFGTILPLREGDGPTL-------------FCFHPASGFAWQFSVLSRYLDpqWSIYGIQSPRpdgPMQTa 1112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  2280 DSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQqspAPTHNSLFLFDGSPtyvlAYTQSYRAKLTPGC 2359
Cdd:PRK10252 1113 TSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRAR---GEEVAFLGLLDTWP----PETQNWREKEANGL 1185
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 41872631  2360 EAEAETEAicffvqqftDMEHNRVLEAL---LP---LKGLEERVAAAVDLIIKSHQ 2409
Cdd:PRK10252 1186 DPEVLAEI---------DREREAFLAAQqgsLStelFTTIEGNYADAVRLLTTAHS 1232
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2125-2179 2.78e-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: 55.26  E-value: 2.78e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 41872631   2125 RDLVEAVAHILGIrDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREV 2179
Cdd:pfam00550    1 ERLRELLAEVLGV-PAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDL 54
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1900-2063 2.06e-08

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 57.57  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1900 LAQWLIQRGVQkLVLTSRSGIRTgyqAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDG 1978
Cdd:COG0300   21 LARALAARGAR-VVLVARDAERL---EALAAELRAAGARVEVVALDVTDPDAVAALAEAVlARFGPIDVLVNNAGVGGGG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1979 LLENQTPEFFQDVCKPKYSGTLNLdrvTREACPEL-----DYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHE-- 2051
Cdd:COG0300   97 PFEELDLEDLRRVFEVNVFGPVRL---TRALLPLMrargrGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAEla 173
                        170
                 ....*....|....
gi 41872631 2052 --GLPGLAVQWGAI 2063
Cdd:COG0300  174 ptGVRVTAVCPGPV 187
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2124-2187 8.71e-08

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: 51.39  E-value: 8.71e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41872631 2124 QRDLVEAVAHILGIrDLAAVNLDSSL-ADLGLDSLMSVEVRQTLERELNLVLSVREVRQL-TLRKL 2187
Cdd:COG0236    7 EERLAEIIAEVLGV-DPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYpTVADL 71
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
1901-2042 5.52e-07

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 53.27  E-value: 5.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1901 AQWLIQRGVqKLVLTSRSGIRtgyQAKQVRRWRR-QGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDG 1978
Cdd:PRK05557   22 AERLAAQGA-NVVINYASSEA---GAEALVAEIGaLGGKALAVQGDVSDAESVERAVDEAkAEFGGVDILVNNAGITRDN 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41872631  1979 LLENQTPEFFQDVCKPKYSGTLNldrVTREACPEL-----DYFVVFSSVSCGRGNAGQSNYGFANSAME 2042
Cdd:PRK05557   98 LLMRMKEEDWDRVIDTNLTGVFN---LTKAVARPMmkqrsGRIINISSVVGLMGNPGQANYAASKAGVI 163
 
Name Accession Description Interval E-value
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1-1358 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: 682.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1 MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTD-DDRRWKAGLYGLP----------RRSGKLKDLSRFDASFFGVHP 69
Cdd:COG3321    3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEvPADRWDADAYYDPdpdapgktyvRWGGFLDDVDEFDALFFGISP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   70 KQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFD 149
Cdd:COG3321   83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  150 FRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVV 229
Cdd:COG3321  163 LRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  230 AVLLtkKSLAR------RVYATILNAGTNTDGfKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQ 303
Cdd:COG3321  243 VVVL--KRLSDalrdgdRIYAVIRGSAVNQDG-RSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPI 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  304 ELNGITRALCATRQE--PLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPaLLDGRLQVVDQ-- 379
Cdd:COG3321  320 EAAALTAAFGQGRPAdqPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID-FENSPFYVNTElr 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  380 PLPVRGG--NVGINSFGFGGSNVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSmLNDI 457
Cdd:COG3321  399 PWPAGGGprRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLD-LADV 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  458 AAVPAT---AMPFRGyAVLG---------------GERGGPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDR-FRD 518
Cdd:COG3321  478 AYTLATgraHFEHRL-AVVAssreelaaklralaaGEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYETEPvFRA 556
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  519 SILRSDEAVKPF-GLKVSQLLLSTDE-STFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQ 596
Cdd:COG3321  557 ALDECDALLRPHlGWSLREVLFPDEEeSRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSL 636
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  597 EEAVLAAYWRGQCIKEAHlPPGAMAAVGLSWEECKQRCP--PGVVPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKE 674
Cdd:COG3321  637 EDALRLVAARGRLMQALP-GGGAMLAVGLSEEEVEALLAgyDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARR 715
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  675 VRTGGmAFHSYFMEAIAPPLLQELKKVirEPKPRSARWLSTSipEAQWHSSLARTssAEYNVNNLVSPVLFQEALWHVPE 754
Cdd:COG3321  716 LPVSH-AFHSPLMEPALEEFRAALAGV--TPRAPRIPLISNV--TGTWLTGEALD--ADYWVRHLRQPVRFADAVEALLA 788
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  755 --HAVVLEIAPHALLQAVLKRGLK--PSCTIIPLMKKDhRDNLEFFLAGIGRLHLSGIDANPNALFPPvefPAPRGTPLi 830
Cdd:COG3321  789 dgVRVFLEVGPGPVLTGLVRQCLAaaGDAVVLPSLRRG-EDELAQLLTALAQLWVAGVPVDWSALYPG---RGRRRVPL- 863
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  831 sPLIKWDHSLAWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVwkTLARALGLGVEQL 910
Cdd:COG3321  864 -PTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALA--ALLALVALAAAAA 940
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  911 PVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQWDDPDPRLFDHPESPTPNPTEPLFLAQAEV 990
Cdd:COG3321  941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  991 YKELRLRGYDYGPHFQGILEASLEGDSGRLLWKDNWVsfmDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQ 1070
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAA---AAALALALAALLLLAALAELALAAAALALAAALAAAALAL 1097
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1071 DKAQVADVVVSRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQT 1150
Cdd:COG3321 1098 ALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1151 KVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQVLAQERPKLPEDPLLSGLLDSPALKACLDT 1230
Cdd:COG3321 1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257
                       1290      1300      1310      1320      1330      1340      1350      1360
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1231 AVENMPSLKMKVVEVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSA 1310
Cdd:COG3321 1258 ALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAV 1337
                       1370      1380      1390      1400
                 ....*....|....*....|....*....|....*....|....*...
gi 41872631 1311 DLLVCNCAVAALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVA 1358
Cdd:COG3321 1338 AAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
2-404 1.01e-174

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: 542.53  E-value: 1.01e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    2 EEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDD-DRRWKAGLY---------GLPRRSGKLKDLSRFDASFFGVHPKQ 71
Cdd:cd00833    1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIpEDRWDADGYypdpgkpgkTYTRRGGFLDDVDAFDAAFFGISPRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   72 AHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFDFR 151
Cdd:cd00833   81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  152 GPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAV 231
Cdd:cd00833  161 GPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  232 LLTKKSLARR----VYATILNAGTNTDGFKeQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNG 307
Cdd:cd00833  241 VLKRLSDALRdgdrIYAVIRGSAVNQDGRT-KGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  308 ITRALCATRQE--PLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPaLLDGRLQVVDQPLP--- 382
Cdd:cd00833  320 LAKVFGGSRSAdqPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKID-FEESPLRVPTEARPwpa 398
                        410       420
                 ....*....|....*....|...
gi 41872631  383 -VRGGNVGINSFGFGGSNVHIIL 404
Cdd:cd00833  399 pAGPRRAGVSSFGFGGTNAHVIL 421
Acyl_transf_1 pfam00698
Acyl transferase domain;
493-810 2.08e-132

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 418.03  E-value: 2.08e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    493 WFICSGMGTQWRGMGLSLMRL-DRFRDSILRSDEAVKP-FGLKVSQLLLSTDESTFDDIVHSFVSLTAIQIGLIDLLSCM 570
Cdd:pfam00698    1 VFVFSGQGSQWAGMGMQLLKTsPAFAAVIDRADEAFKPqYGFSVSDVLRNNPEGTLDGTQFVQPALFAMQIALAALLQSY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    571 GLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEAHlPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVT 650
Cdd:pfam00698   81 GVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLA-GPGGMAAVELSAEEVEQRWPDDVVGAVVNSPRSVV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    651 ISGPQAPVFEFVEQLRKEGVFAkEVRTGGMAFHSYFMEAIAPPLLQELKKvIREPKPRSARWLSTSIPEaqwhsSLARTS 730
Cdd:pfam00698  160 ISGPQEAVRELVERVSKEGVGA-LVENVNYAVHSPQMDAIAPALLSALAD-IAPRTPRVPFISSTSIDP-----SDQRTL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    731 SAEYNVNNLVSPVLFQEALWHV--PEHAVVLEIAPHALLQAVLKRGLK-----PSCTIIPLMKKDHRDNLEFFLAGIGRL 803
Cdd:pfam00698  233 SAEYWVRNLRSPVRFAEAILSAaePGPLVFIEISPHPLLLAALIDTLKsasdgKVATLVGTLIRDQTDFLVTFLYILAVA 312

                   ....*..
gi 41872631    804 HLSGIDA 810
Cdd:pfam00698  313 HLTGSAP 319
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
1564-1854 2.29e-130

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 410.63  E-value: 2.29e-130
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1564 CTVYYASLNFRDIMLATGKLSPDAipgkwtsqdsLLGMEFSGRD----------ASGKRVMGLVPAkGLATSVLLSPDFL 1633
Cdd:smart00829    1 IEVRAAGLNFRDVLIALGLYPGEA----------VLGGECAGVVtrvgpgvtglAVGDRVMGLAPG-AFATRVVTDARLV 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1634 WDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLqaRFP 1713
Cdd:smart00829   70 VPIPDGWSFEEAATVPVVFLTAYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEKRDFL--RAL 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1714 QLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHG 1793
Cdd:smart00829  148 GIPDDHIFSSRDLSFADEILRATGGRGVDVVLNSLSGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLAMAPFRPNVSYHA 227
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41872631    1794 VLLDAFFnESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:smart00829  228 VDLDALE-EGPDRIRELLAEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
4-404 2.76e-118

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: 376.67  E-value: 2.76e-118
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631       4 VVIAGMSGKLPESENLQEFWDNLIGGVDmvtdddrrwkaglyglprrsgklkDLSRFDASFFGVHPKQAHTMDPQLRLLL 83
Cdd:smart00825    1 IAIVGMSCRFPGADDPEEFWDLLLAGLD------------------------DVDLFDAAFFGISPREAEAMDPQQRLLL 56
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631      84 EVTYEAIVDGGINPDSLRGTHTGVWVGVSGSEtsealsrdpetlvgYSMvgcqrammanrlsfffdfrgpsiALDTACSS 163
Cdd:smart00825   57 EVAWEALEDAGIDPESLRGSRTGVFVGVSSSD--------------YSV-----------------------TVDTACSS 99
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     164 SLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARR-- 241
Cdd:smart00825  100 SLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRdg 179
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     242 --VYATILNAGTNTDGFKEqGVTFPSGDIQeqlirslyqsagvapesfeyieahgtgtkvgdpqelngitralcatrqep 319
Cdd:smart00825  180 dpILAVIRGSAVNQDGRSN-GITAPSGPAQ-------------------------------------------------- 208
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     320 LLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPaLLDGRLQVVDQPLPVRGGN----VGINSFGF 395
Cdd:smart00825  209 LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHID-LEESPLRVPTELTPWPPPGrprrAGVSSFGF 287

                    ....*....
gi 41872631     396 GGSNVHIIL 404
Cdd:smart00825  288 GGTNAHVIL 296
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
1566-1854 1.62e-112

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 359.96  E-value: 1.62e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1566 VYYASLNFRDIMLATGKLSPDaipgkwtsqDSLLGMEFSGRD----------ASGKRVMGLVPaKGLATSVLLSPDFLWD 1635
Cdd:cd05195    7 VKAAGLNFRDVLVALGLLPGD---------ETPLGLECSGIVtrvgsgvtglKVGDRVMGLAP-GAFATHVRVDARLVVK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1636 VPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPql 1715
Cdd:cd05195   77 IPDSLSFEEAATLPVAYLTAYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGG-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1716 DSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVL 1795
Cdd:cd05195  155 PVDHIFSSRDLSFADGILRATGGRGVDVVLNSLSGELLRASWRCLAPFGRFVEIGKRDILSNSKLGMRPFLRNVSFSSVD 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 41872631 1796 LDAFFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd05195  235 LDQLARERPELLRELLREVLELLEAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
1876-2112 5.85e-100

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: 330.18  E-value: 5.85e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1876 ISKTFCPA--HKSYIIAGGLGGFGLELAQWLIQRGVQK-LVLTSRSGIRTGyQAKQVRRWRRQ---GVQVQVSTSNISSL 1949
Cdd:cd08954  208 ILKTNYPInlGKSYLITGGSGGLGLEILKWLVKRGAVEnIIILSRSGMKWE-LELLIREWKSQnikFHFVSVDVSDVSSL 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1950 EGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNA 2029
Cdd:cd08954  287 EKAINLILNAPKIGPIGGIFHLAFVLIDKVLEIDTESLFISVNKAKVMGAINLHNQSIKRCWKLDYFVLFSSVSSIRGSA 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2030 GQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGIlVETMSTNDTIVS--GTLPQRMASCLEVLDLFLN--QPHMV 2105
Cdd:cd08954  367 GQCNYVCANSVLDSLSRYRKSIGLPSIAINWGAIGDVGF-VSRNESVDTLLGgqGLLPQSINSCLGTLDLFLQnpSPNLV 445

                 ....*..
gi 41872631 2106 LSSFVLA 2112
Cdd:cd08954  446 LSSFNFA 452
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
2-239 2.50e-85

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: 279.91  E-value: 2.50e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631      2 EEVVIAGMSGKLPESENLQEFWDNLIGGVDMVT--DDDRRWKAGLYGLPRR--------SGKLKDLSRFDASFFGVHPKQ 71
Cdd:pfam00109    1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISeiPADRWDPDKLYDPPSRiagkiytkWGGLDDIFDFDPLFFGISPRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     72 AHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSE--ALSRDPETLVGYS-MVGCQRAMMANRLSFFF 148
Cdd:pfam00109   81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAAllLLDEDGGPRRGSPfAVGTMPSVIAGRISYFL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    149 DFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGV 228
Cdd:pfam00109  161 GLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGV 240
                          250
                   ....*....|.
gi 41872631    229 VAVLLTKKSLA 239
Cdd:pfam00109  241 GAVVLKRLSDA 251
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
1566-1856 3.23e-67

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 230.80  E-value: 3.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1566 VYYASLNFRDIMLATGKLSPD----AIPGkwtsqdsllgMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPD 1631
Cdd:COG0604   34 VKAAGVNPADLLIRRGLYPLPpglpFIPG----------SDAAGvvvavgegvtGFKVGDRVAGLGRGGGYAEYVVVPAD 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1632 FLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQAr 1711
Cdd:COG0604  104 QLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRA- 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1712 fpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTF 1791
Cdd:COG0604  183 ---LGADHVIDYREEDFAERVRALTGGRGVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTL 259
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41872631 1792 HGVLLDAFFNESS-ADWREVWALVQAgirdGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 1856
Cdd:COG0604  260 TGFTLFARDPAERrAALAELARLLAA----GKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTV 321
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
1555-1855 5.69e-62

Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176203 [Multi-domain]  Cd Length: 323  Bit Score: 215.83  E-value: 5.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1555 QPTCPGAQLCTVYYASLNFRDIMLATGK--LSPDA--IPGkwtsqdsllgMEFSGRDAS----------GKRVMGLVPAK 1620
Cdd:cd08241   23 EPGAPGEVRIRVEAAGVNFPDLLMIQGKyqVKPPLpfVPG----------SEVAGVVEAvgegvtgfkvGDRVVALTGQG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1621 GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVG 1700
Cdd:cd08241   93 GFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQPGETVLVLGAAGGVGLAAVQLAKALGARVIAAAS 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1701 SAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGkF------DL 1774
Cdd:cd08241  173 SEEKLALARA----LGADHVIDYRDPDLRERVKALTGGRGVDVVYDPVGGDVFEASLRSLAWGGRLLVIG-FasgeipQI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1775 SQNHPLgmaifLKNVTFHGVLLDAFFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd08241  248 PANLLL-----LKNISVVGVYWGAYARREPELLRANLAELFDLLAEGKIRPHVSAVFPLEQAAEALRALADRKATGKVVL 322

                 .
gi 41872631 1855 Q 1855
Cdd:cd08241  323 T 323
PKS_AT smart00827
Acyl transferase domain in polyketide synthase (PKS) enzymes;
497-788 5.41e-60

Acyl transferase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214838 [Multi-domain]  Cd Length: 298  Bit Score: 209.18  E-value: 5.41e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     497 SGMGTQWRGMGLSLMRLDR-FRDSILRSDEAVKPFGLK--VSQLLLSTDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLR 573
Cdd:smart00827    3 TGQGSQWAGMGRELYETEPvFREALDECDAALQPLLGWslLDVLLGEDGAASLLDTEVAQPALFAVQVALARLLRSWGVR 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     574 PDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEAHlPPGAMAAVGLSWEECKQRC---PPGVVPACHNSKDTVT 650
Cdd:smart00827   83 PDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALP-GGGAMLAVGLSEEEVEPLLagvPDRVSVAAVNSPSSVV 161
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     651 ISGPQAPVFEFVEQLRKEGVFAKEVRTgGMAFHSYFMEAIAPPLLQELKKVirEPKPRSARWLSTSipEAQWHSSlARTS 730
Cdd:smart00827  162 LSGDEDAVDELAARLEAEGIFARRLKV-DHAFHSPHMEPILDEFRAALAGL--TPRPPRIPFVSTV--TGTLIDG-AELD 235
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41872631     731 SAEYNVNNLVSPVLFQEA---LWHVPEHAVVLEIAPHALLQAVLKRGLK--PSCTIIPLMKKD 788
Cdd:smart00827  236 DADYWVRNLREPVRFADAvraLLAEGGVTVFLEVGPHPVLTGPIKQTLAaaGSAVVLPSLRRG 298
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
4-405 1.27e-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: 200.32  E-value: 1.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    4 VVIAGMSGKLPESENLQEFWDNLIGG---VDMVTDDDRRwkaglyGLPRR-SGKLKDlsrFDASFFgVHPKQAHTMDPQL 79
Cdd:COG0304    3 VVITGLGAVSPLGNGVEEFWEALLAGrsgIRPITRFDAS------GLPVRiAGEVKD---FDPEEY-LDRKELRRMDRFT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   80 RLLLEVTYEAIVDGGINPDSLRGTHTGVWVG--VSGSETSEA-----LSRDPE----TLVGYSMVGcqraMMANRLSFFF 148
Cdd:COG0304   73 QYALAAAREALADAGLDLDEVDPDRTGVIIGsgIGGLDTLEEayralLEKGPRrvspFFVPMMMPN----MAAGHVSIRF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  149 DFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLS-----PEGTCKAFDTAGNGYC 223
Cdd:COG0304  149 GLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALStrnddPEKASRPFDKDRDGFV 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  224 RSEGVVAVLLTKKSLAR----RVYATILNAGTNTDGFKeqgVTF--PSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGT 297
Cdd:COG0304  229 LGEGAGVLVLEELEHAKargaKIYAEVVGYGASSDAYH---ITApaPDGEGAARAMRAALKDAGLSPEDIDYINAHGTST 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  298 KVGDPQELNGITRALcATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPalLDGrlqVV 377
Cdd:COG0304  306 PLGDAAETKAIKRVF-GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECD--LDY---VP 379
                        410       420
                 ....*....|....*....|....*...
gi 41872631  378 DQPLPVRGGNVGINSFGFGGSNVHIILR 405
Cdd:COG0304  380 NEAREAKIDYALSNSFGFGGHNASLVFK 407
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
3-404 2.92e-54

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: 196.22  E-value: 2.92e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    3 EVVIAGMSGKLPESENLQEFWDNLIGG---VDMVTDDDRRWKAglyglPRRSGKLKDlsrFDASFFGVhPKQAHTMDPQL 79
Cdd:cd00834    2 RVVITGLGAVTPLGNGVEEFWEALLAGrsgIRPITRFDASGFP-----SRIAGEVPD---FDPEDYLD-RKELRRMDRFA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   80 RLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGS------ETSEALS-----RDPETLVGYSMVGcqraMMANRLSFFF 148
Cdd:cd00834   73 QFALAAAEEALADAGLDPEELDPERIGVVIGSGIGglatieEAYRALLekgprRVSPFFVPMALPN----MAAGQVAIRL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  149 DFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLS-----PEGTCKAFDTAGNGYC 223
Cdd:cd00834  149 GLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALStrnddPEKASRPFDKDRDGFV 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  224 RSEGVVAVLLTKKSLAR----RVYATILNAGTNTDGFKeqgVTFPS--GDIQEQLIRSLYQSAGVAPESFEYIEAHGTGT 297
Cdd:cd00834  229 LGEGAGVLVLESLEHAKargaKIYAEILGYGASSDAYH---ITAPDpdGEGAARAMRAALADAGLSPEDIDYINAHGTST 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  298 KVGDPQELNGITRALCaTRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPalLDGrlqVV 377
Cdd:cd00834  306 PLNDAAESKAIKRVFG-EHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD--LDY---VP 379
                        410       420
                 ....*....|....*....|....*..
gi 41872631  378 DQPLPVRGGNVGINSFGFGGSNVHIIL 404
Cdd:cd00834  380 NEAREAPIRYALSNSFGFGGHNASLVF 406
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
1901-2106 2.48e-53

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: 192.60  E-value: 2.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1901 AQWLIQRGVQKLVLTSRSGIRTGYQAkQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL 1980
Cdd:cd05274  167 ARWLAARGARHLVLLSRRGPAPRAAA-RAALLRAGGARVSVVRCDVTDPAALAALLAELAAGGPLAGVIHAAGVLRDALL 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1981 ENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQW 2060
Cdd:cd05274  246 AELTPAAFAAVLAAKVAGALNLHELTPDL--PLDFFVLFSSVAALLGGAGQAAYAAANAFLDALAAQRRRRGLPATSVQW 323
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 41872631 2061 GAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVL 2106
Cdd:cd05274  324 GAWAGGGMAAAAALRARLARSGLGPLAPAEALEALEALLASDAPQA 369
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
1566-1854 4.40e-53

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 189.96  E-value: 4.40e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1566 VYYASLNFRDIMLATGKLSPdaiPGKWTSqdsLLGMEFSGRDAS----------GKRVMGLVPAKGLATSVLLSPDFLWD 1635
Cdd:cd05276   34 VAAAGVNRADLLQRQGLYPP---PPGASD---ILGLEVAGVVVAvgpgvtgwkvGDRVCALLAGGGYAEYVVVPAGQLLP 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1636 VPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpQL 1715
Cdd:cd05276  108 VPEGLSLVEAAALPEVFFTAWQNLFQLGGLKAGETVLIHGGASGVGTAAIQLAKALGARVIATAGSEEKLEACR----AL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1716 DSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG-------KFDLsqnhplgMAIFLKN 1788
Cdd:cd05276  184 GADVAINYRTEDFAEEVKEATGGRGVDVILDMVGGDYLARNLRALAPDGRLVLIGllggakaELDL-------APLLRKR 256
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41872631 1789 VTFHG------------VLLDAFfnessadWREVWALvqagIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd05276  257 LTLTGstlrsrsleekaALAAAF-------REHVWPL----FASGRIRPVIDKVFPLEEAAEAHRRMESNEHIGKIVL 323
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
1897-2065 2.81e-52

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: 182.30  E-value: 2.81e-52
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1897 GLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVL 1975
Cdd:smart00822   13 GRALARWLAERGARRLVLLSRSGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIpAVEGPLTGVIHAAGVL 92
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1976 RDGLLENQTPEFFQDVCKPKYSGTLNLDRVTReaCPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPG 2055
Cdd:smart00822   93 DDGVLASLTPERFAAVLAPKAAGAWNLHELTA--DLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRRARGLPA 170
                           170
                    ....*....|
gi 41872631    2056 LAVQWGAIGD 2065
Cdd:smart00822  171 LSIAWGAWAE 180
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
1316-1522 6.79e-52

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: 191.12  E-value: 6.79e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1316 NCAVAALGDPASalSNMVAALREGGFLLLHTLLRGHPLGDIVAFlTSTEPQYGQGILSQDAWESLFS---RVSLRLVGLK 1392
Cdd:cd08954    5 VCNLVLNGNLQS--ENLYALLKPNGFLLFVEPLKGSTLGDTWWL-TDNDIRKQSCLLSQEQWNQLLKstqEVSIKLSGVK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1393 KSFYGSTLflCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEdSSRPVWLKAINCATSGVVGLVNCLRREPGGNRLRCV 1472
Cdd:cd08954   82 KSFYGSVL--CRIQSPTDKSEFLPVEEQTFEYVEILKSLLATA-SCKPVLLTADGCESSGVIGAVRYFREEPQLKLIRCL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 41872631 1473 LLSNLSSTSHvPEVDPGSAELQKVLQGDLVMNVYRDGAWGAFRHFLLEED 1522
Cdd:cd08954  159 FVSNLNSQKE-PIIRNGKVYYERVKKNSNIKNVYKSGSWGDFRHLLLDLS 207
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
362-472 4.21e-51

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: 176.20  E-value: 4.21e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    362 PNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQG 441
Cdd:pfam16197    1 PNPDIPALLDGRLKVVTEPTPWPGGIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLVLLSGRTEEAVKALLEKL 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 41872631    442 LRHSQDLAFLSMLNDIAAVPATAMPFRGYAV 472
Cdd:pfam16197   81 ENHLDDAEFLSLLNDIHSLPISGHPYRGYAI 111
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
4-835 3.36e-50

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: 197.92  E-value: 3.36e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631      4 VVIAGMSGKLPESENLQEFWDNLIGGVDMVTD-DDRRWKAGLY----------GLPRRSGKLKDLSrFDASFFGVHPKQA 72
Cdd:TIGR02813    9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITDvPSDHWAKDDYydsdkseadkSYCKRGGFLPEVD-FNPMEFGLPPNIL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     73 HTMDPQLRLLLEVTYEAIVDGGInPDSLRGTHTGVWVGVSGSET-SEALS-------------------RDPETL----- 127
Cdd:TIGR02813   88 ELTDISQLLSLVVAKEVLNDAGL-PDGYDRDKIGITLGVGGGQKqSSSLNarlqypvlkkvfkasgvedEDSEMLikkfq 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    128 ---VGY---SMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFL 201
Cdd:TIGR02813  167 dqyIHWeenSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFS 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    202 RLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARR----VYATILNAGTNTDGfKEQGVTFPSGDIQEQLIRSLY 277
Cdd:TIGR02813  247 KTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERdgdrIYAVIKGVGASSDG-KFKSIYAPRPEGQAKALKRAY 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    278 QSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEP--LLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAP 355
Cdd:TIGR02813  326 DDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPP 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    356 NLHFHSPNPEI-----PALLDGR----LQVVDQpLPVRGgnvGINSFGFGGSNVHIIL---RPNTQPPPAPAPHAtLPRL 423
Cdd:TIGR02813  406 TINVDQPNPKLdiensPFYLNTEtrpwMQREDG-TPRRA---GISSFGFGGTNFHMVLeeySPKHQRDDQYRQRA-VAQT 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    424 LRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAV-------PATAMPFRGYAVLGG--------------ERGGPEV 482
Cdd:TIGR02813  481 LLFTAANEKALVSSLKDWKNKLSAKADDQPYAFNALAventlrtIAVALARLGFVAKNAdelitmleqaitqlEAKSCEE 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    483 QQVPAG-----------ERPLWFICSGMGTQWRGMGLSLM-RLDRFRDSILRSDEAVKPFGL-KVSQLLLS----TDEST 545
Cdd:TIGR02813  561 WQLPSGisyrksalvveSGKVAALFAGQGSQYLNMGRELAcNFPEVRQAAADMDSVFTQAGKgALSPVLYPipvfNDESR 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    546 ------FDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKE--AHLPP 617
Cdd:TIGR02813  641 kaqeeaLTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMAAptGEADI 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    618 GAMAAVGLsweecKQRCPPGVVPAC-----------HNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGmAFHSYF 686
Cdd:TIGR02813  721 GFMYAVIL-----AVVGSPTVIANCikdfegvsianYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSG-AFHTPL 794
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    687 MEAIAPPLLQELKKViREPKPRSARWLSTSipeAQWHSSLARTSSAEYNvNNLVSPVLFQEALWHVPEHA--VVLEIAPH 764
Cdd:TIGR02813  795 VAHAQKPFSAAIDKA-KFNTPLVPLYSNGT---GKLHSNDAAAIKKALK-NHMLQSVHFSEQLEAMYAAGarVFVEFGPK 869
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    765 ALLQAVLKRGLKPS----CTII--PLMKKDHRDNLEFF---LAGIGrLHLSGIDANPNALFPPVEfPAP-----RGTPLI 830
Cdd:TIGR02813  870 NILQKLVENTLKDKenelCAISinPNPKGDSDMQLRQAavqLAVLG-LELTEIDPYQAEKRPPAA-TSPmniklNAANYI 947

                   ....*
gi 41872631    831 SPLIK 835
Cdd:TIGR02813  948 SPATR 952
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
1556-1856 2.37e-49

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 179.38  E-value: 2.37e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1556 PTC-PGAQLCTVYYASLNFRDIMLATGK--LSPDAIPgkwtsqdsLLGMEFSG----------RDASGKRVMGLVPAKGL 1622
Cdd:TIGR02824   23 PVPkAGEVLIRVAAAGVNRPDLLQRAGKypPPPGASD--------ILGLEVAGevvavgegvsRWKVGDRVCALVAGGGY 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1623 ATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSA 1702
Cdd:TIGR02824   95 AEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWSNLFQRGGLKAGETVLIHGGASGIGTTAIQLAKAFGARVFTTAGSD 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1703 EKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG-------KFDLs 1775
Cdd:TIGR02824  175 EKCAACEA----LGADIAINYREEDFVEVVKAETGGKGVDVILDIVGGSYLNRNIKALALDGRIVQIGfqggrkaELDL- 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1776 qnhplgMAIFLKNVTFHGVLL----DAFFNESSADWRE-VWALvqagIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIG 1850
Cdd:TIGR02824  250 ------GPLLAKRLTITGSTLrarpVAEKAAIAAELREhVWPL----LASGRVRPVIDKVFPLEDAAQAHALMESGDHIG 319

                   ....*.
gi 41872631   1851 KVVVQV 1856
Cdd:TIGR02824  320 KIVLTV 325
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
2242-2488 4.91e-47

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 169.11  E-value: 4.91e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   2242 RPLFLVHPIEGSTTVFHSLASRLSIPTygLQCTRAAP--------LDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACV 2313
Cdd:pfam00975    1 RPLFCFPPAGGSASSFRSLARRLPPPA--EVLAVQYPgrgrgeppLNSIEALADEYAEALRQIQPEGPYALFGHSMGGML 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   2314 AFEMCSQLQAQqspAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPgceaeaeteaicfFVQQFTDMEHNrvLEALLP---- 2389
Cdd:pfam00975   79 AFEVARRLERQ---GEAVRSLFLSDASAPHTVRYEASRAPDDDE-------------VVAEFTDEGGT--PEELLEdeel 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   2390 LKGLEERVAAAVDLIIKSHQGLDRQelsfaarsfyykLRAAEQYTPKAKYHGNVMLlraktggaygedlgaDYNLSQVCD 2469
Cdd:pfam00975  141 LSMLLPALRADYRALESYSCPPLDA------------QSATLFYGSDDPLHDADDL---------------AEWVRDHTP 193
                          250
                   ....*....|....*....
gi 41872631   2470 GKVSVHVIEGDHRTLLEGS 2488
Cdd:pfam00975  194 GEFDVHVFDGDHFYLIEHL 212
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
1554-1854 1.20e-46

polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 170.69  E-value: 1.20e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1554 AQPTCPGAQLCTVYYASLNFRDIMLATGkLSPDAIPGKWTSqdsllGMEFSG-RDASGKRVMGLVPAK-----------G 1621
Cdd:cd08251    2 VAPPGPGEVRIQVRAFSLNFGDLLCVRG-LYPTMPPYPFTP-----GFEASGvVRAVGPHVTRLAVGDeviagtgesmgG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1622 LATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGS 1701
Cdd:cd08251   76 HATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFA-RAGLAKGEHILIQTATGGTGLMAVQLARLKGAEIYATASS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1702 AEKRAYLQarfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLG 1781
Cdd:cd08251  155 DDKLEYLK----QLGVPHVINYVEEDFEEEIMRLTGGRGVDVVINTLSGEAIQKGLNCLAPGGRYVEIAMTALKSAPSVD 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41872631 1782 MAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd08251  231 LSVLSNNQSFHSVDLRKLLLLDPEFIADYQAEMVSLVEEGELRPTVSRIFPFDDIGEAYRYLSDRENIGKVVV 303
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
243-360 2.46e-44

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: 156.96  E-value: 2.46e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    243 YATILNAGTNTDGfKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCA-TRQEPLL 321
Cdd:pfam02801    1 YAVIKGSAVNHDG-RHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSgARKQPLA 79
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 41872631    322 IGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH 360
Cdd:pfam02801   80 IGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1554-1856 3.18e-42

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 158.88  E-value: 3.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1554 AQPTC-PGAQLCTVYYASLNFRDIMLATGKLS-PDAIPGkwtsqdsLLGMEFSG----------RDASGKRVMGLVPAKG 1621
Cdd:cd08272   21 PRPQPgPGQVLVRVHASGVNPLDTKIRRGGAAaRPPLPA-------ILGCDVAGvveavgegvtRFRVGDEVYGCAGGLG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1622 -----LATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVF 1696
Cdd:cd08272   94 glqgsLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEGLVDRAAVQAGQTVLIHGGAGGVGHVAVQLAKAAGARVY 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1697 TTVgSAEKRAYLQarfpQLDSTsFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGkfdLSQ 1776
Cdd:cd08272  174 ATA-SSEKAAFAR----SLGAD-PIIYYRETVVEYVAEHTGGRGFDVVFDTVGGETLDASFEAVALYGRVVSIL---GGA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1777 NHPLGMAIFlKNVTFHGV--LLDAFFNESSADWREVWALVQAGIRDGVVRP-LKCTVFHGAQVEDAFRYMAQGKHIGKVV 1853
Cdd:cd08272  245 THDLAPLSF-RNATYSGVftLLPLLTGEGRAHHGEILREAARLVERGQLRPlLDPRTFPLEEAAAAHARLESGSARGKIV 323

                 ...
gi 41872631 1854 VQV 1856
Cdd:cd08272  324 IDV 326
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
80-404 1.20e-41

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: 157.41  E-value: 1.20e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   80 RLLLEVTYEAIVDGGINPDSLRGTHTGVWVGvSGSETSEALSRDPETLVGYSMVGCQRAMM---ANRLSFFFDFRGPSIA 156
Cdd:cd00825   13 ILGFEAAERAIADAGLSREYQKNPIVGVVVG-TGGGSPRFQVFGADAMRAVGPYVVTKAMFpgaSGQIATPLGIHGPAYD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  157 LDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKK 236
Cdd:cd00825   92 VSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEEL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  237 SLARR----VYATILNAGTNTDGFKEqGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRAL 312
Cdd:cd00825  172 EHALArgahIYAEIVGTAATIDGAGM-GAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEF 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  313 catRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIpalldgrLQVVDQPLPVRGGNVGINS 392
Cdd:cd00825  251 ---GDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAG-------LNIVTETTPRELRTALLNG 320
                        330
                 ....*....|..
gi 41872631  393 FGFGGSNVHIIL 404
Cdd:cd00825  321 FGLGGTNATLVL 332
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
1886-2065 7.73e-41

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: 149.63  E-value: 7.73e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1886 SYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGP 1964
Cdd:pfam08659    2 TYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIkAEGPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1965 VGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERI 2044
Cdd:pfam08659   82 IRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDE--PLDFFVLFSSIAGLLGSPGQANYAAANAFLDAL 159
                          170       180
                   ....*....|....*....|.
gi 41872631   2045 CEKRRHEGLPGLAVQWGAIGD 2065
Cdd:pfam08659  160 AEYRRSQGLPATSINWGPWAE 180
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1566-1856 4.65e-39

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 150.04  E-value: 4.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1566 VYYASLNFRDIMLATGkLSPDAIPGKWTsqdslLGMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPDFLWD 1635
Cdd:cd08275   33 VEACGLNFADLMARQG-LYDSAPKPPFV-----PGFECAGtveavgegvkDFKVGDRVMGLTRFGGYAEVVNVPADQVFP 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1636 VPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLgcRVFTTVG--SAEKRAYLQARFp 1713
Cdd:cd08275  107 LPDGMSFEEAAAFPVNYLTAYYALFELGNLRPGQSVLVHSAAGGVGLAAGQLCKTV--PNVTVVGtaSASKHEALKENG- 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1714 qldstsFANSRDTSFEQHV--LWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLK---- 1787
Cdd:cd08275  184 ------VTHVIDYRTQDYVeeVKKISPEGVDIVLDALGGEDTRKSYDLLKPMGRLVVYGAANLVTGEKRSWFKLAKkwwn 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1788 ------------NVTFHGVLLDAFFNESSADwREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQ 1855
Cdd:cd08275  258 rpkvdpmkliseNKSVLGFNLGWLFEERELL-TEVMDKLLKLYEEGKIKPKIDSVFPFEEVGEAMRRLQSRKNIGKVVLT 336

                 .
gi 41872631 1856 V 1856
Cdd:cd08275  337 P 337
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
2-404 9.84e-39

"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: 151.05  E-value: 9.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    2 EEVVIAGMSGKLPESENL---QEFWDNLIGGVDMVTDDDRRwkagLYGLPRRSGKlkDLSRFDasFFGVHPKQAHTMDPQ 78
Cdd:cd00828    1 SRVVITGIGVVSPHGEGCdevEEFWEALREGRSGIAPVARL----KSRFDRGVAG--QIPTGD--IPGWDAKRTGIVDRT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   79 LRLLLEVTYEAIVDGGIN-PDSLRGTHTGVWVGVSGSETsEALSRD-------------PETLVGYSMVGCQRAMMANRL 144
Cdd:cd00828   73 TLLALVATEEALADAGITdPYEVHPSEVGVVVGSGMGGL-RFLRRGgkldaravnpyvsPKWMLSPNTVAGWVNILLLSS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  145 sfffdfRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINvLLKPNTSVQFLRLGMLS-----PEGTCKAFDTAG 219
Cdd:cd00828  152 ------HGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVE-DPLEEGLSGFANMGALStaeeePEEMSRPFDETR 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  220 NGYCRSEGVVAVLLTKKSLAR----RVYATILNAGTNTDGFKEQGVtfPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGT 295
Cdd:cd00828  225 DGFVEAEGAGVLVLERAELALargaPIYGRVAGTASTTDGAGRSVP--AGGKGIARAIRTALAKAGLSLDDLDVISAHGT 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  296 GTKVGDPQELNGITRALcATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPALLDGRLq 375
Cdd:cd00828  303 STPANDVAESRAIAEVA-GALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGL- 380
                        410       420
                 ....*....|....*....|....*....
gi 41872631  376 vvDQPLPVRGGNVGINSFGFGGSNVHIIL 404
Cdd:cd00828  381 --SRDLNLKVRAALVNAFGFGGSNAALVL 407
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
1604-1856 3.58e-38

Alcohol dehydrogenases of the MDR family; This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 147.40  E-value: 3.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1604 SGRDA--SGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVG 1681
Cdd:cd08266  101 AGRENlcAQYGILGEHVDGGYAEYVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHMLVTRARLRPGETVLVHGAGSGVG 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1682 QAAIAIALSLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLA 1761
Cdd:cd08266  181 SAAIQIAKLFGATVIATAGSEDKLERAKE----LGADYVIDYRKEDFVREVRELTGKRGVDVVVEHVGAATWEKSLKSLA 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1762 THGRFLEIG-------KFDLsqnhplgMAIFLKNVTFHGVlldafFNESSADWREVWALVQAgirdGVVRPLKCTVFHGA 1834
Cdd:cd08266  257 RGGRLVTCGattgyeaPIDL-------RHVFWRQLSILGS-----TMGTKAELDEALRLVFR----GKLKPVIDSVFPLE 320
                        250       260
                 ....*....|....*....|..
gi 41872631 1835 QVEDAFRYMAQGKHIGKVVVQV 1856
Cdd:cd08266  321 EAAEAHRRLESREQFGKIVLTP 342
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1566-1814 4.47e-38

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 145.16  E-value: 4.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1566 VYYASLNFRDIMLATGKLSPDAIPGkwtsqdSLLGMEFSGR-DASGKRVMGLVPAK------------------------ 1620
Cdd:cd05188    6 VEAAGLCGTDLHIRRGGYPPPPKLP------LILGHEGAGVvVEVGPGVTGVKVGDrvvvlpnlgcgtcelcrelcpggg 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1621 --------GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHsGSGGVGQAAIAIALSLG 1692
Cdd:cd05188   80 ilgegldgGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDTVLVL-GAGGVGLLAAQLAKAAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1693 CRVFTTVGSAEKRAYLQarfpQLDSTSFANSRDTSFEQHVLWhTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGK 1771
Cdd:cd05188  159 ARVIVTDRSDEKLELAK----ELGADHVIDYKEEDLEEELRL-TGGGGADVVIDAVgGPETLAQALRLLRPGGRIVVVGG 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 41872631 1772 FDLSQNHPLGMAIFLKNVTFHGVLLDaffneSSADWREVWALV 1814
Cdd:cd05188  234 TSGGPPLDDLRRLLFKELTIIGSTGG-----TREDFEEALDLL 271
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
1901-2071 4.49e-36

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: 142.42  E-value: 4.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1901 AQWLIQRGVQKLVLTSRSGIrTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAE-AAQLGPVGGVFNLAVVLRDGL 1979
Cdd:cd08955  166 AEWLVERGARHLVLTGRRAP-SAAARQAIAALEEAGAEVVVLAADVSDRDALAAALAQiRASLPPLRGVIHAAGVLDDGV 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1980 LENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQ 2059
Cdd:cd08955  245 LANQDWERFRKVLAPKVQGAWNLHQLTQDL--PLDFFVLFSSVASLLGSPGQANYAAANAFLDALAHYRRARGLPALSIN 322
                        170
                 ....*....|..
gi 41872631 2060 WGAIGDVGILVE 2071
Cdd:cd08955  323 WGPWAEVGMAAS 334
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1553-1856 5.96e-36

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 140.81  E-value: 5.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1553 HAQPTCPGAQ--LCTVYYASLNFRDIMLATGKLSPDAIPGkwtsqdSLLGMEFSGR-DASGKRVMGLVPAK--------- 1620
Cdd:cd08268   19 ELPVPAPGAGevLIRVEAIGLNRADAMFRRGAYIEPPPLP------ARLGYEAAGVvEAVGAGVTGFAVGDrvsvipaad 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1621 -----GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRV 1695
Cdd:cd08268   93 lgqygTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELAGLRPGDSVLITAASSSVGLAAIQIANAAGATV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1696 FTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLS 1775
Cdd:cd08268  173 IATTRTSEKRDALLA----LGAAHVIVTDEEDLVAEVLRITGGKGVDVVFDPVGGPQFAKLADALAPGGTLVVYGALSGE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1776 QNhPLGM-AIFLKNVTFHGVLLDAFFNESSADwREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd08268  249 PT-PFPLkAALKKSLTFRGYSLDEITLDPEAR-RRAIAFILDGLASGALKPVVDRVFPFDDIVEAHRYLESGQQIGKIVV 326

                 ..
gi 41872631 1855 QV 1856
Cdd:cd08268  327 TP 328
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
1626-1856 1.47e-35

Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 139.26  E-value: 1.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1626 VLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKR 1705
Cdd:cd08253  103 VVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAGAKAGETVLVHGGSGAVGHAAVQLARWAGARVIATASSAEGA 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1706 AYlqARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGmAIF 1785
Cdd:cd08253  183 EL--VR--QAGADAVFNYRAEDLADRILAATAGQGVDVIIEVLANVNLAKDLDVLAPGGRIVVYGSGGLRGTIPIN-PLM 257
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41872631 1786 LKNVTFHGVLLdafFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 1856
Cdd:cd08253  258 AKEASIRGVLL---YTATPEERAAAAEAIAAGLADGALRPVIAREYPLEEAAAAHEAVESGGAIGKVVLDP 325
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1569-1856 1.40e-34

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 136.90  E-value: 1.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1569 ASLNFRDIMLATGK----LSPDAIPG---------------KWTSQDSLLGMEF----SGR--DASGKRVMGLVPAKGLA 1623
Cdd:cd08276   37 VSLNYRDLLILNGRypppVKDPLIPLsdgagevvavgegvtRFKVGDRVVPTFFpnwlDGPptAEDEASALGGPIDGVLA 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1624 TSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHsGSGGVGQAAIAIALSLGCRVFTTVGSAE 1703
Cdd:cd08276  117 EYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFGLGPLKPGDTVLVQ-GTGGVSLFALQFAKAAGARVIATSSSDE 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1704 KRAYLQArfpqLDSTSFANSRDTS-FEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGM 1782
Cdd:cd08276  196 KLERAKA----LGADHVINYRTTPdWGEEVLKLTGGRGVDHVVEVGGPGTLAQSIKAVAPGGVISLIGFLSGFEAPVLLL 271
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41872631 1783 AIFLKNVTFHGVlldafFNESSADWRevwALVQAGIRDGvVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 1856
Cdd:cd08276  272 PLLTKGATLRGI-----AVGSRAQFE---AMNRAIEAHR-IRPVIDRVFPFEEAKEAYRYLESGSHFGKVVIRV 336
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
1566-1854 1.99e-34

alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 135.77  E-value: 1.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1566 VYYASLNFRDIMLATGKLS---PDAIPgkwtsqdSLLGMEFSGR-DASGK---------RVMGLVPAK---GLATSVLLS 1629
Cdd:cd05289   34 VHAAGVNPVDLKIREGLLKaafPLTLP-------LIPGHDVAGVvVAVGPgvtgfkvgdEVFGMTPFTrggAYAEYVVVP 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1630 PDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVgSAEKRAYLQ 1709
Cdd:cd05289  107 ADELALKPANLSFEEAAALPLAGLTAWQALFELGGLKAGQTVLIHGAAGGVGSFAVQLAKARGARVIATA-SAANADFLR 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1710 ArfpqLDSTSFANSRDTSFEQHVLWHtggkGVDLVLNSLAEEKLQASVRCLATHGRFLEIgkfdlsqnhpLGMAIFLKNV 1789
Cdd:cd05289  186 S----LGADEVIDYTKGDFERAAAPG----GVDAVLDTVGGETLARSLALVKPGGRLVSI----------AGPPPAEQAA 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41872631 1790 TFHGVLLDAFF-NESSADWREVWALVqagiRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd05289  248 KRRGVRAGFVFvEPDGEQLAELAELV----EAGKLRPVVDRVFPLEDAAEAHERLESGHARGKVVL 309
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1-406 3.91e-33

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 134.74  E-value: 3.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     1 MEEVVIAGMSGKLPESENLQEFWDNLIGG---VDMVTDDDRRwkaglyGLPRR-SGKLKDLSR-----FDASFFgVHPKQ 71
Cdd:PRK06333    3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGqsgIRTLTDFPVG------DLATKiGGQVPDLAEdaeagFDPDRY-LDPKD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    72 AHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTH-TGVWV--GVSGSET-SEA----LSRDPETL----VGYSMVGcqraM 139
Cdd:PRK06333   76 QRKMDRFILFAMAAAKEALAQAGWDPDTLEDRErTATIIgsGVGGFPAiAEAvrtlDSRGPRRLspftIPSFLTN----M 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   140 MANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLS------PEGTCK 213
Cdd:PRK06333  152 AAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALStrfndaPEQASR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   214 AFDTAGNGYCRSEGvvAVLLTKKSL----AR--RVYATILNAGTNTDGFKeqgVTFP--SGDIQEQLIRSLYQSAGVAPE 285
Cdd:PRK06333  232 PFDRDRDGFVMGEG--AGILVIETLehalARgaPPLAELVGYGTSADAYH---MTAGpeDGEGARRAMLIALRQAGIPPE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   286 SFEYIEAHGTGTKVGDPQELNGITRALCATRQepLLIGSTKSNMGHPEPAS-GLAALAKVlLSLEHGLWAPNLHFHSPNP 364
Cdd:PRK06333  307 EVQHLNAHATSTPVGDLGEVAAIKKVFGHVSG--LAVSSTKSATGHLLGAAgGVEAIFTI-LALRDQIAPPTLNLENPDP 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 41872631   365 EIpallDGrLQVVD---QPLPVRggnVGI-NSFGFGGSNVHIILRP 406
Cdd:PRK06333  384 AA----EG-LDVVAnkaRPMDMD---YALsNGFGFGGVNASILFRR 421
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1566-1854 6.01e-33

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 131.57  E-value: 6.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1566 VYYASLNFRDIMLATGKLSPD-AIPGKWTsqdslLGMEFSGR-DASGK---------RVMGLVPAKG---LATSVLLSPD 1631
Cdd:cd08267   33 VHAASVNPVDWKLRRGPPKLLlGRPFPPI-----PGMDFAGEvVAVGSgvtrfkvgdEVFGRLPPKGggaLAEYVVAPES 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1632 FLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVfTTVGSAEKRAYLQar 1711
Cdd:cd08267  108 GLAKKPEGVSFEEAAALPVAGLTALQALRDAGKVKPGQRVLINGASGGVGTFAVQIAKALGAHV-TGVCSTRNAELVR-- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1712 fpQLDSTSFANSRDTSFeqhVLWHTGGKGVDLVLNSLAEEK--LQASVRCLATHGRFLEIGkfdlSQNHPLGMAIFLKNV 1789
Cdd:cd08267  185 --SLGADEVIDYTTEDF---VALTAGGEKYDVIFDAVGNSPfsLYRASLALKPGGRYVSVG----GGPSGLLLVLLLLPL 255
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41872631 1790 TFHGV---LLDAFFNESSADWREVWALVQAGIrdgvVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd08267  256 TLGGGgrrLKFFLAKPNAEDLEQLAELVEEGK----LKPVIDSVYPLEDAPEAYRRLKSGRARGKVVI 319
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
2042-2491 1.71e-31

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 135.22  E-value: 1.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2042 ERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKAAAYRDR 2121
Cdd:COG3319  410 LREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLA 489
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2122 DSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELA 2201
Cdd:COG3319  490 ALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLL 569
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2202 CPTPKEDGLAQQQTQLNLRSLLVNPEGPTlmrlnsvqSSERPLFLVHPIEGSTTVFHSLASRLS--IPTYGLQC----TR 2275
Cdd:COG3319  570 APTLAALAAALAAAAAAAALSPLVPLRAG--------GSGPPLFCVHPAGGNVLCYRPLARALGpdRPVYGLQApgldGG 641
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2276 AAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQ-QSPApthnSLFLFDgspTYVLAYTqsyrak 2354
Cdd:COG3319  642 EPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQgEEVA----LLVLLD---SYAPGAL------ 708
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2355 ltpgcEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSH--QGLDRQELSFAARSFYYKLRAAEQ 2432
Cdd:COG3319  709 -----ARLDEAELLAALLRDLARGVDLPLDAEELRALDPEERLARLLERLREAGlpAGLDAERLRRLLRVFRANLRALRR 783
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 41872631 2433 YTPKAkYHGNVMLLRAkTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLE 2491
Cdd:COG3319  784 YRPRP-YDGPVLLFRA-EEDPPGRADDPALGWRPLVAGGLEVHDVPGDHFSMLREPHVA 840
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
1-405 3.76e-31

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 128.75  E-value: 3.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     1 MEEVVIAGMSGKLPESENLQEFWDNLIGGvdmvtdddrrwkaglyglprRSGkLKDLSRFDASFFGVH------------ 68
Cdd:PRK07314    1 KRRVVVTGLGAVSPLGNDVESTWKNLLAG--------------------KSG-IGPITHFDTSDLAVKiagevkdfnpdd 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    69 ---PKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWV--GVSGSETSEalsrdpETLVGYSMVGCQR------ 137
Cdd:PRK07314   60 ymsRKEARRMDRFIQYGIAAAKQAVEDAGLEITEENADRIGVIIgsGIGGLETIE------EQHITLLEKGPRRvspffv 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   138 -AMMAN----RLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINvllKPNTsvqflRLGM------- 205
Cdd:PRK07314  134 pMAIINmaagHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAE---AAIT-----PLGIagfaaar 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   206 -LS-----PEGTCKAFDTAGNGYCRSEGVVAVLLT--KKSLAR--RVYATILNAGTNTDGFKeqgVTFPS--GDIQEQLI 273
Cdd:PRK07314  206 aLStrnddPERASRPFDKDRDGFVMGEGAGILVLEelEHAKARgaKIYAEVVGYGMTGDAYH---MTAPApdGEGAARAM 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   274 RSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEpLLIGSTKSNMGHPEPASG-LAALAKVlLSLEHGL 352
Cdd:PRK07314  283 KLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFGEHAYK-VAVSSTKSMTGHLLGAAGaVEAIFSV-LAIRDQV 360
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 41872631   353 WAPNLHFHSPNPEIPalLDgrlQVVDQPLPvRGGNVGI-NSFGFGGSNVHIILR 405
Cdd:PRK07314  361 IPPTINLDNPDEECD--LD---YVPNEARE-RKIDYALsNSFGFGGTNASLVFK 408
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
18-405 7.65e-31

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 127.89  E-value: 7.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    18 NLQEFWDNLIGG---VDMVTD--------DDRRWKAGLY--GLPRRSGKLKDLSRFDASFFGVHPKQahtmDPQLRLLLE 84
Cdd:PTZ00050    8 GAESTWEALIAGksgIRKLTEfpkflpdcIPEQKALENLvaAMPCQIAAEVDQSEFDPSDFAPTKRE----SRATHFAMA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    85 VTYEAIVDGGINPDS-LRGTHTGVWVGVS-------GSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIA 156
Cdd:PTZ00050   84 AAREALADAKLDILSeKDQERIGVNIGSGigsladlTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLKGPSGS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   157 LDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLS------PEGTCKAFDTAGNGYCRSEGVVA 230
Cdd:PTZ00050  164 AVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtkynddPQRASRPFDKDRAGFVMGEGAGI 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   231 VLLTKKSLARR----VYATILNAGTNTDGFKeqgVTFPSGDiQEQLIRSLYQ----SAGVAPESFEYIEAHGTGTKVGDP 302
Cdd:PTZ00050  244 LVLEELEHALRrgakIYAEIRGYGSSSDAHH---ITAPHPD-GRGARRCMENalkdGANININDVDYVNAHATSTPIGDK 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   303 QELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEipalLDGRLQVVDQPLP 382
Cdd:PTZ00050  320 IELKAIKKVFGDSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAE----CDLNLVQGKTAHP 395
                         410       420
                  ....*....|....*....|....
gi 41872631   383 VRGGNVGI-NSFGFGGSNVHIILR 405
Cdd:PTZ00050  396 LQSIDAVLsTSFGFGGVNTALLFT 419
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
1563-1856 2.26e-29

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 121.68  E-value: 2.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1563 LCTVYYASLNFRDIMLATGKLSPDaiPGkwtsQDSLLGMEFSG----------RDASGKRVMGLVPAKGLATSVLLSPDF 1632
Cdd:PTZ00354   32 LIKVSAAGVNRADTLQRQGKYPPP--PG----SSEILGLEVAGyvedvgsdvkRFKEGDRVMALLPGGGYAEYAVAHKGH 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1633 LWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarf 1712
Cdd:PTZ00354  106 VMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDFCK--- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1713 pQLDSTSFANSRD-TSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG--------KFDLsqnhplgMA 1783
Cdd:PTZ00354  183 -KLAAIILIRYPDeEGFAPKVKKLTGEKGVNLVLDCVGGSYLSETAEVLAVDGKWIVYGfmggakveKFNL-------LP 254
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41872631  1784 IFLKNVTFHGVLL----DAFFNESSADW-REVWALvqagIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 1856
Cdd:PTZ00354  255 LLRKRASIIFSTLrsrsDEYKADLVASFeREVLPY----MEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLTV 328
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
1901-2077 5.87e-28

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: 119.78  E-value: 5.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1901 AQWLIQRGVQKLVLTSRSGI--RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRD 1977
Cdd:cd08953  222 ARALARRYGARLVLLGRSPLppEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVrERYGAIDGVIHAAGVLRD 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1978 GLLENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRR--HEGLPG 2055
Cdd:cd08953  302 ALLAQKTAEDFEAVLAPKVDGLLNLAQALADE--PLDFFVLFSSVSAFFGGAGQADYAAANAFLDAFAAYLRqrGPQGRV 379
                        170       180
                 ....*....|....*....|..
gi 41872631 2056 LAVQWGAIGDVGilvetMSTND 2077
Cdd:cd08953  380 LSINWPAWREGG-----MAADL 396
FabD COG0331
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...
494-776 4.81e-27

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: 114.07  E-value: 4.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  494 FICSGMGTQWRGMGLSLMRL-DRFRDSILRSDEAVkpfGLKVSQLLLSTDESTFDDIVHSFVSLTAIQIGLIDLLSCMGL 572
Cdd:COG0331    5 FLFPGQGSQYVGMGKDLYENfPVAREVFEEASEAL---GYDLSALCFEGPEEELNLTENTQPAILAASVAAYRALEEEGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  573 RPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEA-HLPPGAMAAV-GLSWEECKQRC-----PPGVVPACHNS 645
Cdd:COG0331   82 RPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAvPAGPGGMAAVlGLDDEEVEALCaeaaqGEVVEIANYNS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  646 KDTVTISGPQAPVFEFVEQLRKEGvfAKEVR----TGgmAFHSYFMEAIAPPLLQELKKV-IREPKPR-----SARWLST 715
Cdd:COG0331  162 PGQIVISGEKEAVEAAAELAKEAG--AKRAVplpvSG--PFHTPLMAPAAEKLAEALAAVtFADPKIPvvsnvDAAPVTD 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41872631  716 --SIPEAqwhssLARtssaeynvnNLVSPVLFQEALWHVPEHAV--VLEIAPHALLQAVLKRGLK 776
Cdd:COG0331  238 peEIREL-----LVR---------QLTSPVRWDESVEALAEAGVttFVELGPGKVLSGLVKRIDP 288
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
141-404 7.26e-27

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 116.27  E-value: 7.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   141 ANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLS-----PEGTCKAF 215
Cdd:PRK06501  155 ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALStqndpPEKASKPF 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   216 DTAGNGYCRSEGVVAVLLT--KKSLAR--RVYATILNAGTNTDGFkEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIE 291
Cdd:PRK06501  235 SKDRDGFVMAEGAGALVLEslESAVARgaKILGIVAGCGEKADSF-HRTRSSPDGSPAIGAIRAALADAGLTPEQIDYIN 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   292 AHGTGTKVGDPQELNGITrALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPalld 371
Cdd:PRK06501  314 AHGTSTPENDKMEYLGLS-AVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIP---- 388
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 41872631   372 grLQVVdqPLPVRGGNVGI---NSFGFGGSNVHIIL 404
Cdd:PRK06501  389 --LDVV--PNVARDARVTAvlsNSFGFGGQNASLVL 420
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1563-1855 1.95e-26

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 112.74  E-value: 1.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1563 LCTVYYASLNFRDIMLATGkLSPDAIPGKWTSQDSLLGMEFS-GRDAS----GKRVMGLVPAKGLATSVLLSPDFLWDVP 1637
Cdd:cd08273   31 VVKVEASGVSFADVQMRRG-LYPDQPPLPFTPGYDLVGRVDAlGSGVTgfevGDRVAALTRVGGNAEYINLDAKYLVPVP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1638 SNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVgSAEKRAYLQarfpQLDS 1717
Cdd:cd08273  110 EGVDAAEAVCLVLNYVTAYQMLHRAAKVLTGQRVLIHGASGGVGQALLELALLAGAEVYGTA-SERNHAALR----ELGA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1718 TSFANSRDTSFEQHVLwhtgGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGK------FDLSQNHPLGMAIFL----- 1786
Cdd:cd08273  185 TPIDYRTKDWLPAMLT----PGGVDVVFDGVGGESYEESYAALAPGGTLVCYGGnssllqGRRSLAALGSLLARLaklkl 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41872631 1787 ----KNVTFHGVllDAFFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQ 1855
Cdd:cd08273  261 lptgRRATFYYV--WRDRAEDPKLFRQDLTELLDLLAKGKIRPKIAKRLPLSEVAEAHRLLESGKVVGKIVLL 331
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
1-405 2.12e-26

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 114.31  E-value: 2.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     1 MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVT--DDDRRWkAGL----------YGLPrrsgklKDLSRfdasffgvh 68
Cdd:PRK09116    1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRrmPEWDRY-DGLntrlaapiddFELP------AHYTR--------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    69 pKQAHTMDPQLRLLLEVTYEAIVDGG-INPDSLRGTHTGVWVGVSGSETSEA-------LSRDPETLVGYSMVgcqrAMM 140
Cdd:PRK09116   65 -KKIRSMGRVSLMATRASELALEDAGlLGDPILTDGRMGIAYGSSTGSTDPIgafgtmlLEGSMSGITATTYV----RMM 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   141 ----ANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLkPNTSVQFLRLGMLS-----PEGT 211
Cdd:PRK09116  140 phttAVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELC-PTEAAVFDTLFATStrndaPELT 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   212 CKAFDTAGNGYCRSEGVVAVLLTK--KSLAR--RVYATILNAGTNTDGfkeQGVTFPSGDIQEQLIRSLYQSAGVAPESF 287
Cdd:PRK09116  219 PRPFDANRDGLVIGEGAGTLVLEEleHAKARgaTIYAEIVGFGTNSDG---AHVTQPQAETMQIAMELALKDAGLAPEDI 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   288 EYIEAHGTGTKVGDPQElngiTRALCATRQEPLLIGSTKSNMGHPEPASGlaALaKVLLSLE---HGLWAPNLHFHSPNP 364
Cdd:PRK09116  296 GYVNAHGTATDRGDIAE----SQATAAVFGARMPISSLKSYFGHTLGACG--AL-EAWMSIEmmnEGWFAPTLNLTQVDP 368
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 41872631   365 EIPAlLDgrlQVVDQPLPVRGGNVGINSFGFGGSNVHIILR 405
Cdd:PRK09116  369 ACGA-LD---YIMGEAREIDTEYVMSNNFAFGGINTSLIFK 405
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
1901-2067 2.39e-25

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: 112.65  E-value: 2.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1901 AQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL 1980
Cdd:cd08952  247 ARWLARRGAEHLVLTSRRGPDAPGAAELVAELTALGARVTVAACDVADRDALAALLAALPAGHPLTAVVHAAGVLDDGPL 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1981 ENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQW 2060
Cdd:cd08952  327 DDLTPERLAEVLRAKVAGARHLDELTRDR--DLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALAERRRARGLPATSVAW 404

                 ....*..
gi 41872631 2061 GAIGDVG 2067
Cdd:cd08952  405 GPWAGGG 411
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
4-405 3.57e-25

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 110.86  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     4 VVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRrWKAGLYGlPRRSGKLKDlsrFDASFFgVHPKQAHTMDPQLRLLL 83
Cdd:PRK08722    6 VVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEH-FDTTNFS-TRFAGLVKD---FNCEEY-MSKKDARKMDLFIQYGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    84 EVTYEAIVDGGINPDSLRGTHTGVWVG--VSGSETSEA-----LSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIA 156
Cdd:PRK08722   80 AAGIQALDDSGLEVTEENAHRIGVAIGsgIGGLGLIEAghqalVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   157 LDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLS-----PEGTCKAFDTAGNGYCRSEGVVAV 231
Cdd:PRK08722  160 ISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALStrndePQKASRPWDKDRDGFVLGDGAGMM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   232 LLTK----KSLARRVYATILNAGTNTDGFKEQGVTfPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNG 307
Cdd:PRK08722  240 VLEEyehaKARGAKIYAELVGFGMSGDAYHMTSPS-EDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   308 ITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHspNPEIPALLDgrlQVVDQPLPVRGGN 387
Cdd:PRK08722  319 IKRALGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLD--DPEEGLDID---LVPHTARKVESME 393
                         410
                  ....*....|....*....
gi 41872631   388 VGI-NSFGFGGSNVHIILR 405
Cdd:PRK08722  394 YAIcNSFGFGGTNGSLIFK 412
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
88-405 1.70e-24

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 108.60  E-value: 1.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    88 EAIVDGGINPDSLRGTHTGVWVGVSGSETS---EAL--SRDPETL--VGYSMVgcQRAMMANR---LSFFFDFRGPSIAL 157
Cdd:PRK07967   81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRnqvEAAdaMRGPRGPkrVGPYAV--TKAMASTVsacLATPFKIKGVNYSI 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   158 DTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLlKPNTSVQFLRLGMLS------PEGTCKAFDT-------AGNGycr 224
Cdd:PRK07967  159 SSACATSAHCIGNAVEQIQLGKQDIVFAGGGEEL-DWEMSCLFDAMGALStkyndtPEKASRAYDAnrdgfviAGGG--- 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   225 seGVVAVLLTKKSLAR--RVYATILNAGTNTDGFKeqgVTFPSGdiqEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDP 302
Cdd:PRK07967  235 --GVVVVEELEHALARgaKIYAEIVGYGATSDGYD---MVAPSG---EGAVRCMQMALATVDTPIDYINTHGTSTPVGDV 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   303 QELNGItRALCATRQEPllIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPALLDGRLQVVDQPLp 382
Cdd:PRK07967  307 KELGAI-REVFGDKSPA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAEL- 382
                         330       340
                  ....*....|....*....|...
gi 41872631   383 vrgGNVGINSFGFGGSNVHIILR 405
Cdd:PRK07967  383 ---TTVMSNSFGFGGTNATLVFR 402
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
81-405 1.71e-24

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 108.22  E-value: 1.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    81 LLLEVTYEAIVDGGINPDSlrgTHTGVWVGvsgseTSEALSRDPETLVGYSMVGCQRAMMANRLSFFFDF---------- 150
Cdd:PRK05952   59 LTKTVVTAALKDAGLTPPL---TDCGVVIG-----SSRGCQGQWEKLARQMYQGDDSPDEELDLENWLDTlphqaaiaaa 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   151 -----RGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGtCKAFDTAGNGYCRS 225
Cdd:PRK05952  131 rqigtQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLG 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   226 EGVVAVLLTKKSLAR----RVYATILNAGTNTDGFKeqgVTFPSGD-------IQEQLIRSlyqsaGVAPESFEYIEAHG 294
Cdd:PRK05952  210 EGGAILVLESAELAQkrgaKIYGQILGFGLTCDAYH---MSAPEPDgksaiaaIQQCLARS-----GLTPEDIDYIHAHG 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   295 TGTKVGDPQELNGItRALCATRqepLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEipalldgrL 374
Cdd:PRK05952  282 TATRLNDQREANLI-QALFPHR---VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFD--------L 349
                         330       340       350
                  ....*....|....*....|....*....|.
gi 41872631   375 QVVDQPLPVRGGNVGINSFGFGGSNVHIILR 405
Cdd:PRK05952  350 NFVRQAQQSPLQNVLCLSFGFGGQNAAIALG 380
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
106-404 2.62e-24

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 108.01  E-value: 2.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   106 GVWVGVSGS---ETSEALS-RDPETlvGYSMVGCQRAMM-----ANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIH 176
Cdd:PRK09185   98 GVVLGTSTSgilEGELAYRrRDPAH--GALPADYHYAQQelgslADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLE 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   177 SGQCPAAIVGGINVLLKpnTSVQ-FLRLGMLSPEgTCKAFDTAGNGYCRSEGVVAVLLTKKSLARrvyATILNAGTNTDG 255
Cdd:PRK09185  176 AGLCDAAIVGGVDSLCR--LTLNgFNSLESLSPQ-PCRPFSANRDGINIGEAAAFFLLEREDDAA---VALLGVGESSDA 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   256 FkEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQElngiTRALCATRQEPLLIGSTKSNMGHPEPA 335
Cdd:PRK09185  250 H-HMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAME----SRAVAAVFGDGVPCSSTKGLTGHTLGA 324
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41872631   336 SGL--AALAkvLLSLEHGLWAPNLHFHSPNPEIPA--LLDGRlqvvdQPLPVRggNVGINSFGFGGSNVHIIL 404
Cdd:PRK09185  325 AGAveAAIC--WLALRHGLPPHGWNTGQPDPALPPlyLVENA-----QALAIR--YVLSNSFAFGGNNCSLIF 388
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
148-405 1.79e-23

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 105.88  E-value: 1.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   148 FDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLG-MLS------PEGTCKAFDTAGN 220
Cdd:PRK07103  154 FGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGaMGSdrfadePEAACRPFDQDRD 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   221 GYCRSEGVVAVLLTKKSLARR----VYATILNAGTNTDGFKEqgvTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTG 296
Cdd:PRK07103  234 GFIYGEACGAVVLESAESARRrgarPYAKLLGWSMRLDANRG---PDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTG 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   297 TKVGDPQELngitRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLwapnLHfhsPNPEIPALLDGRLQV 376
Cdd:PRK07103  311 SPLGDETEL----AALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGF----LH---PSRNLDEPIDERFRW 379
                         250       260       270
                  ....*....|....*....|....*....|
gi 41872631   377 V-DQPLPVRGGNVGINSFGFGGSNVHIILR 405
Cdd:PRK07103  380 VgSTAESARIRYALSLSFGFGGINTALVLE 409
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
1621-1854 4.08e-23

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 102.88  E-value: 4.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1621 GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIHsGSGGVGQAAIAIALSLGCRVFTTVG 1700
Cdd:COG1064  117 GYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRALR-RAGVGPGDRVAVI-GAGGLGHLAVQIAKALGAEVIAVDR 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1701 SAEKRAylQARfpQLDSTSFANSRDTSFEQhvlWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGkfDLSQNHP 1779
Cdd:COG1064  195 SPEKLE--LAR--ELGADHVVNSSDEDPVE---AVRELTGADVVIDTVgAPATVNAALALLRRGGRLVLVG--LPGGPIP 265
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41872631 1780 LGM-AIFLKNVTFHGVLldaffNESSADWREVWALVQAG-IR-DGVVRPLkctvfhgAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:COG1064  266 LPPfDLILKERSIRGSL-----IGTRADLQEMLDLAAEGkIKpEVETIPL-------EEANEALERLRAGKVRGRAVL 331
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
151-402 8.21e-23

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 104.04  E-value: 8.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   151 RGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLK--PNTSVQFLRLGMLS----PEGTCKAFDTAGNGYCR 224
Cdd:PRK07910  161 KAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEavPIAGFAQMRIVMSTnnddPAGACRPFDKDRDGFVF 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   225 SE-GVVAVLLTK---KSLARRVYATILNAGTNTDGFkEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVG 300
Cdd:PRK07910  241 GEgGALMVIETEehaKARGANILARIMGASITSDGF-HMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVG 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   301 DPQELNGITRALCATRQEpllIGSTKSNMGHPEPASGlaALAKVL--LSLEHGLWAPNLHFHSPNPEIPalldgrLQVV- 377
Cdd:PRK07910  320 DVAEGKAINNALGGHRPA---VYAPKSALGHSVGAVG--AVESILtvLALRDGVIPPTLNLENLDPEID------LDVVa 388
                         250       260
                  ....*....|....*....|....*...
gi 41872631   378 DQPlpvRGGNVGI---NSFGFGGSNVHI 402
Cdd:PRK07910  389 GEP---RPGNYRYainNSFGFGGHNVAL 413
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
80-404 1.02e-22

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: 99.83  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   80 RLLLEVTYEAIVDGGINPDSLrgthTGVWVGvsgsetseALSRDPEtlvgYSMVGCQRAMMANRLSfffdfrGPSIALDT 159
Cdd:cd00327    9 ELGFEAAEQAIADAGLSKGPI----VGVIVG--------TTGGSGE----FSGAAGQLAYHLGISG------GPAYSVNQ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  160 ACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLkpntsvqflrlgmlspegtckafdtagngycRSEGVVAVLLTKKSLA 239
Cdd:cd00327   67 ACATGLTALALAVQQVQNGKADIVLAGGSEEFV-------------------------------FGDGAAAAVVESEEHA 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  240 RR----VYATILNAGTNTDGFKEqgVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGItraLCAT 315
Cdd:cd00327  116 LRrgahPQAEIVSTAATFDGASM--VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALG---LDPD 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  316 RQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWApnlhfhspnpeipalldgrlqvvdqPLPVRGGNVGINSFGF 395
Cdd:cd00327  191 GVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIP-------------------------PTPREPRTVLLLGFGL 245

                 ....*....
gi 41872631  396 GGSNVHIIL 404
Cdd:cd00327  246 GGTNAAVVL 254
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
54-405 1.08e-22

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 103.27  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    54 LKDLSRFDASFFGVH---------------PKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGV--WVGVSGSET 116
Cdd:PRK08439   33 IKKITLFDASDFPVQiageitdfdptevmdPKEVKKADRFIQLGLKAAREAMKDAGFLPEELDAERFGVssASGIGGLPN 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   117 SEALS-----RDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVL 191
Cdd:PRK08439  113 IEKNSiicfeKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   192 LKPNTSVQFLRLGMLS-----PEGTCKAFDTAGNGYCRSEGVVAVLLTK--KSLAR--RVYATILnagtntdGFKEQG-- 260
Cdd:PRK08439  193 ICPVGIGGFAAMKALStrnddPKKASRPFDKDRDGFVMGEGAGALVLEEyeSAKKRgaKIYAEII-------GFGESGda 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   261 --VTFPSGDIQEQLIRSLYQSAGVAPesFEYIEAHGTGTKVGDPQELNGITRALCATRQEPlLIGSTKSNMGHPEPASGl 338
Cdd:PRK08439  266 nhITSPAPEGPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALKELFGSKEKVP-PVSSTKGQIGHCLGAAG- 341
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41872631   339 aALAKV--LLSLEHGLWAPNLHFHSPNPEIPalldgrLQVVdqPLPVRGGNVGI---NSFGFGGSNVHIILR 405
Cdd:PRK08439  342 -AIEAVisIMAMRDGILPPTINQETPDPECD------LDYI--PNVARKAELNVvmsNSFGFGGTNGVVIFK 404
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
4-406 1.35e-22

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 104.68  E-value: 1.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     4 VVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRrwkAGLYGLPRR-SGKLKDLSRfDAsffGVHPKQAHTMDPQLRLL 82
Cdd:PLN02787  131 VVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIER---FDCSQFPTRiAGEIKSFST-DG---WVAPKLSKRMDKFMLYL 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    83 LEVTYEAIVDGGINPD---SLRGTHTGVWVGVSG------SETSEALSRDPETL----VGYSMVGCQRAMMANRLSFFfd 149
Cdd:PLN02787  204 LTAGKKALADGGITEDvmkELDKTKCGVLIGSAMggmkvfNDAIEALRISYRKMnpfcVPFATTNMGSAMLAMDLGWM-- 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   150 frGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLS-----PEGTCKAFDTAGNGYCR 224
Cdd:PLN02787  282 --GPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSqrnddPTKASRPWDMNRDGFVM 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   225 SEGVVAVLLTKKSLARR----VYATILNAGTNTDGFKeqgVTFPSGDIQEQLI---RSLYQSaGVAPESFEYIEAHGTGT 297
Cdd:PLN02787  360 GEGAGVLLLEELEHAKKrganIYAEFLGGSFTCDAYH---MTEPHPEGAGVILcieKALAQS-GVSKEDVNYINAHATST 435
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   298 KVGDPQELNGITRalCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPA--LLDGRLQ 375
Cdd:PLN02787  436 KAGDLKEYQALMR--CFGQNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTkvLVGPKKE 513
                         410       420       430
                  ....*....|....*....|....*....|.
gi 41872631   376 VVDQPLPVRggnvgiNSFGFGGSNVHIILRP 406
Cdd:PLN02787  514 RLDIKVALS------NSFGFGGHNSSILFAP 538
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1635-1856 1.89e-22

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 100.81  E-value: 1.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1635 DVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVgSAEKRAYLQarfpQ 1714
Cdd:cd08271  109 PLPDSLSFEEAAALPCAGLTAYQALFKKLRIEAGRTILITGGAGGVGSFAVQLAKRAGLRVITTC-SKRNFEYVK----S 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1715 LDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEI-GKFDLSQNHPlgmaiFLKNVTFHG 1793
Cdd:cd08271  184 LGADHVIDYNDEDVCERIKEITGGRGVDAVLDTVGGETAAALAPTLAFNGHLVCIqGRPDASPDPP-----FTRALSVHE 258
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1794 VLLDAF-FNESSADWREvwaLVQAG------IRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 1856
Cdd:cd08271  259 VALGAAhDHGDPAAWQD---LRYAGeellelLAAGKLEPLVIEVLPFEQLPEALRALKDRHTRGKIVVTI 325
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
121-405 6.53e-22

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 99.80  E-value: 6.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   121 SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQF 200
Cdd:PRK14691   51 SRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGF 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   201 LRLGMLS------PEGTCKAFDTAGNGYCRSEGVVAVLLTK--KSLAR--RVYATILNAGTNTDGFKEQGVTfPSGDIQE 270
Cdd:PRK14691  131 AAARALSthfnstPEKASRPFDTARDGFVMGEGAGLLIIEEleHALARgaKPLAEIVGYGTSADAYHMTSGA-EDGDGAY 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   271 QLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALcaTRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEH 350
Cdd:PRK14691  210 RAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLF--GESNALAITSTKSATGHLLGAAGGLETIFTVLALRD 287
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 41872631   351 GLWAPNLHFHSPNPEIPAL--LDGRLQVVDQPLPVRggnvgiNSFGFGGSNVHIILR 405
Cdd:PRK14691  288 QIVPATLNLENPDPAAKGLniIAGNAQPHDMTYALS------NGFGFAGVNASILLK 338
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
4-404 1.27e-21

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 100.64  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     4 VVIAGMSGKLPESENLQEFWDNLIG---GVDMVTDDDRRWK--------AGLYGLPRRSGKLKDLSRFDASFFGVHPKQA 72
Cdd:PLN02836    8 VVVTGLGLVTPLGCGVETTWRRLIAgecGVRALTQDDLKMKsedeetqlYTLDQLPSRVAALVPRGTGPGDFDEELWLNS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    73 HTMDPQLRLLLEVTYEAIVDGGINP-DSLRGTHTGVWVGVSGSETSEALsrDPETLVgysmvgCQRAMmaNRLSFFF--- 148
Cdd:PLN02836   88 RSSSRFIGYALCAADEALSDARWLPsEDEAKERTGVSIGGGIGSITDIL--EAAQLI------CEKRL--RRLSPFFvpr 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   149 --------------DFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLS------P 208
Cdd:PLN02836  158 ilinmaaghvsiryGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALStkfnscP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   209 EGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARR----VYATILNAGTNTDGFKeqgVTFPSGDIQEQLI---RSLYQSaG 281
Cdd:PLN02836  238 TEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRrgakIYAEVRGYGMSGDAHH---ITQPHEDGRGAVLamtRALQQS-G 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   282 VAPESFEYIEAHGTGTKVGDPQELNGITRALC--ATRQEpLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHF 359
Cdd:PLN02836  314 LHPNQVDYVNAHATSTPLGDAVEARAIKTVFSehATSGG-LAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNL 392
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 41872631   360 HSPNpeiPALLDGRLQVVDQP-LPVRGgnVGINSFGFGGSNVHIIL 404
Cdd:PLN02836  393 ERPD---PIFDDGFVPLTASKaMLIRA--ALSNSFGFGGTNASLLF 433
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
1901-2089 2.14e-21

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: 100.03  E-value: 2.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1901 AQWLIQR-GVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGL 1979
Cdd:cd08956  210 ARHLVTEhGVRHLLLVSRRGPDAPGAAELVAELAALGAEVTVAACDVADRAALAALLAAVPADHPLTAVVHAAGVLDDGV 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1980 LENQTPEFFQDVCKPKYSGTLNLDRVTREAcpELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQ 2059
Cdd:cd08956  290 LTSLTPERLDAVLRPKVDAAWHLHELTRDL--DLAAFVLFSSAAGVLGSPGQANYAAANAFLDALAQHRRARGLPATSLA 367
                        170       180       190
                 ....*....|....*....|....*....|
gi 41872631 2060 WGAIGDVGILVETMSTNDtivsgtlPQRMA 2089
Cdd:cd08956  368 WGLWAQASGMTAHLSDAD-------LARLA 390
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
1679-1816 6.44e-21

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 90.74  E-value: 6.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1679 GVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASV 1757
Cdd:pfam00107    1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELAK----ELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVgSPATLEQAL 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1758 RCLATHGRFLEIGKFdlSQNHPLGMA-IFLKNVTFHGVLLDaffneSSADWREVWALVQA 1816
Cdd:pfam00107   77 KLLRPGGRVVVVGLP--GGPLPLPLApLLLKELTILGSFLG-----SPEEFPEALDLLAS 129
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
1568-1856 8.68e-20

Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 92.89  E-value: 8.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1568 YASLNFRDIMLATG--KLSPDAIPGkwtsqdsllgMEFSGR-DASGKRVMGLVP--------AKG-LATSVLLSPDFLWD 1635
Cdd:cd05286   35 AIGVNFIDTYFRSGlyPLPLPFVLG----------VEGAGVvEAVGPGVTGFKVgdrvayagPPGaYAEYRVVPASRLVK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1636 VPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAylQARfpQL 1715
Cdd:cd05286  105 LPDGISDETAAALLLQGLTAHYLLRETYPVKPGDTVLVHAAAGGVGLLLTQWAKALGATVIGTVSSEEKAE--LAR--AA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1716 DSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGK-------FDLSQnhpLGMaiflKN 1788
Cdd:cd05286  181 GADHVINYRDEDFVERVREITGGRGVDVVYDGVGKDTFEGSLDSLRPRGTLVSFGNasgpvppFDLLR---LSK----GS 253
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41872631 1789 VTF-HGVLLDafFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQV 1856
Cdd:cd05286  254 LFLtRPSLFH--YIATREELLARAAELFDAVASGKLKVEIGKRYPLADAAQAHRDLESRKTTGKLLLIP 320
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1635-1854 1.41e-19

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 92.75  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1635 DVPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFtTVGSAEKRAYLQArfpq 1714
Cdd:cd08274  146 PVNSPLSDVELATFPCSYSTAENMLE-RAGVGAGETVLVTGASGGVGSALVQLAKRRGAIVI-AVAGAAKEEAVRA---- 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1715 LDSTSFANSRDTSFEQHVLwhTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG-------KFDLSQnhplgmaIFLK 1787
Cdd:cd08274  220 LGADTVILRDAPLLADAKA--LGGEPVDVVADVVGGPLFPDLLRLLRPGGRYVTAGaiagpvvELDLRT-------LYLK 290
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41872631 1788 NVTFHGvlldaffneSSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd08274  291 DLTLFG---------STLGTREVFRRLVRYIEEGEIRPVVAKTFPLSEIREAQAEFLEKRHVGKLVL 348
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
1654-1854 2.03e-19

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 92.16  E-value: 2.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1654 TAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLqarfpqldsTSFA------NSRDTS 1727
Cdd:cd05288  132 TAYFGLTEIGKPKPGETVVVSAAAGAVGSVVGQIAKLLGARVVGIAGSDEKCRWL---------VEELgfdaaiNYKTPD 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1728 FEQhVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG------KFDLSQNHPLGMAIFlKNVTFHGVLLDAFFN 1801
Cdd:cd05288  203 LAE-ALKEAAPDGIDVYFDNVGGEILDAALTLLNKGGRIALCGaisqynATEPPGPKNLGNIIT-KRLTMQGFIVSDYAD 280
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41872631 1802 EssadWREVWALVQAGIRDGVVRPlKCTVFHG-AQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd05288  281 R----FPEALAELAKWLAEGKLKY-REDVVEGlENAPEAFLGLFTGKNTGKLVV 329
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
1590-1856 3.03e-18

enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176211 [Multi-domain]  Cd Length: 339  Bit Score: 88.79  E-value: 3.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1590 GKWTSQDSLLGMEFSGR------DAS----GKRVMGLV-------PAKG-LATSVLLSPDFLWDVPSNWTLEEAASVPVV 1651
Cdd:cd08249   49 GFIPSYPAILGCDFAGTvvevgsGVTrfkvGDRVAGFVhggnpndPRNGaFQEYVVADADLTAKIPDNISFEEAATLPVG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1652 YSTAYYALVVR----------GRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVgSAEKRAYLQarfpQLDSTSFA 1721
Cdd:cd08249  129 LVTAALALFQKlglplpppkpSPASKGKPVLIWGGSSSVGTLAIQLAKLAGYKVITTA-SPKNFDLVK----SLGADAVF 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1722 NSRDTSFEQHVLWHTGGKgVDLVLNSLAE-EKLQASVRCLATHGRfleiGKFDLSQNHPLGmAIFLKNVTFHGVLLDAFF 1800
Cdd:cd08249  204 DYHDPDVVEDIRAATGGK-LRYALDCISTpESAQLCAEALGRSGG----GKLVSLLPVPEE-TEPRKGVKVKFVLGYTVF 277
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41872631 1801 NESSADW---REVWALVQAGIRDGVVRPLKCTVFHG--AQVEDAFRYMAQGKHIG-KVVVQV 1856
Cdd:cd08249  278 GEIPEDRefgEVFWKYLPELLEEGKLKPHPVRVVEGglEGVQEGLDLLRKGKVSGeKLVVRL 339
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
874-1108 1.11e-17

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: 86.27  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    874 YLVDHTLDGRVLFPATGYLSIVWKTLARALGlgvEQLPVVFEDVVLHQATILPKTGTVSLEVRLLE------ASRAFEV- 946
Cdd:pfam14765   29 WLRDHRVGGTVVLPGAGYLEMALEAARQLFG---GSGAVALRDVSILKALVLPEDDPVEVQTSLTPeedgadSWWEFEIf 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    947 -----SENGNLVVSGKVYQWDDPDPRLFDHPE--SPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEA-SLEGDS- 1017
Cdd:pfam14765  106 sraggGWEWTLHATGTVRLAPGEPAAPVDLESlpARCAQPADPRSVSSAEFYERLAARGLFYGPAFQGLRRIwRGDGEAl 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1018 GRLLWKDNWV----------SFMDTMLQ-----MSILGSAKHGLYLPTRVTAIHI-DPATHRQKLY------TLQDKAQV 1075
Cdd:pfam14765  186 AEARLPEAAAggespyllhpALLDAALQllgaaLPAEAEHADQAYLPVGIERLRIyRSLPPGEPLWvharleRRGGRTIV 265
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 41872631   1076 ADVVvsrwlrVTVAGG---VHISGLHTESAPRRQQE 1108
Cdd:pfam14765  266 GDLT------LVDEDGrvvARIEGLRLRRVEREALL 295
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
1610-1853 1.29e-17

2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 86.56  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1610 GKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIAL 1689
Cdd:cd05282   81 GQRVLPLGGEGTWQEYVVAPADDLIPVPDSISDEQAAMLYINPLTAWLMLTEYLKLPPGDWVIQNAANSAVGRMLIQLAK 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1690 SLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEI 1769
Cdd:cd05282  161 LLGFKTINVVRRDEQVEELKA----LGADEVIDSSPEDLAQRVKEATGGAGARLALDAVGGESATRLARSLRPGGTLVNY 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1770 GKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESSAD-WREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKH 1848
Cdd:cd05282  237 GLLSGEPVPFPRSVFIFKDITVRGFWLRQWLHSATKEaKQETFAEVIKLVEAGVLTTPVGAKFPLEDFEEAVAAAEQPGR 316

                 ....*
gi 41872631 1849 IGKVV 1853
Cdd:cd05282  317 GGKVL 321
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1636-1854 1.69e-17

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 86.22  E-value: 1.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1636 VPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFpql 1715
Cdd:cd08259  132 LPDNVSDESAALAACVVGTAVHALK-RAGVKKGDTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSPEKLKILKELG--- 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1716 dstSFANSRDTSFEQHVlWHTGgkGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNH-PLGMAIfLKNVTFHGV 1794
Cdd:cd08259  208 ---ADYVIDGSKFSEDV-KKLG--GADVVIELVGSPTIEESLRSLNKGGRLVLIGNVTPDPAPlRPGLLI-LKEIRIIGS 280
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1795 LldaffNESSADWREVWALVQAgirdGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd08259  281 I-----SATKADVEEALKLVKE----GKIKPVIDRVVSLEDINEALEDLKSGKVVGRIVL 331
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
1722-1854 2.83e-17

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 80.45  E-value: 2.83e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1722 NSRDTSFEQHvlwhTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNhPLGMAIFLKNVTFHGVLLDAFFN 1801
Cdd:pfam13602    8 DYRTTDFVQA----TGGEGVDVVLDTVGGEAFEASLRVLPGGGRLVTIGGPPLSAG-LLLPARKRGGRGVKYLFLFVRPN 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 41872631   1802 ESSADWREVWALVQAGirdgVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:pfam13602   83 LGADILQELADLIEEG----KLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
1621-1856 4.41e-17

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 85.19  E-value: 4.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1621 GLATSVLLSPDFLWDVPSNWTLEEAASVPVVySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGC-RVFTTV 1699
Cdd:COG1063  117 GFAEYVRVPAANLVKVPDGLSDEAAALVEPL-AVALHA-VERAGVKPGDTVLV-IGAGPIGLLAALAARLAGAaRVIVVD 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1700 GSAEKRAylQARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIG------KF 1772
Cdd:COG1063  194 RNPERLE--LAR--ELGADAVVNPREEDLVEAVRELTGGRGADVVIEAVgAPAALEQALDLVRPGGTVVLVGvpggpvPI 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1773 DLsqnhplgMAIFLKNVTFHGVlldafFNESSADWREVWALVQAGIRDgvVRPLKCTVFHGAQVEDAFRYMAQGK-HIGK 1851
Cdd:COG1063  270 DL-------NALVRKELTLRGS-----RNYTREDFPEALELLASGRID--LEPLITHRFPLDDAPEAFEAAADRAdGAIK 335

                 ....*
gi 41872631 1852 VVVQV 1856
Cdd:COG1063  336 VVLDP 340
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
1555-1854 2.18e-16

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 83.43  E-value: 2.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1555 QPTCPGAQLCTVYYASLNFRDIMLATGKLSpdAIPGKWTSQDSLL--GMEFS---GRDASG---------KR------VM 1614
Cdd:cd08248   25 VIRKPNQVLIKVHAASVNPIDVLMRSGYGR--TLLNKKRKPQSCKysGIEFPltlGRDCSGvvvdigsgvKSfeigdeVW 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1615 GLVPAKG---LATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGET----LLIHSGSGGVGQAAIAI 1687
Cdd:cd08248  103 GAVPPWSqgtHAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGLNPKNAagkrVLILGGSGGVGTFAIQL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1688 ALSLGCRVFTTVGS--AEKRAYLQARfpqlDSTSFANsrdTSFEQHVLWHTggkGVDLVLNSLAEEKLQASVRCLATHGR 1765
Cdd:cd08248  183 LKAWGAHVTTTCSTdaIPLVKSLGAD----DVIDYNN---EDFEEELTERG---KFDVILDTVGGDTEKWALKLLKKGGT 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1766 FLEIG----KFDLSQNHPLGMA----IFLKNVTFH---GVLLD-AFFNESSADWREVWALVQagirDGVVRPLKCTVFHG 1833
Cdd:cd08248  253 YVTLVspllKNTDKLGLVGGMLksavDLLKKNVKSllkGSHYRwGFFSPSGSALDELAKLVE----DGKIKPVIDKVFPF 328
                        330       340
                 ....*....|....*....|.
gi 41872631 1834 AQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd08248  329 EEVPEAYEKVESGHARGKTVI 349
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
1654-1854 3.62e-16

Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 82.30  E-value: 3.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1654 TAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQhVL 1733
Cdd:cd08250  126 TASIALEEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIGTCSSDEKAEFLKS----LGCDRPINYKTEDLGE-VL 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1734 WHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG---------KFDLSQNHPLGMAIFLKNVTFHGVLLDAFfnesS 1804
Cdd:cd08250  201 KKEYPKGVDVVYESVGGEMFDTCVDNLALKGRLIVIGfisgyqsgtGPSPVKGATLPPKLLAKSASVRGFFLPHY----A 276
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 41872631 1805 ADWREVWALVQAGIRDGVVRP-LKCTVFHGAQ-VEDAFRYMAQGKHIGKVVV 1854
Cdd:cd08250  277 KLIPQHLDRLLQLYQRGKLVCeVDPTRFRGLEsVADAVDYLYSGKNIGKVVV 328
PKS_DH smart00826
Dehydratase domain in polyketide synthase (PKS) enzymes;
874-1008 7.97e-16

Dehydratase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214837  Cd Length: 167  Bit Score: 77.27  E-value: 7.97e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631     874 YLVDHTLDGRVLFPATGYLSIVWKTLARALGLGVEQLpvvfEDVVLHQATILPKTGTVSLEVRLLEA----SRAFEV--- 946
Cdd:smart00826   29 WLADHRVGGTVVLPGAAYVELALAAADEVGGGAPARL----EELTLEAPLVLPEDGAVRVQVVVGAPdedgRRTFTVysr 104
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41872631     947 -SENGNLV--VSGKV-YQWDDPDPRLFDHPESPTPNPTEplfLAQAEVYKELRLRGYDYGPHFQGI 1008
Cdd:smart00826  105 pDGDGPWTrhATGTLrPAAAAPAAPAADLAAWPPAGAEP---VDVDDLYERLAARGLEYGPAFQGL 167
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1636-1817 7.76e-15

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 78.41  E-value: 7.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1636 VPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHsGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYlqARfpQL 1715
Cdd:cd08260  134 LPDDVDFVTAAGLGCRFATAFRALVHQARVKPGEWVAVH-GCGGVGLSAVMIASALGARVIAVDIDDDKLEL--AR--EL 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1716 DSTSFANSRDT-SFEQHVLWHTGGkGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGKFDLSQNH-PLGMA-IFLKNVTF 1791
Cdd:cd08260  209 GAVATVNASEVeDVAAAVRDLTGG-GAHVSVDALgIPETCRNSVASLRKRGRHVQVGLTLGEEAGvALPMDrVVARELEI 287
                        170       180
                 ....*....|....*....|....*.
gi 41872631 1792 HGVlldafFNESSADWREVWALVQAG 1817
Cdd:cd08260  288 VGS-----HGMPAHRYDAMLALIASG 308
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
1636-1854 1.56e-14

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 77.38  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1636 VPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpql 1715
Cdd:PRK13771  132 VPPNVSDEGAVIVPCVTGMVYRGLR-RAGVKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVS------ 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1716 dstsfansrdtSFEQHVLwhTGGK---------GVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNH--PLGMAI 1784
Cdd:PRK13771  205 -----------KYADYVI--VGSKfseevkkigGADIVIETVGTPTLEESLRSLNMGGKIIQIGNVDPSPTYslRLGYII 271
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1785 fLKNVTFHGVLldaffNESSADWREVWALVqagiRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:PRK13771  272 -LKDIEIIGHI-----SATKRDVEEALKLV----AEGKIKPVIGAEVSLSEIDKALEELKDKSRIGKILV 331
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
1604-1854 2.07e-14

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 76.88  E-value: 2.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1604 SGRDASGKRV------MGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGS 1677
Cdd:cd08243   73 GGTFTPGQRVatamggMGRTFDGSYAEYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGSLFRSLGLQPGDTLLIRGGT 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1678 GGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQAR---FPQLDstsfansrDTSFEQHVLwhTGGKGVDLVLNSLAEEKLQ 1754
Cdd:cd08243  153 SSVGLAALKLAKALGATVTATTRSPERAALLKELgadEVVID--------DGAIAEQLR--AAPGGFDKVLELVGTATLK 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1755 ASVRCLATHGRFLEIG---------KFDLSQNHPLGMAIFLknvtFHGVLLDafFNESSADWrevwaLVQAgIRDGVVRP 1825
Cdd:cd08243  223 DSLRHLRPGGIVCMTGllggqwtleDFNPMDDIPSGVNLTL----TGSSSGD--VPQTPLQE-----LFDF-VAAGHLDI 290
                        250       260
                 ....*....|....*....|....*....
gi 41872631 1826 LKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd08243  291 PPSKVFTFDEIVEAHAYMESNRAFGKVVV 319
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2111-2179 3.81e-14

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: 69.97  E-value: 3.81e-14
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41872631    2111 LAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREV 2179
Cdd:smart00823    1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLV 69
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
1636-1855 4.66e-14

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 76.16  E-value: 4.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1636 VPSNWTLEEAASVPVVYSTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGC-RVFTTVGSAEKRAYLQARFPq 1714
Cdd:cd05278  137 IPDGLPDEDALMLSDILPTGFHG-AELAGIKPGSTVAV-IGAGPVGLCAVAGARLLGAaRIIAVDSNPERLDLAKEAGA- 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1715 ldsTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLA-EEKLQASVRCLATHGRFLEIGKFDLSQ-NHPLGMAiFLKNVTFH 1792
Cdd:cd05278  214 ---TDIINPKNGDIVEQILELTGGRGVDCVIEAVGfEETFEQAVKVVRPGGTIANVGVYGKPDpLPLLGEW-FGKNLTFK 289
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41872631 1793 GVLLDAffnessadWREVWALVQAgIRDGVVRPLK-CT-VFHGAQVEDAFRYMAQGK-HIGKVVVQ 1855
Cdd:cd05278  290 TGLVPV--------RARMPELLDL-IEEGKIDPSKlIThRFPLDDILKAYRLFDNKPdGCIKVVIR 346
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
494-773 5.15e-14

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: 75.20  E-value: 5.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    494 FICSGMGTQWRGMGLSLmrLDRFRDSILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQIGLIDLLSCMG-L 572
Cdd:TIGR00128    5 YVFPGQGSQTVGMGKDL--YEQYPIAKELFDQASEALGYDLKKLCQEGPAEELNKTQYTQPALYVVSAILYLKLKEQGgL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    573 RPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEAHLPP-GAMAAV-GLSWEECKQRCP----PGVVPACHNSK 646
Cdd:TIGR00128   83 KPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAVPEGgGAMAAViGLDEEQLAQACEeateNDVDLANFNSP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    647 DTVTISGPQAPVfEFVEQLRKEgVFAKEVRTGGM--AFHSYFMEAIAPPLLQELKKVIRepKPRSARWLSTSIPEAQWHS 724
Cdd:TIGR00128  163 GQVVISGTKDGV-EAAAALFKE-MGAKRAVPLEVsgAFHSRFMKPAAEKFAETLEACQF--NDPTVPVISNVDAKPYTNG 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 41872631    725 SLARTSSAEynvnNLVSPVLFQEALWHVPE--HAVVLEIAPHALLQAVLKR 773
Cdd:TIGR00128  239 DRIKEKLSE----QLTSPVRWTDSVEKLMArgVTEFAEVGPGKVLTGLIKR 285
PRK10754 PRK10754
NADPH:quinone reductase;
1571-1770 1.74e-12

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 70.92  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1571 LNFRDIMLATGKLSPDAIPgkwtsqdSLLGMEFSG----------RDASGKRVMGLVPAKGLATSVLLSP-DFLWDVPSN 1639
Cdd:PRK10754   40 INYIDTYIRSGLYPPPSLP-------SGLGTEAAGvvskvgsgvkHIKVGDRVVYAQSALGAYSSVHNVPaDKAAILPDA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1640 WTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKraylQARFPQLDSTS 1719
Cdd:PRK10754  113 ISFEQAAASFLKGLTVYYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGSAQK----AQRAKKAGAWQ 188
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 41872631  1720 FANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG 1770
Cdd:PRK10754  189 VINYREENIVERVKEITGGKKVRVVYDSVGKDTWEASLDCLQRRGLMVSFG 239
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2126-2409 3.93e-12

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 72.38  E-value: 3.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  2126 DLVEAVAHILGirdLAAVNLDSSLADLGLDSLMSVEVRQTLERELNlvlsvrevRQLTLRKLQELSSKADEASELAcptp 2205
Cdd:PRK10252  982 IIAAAFSSLLG---CDVVDADADFFALGGHSLLAMKLAAQLSRQFA--------RQVTPGQVMVASTVAKLATLLD---- 1046
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  2206 kEDGLAQQQTQLNLRSLLVNPEGPTLmrlnsvqsserplFLVHPIEGSTTVFHSLASRLS--IPTYGLQCTR---AAPL- 2279
Cdd:PRK10252 1047 -AEEDESRRLGFGTILPLREGDGPTL-------------FCFHPASGFAWQFSVLSRYLDpqWSIYGIQSPRpdgPMQTa 1112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  2280 DSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQqspAPTHNSLFLFDGSPtyvlAYTQSYRAKLTPGC 2359
Cdd:PRK10252 1113 TSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRAR---GEEVAFLGLLDTWP----PETQNWREKEANGL 1185
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 41872631  2360 EAEAETEAicffvqqftDMEHNRVLEAL---LP---LKGLEERVAAAVDLIIKSHQ 2409
Cdd:PRK10252 1186 DPEVLAEI---------DREREAFLAAQqgsLStelFTTIEGNYADAVRLLTTAHS 1232
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
1243-1342 1.40e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 62.77  E-value: 1.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1243 VEVLAGHGHLYSRIPGLLSphpllQLSYTATDRHPQALEAAQAELQQ---HDVAQGQWDPADPAPSALGSADLLVCNCAV 1319
Cdd:pfam08242    1 LEIGCGTGTLLRALLEALP-----GLEYTGLDISPAALEAARERLAAlglLNAVRVELFQLDLGELDPGSFDVVVASNVL 75
                           90       100
                   ....*....|....*....|...
gi 41872631   1320 AALGDPASALSNMVAALREGGFL 1342
Cdd:pfam08242   76 HHLADPRAVLRNIRRLLKPGGVL 98
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
1566-1856 1.59e-11

AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group contains members identified in targeting of yeast membrane proteins ATPase. AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast, identified as a multicopy suppressor of pma1 mutants which cause temperature sensitive growth arrest due to the inability of ATPase to target to the cell surface. This family is homologous to the medium chain family of dehydrogenases and reductases. Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176209 [Multi-domain]  Cd Length: 352  Bit Score: 68.45  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1566 VYYASLNFRDIMLATGKlspdaIPGKWTSQdSLLGMEFSGRDAS-----------GKRVMGLVP----AKG-LATSVLLS 1629
Cdd:cd08247   35 VHAAALNPVDLKLYNSY-----TFHFKVKE-KGLGRDYSGVIVKvgsnvasewkvGDEVCGIYPhpygGQGtLSQYLLVD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1630 P--DF--LWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVR-PGETLLIHSGSGGVGQAAIAIALSLGcRVFTTVGSAEK 1704
Cdd:cd08247  109 PkkDKksITRKPENISLEEAAAWPLVLGTAYQILEDLGQKLgPDSKVLVLGGSTSVGRFAIQLAKNHY-NIGTVVGTCSS 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1705 RAYLQARFPQLDstSFANSRDTSFEQH---VLWHTGGKG-VDLVLNSLAEEKLQAS----VRCLATHGRFLEI-G----- 1770
Cdd:cd08247  188 RSAELNKKLGAD--HFIDYDAHSGVKLlkpVLENVKGQGkFDLILDCVGGYDLFPHinsiLKPKSKNGHYVTIvGdykan 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1771 -KFDLSQNHP---------LGMAIFLK-NVTFhgVLLDAffnesSADWREVWAlvqAGIRDGVVRPLKCTVFHGAQVEDA 1839
Cdd:cd08247  266 yKKDTFNSWDnpsanarklFGSLGLWSyNYQF--FLLDP-----NADWIEKCA---ELIADGKVKPPIDSVYPFEDYKEA 335
                        330
                 ....*....|....*..
gi 41872631 1840 FRYMAQGKHIGKVVVQV 1856
Cdd:cd08247  336 FERLKSNRAKGKVVIKV 352
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
1610-1853 1.67e-11

Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 68.16  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1610 GKRVMGLVPAK--GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYyALVVRGRVRPGETLLIHSGSGGVGQAAIAI 1687
Cdd:cd08244   84 GRRVVAHTGRAggGYAELAVADVDSLHPVPDGLDLEAAVAVVHDGRTAL-GLLDLATLTPGDVVLVTAAAGGLGSLLVQL 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1688 ALSLGCRVFTTVGSAEKRAYLQArfpqLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFL 1767
Cdd:cd08244  163 AKAAGATVVGAAGGPAKTALVRA----LGADVAVDYTRPDWPDQVREALGGGGVTVVLDGVGGAIGRAALALLAPGGRFL 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1768 EIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFnesSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGK 1847
Cdd:cd08244  239 TYGWASGEWTALDEDDARRRGVTVVGLLGVQAE---RGGLRALEARALAEAAAGRLVPVVGQTFPLERAAEAHAALEARS 315

                 ....*.
gi 41872631 1848 HIGKVV 1853
Cdd:cd08244  316 TVGKVL 321
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1555-1710 1.87e-11

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 67.78  E-value: 1.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1555 QPtCPGAQLCTVYYASLNFRDIMLATgKLSPDAIPGkwtsQDSLLGMEFSGRDASG----KRVMGLVPAKGLATSVLLSP 1630
Cdd:cd08270   23 QP-APHEALVRVAAISLNRGELKFAA-ERPDGAVPG----WDAAGVVERAAADGSGpavgARVVGLGAMGAWAELVAVPT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1631 DFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRpGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQA 1710
Cdd:cd08270   97 GWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPLL-GRRVLVTGASGGVGRFAVQLAALAGAHVVAVVGSPARAEGLRE 175
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
1621-1854 2.21e-11

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 68.04  E-value: 2.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1621 GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVFTTVG 1700
Cdd:cd08254  119 GFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVVRAGEVKPGETVLV-IGLGGLGLNAVQIAKAMGAAVIAVDI 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1701 SAEKRAylQARfpQLDSTSFANSRDTSFEQHVLwHTGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLEIGkfdlsqnhp 1779
Cdd:cd08254  198 KEEKLE--LAK--ELGADEVLNSLDDSPKDKKA-AGLGGGFDVIFDfVGTQPTFEDAQKAVKPGGRIVVVG--------- 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1780 LGMaiflKNVTFHGVLLDAF-------FNESSADWREVWALVQAGIRDGVV--RPLKctvfhgaQVEDAFRYMAQGKHIG 1850
Cdd:cd08254  264 LGR----DKLTVDLSDLIARelriigsFGGTPEDLPEVLDLIAKGKLDPQVetRPLD-------EIPEVLERLHKGKVKG 332

                 ....
gi 41872631 1851 KVVV 1854
Cdd:cd08254  333 RVVL 336
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
1616-1855 5.07e-11

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 66.85  E-value: 5.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1616 LVPAKGLATSVLLSpdflwdVPSNWTLEEAASV-PVvySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCR 1694
Cdd:cd08235  122 RVPAWAVKRGGVLK------LPDNVSFEEAALVePL--ACCINA-QRKAGIKPGDTVLV-IGAGPIGLLHAMLAKASGAR 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1695 -VFTTVGSAEKRAylQARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQA-SVRCLATHGRFLEIGKF 1772
Cdd:cd08235  192 kVIVSDLNEFRLE--FAK--KLGADYTIDAAEEDLVEKVRELTDGRGADVVIVATGSPEAQAqALELVRKGGRILFFGGL 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1773 DLSQNHPLGMA-IFLKNVTFHGVlldafFNESSADWREVWALVQAGIRDgvVRPLKCTVFHGAQVEDAFRYMAQGKHIgK 1851
Cdd:cd08235  268 PKGSTVNIDPNlIHYREITITGS-----YAASPEDYKEALELIASGKID--VKDLITHRFPLEDIEEAFELAADGKSL-K 339

                 ....
gi 41872631 1852 VVVQ 1855
Cdd:cd08235  340 IVIT 343
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
1654-1856 5.32e-11

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 66.62  E-value: 5.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1654 TAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLqarfpqLDSTSFA---NSRDTSFEQ 1730
Cdd:COG2130  133 TAYFGLLDIGKPKAGETVVVSAAAGAVGSVVGQIAKLKGCRVVGIAGGAEKCRYL------VEELGFDaaiDYKAGDLAA 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1731 HvLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRF-------------LEIGkfdlsqnhPLGMAIFLKN-VTFHGVLL 1796
Cdd:COG2130  207 A-LAAACPDGIDVYFDNVGGEILDAVLPLLNTFARIavcgaisqynatePPPG--------PRNLGQLLVKrLRMQGFIV 277
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41872631 1797 DAFFnessADWREVWALVQAGIRDGVVRPlKCTVFHG-AQVEDAFRYMAQGKHIGKVVVQV 1856
Cdd:COG2130  278 FDHA----DRFPEFLAELAGWVAEGKLKY-RETVVEGlENAPEAFLGLFEGENFGKLLVKV 333
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1617-1770 1.58e-10

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 65.47  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1617 VPAKGLATsvllspdflwdVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVF 1696
Cdd:cd08263  148 VPATALAP-----------LPESLDYTESAVLGCAGFTAYGALKHAADVRPGETVAV-IGVGGVGSSAIQLAKAFGASPI 215
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41872631 1697 TTVG-SAEKRAylQARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLA-EEKLQASVRCLATHGRFLEIG 1770
Cdd:cd08263  216 IAVDvRDEKLA--KAK--ELGATHTVNAAKEDAVAAIREITGGRGVDVVVEALGkPETFKLALDVVRDGGRAVVVG 287
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
37-399 1.75e-10

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: 65.46  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   37 DRRWKAGLYGlprRSGkLKDLSRFDASFF---------GVHPKqAH-------TMDPQLRLLLEVTYEAIVDGGINPDSL 100
Cdd:cd00832   19 EEYWKAVLDG---RSG-LGPITRFDPSGYparlagevpDFDAA-EHlpgrllpQTDRMTRLALAAADWALADAGVDPAAL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  101 RGTHTGVwVGVSGS--------ETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAY 172
Cdd:cd00832   94 PPYDMGV-VTASAAggfefgqrELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVAEQAGGLDALAQAR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  173 QAIHSGQcPAAIVGGINVLLKPNTSVQFLRLGMLS----PEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR----RVYA 244
Cdd:cd00832  173 RLVRRGT-PLVVSGGVDSALCPWGWVAQLSSGRLStsddPARAYLPFDAAAAGYVPGEGGAILVLEDAAAARergaRVYG 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  245 TILNAGTNTDGFKEQGVtfPSGdiQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALcATRQEPllIGS 324
Cdd:cd00832  252 EIAGYAATFDPPPGSGR--PPG--LARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAVF-GPRGVP--VTA 324
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41872631  325 TKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPALLdgrlqVVDQPLPVRGGNVGINSFGFGGSN 399
Cdd:cd00832  325 PKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDL-----VTGRPRPAALRTALVLARGRGGFN 394
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
1610-1839 5.33e-10

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 62.67  E-value: 5.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1610 GKRVMGLVPAkglATSVLLSPDFLWDVPSNWTLEEAASVPVVySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIAL 1689
Cdd:cd08255   45 GDRVFCFGPH---AERVVVPANLLVPLPDGLPPERAALTALA-ATALNG-VRDAEPRLGERVAV-VGLGLVGLLAAQLAK 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1690 SLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDtsfeqhvlwhTGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLE 1768
Cdd:cd08255  119 AAGAREVVGVDPDAARRELAEALGPADPVAADTADE----------IGGRGADVVIEaSGSPSALETALRLLRDRGRVVL 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1769 IGKFDLSQNhPLGMAiflknvtFHGVLLDAFFNESSA--------DWREVWALVQAG--IRDGVVRPLkctVFHGAQVED 1838
Cdd:cd08255  189 VGWYGLKPL-LLGEE-------FHFKRLPIRSSQVYGigrydrprRWTEARNLEEALdlLAEGRLEAL---ITHRVPFED 257

                 .
gi 41872631 1839 A 1839
Cdd:cd08255  258 A 258
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
1623-1856 5.85e-10

crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase/reductase family, catalyzes the NADPH-dependent conversion of crotonyl-CoA to butyryl-CoA, a step in (2S)-methylmalonyl-CoA production for straight-chain fatty acid biosynthesis. Like enoyl reductase, another enzyme in fatty acid synthesis, crotonyl-CoA reductase is a member of the zinc-dependent alcohol dehydrogenase-like medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 63.97  E-value: 5.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1623 ATSVLLSPDFLwdvpsnwTLEEAASVPVVYSTAYYALVVR--GRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVG 1700
Cdd:cd08246  154 ATQLMPKPKHL-------SWEEAAAYMLVGATAYRMLFGWnpNTVKPGDNVLIWGASGGLGSMAIQLARAAGANPVAVVS 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1701 SAEKRAYLQA--------------RFPQLDSTSFANSRDT----SFEQHVLWHTGGK-GVDLVLNSLAEEKLQASVRcLA 1761
Cdd:cd08246  227 SEEKAEYCRAlgaegvinrrdfdhWGVLPDVNSEAYTAWTkearRFGKAIWDILGGReDPDIVFEHPGRATFPTSVF-VC 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1762 THGrfleigkfdlsqnhplGMAIFLKNVTFHGVLLDAFF---------NESSADWREVWALVQAgIRDGVVRPLKCTVFH 1832
Cdd:cd08246  306 DRG----------------GMVVICAGTTGYNHTYDNRYlwmrqkriqGSHFANDREAAEANRL-VMKGRIDPCLSKVFS 368
                        250       260
                 ....*....|....*....|....*
gi 41872631 1833 GAQVEDAFRYMAQGKH-IGKVVVQV 1856
Cdd:cd08246  369 LDETPDAHQLMHRNQHhVGNMAVLV 393
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2125-2179 2.78e-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: 55.26  E-value: 2.78e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 41872631   2125 RDLVEAVAHILGIrDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREV 2179
Cdd:pfam00550    1 ERLRELLAEVLGV-PAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDL 54
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
1623-1854 3.37e-09

2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 61.08  E-value: 3.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1623 ATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSA 1702
Cdd:cd08290  102 RTHAVVPADDLIKVPNDVDPEQAATLSVNPCTAYRLLEDFVKLQPGDWVIQNGANSAVGQAVIQLAKLLGIKTINVVRDR 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1703 EKRAYLQARFPQLDSTSFAN---SRDTSFEQhVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKfdLSQNH- 1778
Cdd:cd08290  182 PDLEELKERLKALGADHVLTeeeLRSLLATE-LLKSAPGGRPKLALNCVGGKSATELARLLSPGGTMVTYGG--MSGQPv 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1779 --PLGMAIFlKNVTFHGVLLDAFF-NESSADWREVWALVQAGIRDGVVRPLKCTVFHGA---QVEDAF-RYMAQGKHiGK 1851
Cdd:cd08290  259 tvPTSLLIF-KDITLRGFWLTRWLkRANPEEKEDMLEELAELIREGKLKAPPVEKVTDDpleEFKDALaNALKGGGG-GK 336

                 ...
gi 41872631 1852 VVV 1854
Cdd:cd08290  337 QVL 339
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
1637-1855 5.14e-09

Arginate lyase and other MDR family members; This group contains a structure identified as an arginate lyase. Other members are identified quinone reductases, alginate lyases, and other proteins related to the zinc-dependent dehydrogenases/reductases. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 60.62  E-value: 5.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1637 PSNWTLEEAASVPVVYSTAYYALVVRGRVRP-----GETLLIHSGSGGVGQAAIAIA-LSLGCRVFTTVGSAEKRAYLQa 1710
Cdd:cd08252  114 PKSLSFAEAAALPLTSLTAWEALFDRLGISEdaeneGKTLLIIGGAGGVGSIAIQLAkQLTGLTVIATASRPESIAWVK- 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1711 rfpQLDSTSFANSRDTSFEQhvLWHTGGKGVDLVLNSLA-EEKLQASVRCLATHGRFLEI----GKFDLsqnhplgMAIF 1785
Cdd:cd08252  193 ---ELGADHVINHHQDLAEQ--LEALGIEPVDYIFCLTDtDQHWDAMAELIAPQGHICLIvdpqEPLDL-------GPLK 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1786 LKNVTFHGVLLdafFNES---SADWR-------EVWALVQAGIrdgvvrpLKCTV---FHG---AQVEDAFRYMAQGKHI 1849
Cdd:cd08252  261 SKSASFHWEFM---FTRSmfqTPDMIeqheilnEVADLLDAGK-------LKTTLtetLGPinaENLREAHALLESGKTI 330

                 ....*.
gi 41872631 1850 GKVVVQ 1855
Cdd:cd08252  331 GKIVLE 336
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
1612-1854 7.08e-09

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 60.28  E-value: 7.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1612 RVMGLVPAKGLATSVLLsPDFLWDVPSNWTLEEAASV-PvvYSTAYYAlVVRGRVRPGETLLIHsGSGGVGQAAIAIALS 1690
Cdd:cd08261  107 QVLGVHRDGGFAEYIVV-PADALLVPEGLSLDQAALVeP--LAIGAHA-VRRAGVTAGDTVLVV-GAGPIGLGVIQVAKA 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1691 LGCRVFTTVGSAEKRAYlqARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGR--FL 1767
Cdd:cd08261  182 RGARVIVVDIDDERLEF--AR--ELGADDTINVGDEDVAARLRELTDGEGADVVIDATgNPASMEEAVELVAHGGRvvLV 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1768 EIGKFDLSQNHPlgmAIFLKNVTFHGvlldaffneSSADWREVWALVQAGIRDGVVRPLK-CT-VFHGAQVEDAFRYMAQ 1845
Cdd:cd08261  258 GLSKGPVTFPDP---EFHKKELTILG---------SRNATREDFPDVIDLLESGKVDPEAlIThRFPFEDVPEAFDLWEA 325
                        250
                 ....*....|
gi 41872631 1846 -GKHIGKVVV 1854
Cdd:cd08261  326 pPGGVIKVLI 335
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
1626-1854 7.74e-09

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 59.86  E-value: 7.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1626 VLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVvRGRVRPGETLLIhSGSGG-VGQAAIAIALSLGCRVFTTVGSAEK 1704
Cdd:cd08297  125 AIADARYVTPIPDGLSFEQAAPLLCAGVTVYKALK-KAGLKPGDWVVI-SGAGGgLGHLGVQYAKAMGLRVIAIDVGDEK 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1705 RAYlqARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLEIGkfdLSQNHPLGMA 1783
Cdd:cd08297  203 LEL--AK--ELGADAFVDFKKSDDVEAVKELTGGGGAHAVVVtAVSAAAYEQALDYLRPGGTLVCVG---LPPGGFIPLD 275
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41872631 1784 IF---LKNVTFHGVLLDaffneSSADWREVWALVqagiRDGVVRPlKCTVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd08297  276 PFdlvLRGITIVGSLVG-----TRQDLQEALEFA----ARGKVKP-HIQVVPLEDLNEVFEKMEEGKIAGRVVV 339
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
1613-1776 9.51e-09

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 59.67  E-value: 9.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1613 VMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALvVRGRVRPGETLLIHSGSGGVGQAAIAIALSLG 1692
Cdd:cd08264  109 IIGVVSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHAL-KTAGLGPGETVVVFGASGNTGIFAVQLAKMMG 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1693 CRVFTTVGsaekRAYLQaRFPQLDSTSFANSRDTSFEqhvlwhtGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIG-- 1770
Cdd:cd08264  188 AEVIAVSR----KDWLK-EFGADEVVDYDEVEEKVKE-------ITKMADVVINSLGSSFWDLSLSVLGRGGRLVTFGtl 255
                        170
                 ....*....|.
gi 41872631 1771 -----KFDLSQ 1776
Cdd:cd08264  256 tggevKLDLSD 266
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
1622-1856 9.90e-09

Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 59.81  E-value: 9.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1622 LATSVLLSPDFLWDVPSNWTLEEAASV-PVvySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVFTTVG 1700
Cdd:cd05285  119 LCRYVNHPADFCHKLPDNVSLEEGALVePL--SVGVHA-CRRAGVRPGDTVLV-FGAGPIGLLTAAVAKAFGATKVVVTD 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1701 SAEKRayLQ-ARfpQLDSTSFANSRDTSFEQHVLWH---TGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLEIGKFDLS 1775
Cdd:cd05285  195 IDPSR--LEfAK--ELGATHTVNVRTEDTPESAEKIaelLGGKGPDVVIEcTGAESCIQTAIYATRPGGTVVLVGMGKPE 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1776 QNHPLgMAIFLKNVTFHGVLLDAffNessaDWREVWALVQAGIRDgvVRPLKCTVFHGAQVEDAFRYMAQGKHIG-KVVV 1854
Cdd:cd05285  271 VTLPL-SAASLREIDIRGVFRYA--N----TYPTAIELLASGKVD--VKPLITHRFPLEDAVEAFETAAKGKKGViKVVI 341

                 ..
gi 41872631 1855 QV 1856
Cdd:cd05285  342 EG 343
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1900-2063 2.06e-08

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 57.57  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1900 LAQWLIQRGVQkLVLTSRSGIRTgyqAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDG 1978
Cdd:COG0300   21 LARALAARGAR-VVLVARDAERL---EALAAELRAAGARVEVVALDVTDPDAVAALAEAVlARFGPIDVLVNNAGVGGGG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1979 LLENQTPEFFQDVCKPKYSGTLNLdrvTREACPEL-----DYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHE-- 2051
Cdd:COG0300   97 PFEELDLEDLRRVFEVNVFGPVRL---TRALLPLMrargrGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAEla 173
                        170
                 ....*....|....
gi 41872631 2052 --GLPGLAVQWGAI 2063
Cdd:COG0300  174 ptGVRVTAVCPGPV 187
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2124-2187 8.71e-08

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: 51.39  E-value: 8.71e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41872631 2124 QRDLVEAVAHILGIrDLAAVNLDSSL-ADLGLDSLMSVEVRQTLERELNLVLSVREVRQL-TLRKL 2187
Cdd:COG0236    7 EERLAEIIAEVLGV-DPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYpTVADL 71
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
1514-1854 2.03e-07

Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 55.63  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1514 FRHFLLEEDkpeEPTAHAFVSTLTRGDLSsirwvcsslrhaqptcPGAQLCTVYYASLNFRDIMLATGKlspdaipGKWT 1593
Cdd:cd05280    1 FKALVVEEQ---DGGVSLFLRTLPLDDLP----------------EGDVLIRVHYSSLNYKDALAATGN-------GGVT 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1594 SQDSL-LGMEFSGRDAS--------GKRV------MGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAAsvpvVYSTAYY- 1657
Cdd:cd05280   55 RNYPHtPGIDAAGTVVSsddprfreGDEVlvtgydLGMNTDGGFAEYVRVPADWVVPLPEGLSLREAM----ILGTAGFt 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1658 -ALVV----RGRVRP--GEtLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYL------QARFPQ---------L 1715
Cdd:cd05280  131 aALSVhrleDNGQTPedGP-VLVTGATGGVGSIAVAILAKLGYTVVALTGKEEQADYLkslgasEVLDREdlldeskkpL 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1716 DSTSFANSRDTsfeqhvlwhTGGKGVDLVLNSLAEEKLQASVrclathGrflEIGKFDLSQNhplGMAIFLKNVTFHGVl 1795
Cdd:cd05280  210 LKARWAGAIDT---------VGGDVLANLLKQTKYGGVVASC------G---NAAGPELTTT---VLPFILRGVSLLGI- 267
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41872631 1796 lDAffNESSADWRE-VWALV----QAGIRDGVVRplkctVFHGAQVEDAFRYMAQGKHIGKVVV 1854
Cdd:cd05280  268 -DS--VNCPMELRKqVWQKLatewKPDLLEIVVR-----EISLEELPEAIDRLLAGKHRGRTVV 323
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
1901-2064 2.42e-07

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: 54.41  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1901 AQWLIQRGVqKLVLTSRSGIRtgyqAKQVRRW-RRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDG 1978
Cdd:COG1028   23 ARALAAEGA-RVVITDRDAEA----LEAAAAElRAAGGRALAVAADVTDEAAVEALVAAAvAAFGRLDILVNNAGITPPG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1979 LLENQTPEFFQDVCKPKYSGTLNLdrvTREACPEL---DY--FVVFSSVSCGRGNAGQSNYGFANSAMERICEkrrhegl 2053
Cdd:COG1028   98 PLEELTEEDWDRVLDVNLKGPFLL---TRAALPHMrerGGgrIVNISSIAGLRGSPGQAAYAASKAAVVGLTR------- 167
                        170
                 ....*....|.
gi 41872631 2054 pGLAVQWGAIG 2064
Cdd:COG1028  168 -SLALELAPRG 177
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
1901-2042 5.52e-07

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 53.27  E-value: 5.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1901 AQWLIQRGVqKLVLTSRSGIRtgyQAKQVRRWRR-QGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDG 1978
Cdd:PRK05557   22 AERLAAQGA-NVVINYASSEA---GAEALVAEIGaLGGKALAVQGDVSDAESVERAVDEAkAEFGGVDILVNNAGITRDN 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41872631  1979 LLENQTPEFFQDVCKPKYSGTLNldrVTREACPEL-----DYFVVFSSVSCGRGNAGQSNYGFANSAME 2042
Cdd:PRK05557   98 LLMRMKEEDWDRVIDTNLTGVFN---LTKAVARPMmkqrsGRIINISSVVGLMGNPGQANYAASKAGVI 163
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
1633-1853 1.02e-06

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 53.41  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1633 LWDVPSNWTLEEAASVPVVYSTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVFTTVGSAEKR---AYLQ 1709
Cdd:cd08284  134 LLKLPDGLSDEAALLLGDILPTGYFG-AKRAQVRPGDTVAV-IGCGPVGLCAVLSAQVLGAARVFAVDPVPERlerAAAL 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1710 ARFPqldstsfANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGkfdLSQNHPL---GMAIF 1785
Cdd:cd08284  212 GAEP-------INFEDAEPVERVREATEGRGADVVLEAVgGAAALDLAFDLVRPGGVISSVG---VHTAEEFpfpGLDAY 281
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41872631 1786 LKNVTFHGVLLDAffnesSADWREVWALVQAGIRDGVV-----RPLkctvfhgAQVEDAFRYMAQGKhIGKVV 1853
Cdd:cd08284  282 NKNLTLRFGRCPV-----RSLFPELLPLLESGRLDLEFlidhrMPL-------EEAPEAYRLFDKRK-VLKVV 341
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
1621-1817 1.32e-06

Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 52.70  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1621 GLATSVLLSPDFLWDVPSNWTLEEAA-SVPVvySTAYYALVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVfTTV 1699
Cdd:cd08258  119 GFAEYVLVPEESLHELPENLSLEAAAlTEPL--AVAVHAVAERSGIRPGDTVVV-FGPGPIGLLAAQVAKLQGATV-VVV 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1700 GSAEKRAYLQ-ARFPQLDSTsfaNSRDTSFEQHVLWHTGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLEIGKFdlsqn 1777
Cdd:cd08258  195 GTEKDEVRLDvAKELGADAV---NGGEEDLAELVNEITDGDGADVVIEcSGAVPALEQALELLRKGGRIVQVGIF----- 266
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 41872631 1778 HPLGMAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAG 1817
Cdd:cd08258  267 GPLAASIDVERIIQKELSVIGSRSSTPASWETALRLLASG 306
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
1621-1817 1.47e-06

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 52.93  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1621 GLATSVLLSPDFLWDVPSNWTLEEAASV-PVvySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGC-RVFTT 1698
Cdd:cd08233  128 GFAEYVVVPAYHVHKLPDNVPLEEAALVePL--AVAWHA-VRRSGFKPGDTALV-LGAGPIGLLTILALKAAGAsKIIVS 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1699 VGSAEKRAYLQARFpqldSTSFANSRDTSFEQHVLWHTGGKGVDLVLN-SLAEEKLQASVRCLATHGRFLEIGKFDlsqn 1777
Cdd:cd08233  204 EPSEARRELAEELG----ATIVLDPTEVDVVAEVRKLTGGGGVDVSFDcAGVQATLDTAIDALRPRGTAVNVAIWE---- 275
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 41872631 1778 HPLgmAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAG 1817
Cdd:cd08233  276 KPI--SFNPNDLVLKEKTLTGSICYTREDFEEVIDLLASG 313
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
1610-1709 1.88e-06

13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 hydroxydehydrogenase activity; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto- 13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176254 [Multi-domain]  Cd Length: 329  Bit Score: 52.65  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1610 GKRVMGlvpAKGLATSVLLSPD---FLWDVPSNW--TLEEAASVPVVY---STAYYALVVRGRVRPGETLLIHSGSGGVG 1681
Cdd:cd08294   81 GTIVVA---SFGWRTHTVSDGKdqpDLYKLPADLpdDLPPSLALGVLGmpgLTAYFGLLEICKPKAGETVVVNGAAGAVG 157
                         90       100
                 ....*....|....*....|....*...
gi 41872631 1682 QAAIAIALSLGCRVFTTVGSAEKRAYLQ 1709
Cdd:cd08294  158 SLVGQIAKIKGCKVIGCAGSDDKVAWLK 185
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
1610-1855 3.15e-06

6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 51.85  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1610 GKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIhSGSGGVGQAAIAIAL 1689
Cdd:cd08240  118 KGRALGIFQDGGYAEYVIVPHSRYLVDPGGLDPALAATLACSGLTAYSAVKKLMPLVADEPVVI-IGAGGLGLMALALLK 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1690 SLGCRVFTTVG-SAEKRAYLQARfpqlDSTSFANSRDTSFEQHVLWHTGGkGVDLVLNSL-AEEKLQASVRCLATHGRFL 1767
Cdd:cd08240  197 ALGPANIIVVDiDEAKLEAAKAA----GADVVVNGSDPDAAKRIIKAAGG-GVDAVIDFVnNSATASLAFDILAKGGKLV 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1768 EIGKFDLSQNHPLGMaIFLKNVTFHGVLLDaffneSSADWREVWALVQAgirdGVVRPLKCTVFHGAQVEDAFRYMAQGK 1847
Cdd:cd08240  272 LVGLFGGEATLPLPL-LPLRALTIQGSYVG-----SLEELRELVALAKA----GKLKPIPLTERPLSDVNDALDDLKAGK 341

                 ....*...
gi 41872631 1848 HIGKVVVQ 1855
Cdd:cd08240  342 VVGRAVLK 349
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1929-2042 5.50e-06

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 50.25  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1929 VRRWRRQGVQVQVSTSNISSLEGARGLIAEAA-QLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTR 2007
Cdd:PRK12825   48 VEAVEALGRRAQAVQADVTDKAALEAAVAAAVeRFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVV 127
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 41872631  2008 EACPELDY--FVVFSSVSCGRGNAGQSNYGFANSAME 2042
Cdd:PRK12825  128 PPMRKQRGgrIVNISSVAGLPGWPGRSNYAAAKAGLV 164
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
1654-1855 5.85e-06

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 50.76  E-value: 5.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1654 TAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQarfpQLDSTSFANSRDTSFEQHVL 1733
Cdd:TIGR02825  125 TAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKVAYLK----KLGFDVAFNYKTVKSLEETL 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1734 WHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDL-SQNHPLGMAIFLKNVTFHGVLLDAF-FNESSADWRE-- 1809
Cdd:TIGR02825  201 KKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTyNRTGPLPPGPPPEIVIYQELRMEGFiVNRWQGEVRQka 280
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 41872631   1810 -----VWALvqagirDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQ 1855
Cdd:TIGR02825  281 lkellKWVL------EGKIQYKEYVIEGFENMPAAFMGMLKGENLGKTIVK 325
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
65-189 1.23e-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: 49.95  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   65 FGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLrgthTGVWVGVSGSETSealsrdpetlvgYSMVGcqrAMMANRL 144
Cdd:cd00829    3 VGMTPFGRRSDRSPLELAAEAARAALDDAGLEPADI----DAVVVGNAAGGRF------------QSFPG---ALIAEYL 63
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 41872631  145 SFFfdfRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGIN 189
Cdd:cd00829   64 GLL---GKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAE 105
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
2244-2336 1.23e-05

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 49.08  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 2244 LFLVHPIEGSTTVFHSLASRL--SIPTYGLQC------TRAAPLDSIHSLAAyyiDCIRQVQP--EGPYRVAGYSYGACV 2313
Cdd:COG3208    9 LFCFPYAGGSASAYRPWAAALppDIEVLAVQLpgrgdrLGEPPLTSLEELAD---DLAEELAPllDRPFALFGHSMGALL 85
                         90       100
                 ....*....|....*....|...
gi 41872631 2314 AFEMCSQLQAQQSPAPTHnsLFL 2336
Cdd:COG3208   86 AFELARRLERRGRPLPAH--LFV 106
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
1258-1406 1.57e-05

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 47.69  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1258 GLLSPHpLLQLSY--TATDRHPQALEAAQAELQQHDVAQGqwDPADPAPSAlGSADLLVCNCAVAALGDPASALSNMVAA 1335
Cdd:COG4976   58 GLLGEA-LRPRGYrlTGVDLSEEMLAKAREKGVYDRLLVA--DLADLAEPD-GRFDLIVAADVLTYLGDLAAVFAGVARA 133
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41872631 1336 LREGGFLllhtllrghplgdivAFLTSTEPQYGQGILSQDAWESLFSRVSLRLVGLkksfygstLFLCRRP 1406
Cdd:COG4976  134 LKPGGLF---------------IFSVEDADGSGRYAHSLDYVRDLLAAAGFEVPGL--------LVVARKP 181
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
1968-2063 1.70e-05

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: 47.90  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1968 VFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPE--LDYFVVFSSVSCGRGNAGQSNYGFANSAMERIC 2045
Cdd:cd02266   35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAkrLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114
                         90       100
                 ....*....|....*....|..
gi 41872631 2046 EKRRHE----GLPGLAVQWGAI 2063
Cdd:cd02266  115 QQWASEgwgnGLPATAVACGTW 136
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
1654-1746 2.11e-05

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 49.24  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1654 TAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARF-----------PQLDST---S 1719
Cdd:cd08295  138 TAYAGFYEVCKPKKGETVFVSAASGAVGQLVGQLAKLKGCYVVGSAGSDEKVDLLKNKLgfddafnykeePDLDAAlkrY 217
                         90       100
                 ....*....|....*....|....*..
gi 41872631 1720 FANSRDTSFEqhvlwHTGGKGVDLVLN 1746
Cdd:cd08295  218 FPNGIDIYFD-----NVGGKMLDAVLL 239
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
1633-1854 2.48e-05

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 49.15  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1633 LWDVPSNWTLEEAASV-PVvySTAYYAlVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGC-RVFTTVGSAEKRAYlqA 1710
Cdd:cd08236  127 LIKIPDHVDYEEAAMIePA--AVALHA-VRLAGITLGDTVVV-IGAGTIGLLAIQWLKILGAkRVIAVDIDDEKLAV--A 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1711 RfpQLDSTSFANSRDTSFEQhVLWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGkfDLSQNHPLGMA----IF 1785
Cdd:cd08236  201 R--ELGADDTINPKEEDVEK-VRELTEGRGADLVIEAAgSPATIEQALALARPGGKVVLVG--IPYGDVTLSEEafekIL 275
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41872631 1786 LKNVTFHGvlldaFFNESSA-----DWREVWALVQAGIRDgvVRPLKCTVFHGAQVEDAFRYMAQGK-HIGKVVV 1854
Cdd:cd08236  276 RKELTIQG-----SWNSYSApfpgdEWRTALDLLASGKIK--VEPLITHRLPLEDGPAAFERLADREeFSGKVLL 343
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
1269-1346 2.52e-05

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: 45.78  E-value: 2.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41872631 1269 SYTATDRHPQALEAAQAELQQHDVAQGQWDpADPAPSALGSADLLVCNCAVAALGDPASALSNMVAALREGGFLLLHT 1346
Cdd:COG2227   48 DVTGVDISPEALEIARERAAELNVDFVQGD-LEDLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
1636-1770 2.65e-05

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 49.18  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1636 VPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHsGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQL 1715
Cdd:cd08231  146 VPDNVPDEVAAPANCALATVLAALDRAGPVGAGDTVVVQ-GAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGAD 224
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 41872631 1716 DSTSFANSRDTSFEQHVLWHTGGKGVDLVL----NSLAeekLQASVRCLATHGRFLEIG 1770
Cdd:cd08231  225 ATIDIDELPDPQRRAIVRDITGGRGADVVIeasgHPAA---VPEGLELLRRGGTYVLVG 280
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
1636-1856 3.61e-05

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 48.39  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1636 VPSNWTLEEAASVPVVYSTAYYAlVVRGRVRPGETLLIHsGSGGVGQAAIAIALSLGC-RVFTtVGSAEKRAYLQARFpq 1714
Cdd:cd08285  136 LPDGLTDEQAVMLPDMMSTGFHG-AELANIKLGDTVAVF-GIGPVGLMAVAGARLRGAgRIIA-VGSRPNRVELAKEY-- 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1715 lDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSL-AEEKLQASVRCLATHGRFLEIGKF--DLSQNHPL-----GMAifl 1786
Cdd:cd08285  211 -GATDIVDYKNGDVVEQILKLTGGKGVDAVIIAGgGQDTFEQALKVLKPGGTISNVNYYgeDDYLPIPReewgvGMG--- 286
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41872631 1787 kNVTFHGVLLDAffneSSADWREVWALVQAGIRDgvVRPLKCTVFHG-AQVEDAFRYMA-QGKHIGKVVVQV 1856
Cdd:cd08285  287 -HKTINGGLCPG----GRLRMERLASLIEYGRVD--PSKLLTHHFFGfDDIEEALMLMKdKPDDLIKPVIIF 351
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
1933-2040 4.58e-05

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: 47.16  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1933 RRQGVQVQVSTSNISSLEGARGLIAEAAQ-LGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNldrVTREACP 2011
Cdd:cd05333   45 KALGGNAAALEADVSDREAVEALVEKVEAeFGPVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFN---VTQAVIR 121
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 41872631 2012 EL---DY--FVVFSSVSCGRGNAGQSNY--------GFANSA 2040
Cdd:cd05333  122 AMikrRSgrIINISSVVGLIGNPGQANYaaskagviGFTKSL 163
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
1633-1745 5.21e-05

formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 48.02  E-value: 5.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1633 LWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIhSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRayLQ-AR 1711
Cdd:cd08286  132 LYKLPEGVDEEAAVMLSDILPTGYECGVLNGKVKPGDTVAI-VGAGPVGLAALLTAQLYSPSKIIMVDLDDNR--LEvAK 208
                         90       100       110
                 ....*....|....*....|....*....|....
gi 41872631 1712 fpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVL 1745
Cdd:cd08286  209 --KLGATHTVNSAKGDAIEQVLELTDGRGVDVVI 240
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
1240-1344 7.41e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 45.10  E-value: 7.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1240 MKVVEVLAGHGHLYSRIPGLLSPhpllQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPAD----PAPSALGSADLLVC 1315
Cdd:pfam13847    5 MRVLDLGCGTGHLSFELAEELGP----NAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDieelPELLEDDKFDVVIS 80
                           90       100
                   ....*....|....*....|....*....
gi 41872631   1316 NCAVAALGDPASALSNMVAALREGGFLLL 1344
Cdd:pfam13847   81 NCVLNHIPDPDKVLQEILRVLKPGGRLII 109
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
1663-1746 1.03e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 44.81  E-value: 1.03e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631    1663 GRVRPGETLLIhsGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRdtSFEQHVlwhtggKGVD 1742
Cdd:smart01002   16 GGVPPAKVVVI--GAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESLLGARFTTLYSQAE--LLEEAV------KEAD 85

                    ....
gi 41872631    1743 LVLN 1746
Cdd:smart01002   86 LVIG 89
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1929-2035 1.12e-04

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 46.31  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631  1929 VRRWRRQGVQVQVSTSNISSLEGARGLIAEA-AQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCkpkysgTLNLD---R 2004
Cdd:PRK05653   46 AAELRAAGGEARVLVFDVSDEAAVRALIEAAvEAFGALDILVNNAGITRDALLPRMSEEDWDRVI------DVNLTgtfN 119
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 41872631  2005 VTREACP---ELDY--FVVFSSVSCGRGNAGQSNYG 2035
Cdd:PRK05653  120 VVRAALPpmiKARYgrIVNISSVSGVTGNPGQTNYS 155
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
1240-1362 1.42e-04

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: 44.21  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1240 MKVVEVLAGHGHLYSRIPGLlsphpllQLSYTATDRHPQALEAAQAELQQH----DVAQGqwdPADPAPSALGSADLLVC 1315
Cdd:COG2226   24 ARVLDLGCGTGRLALALAER-------GARVTGVDISPEMLELARERAAEAglnvEFVVG---DAEDLPFPDGSFDLVIS 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 41872631 1316 NCAVAALGDPASALSNMVAALREGGFLLLHTLLRgHPLGDIVAFLTS 1362
Cdd:COG2226   94 SFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP-PDLAELEELLAE 139
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
1240-1389 1.68e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.64  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1240 MKVVEVLAGHGHLYSripgLLSPHpllQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADpapsalGSADLLVCNCAV 1319
Cdd:pfam13489   24 GRVLDFGCGTGIFLR----LLRAQ---GFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVPA------GKFDVIVAREVL 90
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41872631   1320 AALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQG-ILSQDAWESLFSRVSLRLV 1389
Cdd:pfam13489   91 EHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRPRNGHIsLFSARSLKRLLEEAGFEVV 161
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
153-188 2.40e-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: 42.85  E-value: 2.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 41872631  153 PSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGI 188
Cdd:cd00751   76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGV 111
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
1635-1786 2.60e-03

Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 42.53  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1635 DVPsnwtLEEAA----SVPvvysTAYYALVVRGRVRPGETLLIhSGSGGVGQAAI---AIAlslGCRVFTTVG-SAEKRA 1706
Cdd:cd08279  154 DIP----LDRAAllgcGVT----TGVGAVVNTARVRPGDTVAV-IGCGGVGLNAIqgaRIA---GASRIIAVDpVPEKLE 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1707 ylQARfpQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAE-EKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIF 1785
Cdd:cd08279  222 --LAR--RFGATHTVNASEDDAVEAVRDLTDGRGADYAFEAVGRaATIRQALAMTRKGGTAVVVGMGPPGETVSLPALEL 297

                 .
gi 41872631 1786 L 1786
Cdd:cd08279  298 F 298
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
153-187 5.71e-03

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: 41.59  E-value: 5.71e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 41872631  153 PSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGG 187
Cdd:COG0183   80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGG 114
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
1257-1340 7.89e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 37.93  E-value: 7.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631   1257 PGLLSPH--PLLQLSYTATDRHPQALEAAQAELQQHDVaQGQWDPADPA--PSALGSADLLVCNCAVAALGDP--ASALS 1330
Cdd:pfam13649    8 TGRLTLAlaRRGGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEdlPFPDGSFDLVVSSGVLHHLPDPdlEAALR 86
                           90
                   ....*....|
gi 41872631   1331 NMVAALREGG 1340
Cdd:pfam13649   87 EIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
1270-1344 8.05e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 38.03  E-value: 8.05e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41872631   1270 YTATDRHPQALEAAQAELQQHDVAQGQWDPAD-PAPSalGSADLLVCNCAVAALGDPASALSNMVAALREGGFLLL 1344
Cdd:pfam08241   21 VTGVDISPEMLELAREKAPREGLTFVVGDAEDlPFPD--NSFDLVLSSEVLHHVEDPERALREIARVLKPGGILII 94
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
1901-2054 8.40e-03

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: 40.31  E-value: 8.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1901 AQWLIQRGVqKLVLTSRSGIRTGYQAKQVRRWR-RQGVQVQVSTSNISSLEGARGLIAEAA-QLGPVGGVFNLAVVLRDG 1978
Cdd:cd08939   18 AKELVKEGA-NVIIVARSESKLEEAVEEIEAEAnASGQKVSYISADLSDYEEVEQAFAQAVeKGGPPDLVVNCAGISIPG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41872631 1979 LLENQTPEFFQDVCKPKYSGTLNldrVTREACPEL-----DYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGL 2053
Cdd:cd08939   97 LFEDLTAEEFERGMDVNYFGSLN---VAHAVLPLMkeqrpGHIVFVSSQAALVGIYGYSAYCPSKFALRGLAESLRQELK 173

                 .
gi 41872631 2054 P 2054
Cdd:cd08939  174 P 174
 
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

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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