|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
103-697 |
0e+00 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 1139.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 103 KRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCC 182
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 183 ANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSG 262
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 263 TTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSLVNTL 342
Cdd:cd05933 161 TTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 343 REVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGSDLKPFTT-RLADYLVLAKVRQALGFA 421
Cdd:cd05933 241 REVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFyRLAKKLVFKKVRKALGLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 422 KCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGR 501
Cdd:cd05933 321 RCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 502 TIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISNAMLIGDQ 581
Cdd:cd05933 401 HVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGDK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 582 RKFLSMLLTLKCTLDPDTSDQTDNLTEQAMEFCQRVGSRATTVSEIIEKKDEAVYQAIEEGIRRVNMNAAARPYHIQKWA 661
Cdd:cd05933 481 RKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKWV 560
|
570 580 590
....*....|....*....|....*....|....*.
gi 767983694 662 ILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFY 697
Cdd:cd05933 561 ILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
80-700 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 588.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 80 PYTVHRMFYEALDKYGDLIALGFKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAG 159
Cdd:COG1022 10 ADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 160 GIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEV-P 238
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGLRDDPRLLSLDELLALGREVaD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 239 EEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWt 318
Cdd:COG1022 170 PAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGP----GDRTLSFLPLAHVFERTVSYY- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 319 GIQWGAQVCFAE-PDAlkgsLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTC---- 393
Cdd:COG1022 245 ALAAGATVAFAEsPDT----LAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARlagk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 394 -PGSDLKPfTTRLADYLVLAKVRQALG----FAKCqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYN 468
Cdd:COG1022 321 sPSLLLRL-KHALADKLVFSKLREALGgrlrFAVS-----GGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 469 YRLYSSGKLVPGCRVKLvnqdAEgIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELI 548
Cdd:COG1022 395 NRIGTVGPPLPGVEVKI----AE-DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 549 ITAGGENVPPVPIEEAVKmELPIISNAMLIGDQRKFLSMLLtlkcTLDPdtsdqtdnltEQAMEFCQRVGSRATTVSEII 628
Cdd:COG1022 470 VTSGGKNVAPQPIENALK-ASPLIEQAVVVGDGRPFLAALI----VPDF----------EALGEWAEENGLPYTSYAELA 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767983694 629 ekKDEAVYQAIEEGIRRVNmNAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQ 700
Cdd:COG1022 535 --QDPEVRALIQEEVDRAN-AGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
108-682 |
7.74e-149 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 440.49 E-value: 7.74e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 108 WEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 187
Cdd:cd05907 3 WQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 188 VDTqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtqqPNQCCVLVYTSGTTGNP 267
Cdd:cd05907 83 VED------------------------------------------------------------PDDLATIIYTSGTTGRP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 268 KGVMLSQDNITWTARYGSQAgdIRPAEvqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDAlkgSLVNTLREVEP 347
Cdd:cd05907 103 KGVMLSHRNILSNALALAER--LPATE--GDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAE---TLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 348 TSHMGVPRVWEKIMERIQEVAAQSGfiRRKMLLWAmsvtleqnltcpgsdlkpfttrladylVLAKVRqalgFAKCqknf 427
Cdd:cd05907 176 TVFLAVPRVWEKVYAAIKVKAVPGL--KRKLFDLA---------------------------VGGRLR----FAAS---- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 428 yGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQdaegiGEICLWGRTIFMGY 507
Cdd:cd05907 219 -GGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD-----GEILVRGPNVMLGY 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 508 LNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMElPIISNAMLIGDQRKFLSM 587
Cdd:cd05907 293 YKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PLISQAVVIGDGRPFLVA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 588 LLTLKCtldpdtsdqtdnltEQAMEFCQRVGSRATTVSEIIekKDEAVYQAIEEGIRRVNmNAAARPYHIQKWAILERDF 667
Cdd:cd05907 372 LIVPDP--------------EALEAWAEEHGIAYTDVAELA--ANPAVRAEIEAAVEAAN-ARLSRYEQIKKFLLLPEPF 434
|
570
....*....|....*
gi 767983694 668 SISGGELGPTMKLKR 682
Cdd:cd05907 435 TIENGELTPTLKLKR 449
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
87-551 |
2.25e-105 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 327.35 E-value: 2.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 87 FYEALDKYGDLIALGFkrqDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIY 166
Cdd:pfam00501 1 LERQAARTPDKTALEV---GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 167 TTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEAldaii 246
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPP----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 247 dtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 326
Cdd:pfam00501 153 ---DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 327 CFAEPDALK--GSLVNTLREVEPTSHMGVPRVWEKIMEriqevaaqSGFIRRkmllwamsvtleqnltcpgsdlkpfttr 404
Cdd:pfam00501 230 VLPPGFPALdpAALLELIERYKVTVLYGVPTLLNMLLE--------AGAPKR---------------------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 405 ladyLVLAKVRQALgfakcqknfYGAAPMMAETQHFFLGLNIR-LYAGYGLSETSGP---HFMSSPYNYRLYSSGKLVPG 480
Cdd:pfam00501 274 ----ALLSSLRLVL---------SGGAPLPPELARRFRELFGGaLVNGYGLTETTGVvttPLPLDEDLRSLGSVGRPLPG 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983694 481 CRVKLVNQD------AEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITA 551
Cdd:pfam00501 341 TEVKIVDDEtgepvpPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
108-689 |
3.47e-92 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 297.80 E-value: 3.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 108 WEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 187
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 188 VDTQKQLEKILKIWKQLPHLKAVVIYKeppPNKMAN-----VYTMEEFMELGNEVPE---EALDAIIDTQQPNQCCVLVY 259
Cdd:cd17641 89 AEDEEQVDKLLEIADRIPSVRYVIYCD---PRGMRKyddprLISFEDVVALGRALDRrdpGLYEREVAAGKGEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 260 TSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAevqqEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDAlkgSLV 339
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPG----DEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPE---TMM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 340 NTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSV---TLEQNLTCPGSDLKPFTTR-LADYLVLAKVR 415
Cdd:cd17641 239 EDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLglrALDRGKRGRPVSLWLRLASwLADALLFRPLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 416 QALGFAKCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNqdaegIGE 495
Cdd:cd17641 319 DRLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDE-----VGE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 496 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMElPIISNA 575
Cdd:cd17641 394 ILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFS-PYIAEA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 576 MLIGDQRKFLSMLLtlkcTLDPDTsdqTDNLTEQAmefcqrvGSRATTVSEIIEKkdEAVYQAIEEGIRRVNMNAAArPY 655
Cdd:cd17641 473 VVLGAGRPYLTAFI----CIDYAI---VGKWAEQR-------GIAFTTYTDLASR--PEVYELIRKEVEKVNASLPE-AQ 535
|
570 580 590
....*....|....*....|....*....|....
gi 767983694 656 HIQKWAILERDFSISGGELGPTMKLKRLTVLEKY 689
Cdd:cd17641 536 RIRRFLLLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
107-697 |
1.15e-84 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 277.17 E-value: 1.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 107 KWEHISYSQYYLLARRAAKGFLKLGLKQ--AHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCAN 184
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 185 VIMVDtqkqlEKIlkiwkqlphlkavviykepppnkmaNVYTMEEFMELGNEVPEEALDAiidtqQPNQCCVLVYTSGTT 264
Cdd:cd05927 82 IVFCD-----AGV-------------------------KVYSLEEFEKLGKKNKVPPPPP-----KPEDLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 265 GNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYdLWTGIQWGAQVCFAEPDALKgsLVNTLRE 344
Cdd:cd05927 127 GNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFYSGDIRL--LLDDIKA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 345 VEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSvTLEQNLTCPGSdlkpFTTRLADYLVLAKVRQALGfAKCQ 424
Cdd:cd05927 204 LKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALN-YKLAELRSGVV----RASPFWDKLVFNKIKQALG-GNVR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 425 KNFYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLV-----NQDAEGI---GE 495
Cdd:cd05927 278 LMLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVdvpemNYDAKDPnprGE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 496 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIeEAVKMELPIISNA 575
Cdd:cd05927 358 VCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKI-ENIYARSPFVAQI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 576 MLIGDQRKflSMLLTLKCtLDPDTsdqtdnlteqAMEFCQRVGSRATTVSEIIekKDEAVYQAIEEGIRRVNMNAAARPY 655
Cdd:cd05927 437 FVYGDSLK--SFLVAIVV-PDPDV----------LKEWAASKGGGTGSFEELC--KNPEVKKAILEDLVRLGKENGLKGF 501
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 767983694 656 HIQKWAILERD-FSISGGELGPTMKLKRLTVLEKYKGIIDSFY 697
Cdd:cd05927 502 EQVKAIHLEPEpFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
83-579 |
7.42e-75 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 248.57 E-value: 7.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 83 VHRMFYEALDKYGDLIALGFKrqdkWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIV 162
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG----GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 163 TGIYTTSSPEacqyiaydccanvimvdtqkQLEKILKiwkqlpHLKAVVIYkepppnkmanvytmeefmelgnevpeeal 242
Cdd:COG0318 77 VPLNPRLTAE--------------------ELAYILE------DSGARALV----------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 243 daiidtqqpnqCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQW 322
Cdd:COG0318 102 -----------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP----GDVVLVALPLFHVFGLTVGLLAPLLA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 323 GAQ-VCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERiqevaaqsgfirrkmllwamsvtleqnltcpgsdlkpf 401
Cdd:COG0318 167 GATlVLLPRFDP--ERVLELIERERVTVLFGVPTMLARLLRH-------------------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 402 tTRLADYLvLAKVRQAlgfakcqknFYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSgPHFMSSPYNY---RLYSSGKL 477
Cdd:COG0318 207 -PEFARYD-LSSLRLV---------VSGGAPLPPELLERFEErFGVRIVEGYGLTETS-PVVTVNPEDPgerRPGSVGRP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 478 VPGCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIIT 550
Cdd:COG0318 275 LPGVEVRIV--DEDGrelppgeVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
490 500
....*....|....*....|....*....
gi 767983694 551 aGGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:COG0318 352 -GGENVYPAEVEEVL-AAHPGVAEAAVVG 378
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
109-682 |
2.01e-69 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 234.56 E-value: 2.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGgivtgiyttsspeacqyiaydcCANVIMv 188
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALG----------------------AVDVVR- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 DTQKQLEKILKIwkqLPHLKAVVIYKEPPPNKMAnvytmeefmelgnevpeealdaiidtqqpnqccVLVYTSGTTGNPK 268
Cdd:cd17640 61 GSDSSVEELLYI---LNHSESVALVVENDSDDLA---------------------------------TIIYTSGTTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 269 GVMLSQDNITWTARygsQAGDIRPAEVQQeVVVSYLPLSHIAAQIYDlWTGIQWGAQVCFAEPDALKgslvNTLREVEPT 348
Cdd:cd17640 105 GVMLTHANLLHQIR---SLSDIVPPQPGD-RFLSILPIWHSYERSAE-YFIFACGCSQAYTSIRTLK----DDLKRVKPH 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 349 SHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnltcpgsdlkpfttrladyLVLAKVRQALGFAkcqknfy 428
Cdd:cd17640 176 YIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF--------------------------LSGGIFKFGISGG------- 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 429 GAAPMMAETqhFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI------GEICLWGRT 502
Cdd:cd17640 223 GALPPHVDT--FFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekGIVWVRGPQ 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 503 IFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISNAMLIGDQR 582
Cdd:cd17640 301 VMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEAL-MRSPFIEQIMVVGQDQ 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 583 KFLSMLLTlkctldPDtsdqtdnlTEQAMEFCQRVGSR-ATTVSEIIEKKDE-AVYQaiEEGIRRVNMNAAARPY-HIQK 659
Cdd:cd17640 380 KRLGALIV------PN--------FEELEKWAKESGVKlANDRSQLLASKKVlKLYK--NEIKDEISNRPGFKSFeQIAP 443
|
570 580
....*....|....*....|...
gi 767983694 660 WAILErDFSISGGELGPTMKLKR 682
Cdd:cd17640 444 FALLE-EPFIENGEMTQTMKIKR 465
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
107-688 |
6.08e-65 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 223.50 E-value: 6.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 107 KWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVI 186
Cdd:cd05932 3 QVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 187 MVDTqkqlekiLKIWKQLPHLKA--VVIYKEPPPNKMANVYTMEEFMELGNEVPEEAldaiidTQQPNQCCVLVYTSGTT 264
Cdd:cd05932 83 FVGK-------LDDWKAMAPGVPegLISISLPPPSAANCQYQWDDLIAQHPPLEERP------TRFPEQLATLIYTSGTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 265 GNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEpdALKgSLVNTLRE 344
Cdd:cd05932 150 GQPKGVMLTFGSFAWAAQAGIEHIGTEE----NDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE--SLD-TFVEDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 345 VEPTSHMGVPRVWEKIMERIQEVAAQSgfiRRKMLLWAmsvtleqnltcpgsdlkPFTTRLadylVLAKVRQALGFAKCQ 424
Cdd:cd05932 223 ARPTLFFSVPRLWTKFQQGVQDKIPQQ---KLNLLLKI-----------------PVVNSL----VKRKVLKGLGLDQCR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 425 KNFYGAAPMMAETQHFF--LGLNIrlYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQdaegiGEICLWGRT 502
Cdd:cd05932 279 LAGCGSAPVPPALLEWYrsLGLNI--LEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSPA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 503 IFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISNAMLIGDQr 582
Cdd:cd05932 352 LMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKL-AEHDRVEMVCVIGSG- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 583 kfLSMLLTLkCTLDPDTSDQTDNLTEQAMEfcqrvgsraTTVSEIIEKkdeavyqaieegirrvnMNAAARPY-HIQKWA 661
Cdd:cd05932 430 --LPAPLAL-VVLSEEARLRADAFARAELE---------ASLRAHLAR-----------------VNSTLDSHeQLAGIV 480
|
570 580
....*....|....*....|....*..
gi 767983694 662 ILERDFSISGGELGPTMKLKRlTVLEK 688
Cdd:cd05932 481 VVKDPWSIDNGILTPTLKIKR-NVLEK 506
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
111-682 |
4.86e-63 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 218.24 E-value: 4.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIaydccanviMVDT 190
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHS---------LNET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 191 QkqlekilkiwkqlphlkAVVIYKEPPPNKManvytmeefmelgnevpeealdaiidtqqpnqcCVLVYTSGTTGNPKGV 270
Cdd:cd17639 77 E-----------------CSAIFTDGKPDDL---------------------------------ACIMYTSGSTGNPKGV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 271 MLSQDNITwtARYGSQAGDIRPAEVQQEVVVSYLPLSHI---AAQIydlwTGIQWGAQVCFAEPDAL-KGSLVNT---LR 343
Cdd:cd17639 107 MLTHGNLV--AGIAGLGDRVPELLGPDDRYLAYLPLAHIfelAAEN----VCLYRGGTIGYGSPRTLtDKSKRGCkgdLT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 344 EVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGsdlkpftTRLADYLVLAKVRQALGfAKC 423
Cdd:cd17639 181 EFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPG-------TPLLDELVFKKVRAALG-GRL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 424 QKNFYGAAPMMAETQHFflgLNI---RLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI------- 493
Cdd:cd17639 253 RYMLSGGAPLSADTQEF---LNIvlcPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYstdkppp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 494 -GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENvppVPIE--EAVKMELP 570
Cdd:cd17639 330 rGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEY---IALEklESIYRSNP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 571 IISNAMLIGDQRKFLSMLLTLkctldPDTSdqtdnlteQAMEFCQRVGSRATTVSEIIEKKD--EAVYQAIEEgirrvnm 648
Cdd:cd17639 407 LVNNICVYADPDKSYPVAIVV-----PNEK--------HLTKLAEKHGVINSEWEELCEDKKlqKAVLKSLAE------- 466
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 767983694 649 naAARPYHIQKWAILERDFSISG------GELGPTMKLKR 682
Cdd:cd17639 467 --TARAAGLEKFEIPQGVVLLDEewtpenGLVTAAQKLKR 504
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
253-566 |
9.96e-63 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 212.53 E-value: 9.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 253 QCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAaQIYDLWTGIQWGAQVCFAEPD 332
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTE----GDVFLSTLPLFHIG-GLFGLLGALLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 333 aLKGSLVNTLREVEPTSHMGVPRVWEKIMERIqevaaqsgfirrkmllwamsvtleqnltcpgsdlkpfttRLADYlVLA 412
Cdd:cd04433 76 -DPEAALELIEREKVTILLGVPTLLARLLKAP---------------------------------------ESAGY-DLS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 413 KVRQAlgfakcqknFYGAAPMMAETQHFFLGL-NIRLYAGYGLSETSGPHFMSSPYN--YRLYSSGKLVPGCRVKLVNQD 489
Cdd:cd04433 115 SLRAL---------VSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPDDdaRKPGSVGRPVPGVEVRIVDPD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 490 AE-----GIGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 564
Cdd:cd04433 186 GGelppgEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAV 263
|
..
gi 767983694 565 VK 566
Cdd:cd04433 264 LL 265
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
110-579 |
5.30e-62 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 215.15 E-value: 5.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 110 HISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVD 189
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 190 tQKQLEKILKIWKQLPHLKAVVIYKEPPPnKMANVYTMEEFmELGNEVPEEALDAIIDtqqPNQCCVLVYTSGTTGNPKG 269
Cdd:cd05911 90 -PDGLEKVKEAAKELGPKDKIIVLDDKPD-GVLSIEDLLSP-TLGEEDEDLPPPLKDG---KDDTAAILYSSGTTGLPKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 270 VMLSQDNITWTArygSQAGDIRPAEVQ-QEVVVSYLPLSHIAAQIYDLWTgiqwgaqvcfaepdALKGSLVNTLREVEPt 348
Cdd:cd05911 164 VCLSHRNLIANL---SQVQTFLYGNDGsNDVILGFLPLYHIYGLFTTLAS--------------LLNGATVIIMPKFDS- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 349 shmgvprvwEKIMERIQEvaaqsgfiRRKMLLW---AMSVTLeqnLTCPgsDLKPFTtrladylvLAKVRQAlgfakcqk 425
Cdd:cd05911 226 ---------ELFLDLIEK--------YKITFLYlvpPIAAAL---AKSP--LLDKYD--------LSSLRVI-------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 426 nFYGAAPMMAETQHFF--LGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVN---QDAEGI---GEIC 497
Cdd:cd05911 268 -LSGGAPLSKELQELLakRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDddgKDSLGPnepGEIC 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 498 LWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISNAML 577
Cdd:cd05911 347 VRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKEL-IKYKGFQVAPAEL-EAVLLEHPGVADAAV 424
|
..
gi 767983694 578 IG 579
Cdd:cd05911 425 IG 426
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
109-612 |
2.82e-61 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 212.30 E-value: 2.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQyylLARRAAK--GFLKL-GLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIaydccanv 185
Cdd:cd05914 6 EPLTYKD---LADNIAKfaLLLKInGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHI-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 186 imvdtqkqlekilkiwkqLPHLKAVVIYkepppnkmanvytmeefmelgnevpeealdaiidTQQPNQCCVLVYTSGTTG 265
Cdd:cd05914 75 ------------------LNHSEAKAIF----------------------------------VSDEDDVALINYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 266 NPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAepDALKGSLVNTLREV 345
Cdd:cd05914 103 NSKGVMLTYRNIVSNVDGVKEVVLLGKGDK----ILSILPLHHIYPLTFTLLLPLLNGAHVVFL--DKIPSAKIIALAFA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 346 EPTSHMGVPRVWE----KIMERIQEVAAqsgfirrKMLLWAMSVtleqnltcpgsdlKPFTTRLADyLVLAKVRQALGfa 421
Cdd:cd05914 177 QVTPTLGVPVPLViekiFKMDIIPKLTL-------KKFKFKLAK-------------KINNRKIRK-LAFKKVHEAFG-- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 422 kcqKNF----YGAAPMMAETQHFFLGLNIRLYAGYGLSETsGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQDAE-GIGE 495
Cdd:cd05914 234 ---GNIkefvIGGAKINPDVEEFLRTIGFPYTIGYGMTET-APIISYSPPNrIRLGSAGKVIDGVEVRIDSPDPAtGEGE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 496 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIE-EAVKMELPIISn 574
Cdd:cd05914 310 IIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEaKINNMPFVLES- 388
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 767983694 575 amLIGDQRKFLSMLLtlkcTLDPDTSD----QTDNLTEQAME 612
Cdd:cd05914 389 --LVVVQEKKLVALA----YIDPDFLDvkalKQRNIIDAIKW 424
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
80-579 |
2.90e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 213.89 E-value: 2.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 80 PYTVHRMFYEALDKYGDLIALgFKRQDKWehiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAG 159
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAV-YFDGRRT---TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 160 GIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ--KQLEKILKiwkQLPHLKAVVIYkEPPPNKMANVYTmEEFMELGNEV 237
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAAILP---QLPTVRTVIVE-GDGPAAPLAPEV-GEYEELLAAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 238 PEEALDAIIDtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAqiydlW 317
Cdd:PRK06187 156 SDTFDFPDID---ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR----DDVYLVIVPMFHVHA-----W 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 318 T----GIQWGA-QVCFAEPDAlkGSLVNTLREVEPT-SHMgVPRVWEkimeriqevaaqsgfirrkMLLwamsvtleQNL 391
Cdd:PRK06187 224 GlpylALMAGAkQVIPRRFDP--ENLLDLIETERVTfFFA-VPTIWQ-------------------MLL--------KAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 392 TCPGSDLkpfttrladylvlAKVRQALgfakcqknfYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSG-------PHFM 463
Cdd:PRK06187 274 RAYFVDF-------------SSLRLVI---------YGGAALPPALLREFKEkFGIDLVQGYGMTETSPvvsvlppEDQL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 464 SSPYNYRlYSSGKLVPGCRVKLVNQ-------DAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEeGWLHTGDAGRLDADG 536
Cdd:PRK06187 332 PGQWTKR-RSAGRPLPGVEARIVDDdgdelppDGGEVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDG 409
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 767983694 537 FLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:PRK06187 410 YLYITDRIKDVIIS-GGENIYPRELEDAL-YGHPAVAEVAVIG 450
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
44-699 |
1.99e-56 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 203.41 E-value: 1.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 44 PEKVNNAQWDAPEEALWTTRADGRVrlridPSCPQLPyTVHRMFYEALDKYGDLIALGFKRQD-------KWehISYSQY 116
Cdd:PLN02736 13 PEKLQTGKWNVYRSARSPLKLVSRF-----PDHPEIG-TLHDNFVYAVETFRDYKYLGTRIRVdgtvgeyKW--MTYGEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 117 YllARRAA--KGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKqL 194
Cdd:PLN02736 85 G--TARTAigSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQT-L 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 195 EKILKIWKQLPHLKAVVIY-------KEPPPNKMANVYTMEEFMELGNEVPEEALdaiidTQQPNQCCVLVYTSGTTGNP 267
Cdd:PLN02736 162 NTLLSCLSEIPSVRLIVVVggadeplPSLPSGTGVEIVTYSKLLAQGRSSPQPFR-----PPKPEDVATICYTSGTTGTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 268 KGVMLSQDNITWTARYGSQAGDIRPAEVQqevvVSYLPLSHIAAQIYDLWTgIQWGAQVCFAEPDALKgsLVNTLREVEP 347
Cdd:PLN02736 237 KGVVLTHGNLIANVAGSSLSTKFYPSDVH----ISYLPLAHIYERVNQIVM-LHYGVAVGFYQGDNLK--LMDDLAALRP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 348 TSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSV---TLEQnltcpGSDLKPfttrLADYLVLAKVRQALGfAKCQ 424
Cdd:PLN02736 310 TIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAkkqALEN-----GKNPSP----MWDRLVFNKIKAKLG-GRVR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 425 KNFYGAAPMMAETQHFflgLNI----RLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLV--------NQDAE- 491
Cdd:PLN02736 380 FMSSGASPLSPDVMEF---LRIcfggRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVdvpemnytSEDQPy 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 492 GIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEaVKMELPI 571
Cdd:PLN02736 457 PRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKF 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 572 ISNAMLIGDQrkFLSMLLTLkCTLDPDT--------SDQTDNLTeqamEFCQRVGSRATTVSEIIEKKDEAVYQAIEEgi 643
Cdd:PLN02736 536 VAQCFVYGDS--LNSSLVAV-VVVDPEVlkawaaseGIKYEDLK----QLCNDPRVRAAVLADMDAVGREAQLRGFEF-- 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 767983694 644 rrvnmnaaARPYHIqkwaILErDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQE 699
Cdd:PLN02736 607 --------AKAVTL----VPE-PFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAE 649
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
111-579 |
6.48e-55 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 194.37 E-value: 6.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDT 190
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLFDDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 191 qkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtqqpnqcCVLVYTSGTTGNPKGV 270
Cdd:cd17631 101 ----------------------------------------------------------------ALLMYTSGTTGRPKGA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 271 MLSQDNITWTARYGSQAGDIRPAEVQqeVVVsyLPLSHIAA----QIYDLWTGiqwGAQVCFAEPDAlkGSLVNTLREVE 346
Cdd:cd17631 117 MLTHRNLLWNAVNALAALDLGPDDVL--LVV--APLFHIGGlgvfTLPTLLRG---GTVVILRKFDP--ETVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 347 PTSHMGVPRVWEKImeriqevaaqsgfirrkmllwamsvtleqnLTCPGSDlkpfTTRLADylvLAKVrqalgfakcqkn 426
Cdd:cd17631 188 VTSFFLVPTMIQAL------------------------------LQHPRFA----TTDLSS---LRAV------------ 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 427 FYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYR--LYSSGKLVPGCRVKLVNQDAE-----GIGEICLW 499
Cdd:cd17631 219 IYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVDPDGRevppgEVGEIVVR 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 500 GRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:cd17631 299 GPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVEDVL-YEHPAVAEVAVIG 375
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
86-701 |
4.42e-54 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 197.17 E-value: 4.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 86 MFYEALDKYGDLIALGFK-----RQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGG 160
Cdd:PLN02614 50 VFRMSVEKYPNNPMLGRReivdgKPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 161 IVTGIYTTSSPEACQYIAYDCCANVIMVDTQKqlekILKIWKQLP----HLKAVVIYKEPPPNKMAN-------VYTMEE 229
Cdd:PLN02614 130 YCVPLYDTLGAGAVEFIISHSEVSIVFVEEKK----ISELFKTCPnsteYMKTVVSFGGVSREQKEEaetfglvIYAWDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 230 FMELGnevpeEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNI-TWTARYGSQAGDIRPAEVQQEVVVSYLPLSH 308
Cdd:PLN02614 206 FLKLG-----EGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIvTLIAGVIRLLKSANAALTVKDVYLSYLPLAH 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 309 IAAQIYDLWTgIQWGAQVCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLe 388
Cdd:PLN02614 281 IFDRVIEECF-IQHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKF- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 389 QNLTCPGSDLKpfTTRLADYLVLAKVRQALGfAKCQKNFYGAAPMMAETQHFflglnIRLYA------GYGLSETSGPHF 462
Cdd:PLN02614 357 GNMKKGQSHVE--ASPLCDKLVFNKVKQGLG-GNVRIILSGAAPLASHVESF-----LRVVAcchvlqGYGLTESCAGTF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 463 MSSPYNYRLYSS-GKLVPGCRVKL-----VNQDAEGI---GEICLWGRTIFMGYLNMEDKTCEAIDeEGWLHTGDAGRLD 533
Cdd:PLN02614 429 VSLPDELDMLGTvGPPVPNVDIRLesvpeMEYDALAStprGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQ 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 534 ADGFLYITGRLKELIITAGGENVPPVPIEEaVKMELPIISNAMLIGDQrkFLSMLLTLKctldpDTSDQTdnLTEQAME- 612
Cdd:PLN02614 508 PNGSMKIIDRKKNIFKLSQGEYVAVENIEN-IYGEVQAVDSVWVYGNS--FESFLVAIA-----NPNQQI--LERWAAEn 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 613 --------FCQRVGSRATTVSEIIEKKDEAVYQAIEEgIRRVNMNAAARPyhiqkwaiLERDFsisggeLGPTMKLKRLT 684
Cdd:PLN02614 578 gvsgdynaLCQNEKAKEFILGELVKMAKEKKMKGFEI-IKAIHLDPVPFD--------MERDL------LTPTFKKKRPQ 642
|
650
....*....|....*..
gi 767983694 685 VLEKYKGIIDSFYQEQK 701
Cdd:PLN02614 643 LLKYYQSVIDEMYKTTN 659
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
80-582 |
5.62e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 185.49 E-value: 5.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 80 PYTVHRMFYEALDKYGDLIALGFKRQDkwehISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAG 159
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVFGDQR----LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 160 GIVTGIYTTSSPEACQYIAYDCCANVIMVdTQKQLEKILKIWKQLPHLKAVVIYK-EPPPNKMANVYTMEEFMELGNEVP 238
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYILARGDAKALFV-LGLFLGVDYSATTRLPALEHVVICEtEEDDPHTEKMKTFTDFLAAGDPAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 239 EEAldaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIaaqiydlwt 318
Cdd:PRK07656 159 RAP------EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTE----GDRYLAANPFFHV--------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 319 giqWGAQVCFAEPdALKGSLVNTLREVEPtshmgvprvwEKIMERIQEvaaqsgfirRKMLLWAMSVTLEQNLtcpgsdl 398
Cdd:PRK07656 220 ---FGYKAGVNAP-LMRGATILPLPVFDP----------DEVFRLIET---------ERITVLPGPPTMYNSL------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 399 kpFTTRLADYLVLAKVRQALGfakcqknfyGAAPMMAETQHFF---LGLNIRLyAGYGLSETSGPHFMSSPYNYRL---Y 472
Cdd:PRK07656 270 --LQHPDRSAEDLSSLRLAVT---------GAASMPVALLERFeseLGVDIVL-TGYGLSEASGVTTFNRLDDDRKtvaG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 473 SSGKLVPGCRVKLVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKEL 547
Cdd:PRK07656 338 TIGTAIAGVENKIVNELGEEVpvgevGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDM 417
|
490 500 510
....*....|....*....|....*....|....*..
gi 767983694 548 IITaGGENVPPVPIEEaVKMELPIISNAMLIG--DQR 582
Cdd:PRK07656 418 FIV-GGFNVYPAEVEE-VLYEHPAVAEAAVIGvpDER 452
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
85-579 |
3.99e-49 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 179.30 E-value: 3.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 85 RMFYEALDKYGDLIALGFkrQDKWehISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 164
Cdd:cd05936 3 DLLEEAARRFPDKTALIF--MGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 165 IYTTSSPEACQYIAYDCCANVIMVDTQkqLEKILKIWkqlphlkavviykepppnkmanvytmeEFMELGNEVPEEALda 244
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAVS--FTDLLAAG---------------------------APLGERVALTPEDV-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 245 iidtqqpnqcCVLVYTSGTTGNPKGVMLSQDNITWTARygSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGA 324
Cdd:cd05936 128 ----------AVLQYTSGTTGVPKGAMLTHRNLVANAL--QIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 325 QVCFaEPDALKGSLVNTLREVEPTSHMGVPRVWEKIMEriqevaaQSGFIRRkmllwamsvtleqnltcpgsdlkpfttr 404
Cdd:cd05936 196 TIVL-IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLN-------APEFKKR---------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 405 ladylVLAKVRQALGfakcqknfyGAAPMMAETQHFFLGL-NIRLYAGYGLSETSgP--HFMSSPYNYRLYSSGKLVPGC 481
Cdd:cd05936 240 -----DFSSLRLCIS---------GGAPLPVEVAERFEELtGVPIVEGYGLTETS-PvvAVNPLDGPRKPGSIGIPLPGT 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 482 RVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIDEeGWLHTGDAGRLDADGFLYITGRLKELIItAGGE 554
Cdd:cd05936 305 EVKIV--DDDGeelppgeVGELWVRGPQVMKGYWNRPEETAEAFVD-GWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGF 380
|
490 500
....*....|....*....|....*
gi 767983694 555 NVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:cd05936 381 NVYPREVEEVL-YEHPAVAEAAVVG 404
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
111-701 |
4.14e-47 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 177.34 E-value: 4.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDt 190
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQ- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 191 QKQLEKILKIWKQL-PHLKAVVIY-------KEPPPNKMANVYTMEEFMELGNevpeeaLDAIIDTQQPNQCCVLVYTSG 262
Cdd:PLN02861 157 ESKISSILSCLPKCsSNLKTIVSFgdvsseqKEEAEELGVSCFSWEEFSLMGS------LDCELPPKQKTDICTIMYTSG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 263 TTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQE-VVVSYLPLSHIAAQIYDLWTgIQWGAQVCFAEPDALkgSLVNT 341
Cdd:PLN02861 231 TTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATEEdSYFSYLPLAHVYDQVIETYC-ISKGASIGFWQGDIR--YLMED 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 342 LREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLeQNLT--CPGSDLKPFTtrlaDYLVLAKVRQALG 419
Cdd:PLN02861 308 VQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKL-GNLRkgLKQEEASPRL----DRLVFDKIKEGLG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 420 fAKCQKNFYGAAPMMAETQHFFLGLNIR-LYAGYGLSETSGPHFMSSPYNYRLYSS-GKLVPGCRVKLVNQDAEGI---- 493
Cdd:PLN02861 383 -GRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCGGCFTSIANVFSMVGTvGVPMTTIEARLESVPEMGYdals 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 494 ----GEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVpPVPIEEAVKMEL 569
Cdd:PLN02861 462 dvprGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYV-AVENLENTYSRC 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 570 PIISNAMLIGDQrkFLSMLLTLkctLDPDTSDQTD-----NLTEQAMEFCQRVGSRattvseiiekkdeavyQAIEEGIR 644
Cdd:PLN02861 540 PLIASIWVYGNS--FESFLVAV---VVPDRQALEDwaannNKTGDFKSLCKNLKAR----------------KYILDELN 598
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 767983694 645 RVNMNAAARPYHIQKWAILERD-FSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQK 701
Cdd:PLN02861 599 STGKKLQLRGFEMLKAIHLEPNpFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAK 656
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
86-698 |
2.59e-46 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 175.00 E-value: 2.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 86 MFYEALDKYGDLIALGFKR-------QDKWEhiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFA 158
Cdd:PLN02430 47 IFSKSVEKYPDNKMLGWRRivdgkvgPYMWK--TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAH 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 159 GGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYK---EPPPNKMANV----YTMEEFM 231
Cdd:PLN02430 125 SLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLKAIVSFTsvtEEESDKASQIgvktYSWIDFL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 232 ELGNEVPEEaldaiIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTAR----YGSQAGDIRPAEvqqEVVVSYLPLS 307
Cdd:PLN02430 205 HMGKENPSE-----TNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRgvdlFMEQFEDKMTHD---DVYLSFLPLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 308 HIAAQIYDLWTgIQWGAQVCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKM--------L 379
Cdd:PLN02430 277 HILDRMIEEYF-FRKGASVGYYHGDL--NALRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIfnalykykL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 380 LWamsvtleQNLTCPGSDLKPfttrLADYLVLAKVRQALGfAKCQKNFYGAAPMMAETQHFflgLNIR----LYAGYGLS 455
Cdd:PLN02430 354 AW-------MNRGYSHKKASP----MADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEF---LRVTscafVVQGYGLT 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 456 ETSGPHFMSSPYNYRLYSSGKLVPGC---RVKLVNQ---DAEG---IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHT 526
Cdd:PLN02430 419 ETLGPTTLGFPDEMCMLGTVGAPAVYnelRLEEVPEmgyDPLGeppRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 527 GDAGRLDADGFLYITGRLKELIITAGGENVpPVPIEEAVKMELPIISNAMLIGDQrkFLSMLLTLkCTLDPDTSDQ---T 603
Cdd:PLN02430 498 GDIGEILPNGVLKIIDRKKNLIKLSQGEYV-ALEYLENVYGQNPIVEDIWVYGDS--FKSMLVAV-VVPNEENTNKwakD 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 604 DNLTEQAMEFCQRVGSRATTVSEIIEKKDEAVYQAIEEgIRRVNMNaaARPYHIqkwailERDFsisggeLGPTMKLKRL 683
Cdd:PLN02430 574 NGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEY-IKGVILE--TKPFDV------ERDL------VTATLKKRRN 638
|
650
....*....|....*
gi 767983694 684 TVLEKYKGIIDSFYQ 698
Cdd:PLN02430 639 NLLKYYQVEIDEMYR 653
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
109-565 |
3.85e-46 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 169.78 E-value: 3.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 188
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 DTqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtqqpnqcCVLVYTSGTTGNPK 268
Cdd:cd05934 82 DP----------------------------------------------------------------ASILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 269 GVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVcfaepdalkgslvnTLREVEPT 348
Cdd:cd05934 98 GVVITHANLTFAGYYSARRFGLGE----DDVYLTVLPLFHINAQAVSVLAALSVGATL--------------VLLPRFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 349 ShmgvpRVWEKImeriQEVAAQSGFIRRKMllwaMSVTLEQnltcpgsdlkPFTTRLADylvlAKVRQAlgfakcqknfY 428
Cdd:cd05934 160 S-----RFWSDV----RRYGATVTNYLGAM----LSYLLAQ----------PPSPDDRA----HRLRAA----------Y 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 429 GAAPMMAETQHFFLGLNIRLYAGYGLSETSGPhFMSSPYNYRLYSS-GKLVPGCRVKLVNQD-----AEGIGEICL---W 499
Cdd:cd05934 203 GAPNPPELHEEFEERFGVRLLEGYGMTETIVG-VIGPRDEPRRPGSiGRPAPGYEVRIVDDDgqelpAGEPGELVIrglR 281
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767983694 500 GRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIEEAV 565
Cdd:cd05934 282 GWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDM-IRRRGENISSAEVERAI 345
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
125-700 |
5.06e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 168.62 E-value: 5.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 125 KGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQY-IAYDCCANVIMVDtqKQLEKILKIWKQ 203
Cdd:PTZ00216 136 RGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYaLRETECKAIVCNG--KNVPNLLRLMKS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 204 --LPHlkAVVIY-KEPPPNKMA---NVYTMEEFMELGNEvpeEALDAIIDTQQPNQCCVLV-YTSGTTGNPKGVMLSQDN 276
Cdd:PTZ00216 214 ggMPN--TTIIYlDSLPASVDTegcRLVAWTDVVAKGHS---AGSHHPLNIPENNDDLALImYTSGTTGDPKGVMHTHGS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 277 ITwtarYGSQAGDIRPAEV-----QQEVVVSYLPLSHI----AAQIYdlwtgIQWGAQVCFAEPDalkgSLVNT------ 341
Cdd:PTZ00216 289 LT----AGILALEDRLNDLigppeEDETYCSYLPLAHImefgVTNIF-----LARGALIGFGSPR----TLTDTfarphg 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 342 -LREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnltcpgsdlkpFTTRLA-----------DYL 409
Cdd:PTZ00216 356 dLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHA------------------YQSRLRalkegkdtpywNEK 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 410 VLAKVRQALGfAKCQKNFYGAAPMMAETQHFF---LGLNIRlyaGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLV 486
Cdd:PTZ00216 418 VFSAPRAVLG-GRVRAMLSGGGPLSAATQEFVnvvFGMVIQ---GWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLL 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 487 NQD-------AEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENvppV 559
Cdd:PTZ00216 494 DTEeykhtdtPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEY---I 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 560 PIE--EAVKMELPIISN---AMLIGDQRKFLSMLLtlkctldpdtsdqtdnLTEQ--AMEFCQRVGSRAtTVSEIIekKD 632
Cdd:PTZ00216 571 ALEalEALYGQNELVVPngvCVLVHPARSYICALV----------------LTDEakAMAFAKEHGIEG-EYPAIL--KD 631
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767983694 633 EAVYQAIEEGIRRVNMNAAARPYHIQKWA-ILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQ 700
Cdd:PTZ00216 632 PEFQKKATESLQETARAAGRKSFEIVRHVrVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFADE 700
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
110-579 |
3.70e-42 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 160.09 E-value: 3.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 110 HISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVD 189
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 190 TQkQLEKILkiwkqlPHLKAVVIYKEPPPNKMANVytmeefmELGNEVPEEALDAIIDTQqpNQCCVLVYTSGTTGNPKG 269
Cdd:cd05904 112 AE-LAEKLA------SLALPVVLLDSAEFDSLSFS-------DLLFEADEAEPPVVVIKQ--DDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 270 VMLSQDNITwtARYGSQAGDIRPAEVQQEVVVSYLPLSHIaaqiydlwtgiqWGAQVCFAEPDALKGSLVntlreVepts 349
Cdd:cd05904 176 VMLTHRNLI--AMVAQFVAGEGSNSDSEDVFLCVLPMFHI------------YGLSSFALGLLRLGATVV-----V---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 350 hmgVPR-VWEKIMERIQEVAAQSGFIRRKMLLwAMSvtleqnltcpgsdlkpfTTRLADYLVLAKVRQALGfakcqknfy 428
Cdd:cd05904 233 ---MPRfDLEELLAAIERYKVTHLPVVPPIVL-ALV-----------------KSPIVDKYDLSSLRQIMS--------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 429 GAAPMMAETQHFFLGL--NIRLYAGYGLSETSGP---HFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI------GEIC 497
Cdd:cd05904 283 GAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESlppnqtGELW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 498 LWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISNAML 577
Cdd:cd05904 363 IRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKEL-IKYKGFQVAPAEL-EALLLSHPEILDAAV 440
|
..
gi 767983694 578 IG 579
Cdd:cd05904 441 IP 442
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
78-564 |
1.14e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 158.19 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 78 QLPYTVHRMFYEALDKYGDLIALGF----KRQDKWEHISYSQyyLLAR--RAAKGFLKLGLKQAHSVAILGFNSPEwffs 151
Cdd:PRK07529 22 DLPASTYELLSRAAARHPDAPALSFlldaDPLDRPETWTYAE--LLADvtRTANLLHSLGVGPGDVVAFLLPNLPE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 152 AVGTVFAG---GIVTGIYTTSSPEACQYIAYDCCANVIM-------VDTQKQLEKILKiwkQLPHLKAVVIY----KEPP 217
Cdd:PRK07529 96 THFALWGGeaaGIANPINPLLEPEQIAELLRAAGAKVLVtlgpfpgTDIWQKVAEVLA---ALPELRTVVEVdlarYLPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 218 PNKMAnvytmEEFMELGNEVPEEALDAIIDTQQ-----------PNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQ 286
Cdd:PRK07529 173 PKRLA-----VPLIRRKAHARILDFDAELARQPgdrlfsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGAL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 287 AGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSLVntlreveptshmgVPRVWeKIMERIQe 366
Cdd:PRK07529 248 LLGLGP----GDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGPGV-------------IANFW-KIVERYR- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 367 VAAQSGfirrkmLLWAMSVTLEqnltCP--GSDLkpfttrladylvlakvrQALGFAKCqknfyGAAPMMAET-QHFFLG 443
Cdd:PRK07529 309 INFLSG------VPTVYAALLQ----VPvdGHDI-----------------SSLRYALC-----GAAPLPVEVfRRFEAA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 444 LNIRLYAGYGLSETSGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQDAEG----------IGEICLWGRTIFMGYLNmED 512
Cdd:PRK07529 357 TGVRIVEGYGLTEATCVSSVNPPDGeRRIGSVGLRLPYQRVRVVILDDAGrylrdcavdeVGVLCIAGPNVFSGYLE-AA 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 767983694 513 KTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 564
Cdd:PRK07529 436 HNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIR-GGHNIDPAAIEEA 486
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
107-580 |
7.12e-40 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 156.43 E-value: 7.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 107 KWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYiaydcCANVI 186
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCH-----SLNET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 187 MVDT----QKQLEKILKIWKQLPHLKAVVIYKEPPP------NKMAN--VYTMEEFMELGNEVPEEAldaiiDTQQPNQC 254
Cdd:PLN02387 178 EVTTvicdSKQLKKLIDISSQLETVKRVIYMDDEGVdsdsslSGSSNwtVSSFSEVEKLGKENPVDP-----DLPSPNDI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 255 CVLVYTSGTTGNPKGVMLSQDNITWTArygSQAGDIRPAEVQQEVVVSYLPLSHI---AAQIydlwTGIQWGAQVCFAEP 331
Cdd:PLN02387 253 AVIMYTSGSTGLPKGVMMTHGNIVATV---AGVMTVVPKLGKNDVYLAYLPLAHIlelAAES----VMAAVGAAIGYGSP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 332 DAL--------KGSL--VNTLRevePTSHMGVPRVWEKIMERIQE-VAAQSG---------FIRRKMLL---WAMSVTLE 388
Cdd:PLN02387 326 LTLtdtsnkikKGTKgdASALK---PTLMTAVPAILDRVRDGVRKkVDAKGGlakklfdiaYKRRLAAIegsWFGAWGLE 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 389 QnltcpgsdlkpfttRLADYLVLAKVRQALG----FAKCqknfyGAAPMMAETQHFflgLNIRLYA----GYGLSETSGP 460
Cdd:PLN02387 403 K--------------LLWDALVFKKIRAVLGgrirFMLS-----GGAPLSGDTQRF---INICLGApigqGYGLTETCAG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 461 HFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI---------GEICLWGRTIFMGYLNMEDKTCEA--IDEEG--WLHTG 527
Cdd:PLN02387 461 ATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYlisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTG 540
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 767983694 528 DAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISNAMLIGD 580
Cdd:PLN02387 541 DIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAAL-SVSPYVDNIMVHAD 592
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
77-563 |
8.15e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 154.58 E-value: 8.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 77 PQLPYTVHRMFYEALDKYGDLIALGFKRQD-KWehiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWffsaVGT 155
Cdd:PRK08315 12 PLLEQTIGQLLDRTAARYPDREALVYRDQGlRW---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEW----VLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 156 VFAGGIVTGIYTTSSPeacqyiAY------------DCCANVIM--------VDTQKQLEKILKIW-------KQLPHLK 208
Cdd:PRK08315 85 QFATAKIGAILVTINP------AYrlseleyalnqsGCKALIAAdgfkdsdyVAMLYELAPELATCepgqlqsARLPELR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 209 AVVIYKEPPPNKManvYTMEEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAg 288
Cdd:PRK08315 159 RVIFLGDEKHPGM---LNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEA- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 289 dIRPAEvqQEVVVSYLPLSH--------IAAqiydLWTGiqwGAQVCFAEP-DALKgslvnTLREVEP---TSHMGVPrv 356
Cdd:PRK08315 235 -MKLTE--EDRLCIPVPLYHcfgmvlgnLAC----VTHG---ATMVYPGEGfDPLA-----TLAAVEEercTALYGVP-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 357 wekIMeriqevaaqsgFIrrkmllwAMsvtLEQ------NL-----------TCPGSDLKpfttrladylvlakvrqalg 419
Cdd:PRK08315 298 ---TM-----------FI-------AE---LDHpdfarfDLsslrtgimagsPCPIEVMK-------------------- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 420 faKCQKNFYgaapmMAETQhfflglnIrlyaGYGLSETSGPHFMSS---PYNYRLYSSGKLVPGCRVKLVnqDAEG---- 492
Cdd:PRK08315 334 --RVIDKMH-----MSEVT-------I----AYGMTETSPVSTQTRtddPLEKRVTTVGRALPHLEVKIV--DPETgetv 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767983694 493 ----IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEE 563
Cdd:PRK08315 394 prgeQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIEE 467
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
111-579 |
3.31e-38 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 148.61 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDT 190
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 191 QKQLEKI-LKIWKQLPHLKAVVIYKEPPPNKMANvytmeefmELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKG 269
Cdd:cd05926 95 GELGPASrAASKLGLAILELALDVGVLIRAPSAE--------SLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 270 VMLSQDNITWTARYGSQAGDIRPAEvqQEVVVsyLPLSHIAAQIYDLWTGIQWGAQVCFaePDALKGSLV-NTLREVEPT 348
Cdd:cd05926 167 VPLTHRNLAASATNITNTYKLTPDD--RTLVV--MPLFHVHGLVASLLSTLAAGGSVVL--PPRFSASTFwPDVRDYNAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 349 SHMGVPRVWEKIMERIQE----VAAQSGFIRrkmllwamsvtleqnlTCpGSDLKPFTtrladylvlakvrqalgFAKCQ 424
Cdd:cd05926 241 WYTAVPTIHQILLNRPEPnpesPPPKLRFIR----------------SC-SASLPPAV-----------------LEALE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 425 KNFygAAPMMaETqhfflglnirlyagYGLSETSgpHFMSS----PYNYRLYSSGKLVpGCRVKLVNQDAE-----GIGE 495
Cdd:cd05926 287 ATF--GAPVL-EA--------------YGMTEAA--HQMTSnplpPGPRKPGSVGKPV-GVEVRILDEDGEilppgVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 496 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISNA 575
Cdd:cd05926 347 ICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINR-GGEKISPLEVDG-VLLSHPAVLEA 424
|
....
gi 767983694 576 MLIG 579
Cdd:cd05926 425 VAFG 428
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
99-563 |
1.26e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 148.00 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 99 ALGFKRQDKweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQY-I 177
Cdd:PRK12583 36 ALVVRHQAL--RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYaL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 178 AYDCCANVIMVDTQKQ------LEKILK----------IWKQLPHLKAVVIY-KEPPPNKMAnvytMEEFMELGNEVPEE 240
Cdd:PRK12583 114 GQSGVRWVICADAFKTsdyhamLQELLPglaegqpgalACERLPELRGVVSLaPAPPPGFLA----WHELQARGETVSRE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 241 ALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQagdiRPAEVQQEVVVSYLPLSHIAAQIYDLWTGI 320
Cdd:PRK12583 190 ALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAE----SLGLTEHDRLCVPVPLYHCFGMVLANLGCM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 321 QWGAQVCFA----EPDAlkgslvnTLREVEP---TSHMGVPRVWEKIMERIQevaaqsgfiRRKMLLWAMSVTLEQNLTC 393
Cdd:PRK12583 266 TVGACLVYPneafDPLA-------TLQAVEEercTALYGVPTMFIAELDHPQ---------RGNFDLSSLRTGIMAGAPC 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 394 PGSdlkpfttrladylVLAKVRQALgfakcqknfygaapMMAETQhfflglnirlyAGYGLSETSGPHFMSS---PYNYR 470
Cdd:PRK12583 330 PIE-------------VMRRVMDEM--------------HMAEVQ-----------IAYGMTETSPVSLQTTaadDLERR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 471 LYSSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLK 545
Cdd:PRK12583 372 VETVGRTQPHLEVKVVDPDGAtvprgEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSK 451
|
490
....*....|....*...
gi 767983694 546 ELIITaGGENVPPVPIEE 563
Cdd:PRK12583 452 DMIIR-GGENIYPREIEE 468
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
109-581 |
6.95e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 145.00 E-value: 6.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFL-KLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 187
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 188 VDTQKQlEKILKIWKqlphlkavVIYKEPPpnkmanvytmeefmeLGNEVPEEALDA-IIDTQQPNQ--CCVLVYTSGTT 264
Cdd:PRK06839 106 VEKTFQ-NMALSMQK--------VSYVQRV---------------ISITSLKEIEDRkIDNFVEKNEsaSFIICYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 265 GNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAaqiydlwtGIQwgaqvCFAEPDALKGSLVNTLRE 344
Cdd:PRK06839 162 GKPKGAVLTQENMFWNALNNTFAIDLT----MHDRSIVLLPLFHIG--------GIG-----LFAFPTLFAGGVIIVPRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 345 VEPTSH------------MGVPRVWEKIMERIqevaaqsgfirrkmllwamsvtleqnltcpgsdlKPFTTRLAdylvla 412
Cdd:PRK06839 225 FEPTKAlsmiekhkvtvvMGVPTIHQALINCS----------------------------------KFETTNLQ------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 413 KVRQalgfakcqknFY-GAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYR--LYSSGKLVPGCRVKLVNQD 489
Cdd:PRK06839 265 SVRW----------FYnGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIDEN 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 490 AE-----GIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 564
Cdd:PRK06839 335 KNkvevgEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQV 412
|
490
....*....|....*..
gi 767983694 565 VKmELPIISNAMLIGDQ 581
Cdd:PRK06839 413 IN-KLSDVYEVAVVGRQ 428
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
86-579 |
1.70e-36 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 144.21 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 86 MFYeALDKYGDLI-ALGFKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 164
Cdd:cd17642 20 LHK-AMKRYASVPgTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 165 IYTTSSpEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIykepppnkMANVYTMEEFMELGNEVpEEALDA 244
Cdd:cd17642 99 TNDIYN-ERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIII--------LDSKEDYKGYQCLYTFI-TQNLPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 245 IIDTQQ--PN------QCCVLVYTSGTTGNPKGVMLSQDNITwtARYGSQAGDIRPAEVQQEV-VVSYLPLSHiAAQIYD 315
Cdd:cd17642 169 GFNEYDfkPPsfdrdeQVALIMNSSGSTGLPKGVQLTHKNIV--ARFSHARDPIFGNQIIPDTaILTVIPFHH-GFGMFT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 316 LWTGIQWGAQVCFaepdalkgslvntlreveptshmgVPRVWEKI-MERIQEVAAQSGF-IRRKMLLWAMSVTLEQnltc 393
Cdd:cd17642 246 TLGYLICGFRVVL------------------------MYKFEEELfLRSLQDYKVQSALlVPTLFAFFAKSTLVDK---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 394 pgsdlkpftTRLADYLVLAKvrqalgfakcqknfyGAAPMMAETQHFF---LGLN-IRlyAGYGLSETSGPHFMSSPYNY 469
Cdd:cd17642 298 ---------YDLSNLHEIAS---------------GGAPLSKEVGEAVakrFKLPgIR--QGYGLTETTSAILITPEGDD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 470 RLYSSGKLVPGCRVKLVNQDAEGI------GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGR 543
Cdd:cd17642 352 KPGAVGKVVPFFYAKVVDLDTGKTlgpnerGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDR 431
|
490 500 510
....*....|....*....|....*....|....*.
gi 767983694 544 LKELiITAGGENVPPVPIeEAVKMELPIISNAMLIG 579
Cdd:cd17642 432 LKSL-IKYKGYQVPPAEL-ESILLQHPKIFDAGVAG 465
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
259-628 |
7.55e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 138.77 E-value: 7.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 259 YTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSL 338
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDP----DDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYRNPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 339 V--NTLREVE---PTSHMGVPRVWEKIMERiqevaaqsgfirrkmllwamsvtleqnltcPGSdlkpfttrlADylvLAK 413
Cdd:cd05944 85 LfdNFWKLVEryrITSLSTVPTVYAALLQV------------------------------PVN---------AD---ISS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 414 VRQALGfakcqknfyGAAPMMAETQHFF---LGLNIrlYAGYGLSETSGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQD 489
Cdd:cd05944 123 LRFAMS---------GAAPLPVELRARFedaTGLPV--VEGYGLTEATCLVAVNPPDGpKRPGSVGLRLPYARVRIKVLD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 490 AEG----------IGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPV 559
Cdd:cd05944 192 GVGrllrdcapdeVGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIR-GGHNIDPA 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767983694 560 PIEEAVkMELPIISNAMLIGDQRKFLSMLLTLKCTLDPDTSDQTDNLTEQAMEfcqRVGSRATTVSEII 628
Cdd:cd05944 270 LIEEAL-LRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARD---HVPERAAVPKHIE 334
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
112-579 |
6.68e-35 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 139.30 E-value: 6.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 112 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSP---EWFFSAVGtvfAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 188
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHrhlELYYAVPG---MGAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 DtqKQLEKIL-KIWKQLPHLKAVVIYK---EPPPNKMANVYTMEEFMElgnevpEEALDAIIDTQQPNQCCVLVYTSGTT 264
Cdd:cd12119 104 D--RDFLPLLeAIAPRLPTVEHVVVMTddaAMPEPAGVGVLAYEELLA------AESPEYDWPDFDENTAAAICYTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 265 GNPKGVMLSQDNiTWTARYGSQAGDIRPAEvQQEVVVSYLPLSHIAAqiydlW----TGIQWGAQVCFAEPDALKGSLVN 340
Cdd:cd12119 176 GNPKGVVYSHRS-LVLHAMAALLTDGLGLS-ESDVVLPVVPMFHVNA-----WglpyAAAMVGAKLVLPGPYLDPASLAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 341 TLREVEPTSHMGVPRVWEkimeriqevaaqsgfirrkMLLwamsvtleQNLTCPGSDLKPfttrladylvLAKVrqALGf 420
Cdd:cd12119 249 LIEREGVTFAAGVPTVWQ-------------------GLL--------DHLEANGRDLSS----------LRRV--VIG- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 421 akcqknfyGAA--PMMAETqhfFLGLNIRLYAGYGLSETS--------GPHFMSSPY----NYRLySSGKLVPGCRVKLV 486
Cdd:cd12119 289 --------GSAvpRSLIEA---FEERGVRVIHAWGMTETSplgtvarpPSEHSNLSEdeqlALRA-KQGRPVPGVELRIV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 487 NQ-------DAEGIGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPV 559
Cdd:cd12119 357 DDdgrelpwDGKAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKDV-IKSGGEWISSV 434
|
490 500
....*....|....*....|
gi 767983694 560 PIEEAVkMELPIISNAMLIG 579
Cdd:cd12119 435 ELENAI-MAHPAVAEAAVIG 453
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
86-583 |
1.81e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 138.98 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 86 MFYEALDKYGDLIALGF--KRQdkwehiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEwffsAVGTVFA----G 159
Cdd:PRK05605 37 LYDNAVARFGDRPALDFfgATT------TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQ----HIVAFYAvlrlG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 160 GIVT---GIYTTSSPE-------ACQYIAYDCCANVI--MVDTQkQLEKIL--KIWKQLPHLKAVVIyKEPPPNKMAnvy 225
Cdd:PRK05605 107 AVVVehnPLYTAHELEhpfedhgARVAIVWDKVAPTVerLRRTT-PLETIVsvNMIAAMPLLQRLAL-RLPIPALRK--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 226 tMEEFMELG--NEVPEEALDA--------IIDTQQPNQCCV--LVYTSGTTGNPKGVMLSQDNITWTARYGsQA--GDIR 291
Cdd:PRK05605 182 -ARAALTGPapGTVPWETLVDaaiggdgsDVSHPRPTPDDValILYTSGTTGKPKGAQLTHRNLFANAAQG-KAwvPGLG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 292 PaevQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWEKIMEriqevAAQ 370
Cdd:PRK05605 260 D---GPERVLAALPMFHAYGLTLCLTLAVSIGGElVLLPAPDI--DLILDAMKKHPPTWLPGVPPLYEKIAE-----AAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 371 sgfirrkmllwamsvtlEQNLTcpgsdlkpfttrladylvLAKVRQAlgfakcqknFYGAAPMMAETQHFFLGL-NIRLY 449
Cdd:PRK05605 330 -----------------ERGVD------------------LSGVRNA---------FSGAMALPVSTVELWEKLtGGLLV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 450 AGYGLSETSgPHFMSSPYN--YRLYSSGKLVPGCRVKLVNQD------AEG-IGEICLWGRTIFMGYLNMEDKTCEAIdE 520
Cdd:PRK05605 366 EGYGLTETS-PIIVGNPMSddRRPGYVGVPFPDTEVRIVDPEdpdetmPDGeEGELLVRGPQVFKGYWNRPEETAKSF-L 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767983694 521 EGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISNAMLIGDQRK 583
Cdd:PRK05605 444 DGWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEEVLR-EHPGVEDAAVVGLPRE 504
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
94-579 |
5.41e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 136.65 E-value: 5.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 94 YGDLIALGFKR-QDK----WEH--ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIY 166
Cdd:PRK06188 14 YGHLLVSALKRyPDRpalvLGDtrLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 167 TTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVViykepppnKMANVYTMEEFMELGNEVPEEALDAII 246
Cdd:PRK06188 94 PLGSLDDHAYVLEDAGISTLIVDPAPFVERALALLARVPSLKHVL--------TLGPVPDGVDLLAAAAKFGPAPLVAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 247 DTQQPNqccVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIrPAEVQqevvvsYL---PLSHIAAqiydlwtgiqwg 323
Cdd:PRK06188 166 LPPDIA---GLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEW-PADPR------FLmctPLSHAGG------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 324 aqvCFAEPDALKGSLVNTLREVEPTShmgVPRVWEKimERIQEVaaqsgfirrkMLLWAMSVTLeqnLTCPGSdlkpftt 403
Cdd:PRK06188 224 ---AFFLPTLLRGGTVIVLAKFDPAE---VLRAIEE--QRITAT----------FLVPTMIYAL---LDHPDL------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 404 RLADYLVLAKVrqalgfakcqknFYGAAPMMAetqhfflglnIRLYAG-----------YGLSE--------TSGPHFMS 464
Cdd:PRK06188 276 RTRDLSSLETV------------YYGASPMSP----------VRLAEAierfgpifaqyYGQTEapmvitylRKRDHDPD 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 465 SPYnyRLYSSGKLVPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLY 539
Cdd:PRK06188 334 DPK--RLTSCGRPTPGLRVALLDEDgrevAQGeVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYY 410
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 767983694 540 ITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:PRK06188 411 IVDRKKDMIVT-GGFNVFPREVEDVL-AEHPAVAQVAVIG 448
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
112-579 |
5.93e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 133.95 E-value: 5.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 112 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG---IYTtsSPEAC-QYIAydccANVIM 187
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTanpFYT--PAEIAkQAKA----SGAKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 188 VDTQKQLEKILKIWKQLPHLKAVVIyKEPPPNKManvytmeEFMELGNEVPEEALDAIIDtqqPNQCCVLVYTSGTTGNP 267
Cdd:PLN02246 126 IITQSCYVDKLKGLAEDDGVTVVTI-DDPPEGCL-------HFSELTQADENELPEVEIS---PDDVVALPYSSGTTGLP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 268 KGVMLSQDN-ITWTArygsqagdirpaevQQ-------------EVVVSYLPLSHIAAQIYDLWTGIQWGAQVCfaepda 333
Cdd:PLN02246 195 KGVMLTHKGlVTSVA--------------QQvdgenpnlyfhsdDVILCVLPMFHIYSLNSVLLCGLRVGAAIL------ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 334 lkgslvntlreveptshmgvprvwekIMERIqEVAAQSGFIRRKMLLWAMSV-----TLEQNltcpgsdlkPFTTRlADy 408
Cdd:PLN02246 255 --------------------------IMPKF-EIGALLELIQRHKVTIAPFVppivlAIAKS---------PVVEK-YD- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 409 lvLAKVRQALGfakcqknfyGAAPMMAETQHFFLGL--NIRLYAGYGLSEtSGP------HFMSSPYNYRLYSSGKLVPG 480
Cdd:PLN02246 297 --LSSIRMVLS---------GAAPLGKELEDAFRAKlpNAVLGQGYGMTE-AGPvlamclAFAKEPFPVKSGSCGTVVRN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 481 CRVKLVNQDAeGI-------GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGG 553
Cdd:PLN02246 365 AELKIVDPET-GAslprnqpGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 443
|
490 500
....*....|....*....|....*.
gi 767983694 554 EnVPPVPIeEAVKMELPIISNAMLIG 579
Cdd:PLN02246 444 Q-VAPAEL-EALLISHPSIADAAVVP 467
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
111-579 |
2.20e-32 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 130.49 E-value: 2.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFL-KLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSspeacqyiaydccanvimvd 189
Cdd:cd05941 12 ITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSY-------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 190 TQKQLEKILkiwkqlphlkavviykepppnkmanvytmeefmelGNEVPEEALDAiidtqqpnqcCVLVYTSGTTGNPKG 269
Cdd:cd05941 72 PLAELEYVI-----------------------------------TDSEPSLVLDP----------ALILYTSGTTGRPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 270 VMLSQDNITWTARYGSQAGDIRPAEVQQEVvvsyLPLSHIAAQIYDLWTGIQWGAQVCF-AEPDAlkgSLVNTLREVEP- 347
Cdd:cd05941 107 VVLTHANLAANVRALVDAWRWTEDDVLLHV----LPLHHVHGLVNALLCPLFAGASVEFlPKFDP---KEVAISRLMPSi 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 348 TSHMGVPRVWEKIMERIQEVAAQSGFIRrkmllwamsvtleqnltcpgsdlkpfttrladylvlakvrqALGFAKCQKNF 427
Cdd:cd05941 180 TVFMGVPTIYTRLLQYYEAHFTDPQFAR-----------------------------------------AAAAERLRLMV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 428 YGAAPMMAETQHFFLGLN-IRLYAGYGLSETSgphfM--SSPYN--YRLYSSGKLVPGCRVKLVNQ------DAEGIGEI 496
Cdd:cd05941 219 SGSAALPVPTLEEWEAITgHTLLERYGMTEIG----MalSNPLDgeRRPGTVGMPLPGVQARIVDEetgeplPRGEVGEI 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 497 CLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISNAM 576
Cdd:cd05941 295 QVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVL-LAHPGVSECA 373
|
...
gi 767983694 577 LIG 579
Cdd:cd05941 374 VIG 376
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
93-579 |
3.55e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 131.21 E-value: 3.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 93 KYGDLIALGFkRQDKWehiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPE 172
Cdd:PRK08316 23 RYPDKTALVF-GDRSW---TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 173 ACQYIAYDCCANVIMVDTQ--KQLEKILKIWKQLPHLKAVVIYKEPPPNKMANvytmeeFMELGNEVPEEALDAIIDTQQ 250
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPAlaPTAEAALALLPVDTLILSLVLGGREAPGGWLD------FADWAEAGSVAEPDVELADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 251 PNQccvLVYTSGTTGNPKGVMLSQDNITWtaRYGSQ--AGDIRPAEVQqevvVSYLPLSHiAAQIY-----DLWTGiqwG 323
Cdd:PRK08316 173 LAQ---ILYTSGTESLPKGAMLTHRALIA--EYVSCivAGDMSADDIP----LHALPLYH-CAQLDvflgpYLYVG---A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 324 AQVCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWekimeriqevaaqsgfirrkmllwamsVTLeqnLTCPGSDlkpfTT 403
Cdd:PRK08316 240 TNVILDAPDP--ELILRTIEAERITSFFAPPTVW---------------------------ISL---LRHPDFD----TR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 404 RLadylvlakvrQALgfakcQKNFYGAAPM----MAETQHFFLGLniRLYAGYGLSETSGPHFMSSPYNY--RLYSSGKL 477
Cdd:PRK08316 284 DL----------SSL-----RKGYYGASIMpvevLKELRERLPGL--RFYNCYGQTEIAPLATVLGPEEHlrRPGSAGRP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 478 VPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaG 552
Cdd:PRK08316 347 VLNVETRVVDDDgndvAPGeVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKT-G 424
|
490 500
....*....|....*....|....*..
gi 767983694 553 GENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:PRK08316 425 GENVASREVEEAL-YTHPAVAEVAVIG 450
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
108-699 |
4.73e-32 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 131.40 E-value: 4.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 108 WEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAG---GIVTGIYTTSSPE--ACQYIAYDCC 182
Cdd:cd05921 23 WRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGvpaAPVSPAYSLMSQDlaKLKHLFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 183 ANVIMVDTQKQLEKILKIWKqLPHLKAVVIYKEPPPNKMANvytmeeFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSG 262
Cdd:cd05921 103 PGLVFAQDAAPFARALAAIF-PLGTPLVVSRNAVAGRGAIS------FAELAATPPTAAVDAAFAAVGPDTVAKFLFTSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 263 TTGNPKGVMLSQDNITwtaryGSQAGDIRPAEVQQE---VVVSYLPLSHIAAQIYD----LWTG----IQWGAQVcfaeP 331
Cdd:cd05921 176 STGLPKAVINTQRMLC-----ANQAMLEQTYPFFGEeppVLVDWLPWNHTFGGNHNfnlvLYNGgtlyIDDGKPM----P 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 332 DALKGSLVNtLREVEPTSHMGVPRVWEKI---MERiQEVAAQSGFIRRKMLLWAmsvtleqnltcpGSDLKPFT-TRLad 407
Cdd:cd05921 247 GGFEETLRN-LREISPTVYFNVPAGWEMLvaaLEK-DEALRRRFFKRLKLMFYA------------GAGLSQDVwDRL-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 408 ylvlakvrQALGFAKCqknfygaapmmaetqhfflGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVN 487
Cdd:cd05921 311 --------QALAVATV-------------------GERIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 488 QDaeGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRL----DADGFLYITGRLKELIITAGGENVPPVPIE- 562
Cdd:cd05921 364 SG--GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVGPLRa 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 563 EAVKMELPIISNAMLIGDQRKFLSMLLTlkctldPDTSDqtdnlteqamefCQR-VGSRATTVSEIIekKDEAVYQAIEE 641
Cdd:cd05921 442 RAVAACAPLVHDAVVAGEDRAEVGALVF------PDLLA------------CRRlVGLQEASDAEVL--RHAKVRAAFRD 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 767983694 642 GIRRVNMNAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQE 699
Cdd:cd05921 502 RLAALNGEATGSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
251-579 |
9.47e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 126.62 E-value: 9.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 251 PNQCCVLVYTSGTTGNPKGVMLSQDNItwtARYGSQAGDiRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAE 330
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNI---VNNGYFIGE-RLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 331 P--DALKgslvnTLREVEP---TSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnlTCPGSdlkpfttrl 405
Cdd:cd05917 77 PsfDPLA-----VLEAIEKekcTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGA---------PCPPE--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 406 adylVLAKVRQALGFAKCQknfygaapmmaetqhfflglnirlyAGYGLSETSGPHFMSS---PYNYRLYSSGKLVPGCR 482
Cdd:cd05917 134 ----LMKRVIEVMNMKDVT-------------------------IAYGMTETSPVSTQTRtddSIEKRVNTVGRIMPHTE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 483 VKLVnqDAEG--------IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGE 554
Cdd:cd05917 185 AKIV--DPEGgivppvgvPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGE 261
|
330 340
....*....|....*....|....*
gi 767983694 555 NVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:cd05917 262 NIYPREIEEFL-HTHPKVSDVQVVG 285
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
95-566 |
3.51e-31 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 128.51 E-value: 3.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 95 GDLIALGF--KRQDKWEHISYSQYYLLARRAAKGFLKLGlKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPE 172
Cdd:cd05931 7 PDRPAYTFldDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 173 A---CQYIAYDCCANVIMVDTqkqlekilkiwkqlPHLKAVVIYKEPPPnkmanvytmeEFMELGNEVPEEALDAIIDTQ 249
Cdd:cd05931 86 HaerLAAILADAGPRVVLTTA--------------AALAAVRAFAASRP----------AAGTPRLLVVDLLPDTSAADW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 250 QPNQC-----CVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHiaaqiyDLwtgiqwga 324
Cdd:cd05931 142 PPPSPdpddiAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDP----GDVVVSWLPLYH------DM-------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 325 qvcfaepdALKGSLVNTLreveptsHMGVPRVWekiMeriqevaAQSGFIRRKML-LWAMSvtlEQNLTCPGS-----DL 398
Cdd:cd05931 204 --------GLIGGLLTPL-------YSGGPSVL---M-------SPAAFLRRPLRwLRLIS---RYRATISAApnfayDL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 399 --KPFTTRLADYLVLAKVRQALgfakcqkNfyGAAPMMAET-QHF---FLGLNIR---LYAGYGLSE-----TSGPHF-- 462
Cdd:cd05931 256 cvRRVRDEDLEGLDLSSWRVAL-------N--GAEPVRPATlRRFaeaFAPFGFRpeaFRPSYGLAEatlfvSGGPPGtg 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 463 -------------------MSSPYNYRLYSSGKLVPGCRVKLVNQD-----AEG-IGEICLWGRTIFMGYLNMEDKTCE- 516
Cdd:cd05931 327 pvvlrvdrdalagravavaADDPAARELVSCGRPLPDQEVRIVDPEtgrelPDGeVGEIWVRGPSVASGYWGRPEATAEt 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 767983694 517 -----AIDEEGWLHTGDAGRLdADGFLYITGRLKELIITAgGENVPPVPIEEAVK 566
Cdd:cd05931 407 fgalaATDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVR-GRNHYPQDIEATAE 459
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
82-579 |
4.73e-31 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 127.98 E-value: 4.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 82 TVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGI 161
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDR----TLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 162 VTGIYTTSSPEACQYIAYDCCANvIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKmanvytmeEFMELGNEVPEEA 241
Cdd:TIGR03098 77 FVPINPLLKAEQVAHILADCNVR-LLVTSSERLDLLHPALPGCHDLRTLIIVGDPAHAS--------EGHPGEEPASWPK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 242 LDAIIDTQQPNQC------CVLvYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAevqqEVVVSYLPLSHIAAQiYD 315
Cdd:TIGR03098 148 LLALGDADPPHPVidsdmaAIL-YTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPD----DRLLAVLPLSFDYGF-NQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 316 LWTGIQWGAQVCFAEPdALKGSLVNTLREVEPTSHMGVPRVWEKIME-RIQEVAAQSgfIRRkmllwamsvtleqnLTCP 394
Cdd:TIGR03098 222 LTTAFYVGATVVLHDY-LLPRDVLKALEKHGITGLAAVPPLWAQLAQlDWPESAAPS--LRY--------------LTNS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 395 GSDLKPFTtrladylvLAKVRQALGfakcqknfygaapmmaetqhfflglNIRLYAGYGLSETsgphFMSS---P--YNY 469
Cdd:TIGR03098 285 GGAMPRAT--------LSRLRSFLP-------------------------NARLFLMYGLTEA----FRSTylpPeeVDR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 470 RLYSSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCE----AIDEEGWLH-------TGDAGRLD 533
Cdd:TIGR03098 328 RPDSIGKAIPNAEVLVLREDGSecapgEEGELVHRGALVAMGYWNDPEKTAErfrpLPPFPGELHlpelavwSGDTVRRD 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 767983694 534 ADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:TIGR03098 408 EEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVA-YATGLVAEAVAFG 451
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
255-564 |
2.43e-30 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 122.05 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 255 CVLVYTSGTTGNPKGVMLSQDNITWTARyGSQAgdiRPAEVQQEVVVSYLPLSHIAAQiYDLWTGIQWGAQVCFAEPDAL 334
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAA-GLHS---RLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 335 kgsLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFirRKMLLwamsvtleqnltcpgsdlkpfttrladylvlakv 414
Cdd:cd17630 78 ---LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSL--RAVLL---------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 415 rqalgfakcqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQdaegiG 494
Cdd:cd17630 119 --------------GGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----G 179
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 495 EICLWGRTIFMGYLNMEdkTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 564
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAA 246
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
88-579 |
3.45e-30 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 125.99 E-value: 3.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 88 YEALDKY----GDLIALGFKRQDKWE-HISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIV 162
Cdd:COG0365 12 YNCLDRHaegrGDKVALIWEGEDGEErTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 163 TGIYTTSSPEACQYIAYDCCANVIMVD--------TQKQLEKILKIWKQLPHLKAVVIYKEP-PPNKMANVYTMEEFMEL 233
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITAdgglrggkVIDLKEKVDEALEELPSLEHVIVVGRTgADVPMEGDLDWDELLAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 234 -GNEVPEEALDAiidtqqpNQCCVLVYTSGTTGNPKGVMLSQD----NITWTARYGSqagDIRPAEVqqevvvsYLPLSH 308
Cdd:COG0365 172 aSAEFEPEPTDA-------DDPLFILYTSGTTGKPKGVVHTHGgylvHAATTAKYVL---DLKPGDV-------FWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 309 IAaqiydlWTGIQW---------GAQVCFAE-----PDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFI 374
Cdd:COG0365 235 IG------WATGHSyivygpllnGATVVLYEgrpdfPDP--GRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 375 RRKMLlwaMSVtleqnltcpGSDLKPfttrladyLVLAKVRQALGfakcqknfygaapmmaetqhfflglnIRLYAGYGL 454
Cdd:COG0365 307 SLRLL---GSA---------GEPLNP--------EVWEWWYEAVG--------------------------VPIVDGWGQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 455 SETSGpHFMSSPYNYRLY--SSGKLVPGCRVKLVnqDAEG-------IGEICL---W-GrtIFMGYLNMEDKTCEAI--D 519
Cdd:COG0365 341 TETGG-IFISNLPGLPVKpgSMGKPVPGYDVAVV--DEDGnpvppgeEGELVIkgpWpG--MFRGYWNDPERYRETYfgR 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 520 EEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:COG0365 416 FPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESAL-VSHPAVAEAAVVG 473
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
106-564 |
3.71e-30 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 125.17 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 106 DKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANV 185
Cdd:cd05959 25 DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 186 IMVdTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMAnvytmeeFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTG 265
Cdd:cd05959 105 VVV-SGELAPVLAAALTKSEHTLVVLIVSGGAGPEAG-------ALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 266 NPKGVMLSQDNITWTAR-YGSQAGDIRPAevqqEVVVSYLPLSHI----AAQIYDLWTGiqwGAQVCFAE---PDAlkgs 337
Cdd:cd05959 177 RPKGVVHLHADIYWTAElYARNVLGIRED----DVCFSAAKLFFAyglgNSLTFPLSVG---ATTVLMPErptPAA---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 338 LVNTLREVEPTSHMGVPRVWEKIMEriQEVAAQSGFIRRKMLLWAMSVTleqnltcPGSDLKPFTTRladylvlakvrqa 417
Cdd:cd05959 246 VFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEAL-------PAEVGERWKAR------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 418 lgfakcqknfygaapmmaetqhffLGLNIRlyagYGLSETSGPH-FMSS-PYNYRLYSSGKLVPGCRVKLVNQDAE---- 491
Cdd:cd05959 304 ------------------------FGLDIL----DGIGSTEMLHiFLSNrPGRVRYGTTGKPVPGYEVELRDEDGGdvad 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767983694 492 -GIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIEEA 564
Cdd:cd05959 356 gEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDM-LKVSGIWVSPFEVESA 427
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
78-646 |
8.08e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 124.76 E-value: 8.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 78 QLPYTV-------HRMFYEALDKYGDLIALGFKRQDkwehISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFF 150
Cdd:PRK06710 14 EIPSTIsydiqplHKYVEQMASRYPEKKALHFLGKD----ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 151 SAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM-----------VDTQKQLEKIL--KIWKQLPHLKAVV--IYKE 215
Cdd:PRK06710 90 GYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnVQSATKIEHVIvtRIADFLPFPKNLLypFVQK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 216 PPPNKMANVyTMEEFMELGNEVPEE---ALDAIIDTQqpNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAgdIRP 292
Cdd:PRK06710 170 KQSNLVVKV-SESETIHLWNSVEKEvntGVEVPCDPE--NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQW--LYN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 293 AEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKgSLVNTLREVEPTSHMGVPRVWEKIMEriqevaaqsg 372
Cdd:PRK06710 245 CKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMK-MVFEAIKKHKVTLFPGAPTIYIALLN---------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 373 firrkmllwamsvtleqnltcpgsdlkpfTTRLADYLVlAKVRQALGfakcqknfyGAAPMMAETQHFFLGLNI-RLYAG 451
Cdd:PRK06710 314 -----------------------------SPLLKEYDI-SSIRACIS---------GSAPLPVEVQEKFETVTGgKLVEG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 452 YGLSEtsgphfmSSPYNYRLYSSGKLVPGC-RVKLVNQDAE-------------GIGEICLWGRTIFMGYLNMEDKTCeA 517
Cdd:PRK06710 355 YGLTE-------SSPVTHSNFLWEKRVPGSiGVPWPDTEAMimsletgealppgEIGEIVVKGPQIMKGYWNKPEETA-A 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 518 IDEEGWLHTGDAGRLDADGFLYITGRLKELIItAGGENVPPVPIEEaVKMELPIISNAMLIGDQRKFLSMLLTLKCTLDP 597
Cdd:PRK06710 427 VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIV-ASGFNVYPREVEE-VLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE 504
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 767983694 598 DTSDQTDNLTEQAMEFCQrvgsrATTVSEIIEKKDEAVYQAIEEGIRRV 646
Cdd:PRK06710 505 GTECSEEELNQFARKYLA-----AYKVPKVYEFRDELPKTTVGKILRRV 548
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
249-582 |
1.85e-29 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 121.72 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 249 QQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQqeVVVSylPLSHIAAQIYDLWTGIQWGAQVCF 328
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF--LVAS--PMAHQTGFVYGFTLPLLLGAPVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 329 AEP-DALKGslVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRrKMLlwamsvtleqnltCPGSDLKPFTTRLAD 407
Cdd:cd05903 166 QDIwDPDKA--LALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLR-TFV-------------CGGATVPRSLARRAA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 408 YLVLAKVRQALGfakcqknfygaapmMAETQHFFlglnirlyagyGLSEtsgphfmSSPYNYRLYSSGKLVPGCRVKLVN 487
Cdd:cd05903 230 ELLGAKVCSAYG--------------STECPGAV-----------TSIT-------PAPEDRRLYTDGRPLPGVEIKVVD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 488 QD-----AEGIGEICLWGRTIFMGYLNMEDKTCEAiDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIE 562
Cdd:cd05903 278 DTgatlaPGVEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVE 355
|
330 340
....*....|....*....|..
gi 767983694 563 EAVkMELPIISNAMLIG--DQR 582
Cdd:cd05903 356 DLL-LGHPGVIEAAVVAlpDER 376
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
256-579 |
4.28e-29 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 120.14 E-value: 4.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 256 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAepDALK 335
Cdd:cd05912 81 TIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT----EDDNWLCALPLFHISG-LSILMRSVIYGMTVYLV--DKFD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 336 GSLVNTLREVEPTSHMG-VPRVWEKIMERIQEVAAQSgfiRRKMLLWAmsvtleqnltcpgsdlkpfttrladylvlakv 414
Cdd:cd05912 154 AEQVLHLINSGKVTIISvVPTMLQRLLEILGEGYPNN---LRCILLGG-------------------------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 415 rqalGFAkcqknfygAAPMMAETQHfflgLNIRLYAGYGLSETSGPHFMSSPYNY--RLYSSGKLVPGCRVKLVN--QDA 490
Cdd:cd05912 199 ----GPA--------PKPLLEQCKE----KGIPVYQSYGMTETCSQIVTLSPEDAlnKIGSAGKPLFPVELKIEDdgQPP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 491 EGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIItAGGENVPPVPIEEAVKmELP 570
Cdd:cd05912 263 YEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEVLL-SHP 339
|
....*....
gi 767983694 571 IISNAMLIG 579
Cdd:cd05912 340 AIKEAGVVG 348
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
253-581 |
4.75e-29 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 120.63 E-value: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 253 QCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIAAQIYdLWTGIQWGAQVCFAEPD 332
Cdd:TIGR01923 112 QIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGF----TEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDKF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 333 A-LKGSLVNtlrevEPTSHMG-VPrvwekimeriqevaaqsgfirrKMLLWamsvTLEQNLTCpgsdlkpfttrladyLV 410
Cdd:TIGR01923 187 NqLLEMIAN-----ERVTHISlVP----------------------TQLNR----LLDEGGHN---------------EN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 411 LAKVRqaLGFAKCqknfygAAPMMAETQHfflgLNIRLYAGYGLSETSGPHFMSSP--YNYRLySSGKLVPGCRVKLVNQ 488
Cdd:TIGR01923 221 LRKIL--LGGSAI------PAPLIEEAQQ----YGLPIYLSYGMTETCSQVTTATPemLHARP-DVGRPLAGREIKIKVD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 489 DAEGIGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKmE 568
Cdd:TIGR01923 288 NKEGHGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIIS-GGENIYPEEIETVLY-Q 364
|
330
....*....|...
gi 767983694 569 LPIISNAMLIGDQ 581
Cdd:TIGR01923 365 HPGIQEAVVVPKP 377
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
109-579 |
4.85e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 121.53 E-value: 4.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 188
Cdd:PRK06145 26 QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 DtqKQLEKILKiwkqLPHLKAVViykepppNKMANVYTmEEFMELGNEVPEEALDAiidtqqPNQCCVLVYTSGTTGNPK 268
Cdd:PRK06145 106 D--EEFDAIVA----LETPKIVI-------DAAAQADS-RRLAQGGLEIPPQAAVA------PTDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 269 GVMLSQDNITW-----TARYGSQAGDirpaevqQEVVVSylPLSHIAAqiYDLwTGIQWGAQvcfaepdalkGSLVNTLR 343
Cdd:PRK06145 166 GVMHSYGNLHWksidhVIALGLTASE-------RLLVVG--PLYHVGA--FDL-PGIAVLWV----------GGTLRIHR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 344 EVEPtshmgvprvwEKIMERIQEvaaqsgfiRRKMLLWAMSVTLEQNLTCPgsdlkpftTRlaDYLVLAKVRQALGFAKc 423
Cdd:PRK06145 224 EFDP----------EAVLAAIER--------HRLTCAWMAPVMLSRVLTVP--------DR--DRFDLDSLAWCIGGGE- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 424 qknfygAAPMMAETQHFFLGLNIRLYAGYGLSET-SGPHFMSSPYNY-RLYSSGKLVPGCRVKLVNQDAEGI-----GEI 496
Cdd:PRK06145 275 ------KTPESRIRDFTRVFTRARYIDAYGLTETcSGDTLMEAGREIeKIGSTGRALAHVEIRIADGAGRWLppnmkGEI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 497 CLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAM 576
Cdd:PRK06145 349 CMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEVERVI-YELPEVAEAA 425
|
...
gi 767983694 577 LIG 579
Cdd:PRK06145 426 VIG 428
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
256-579 |
1.00e-28 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 117.37 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 256 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQqevvVSYLPLSHIAAQIYDLWTGIQWGAQVC---FAEPD 332
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVY----LNMLPLFHIAGLNLALATFHAGGANVVmekFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 333 ALKgslvntLREVEPTSHMG--VPrvwekIMERIQEVAAQSGfirrkmllwamsvtleqnltcpgsdlkpfttrladyLV 410
Cdd:cd17637 80 ALE------LIEEEKVTLMGsfPP-----ILSNLLDAAEKSG------------------------------------VD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 411 LAKVRQALGFAkcqknfygaAPmmaETQHFFLGL-NIRLYAGYGLSETSGPHFMSsPYNYRLYSSGKLVPGCRVKLVNQD 489
Cdd:cd17637 113 LSSLRHVLGLD---------AP---ETIQRFEETtGATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVDDN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 490 -----AEGIGEICLWGRTIFMGYLNMEDKTCEAIDEeGWLHTGDAGRLDADGFLYITGRL--KELIITaGGENVPPVPIE 562
Cdd:cd17637 180 drpvpAGETGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPAEVE 257
|
330
....*....|....*..
gi 767983694 563 EAVkMELPIISNAMLIG 579
Cdd:cd17637 258 KVI-LEHPAIAEVCVIG 273
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
82-579 |
1.36e-28 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 120.56 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 82 TVHRMFYEALDKYGDLIALGFK-RQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGG 160
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALIFEsSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 161 IVTGIYTTSSPEACQYIAYDCCANVIMVDtqkqlEKILKIWKQLPH-----LKAVVIYKEPPPnKMANVYtmeEFMELGN 235
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTS-----AQFYPMYRQIQQedatpLRHICLTRVALP-ADDGVS---SFTQLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 236 EVPEEALDAII----DTQQpnqccvLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAA 311
Cdd:PRK08008 159 QQPATLCYAPPlstdDTAE------ILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALR----DDDVYLTVMPAFHIDC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 312 QiydlwtgiqwgaqvCFAEPDALkgSLVNTLREVEPTShmgVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNl 391
Cdd:PRK08008 229 Q--------------CTAAMAAF--SAGATFVLLEKYS---ARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQH- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 392 tcpgsdlkpfttRLAD---YLVLAKvrqalgfakcqknfygaapmmAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYN 468
Cdd:PRK08008 289 ------------CLREvmfYLNLSD---------------------QEKDAFEERFGVRLLTSYGMTETIVGIIGDRPGD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 469 YRLYSS-GKLVPGCRVKLVNQD-----AEGIGEICLWG---RTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLY 539
Cdd:PRK08008 336 KRRWPSiGRPGFCYEAEIRDDHnrplpAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFY 415
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 767983694 540 ITGRlKELIITAGGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:PRK08008 416 FVDR-RCNMIKRGGENVSCVELENII-ATHPKIQDIVVVG 453
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
109-572 |
1.42e-28 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 120.46 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVaILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSpeacqyiAYDCCANvimv 188
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEDFIPAFWACVLAGFVPAPLTVPP-------TYDEPNA---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 dtqkQLEKILKIWKQLPhlKAVVIykepppnkmANVYTMEEFMELGNE---------VPEEALDAIIDT----QQPNQCC 255
Cdd:cd05906 106 ----RLRKLRHIWQLLG--SPVVL---------TDAELVAEFAGLETLsglpgirvlSIEELLDTAADHdlpqSRPDDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 256 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAA----QIYDLWTGIQwgaQVcfaep 331
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTP----QDVFLNWVPLDHVGGlvelHLRAVYLGCQ---QV----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 332 dalkgslvNTlrevePTSHM-GVPRVWEKIMERIQevAAQSgfirrkmllWA----MSVTLEQnltcpgsdLKPFTTRLA 406
Cdd:cd05906 239 --------HV-----PTEEIlADPLRWLDLIDRYR--VTIT---------WApnfaFALLNDL--------LEEIEDGTW 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 407 DylvLAKVRQALGfakcqknfyGAAPMMAETQHFFL------GLNIR-LYAGYGLSET-SGPHFMSSPYNY------RLY 472
Cdd:cd05906 287 D---LSSLRYLVN---------AGEAVVAKTIRRLLrllepyGLPPDaIRPAFGMTETcSGVIYSRSFPTYdhsqalEFV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 473 SSGKLVPGCRVKLVNQDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDaDGFLYITGRLKEL 547
Cdd:cd05906 355 SLGRPIPGVSMRIVDDEGQLlpegeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDT 433
|
490 500
....*....|....*....|....*
gi 767983694 548 IITaGGENVPPVPIEEAVKmELPII 572
Cdd:cd05906 434 IIV-NGVNYYSHEIEAAVE-EVPGV 456
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
112-582 |
1.54e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 117.54 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 112 SYSQYYLLARRAAKGFLKLGLKQAHSVAilgFNSPEWF-FSAV--GTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 188
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVA---FQLPGWCeFTIIylACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 DTQ-KQ---LEKILKIWKQLPHLKAVVIykepppnkmanvytmeeFMELGNEVPEEALDAIIDTQQPNQ----------C 254
Cdd:PRK06087 128 PTLfKQtrpVDLILPLQNQLPQLQQIVG-----------------VDKLAPATSSLSLSQIIADYEPLTtaitthgdelA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 255 CVLvYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIaaqiydlwTGIQWGAQVCFaepdaL 334
Cdd:PRK06087 191 AVL-FTSGTEGLPKGVMLTHNNILASERAYCARLNL----TWQDVFMMPAPLGHA--------TGFLHGVTAPF-----L 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 335 KGSLVntlreveptshmgvprvwekIMERIQEVAAQSGFIRRKMLLWAMSVTleqnltcpgsdlkPFTtrladYLVLAKV 414
Cdd:PRK06087 253 IGARS--------------------VLLDIFTPDACLALLEQQRCTCMLGAT-------------PFI-----YDLLNLL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 415 RQ------ALGFAKCqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSgPHFM---SSPYNYRLYSSGKLVPGCRVKL 485
Cdd:PRK06087 295 EKqpadlsALRFFLC-----GGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVvnlDDPLSRFMHTDGYAAAGVEIKV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 486 VNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVP 560
Cdd:PRK06087 369 VDEARKTLppgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVR-GGENISSRE 447
|
490 500
....*....|....*....|....
gi 767983694 561 IEEAVkMELPIISNAMLIG--DQR 582
Cdd:PRK06087 448 VEDIL-LQHPKIHDACVVAmpDER 470
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
96-579 |
2.42e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 116.22 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 96 DLIALGFKRQDkwehISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSavgtvfaggivtgIYttsspeACQ 175
Cdd:PRK03640 17 DRTAIEFEEKK----VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILV-------------IH------ALQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 176 YIAydccANVIMVDTQKQLEKILkiWkQLPHLKA-VVIYKEPPPNKMANVY--TMEEFMELGNEVPEealdaIIDTQQPN 252
Cdd:PRK03640 74 QLG----AVAVLLNTRLSREELL--W-QLDDAEVkCLITDDDFEAKLIPGIsvKFAELMNGPKEEAE-----IQEEFDLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 253 QCCVLVYTSGTTGNPKGVMLSQDNITWTAR-----YGSQAGDIRPAEVqqevvvsylPLSHIAAqIYDLWTGIQWGAQVC 327
Cdd:PRK03640 142 EVATIMYTSGTTGKPKGVIQTYGNHWWSAVgsalnLGLTEDDCWLAAV---------PIFHISG-LSILMRSVIYGMRVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 328 FAEP-DALKgslVNTLREVEPTSHMG-VPRVWEKIMERIQEVAAQSGFirRKMLLW---AMSVTLEQnltcpgsdlkpft 402
Cdd:PRK03640 212 LVEKfDAEK---INKLLQTGGVTIISvVSTMLQRLLERLGEGTYPSSF--RCMLLGggpAPKPLLEQ------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 403 trladylvlakvrqalgfakCQknfygaapmmaetQHfflglNIRLYAGYGLSETSG------PHFMSSpynyRLYSSGK 476
Cdd:PRK03640 274 --------------------CK-------------EK-----GIPVYQSYGMTETASqivtlsPEDALT----KLGSAGK 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 477 LVPGCRVKLVNQDAEG----IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaG 552
Cdd:PRK03640 312 PLFPCELKIEKDGVVVppfeEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIIS-G 389
|
490 500
....*....|....*....|....*..
gi 767983694 553 GENVPPVPIeEAVKMELPIISNAMLIG 579
Cdd:PRK03640 390 GENIYPAEI-EEVLLSHPGVAEAGVVG 415
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
112-565 |
4.68e-27 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 115.47 E-value: 4.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 112 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ 191
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 192 kqlekilkiwkqlphlkavviykepppnkmanvYTMEEFMELGN-----EVPEEALDAIidtqqpnqccVLVYTSGTTGN 266
Cdd:cd12118 111 ---------------------------------FEYEDLLAEGDpdfewIPPADEWDPI----------ALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 267 PKGVMLSQDNItwtarYGSQAGDIRPAEVQQEVVvsYL---PLSHIAAqiydlWTGIqWGaqvcfaePDALKGSLVnTLR 343
Cdd:cd12118 148 PKGVVYHHRGA-----YLNALANILEWEMKQHPV--YLwtlPMFHCNG-----WCFP-WT-------VAAVGGTNV-CLR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 344 EVEPtshmgvPRVWEKI-MERIQEVAAqsgfirrkmllwamSVTLEQNLT-CPGSDLKPFTTRladylvlakVRQALGfa 421
Cdd:cd12118 207 KVDA------KAIYDLIeKHKVTHFCG--------------APTVLNMLAnAPPSDARPLPHR---------VHVMTA-- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 422 kcqknfyGAAP---MMAETQHfflgLNIRLYAGYGLSETSGPHF----------MSSPYNYRLYS----SGKLVPGCRV- 483
Cdd:cd12118 256 -------GAPPpaaVLAKMEE----LGFDVTHVYGLTETYGPATvcawkpewdeLPTEERARLKArqgvRYVGLEEVDVl 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 484 -----KLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPP 558
Cdd:cd12118 325 dpetmKPVPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISS 402
|
....*..
gi 767983694 559 VPIEEAV 565
Cdd:cd12118 403 VEVEGVL 409
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
153-610 |
1.10e-26 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 114.35 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 153 VGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMvdTQKQLEKILKIWKQLPHLK-AVVIYKEpppNKMANVYTMEE-F 230
Cdd:cd05909 49 FALALSGKVPVMLNYTAGLRELRACIKLAGIKTVL--TSKQFIEKLKLHHLFDVEYdARIVYLE---DLRAKISKADKcK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 231 MELGNEVPEEALDAI--IDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSH 308
Cdd:cd05909 124 AFLAGKFPPKWLLRIfgVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNP----EDVVFGALPFFH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 309 IAAQIYDLWTGIQWGAQVCFAePDALKG-SLVNTLREVEPTSHMGVPRVWekimeriqevaaqSGFIRRKMllwamsvtl 387
Cdd:cd05909 200 SFGLTGCLWLPLLSGIKVVFH-PNPLDYkKIPELIYDKKATILLGTPTFL-------------RGYARAAH--------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 388 eqnltcpGSDLkpFTTRLAdylvlakvrqalgfakcqknFYGAAPMMAETQHFFLGL-NIRLYAGYGLSETSGPHFMSSP 466
Cdd:cd05909 257 -------PEDF--SSLRLV--------------------VAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISVNTP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 467 -YNYRLYSSGKLVPGCRVKLVnqDAEG-----IGE---ICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGF 537
Cdd:cd05909 308 qSPNKEGTVGRPLPGMEVKIV--SVETheevpIGEgglLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGF 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767983694 538 LYITGRLKELiITAGGENVPPVPIEEAVKMELPIISN--AMLIGDQRKFLSMLLtlkCTLDPDTSdqTDNLTEQA 610
Cdd:cd05909 385 LTITGRLSRF-AKIAGEMVSLEAIEDILSEILPEDNEvaVVSVPDGRKGEKIVL---LTTTTDTD--PSSLNDIL 453
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
111-578 |
1.45e-25 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 111.61 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDt 190
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 191 QKQLEKILKIwkQLPhlkaVVIYKEpppNKMANVYTMEEFMELGNEVPEEALDAIIdtqQPNQCCVLVYTSGTTGNPKGV 270
Cdd:PLN02330 135 DTNYGKVKGL--GLP----VIVLGE---EKIEGAVNWKELLEAADRAGDTSDNEEI---LQTDLCALPFSSGTTGISKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 271 MLSQDNITwtARYGSQAGDIRPAEVQQEVVVSYLPLSHIaaqiYDLwTGIqwgaqvCFAepdalkgslvnTLREVeptsh 350
Cdd:PLN02330 203 MLTHRNLV--ANLCSSLFSVGPEMIGQVVTLGLIPFFHI----YGI-TGI------CCA-----------TLRNK----- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 351 mgvprvwekimeriQEVAAQSGFIRRKML--LWAMSVTLEQnlTCPGSDLKPFTTRLADYLVLAKVrqalgfaKCQKNFY 428
Cdd:PLN02330 254 --------------GKVVVMSRFELRTFLnaLITQEVSFAP--IVPPIILNLVKNPIVEEFDLSKL-------KLQAIMT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 429 GAAPMMAETQHFFLGL--NIRLYAGYGLSETSGPHFMSSPYN-----YRLYSSGKLVPGCRVKLVNQDA------EGIGE 495
Cdd:PLN02330 311 AAAPLAPELLTAFEAKfpGVQVQEAYGLTEHSCITLTHGDPEkghgiAKKNSVGFILPNLEVKFIDPDTgrslpkNTPGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 496 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGEnVPPVPIeEAVKMELPIISNA 575
Cdd:PLN02330 391 LCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ-VAPAEL-EAILLTHPSVEDA 468
|
...
gi 767983694 576 MLI 578
Cdd:PLN02330 469 AVV 471
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
54-700 |
7.36e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 109.58 E-value: 7.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 54 APEEALWTTRADGRVRLRidpsCPQLPYTVHRMFYEALDKY----GDLIALGfKRQDK--WEHISYSQYYLLARRAAKGF 127
Cdd:PRK08180 12 APPAVEVERRADGTIYLR----SAEPLGDYPRRLTDRLVHWaqeaPDRVFLA-ERGADggWRRLTYAEALERVRAIAQAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 128 LKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTTSS--PEACQYIAYDCCANVIMVDTQKQLEKILKIwk 202
Cdd:PRK08180 87 LDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKLRHVLELLTPGLVFADDGAAFARALAA-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 203 qLPHLKAVVIYKEPPPNKMANVytmeEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTAR 282
Cdd:PRK08180 165 -VVPADVEVVAVRGAVPGRAAT----PFAALLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 283 YGSQAgdIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGaqvcfaepdalkGSL---------------VNTLREVEP 347
Cdd:PRK08180 240 MLAQT--FPFLAEEPPVLVDWLPWNHTFGGNHNLGIVLYNG------------GTLyiddgkptpggfdetLRNLREISP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 348 TSHMGVPRVWEkimeriqevaaqsgfirrkMLLWAmsvtLEQNltcpgsdlkpfttrladylvlAKVRQALgFAKCQKNF 427
Cdd:PRK08180 306 TVYFNVPKGWE-------------------MLVPA----LERD---------------------AALRRRF-FSRLKLLF 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 428 YGAAPM----------MAEtQHffLGLNIRLYAGYGLSETSgPHFMSSpyNYRLYSSGKL---VPGCRVKLVnqDAEGIG 494
Cdd:PRK08180 341 YAGAALsqdvwdrldrVAE-AT--CGERIRMMTGLGMTETA-PSATFT--TGPLSRAGNIglpAPGCEVKLV--PVGGKL 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 495 EICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRL-DAD----GFLYiTGRLKELIITAGGE--NVPPVPIeEAVKM 567
Cdd:PRK08180 413 EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDPAdperGLMF-DGRIAEDFKLSSGTwvSVGPLRA-RAVSA 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 568 ELPIISNAMLIGDQRKFLSMLLTLKctldpdtsdqtdnlteqaMEFCQRVG--SRATTVSEIIEkkDEAVYQAIEEGIRR 645
Cdd:PRK08180 491 GAPLVQDVVITGHDRDEIGLLVFPN------------------LDACRRLAglLADASLAEVLA--HPAVRAAFRERLAR 550
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 767983694 646 VNMNAAARPYHIQKWAILERDFSISGGELgpTMK--LKRLTVLEKYKGIIDSFYQEQ 700
Cdd:PRK08180 551 LNAQATGSSTRVARALLLDEPPSLDAGEI--TDKgyINQRAVLARRAALVEALYADE 605
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
111-567 |
1.46e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 108.43 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFL-KLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV- 188
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVi 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 ------------DTQ-KQ-----LEKILKIWKQ------LPHLKAVViykepPPNKMANVYTMEEFMELGNEVPEEALDA 244
Cdd:PRK08751 131 dnfgttvqqviaDTPvKQvittgLGDMLGFPKAalvnfvVKYVKKLV-----PEYRINGAIRFREALALGRKHSMPTLQI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 245 iidtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQ----AGDIRPAevqQEVVVSYLPLSHIAAQIYDLWTGI 320
Cdd:PRK08751 206 -----EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagTGKLEEG---CEVVITALPLYHIFALTANGLVFM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 321 QWGAqvC---FAEPDALKGsLVNTLREVEPTSHMGVPRVWEKImeriqevaaqsgfirrkmllwamsvtleqnLTCPGSD 397
Cdd:PRK08751 278 KIGG--CnhlISNPRDMPG-FVKELKKTRFTAFTGVNTLFNGL------------------------------LNTPGFD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 398 LKPFTTrladylvlakVRQALGfakcqknfYGAAPMMAETQHFFLGLNIRLYAGYGLSETSgPHFMSSPYNYRLY--SSG 475
Cdd:PRK08751 325 QIDFSS----------LKMTLG--------GGMAVQRSVAERWKQVTGLTLVEAYGLTETS-PAACINPLTLKEYngSIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 476 KLVPGCRVKLVNQDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIIT 550
Cdd:PRK08751 386 LPIPSTDACIKDDAGTVlaigeIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILV 465
|
490
....*....|....*..
gi 767983694 551 AGGeNVPPVPIEEAVKM 567
Cdd:PRK08751 466 SGF-NVYPNEIEDVIAM 481
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
243-579 |
2.04e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 107.82 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 243 DAIIDTQQPnqcCVLVYTSGTTGNPKGVMLSQDNITWTARygSQAGDIRPAEVQQEVVVSYLPLSHIAaqiydlwtGIQw 322
Cdd:PRK07470 157 NAAVDHDDP---CWFFFTSGTTGRPKAAVLTHGQMAFVIT--NHLADLMPGTTEQDASLVVAPLSHGA--------GIH- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 323 gaqvcfaepdalkgSLVNTLREVE----PTSHMGVPRVWEKIME-RIQEVAAQSGFIrrKMLLWAMSVTleqnlTCPGSD 397
Cdd:PRK07470 223 --------------QLCQVARGAAtvllPSERFDPAEVWALVERhRVTNLFTVPTIL--KMLVEHPAVD-----RYDHSS 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 398 LKpfttrladYLVlakvrqalgfakcqknfYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSG------PHFMSS---Py 467
Cdd:PRK07470 282 LR--------YVI-----------------YAGAPMYRADQKRALAkLGKVLVQYFGLGEVTGnitvlpPALHDAedgP- 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 468 NYRLYSSGKLVPGCRVKLvnQDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYI 540
Cdd:PRK07470 336 DARIGTCGFERTGMEVQI--QDDEGrelppgeTGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYI 412
|
330 340 350
....*....|....*....|....*....|....*....
gi 767983694 541 TGRLKELIITaGGENVPPVPIEEAVKMElPIISNAMLIG 579
Cdd:PRK07470 413 TGRASDMYIS-GGSNVYPREIEEKLLTH-PAVSEVAVLG 449
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
138-674 |
3.27e-24 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 107.54 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 138 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQkQLEKILKIWKQLPHLKAVVIY---- 213
Cdd:cd17632 96 VAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAE-HLDLAVEAVLEGGTPPRLVVFdhrp 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 214 ------------KEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQPnqCCVLVYTSGTTGNPKGVMLSQDNIT--W 279
Cdd:cd17632 175 evdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDP--LALLIYTSGSTGTPKGAMYTERLVAtfW 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 280 TARYGSQAGDIRPAevqqeVVVSYLPLSHIAAQIYdLWTGIQWGAQVCF-AEPDAlkGSLVNTLREVEPTSHMGVPRVWE 358
Cdd:cd17632 253 LKVSSIQDIRPPAS-----ITLNFMPMSHIAGRIS-LYGTLARGGTAYFaAASDM--STLFDDLALVRPTELFLVPRVCD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 359 KIMERIQEVaaqsgfIRRKMLLWAMSVTLEQNltcpgsdlkpfttrladylVLAKVRQALGFAKCQKNFYGAAPMMAETQ 438
Cdd:cd17632 325 MLFQRYQAE------LDRRSVAGADAETLAER-------------------VKAELRERVLGGRLLAAVCGSAPLSAEMK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 439 HFFLG-LNIRLYAGYGLSETSGphfmsspynyrLYSSGKLV--PGCRVKLVNQDAEGI---------GEICLWGRTIFMG 506
Cdd:cd17632 380 AFMESlLDLDLHDGYGSTEAGA-----------VILDGVIVrpPVLDYKLVDVPELGYfrtdrphprGELLVKTDTLFPG 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 507 YLNMEDKTCEAIDEEGWLHTGDA-GRLDADGFLYITgRLKELIITAGGENVpPVPIEEAVKMELPIISNAMLIGD-QRKF 584
Cdd:cd17632 449 YYKRPEVTAEVFDEDGFYRTGDVmAELGPDRLVYVD-RRNNVLKLSQGEFV-TVARLEAVFAASPLVRQIFVYGNsERAY 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 585 LSMLLTlkctldPdTSDQTDNLTEQAMefcqrvgsRAttvseiiekkdeavyqAIEEGIRRVNMNAAARPYHIQKWAILE 664
Cdd:cd17632 527 LLAVVV------P-TQDALAGEDTARL--------RA----------------ALAESLQRIAREAGLQSYEIPRDFLIE 575
|
570
....*....|.
gi 767983694 665 RD-FSISGGEL 674
Cdd:cd17632 576 TEpFTIANGLL 586
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
85-564 |
4.83e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 106.57 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 85 RMFYEALDK--------------------YGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFN 144
Cdd:PRK08162 2 NIYEQGLDRnaanyvpltplsfleraaevYPDRPAVIHGDR----RRTWAETYARCRRLASALARRGIGRGDTVAVLLPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 145 SPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQlEKILKIWKQLPHLKAVVIY---KEPPPNKM 221
Cdd:PRK08162 78 IPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFA-EVAREALALLPGPKPLVIDvddPEYPGGRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 222 ANVYTMEEFMELGN-----EVPEEALDAIidtqqpnqccVLVYTSGTTGNPKGV--------MLSQDNI-TWTARygsqa 287
Cdd:PRK08162 157 IGALDYEAFLASGDpdfawTLPADEWDAI----------ALNYTSGTTGNPKGVvyhhrgayLNALSNIlAWGMP----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 288 gdirpaevQQEVVVSYLPLSHIAAQIYDlWT-GIQWGAQVCfaepdalkgslvntLREVEPtshmgvprvwEKIMERIQE 366
Cdd:PRK08162 222 --------KHPVYLWTLPMFHCNGWCFP-WTvAARAGTNVC--------------LRKVDP----------KLIFDLIRE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 367 --VAAQSGF-IRRKMLLWAmsvtleqnltcPGSDLKPFttrlaDYLVLAKVRqalgfakcqknfyGAAP------MMAEt 437
Cdd:PRK08162 269 hgVTHYCGApIVLSALINA-----------PAEWRAGI-----DHPVHAMVA-------------GAAPpaaviaKMEE- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 438 qhfflgLNIRLYAGYGLSETSGP--------HFMSSPYNYRLYSSGK------LVPGCRV------KLVNQDAEGIGEIC 497
Cdd:PRK08162 319 ------IGFDLTHVYGLTETYGPatvcawqpEWDALPLDERAQLKARqgvrypLQEGVTVldpdtmQPVPADGETIGEIM 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983694 498 LWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 564
Cdd:PRK08162 393 FRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVEDV 457
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-627 |
5.99e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 105.60 E-value: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 256 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK 335
Cdd:cd05922 121 LLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA----DDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 336 GSLVNTLREVEPTSHMGVPRVWEkIMERIqevaaqsgfIRRKMLLwamsVTLeQNLTCPGSDLKP-FTTRLADYLVLAkv 414
Cdd:cd05922 196 DAFWEDLREHGATGLAGVPSTYA-MLTRL---------GFDPAKL----PSL-RYLTQAGGRLPQeTIARLRELLPGA-- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 415 rqalgfakcqknfygaapmmaetqhfflglniRLYAGYGLSETSG------PHFMSSpynyRLYSSGKLVPGCRVKLVNQ 488
Cdd:cd05922 259 --------------------------------QVYVMYGQTEATRrmtylpPERILE----KPGSIGLAIPGGEFEILDD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 489 D----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEE 563
Cdd:cd05922 303 DgtptPPGePGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEA 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983694 564 AVkMELPIISNAMLIGDQRKF---LSMLLTLKCTLDPDtsDQTDNLTEQAMEFcqRVGSRATTVSEI 627
Cdd:cd05922 382 AA-RSIGLIIEAAAVGLPDPLgekLALFVTAPDKIDPK--DVLRSLAERLPPY--KVPATVRVVDEL 443
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
251-582 |
8.54e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 105.66 E-value: 8.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 251 PNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFA- 329
Cdd:PRK09088 134 PERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVD----AHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSn 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 330 --EPDALKGSLVNTLREVepTSHMGVPrvweKIMERIQevaAQSGFirrkmllwamsvtleqnltcPGSDLKPFTtrlad 407
Cdd:PRK09088 210 gfEPKRTLGRLGDPALGI--THYFCVP----QMAQAFR---AQPGF--------------------DAAALRHLT----- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 408 ylvlakvrqALgfakcqknFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMS---SPYNYRLYSSGKLVPGCRVK 484
Cdd:PRK09088 256 ---------AL--------FTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGTVFGMSvdcDVIRAKAGAAGIPTPTVQTR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 485 LVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPV 559
Cdd:PRK09088 319 VVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFIS-GGENVYPA 397
|
330 340
....*....|....*....|....*
gi 767983694 560 PIeEAVKMELPIISNAMLIG--DQR 582
Cdd:PRK09088 398 EI-EAVLADHPGIRECAVVGmaDAQ 421
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
204-582 |
1.30e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 105.52 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 204 LPHLKAVVIYKEPPPNKMANVYTMEEFMElgnevpEEALDAIIDTQQ--PNQCCVLVYTSGTTGNPKGVM-----LSQDN 276
Cdd:PRK13295 153 LPALRHVVVVGGDGADSFEALLITPAWEQ------EPDAPAILARLRpgPDDVTQLIYTSGTTGEPKGVMhtantLMANI 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 277 ITWTARYGSQAGDirpaevqqeVVVSYLPLSHIaaqiydlwTGIQWGAQVcfaePDALKGSLVntLREVeptshmgvprv 356
Cdd:PRK13295 227 VPYAERLGLGADD---------VILMASPMAHQ--------TGFMYGLMM----PVMLGATAV--LQDI----------- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 357 WEkimeriqeVAAQSGFIRRKMLLWAMSVTleqnltcpgsdlkPFTTRLADYLVL-AKVRQALGFAKCQknfyGAA--PM 433
Cdd:PRK13295 273 WD--------PARAAELIRTEGVTFTMAST-------------PFLTDLTRAVKEsGRPVSSLRTFLCA----GAPipGA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 434 MAETQHFFLGLNIrlYAGYGLSETSGP--HFMSSPYNYRLYSSGKLVPGCRVKLVnqDAEG-------IGEICLWGRTIF 504
Cdd:PRK13295 328 LVERARAALGAKI--VSAWGMTENGAVtlTKLDDPDERASTTDGCPLPGVEVRVV--DADGaplpagqIGRLQVRGCSNF 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 505 MGYLNMEDKTceAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISNAMLIG--DQR 582
Cdd:PRK13295 404 GGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEI-EALLYRHPAIAQVAIVAypDER 479
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
112-585 |
2.33e-23 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 104.45 E-value: 2.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 112 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ 191
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 192 --KQLEKILKiwkQLPHLKAVVIYKEP---PPNKMANVYTMEEFMElgnevpEEALDAIIDTQQPNQCCVLVYTSGTTGN 266
Cdd:PRK06018 121 fvPILEKIAD---KLPSVERYVVLTDAahmPQTTLKNAVAYEEWIA------EADGDFAWKTFDENTAAGMCYTSGTTGD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 267 PKGVMLSQDNITWTARYGSQAGDIrpAEVQQEVVVSYLPLSHIAAqiydlwtgiqWGaqVCFAEPDA----------LKG 336
Cdd:PRK06018 192 PKGVLYSHRSNVLHALMANNGDAL--GTSAADTMLPVVPLFHANS----------WG--IAFSAPSMgtklvmpgakLDG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 337 SLVNTLREVEPTSH-MGVPRVWEkimeriqevaaqsgfirrkMLLWAMSvtlEQNLTCPgsDLKpfttrladylvlakvR 415
Cdd:PRK06018 258 ASVYELLDTEKVTFtAGVPTVWL-------------------MLLQYME---KEGLKLP--HLK---------------M 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 416 QALGFAKCQKNFYGAapmmaetqhfFLGLNIRLYAGYGLSETS--------GPHFMSSPYNYRL---YSSGKLVPGCRVK 484
Cdd:PRK06018 299 VVCGGSAMPRSMIKA----------FEDMGVEVRHAWGMTEMSplgtlaalKPPFSKLPGDARLdvlQKQGYPPFGVEMK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 485 LVNQDAEGI-------GEICLWGRTIFMGYLNMEDktcEAIDEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVP 557
Cdd:PRK06018 369 ITDDAGKELpwdgktfGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKD-VIKSGGEWIS 444
|
490 500 510
....*....|....*....|....*....|....*
gi 767983694 558 PVPIEE-AVKMelPIISNAMLIG------DQRKFL 585
Cdd:PRK06018 445 SIDLENlAVGH--PKVAEAAVIGvyhpkwDERPLL 477
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
256-582 |
4.85e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 103.75 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 256 VLVYTSGTTGNPKGVMLSQDNITWT-----ARYGSQAGDIRPA-EVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCF 328
Cdd:PRK12492 211 VLQYTGGTTGLAKGAMLTHGNLVANmlqvrACLSQLGPDGQPLmKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHnVLI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 329 AEPDALKGsLVNTLREVEPTSHMGVPRVWEKIMEriqevaaQSGFirRKMLLWAMSVTleqnltcpgsdlkpfttrlady 408
Cdd:PRK12492 291 TNPRDIPG-FIKELGKWRFSALLGLNTLFVALMD-------HPGF--KDLDFSALKLT---------------------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 409 lvlakvrqalgfakcqkNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSgPHFMSSPYN--YRLYSSGKLVPGCRVKLV 486
Cdd:PRK12492 339 -----------------NSGGTALVKATAERWEQLTGCTIVEGYGLTETS-PVASTNPYGelARLGTVGIPVPGTALKVI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 487 NQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGeNVPPVPI 561
Cdd:PRK12492 401 DDDGNELplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF-NVYPNEI 479
|
330 340
....*....|....*....|...
gi 767983694 562 EEAVkMELPIISNAMLIG--DQR 582
Cdd:PRK12492 480 EDVV-MAHPKVANCAAIGvpDER 501
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
112-543 |
2.30e-22 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 100.03 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 112 SYSQyylLARRAAK--GFLK--LGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 187
Cdd:TIGR01733 1 TYRE---LDERANRlaRHLRaaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 188 VDTQKQLEkilkiwkqLPHLKAVVIYKEPPPNKMANvytmeefmelgNEVPEEALDAiiDTQQPNQCCVLvYTSGTTGNP 267
Cdd:TIGR01733 78 TDSALASR--------LAGLVLPVILLDPLELAALD-----------DAPAPPPPDA--PSGPDDLAYVI-YTSGSTGRP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 268 KGVMLSQDNI----TWTAR-YGSQAGDirpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVN 340
Cdd:TIGR01733 136 KGVVVTHRSLvnllAWLARrYGLDPDD---------RVLQFASLSFDAS-VEEIFGALLAGATLVVPPEDEERddAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 341 TLREVEPTSHM-GVPRVWEKIMEriqevAAQSGFIRRKMLlwamsvtleqnltCPGSDlkPFTTRLADylvlaKVRQALG 419
Cdd:TIGR01733 206 ALIAEHPVTVLnLTPSLLALLAA-----ALPPALASLRLV-------------ILGGE--ALTPALVD-----RWRARGP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 420 fakcqknfygaapmmaetqhfflglNIRLYAGYGLSETS----------GPHFMSSPYNYrlyssGKLVPGCRVKLVNQD 489
Cdd:TIGR01733 261 -------------------------GARLINLYGPTETTvwstatlvdpDDAPRESPVPI-----GRPLANTRLYVLDDD 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983694 490 -----AEGIGEICLWGRTIFMGYLNMEDKTCEAI--------DEEGWLHTGDAGRLDADGFLYITGR 543
Cdd:TIGR01733 311 lrpvpVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGR 377
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
257-582 |
2.46e-22 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 98.73 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 257 LVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEvqqevvvSYL---PLSHIaaqiydlwTGIQWGAQVCFaepda 333
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDD-------RYLiinPFFHT--------FGYKAGIVACL----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 334 LKGSlvntlrEVEPTSHMGVPrvweKIMERIQevaaqsgfiRRKMLLWAMSVTLEQNLtcpgsdLKPFTTRLADylvLAK 413
Cdd:cd17638 65 LTGA------TVVPVAVFDVD----AILEAIE---------RERITVLPGPPTLFQSL------LDHPGRKKFD---LSS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 414 VRQALGfakcqknfyGAA---PMMAETQHFFLGLNIRLYAgYGLSEtSGPHFMSSPYNYRL---YSSGKLVPGCRVKLVN 487
Cdd:cd17638 117 LRAAVT---------GAAtvpVELVRRMRSELGFETVLTA-YGLTE-AGVATMCRPGDDAEtvaTTCGRACPGFEVRIAD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 488 QdaegiGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIItAGGENVPPVPIEEAVkM 567
Cdd:cd17638 186 D-----GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGAL-A 258
|
330
....*....|....*..
gi 767983694 568 ELPIISNAMLIG--DQR 582
Cdd:cd17638 259 EHPGVAQVAVIGvpDER 275
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
109-579 |
1.30e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 99.15 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLK-LGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 187
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 188 VDTQKqLEKilkiwkqLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQpnqCCVLVYTSGTTGNP 267
Cdd:PLN02574 145 TSPEN-VEK-------LSPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKPVIKQDD---VAAIMYSSGTTGAS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 268 KGVMLSQDNITWT---------ARYGSQAGDirpaevqqEVVVSYLPLSHI------AAQIYDLWTGIqwgaqVCFAEPD 332
Cdd:PLN02574 214 KGVVLTHRNLIAMvelfvrfeaSQYEYPGSD--------NVYLAALPMFHIyglslfVVGLLSLGSTI-----VVMRRFD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 333 AlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSgfirrkmllwamsvtleqnLTCpgsdLKPFTTrladylvla 412
Cdd:PLN02574 281 A--SDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEV-------------------LKS----LKQVSC--------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 413 kvrqalgfakcqknfyGAAPMMAET-QHFFLGL-NIRLYAGYGLSETS--GPHFMSSPYNYRLYSSGKLVPGCRVKLVNQ 488
Cdd:PLN02574 327 ----------------GAAPLSGKFiQDFVQTLpHVDFIQGYGMTESTavGTRGFNTEKLSKYSSVGLLAPNMQAKVVDW 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 489 DAE------GIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIe 562
Cdd:PLN02574 391 STGcllppgNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKE-IIKYKGFQIAPADL- 468
|
490
....*....|....*..
gi 767983694 563 EAVKMELPIISNAMLIG 579
Cdd:PLN02574 469 EAVLISHPEIIDAAVTA 485
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
109-565 |
1.95e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 98.68 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 188
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 DTQkQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALdaiidtqQPNQCCVLVYTSGTTGNPK 268
Cdd:PRK06155 125 EAA-LLAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAV-------QPGDTAAILYTSGTTGPSK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 269 GVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQiydlwtgiqwgaqvcfaepDALKGSLVNTLREVEpT 348
Cdd:PRK06155 197 GVCCPHAQFYWWGRNSAEDLEIGA----DDVLYTTLPLFHTNAL-------------------NAFFQALLAGATYVL-E 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 349 SHMGVPRVWEkimeRIQEVAAQSGFirrkmLLWAMSVTLeqnltcpgsDLKPFTTRLADYlvlaKVRQALGfakcqknfy 428
Cdd:PRK06155 253 PRFSASGFWP----AVRRHGATVTY-----LLGAMVSIL---------LSQPARESDRAH----RVRVALG--------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 429 GAAPMmAETQHFFLGLNIRLYAGYGLSETSGPhFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI-----GEICLWGRTI 503
Cdd:PRK06155 302 PGVPA-ALHAAFRERFGVDLLDGYGSTETNFV-IAVTHGSQRPGSMGRLAPGFEARVVDEHDQELpdgepGELLLRADEP 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767983694 504 FM---GYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEEAV 565
Cdd:PRK06155 380 FAfatGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKD-AIRRRGENISSFEVEQVL 442
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
138-579 |
7.77e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 96.77 E-value: 7.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 138 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQkqLEKILKIWKQL-PHLKAVVIYKEP 216
Cdd:PRK07786 70 VLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA--LAPVATAVRDIvPLLSTVVVAGGS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 217 PPnkmANVYTMEEFMELGNEVPeealdAIIDTqqPNQCCVLV-YTSGTTGNPKGVMLSQDNITWTARYGsqagdIRPAEV 295
Cdd:PRK07786 148 SD---DSVLGYEDLLAEAGPAH-----APVDI--PNDSPALImYTSGTTGRPKGAVLTHANLTGQAMTC-----LRTNGA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 296 QQEVVVSYL--PLSHIAAqIYDLWTGIQWGAQVCFAEPDALK-GSLVNTLREVEPTSHMGVPRVWekimeriQEVAAQSG 372
Cdd:PRK07786 213 DINSDVGFVgvPLFHIAG-IGSMLPGLLLGAPTVIYPLGAFDpGQLLDVLEAEKVTGIFLVPAQW-------QAVCAEQQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 373 FIRRKMLLWAMSvtleqnltcpgsdlkpfttrladylvlakvrqalgfakcqknfYGAAPM-------MAETqhfFLGLN 445
Cdd:PRK07786 285 ARPRDLALRVLS-------------------------------------------WGAAPAsdtllrqMAAT---FPEAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 446 IrlYAGYGLSETSGPHFMSSPYN--YRLYSSGKLVPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAI 518
Cdd:PRK07786 319 I--LAAFGQTEMSPVTCMLLGEDaiRKLGSVGKVIPTVAARVVDENmndvPVGeVGEIVYRAPTLMSGYWNNPEATAEAF 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767983694 519 DEeGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISNAMLIG 579
Cdd:PRK07786 397 AG-GWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCAEVEN-VLASHPDIVEVAVIG 454
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
120-570 |
1.41e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 95.54 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 120 ARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM--VDTQKQLEKI 197
Cdd:PRK12406 21 AARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIahADLLHGLASA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 198 LKiwkqlPHLKAVVIykePPPNKMANVYTMEEFMElgnEVPEEALD--------AIIDTQQPNQCCVLVYTSGTTGNPKG 269
Cdd:PRK12406 101 LP-----AGVTVLSV---PTPPEIAAAYRISPALL---TPPAGAIDwegwlaqqEPYDGPPVPQPQSMIYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 270 VMLSQDNITWTARYGSQAGDIRPAEvQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFA--EPDALkgsLVNTLREVEP 347
Cdd:PRK12406 170 VRRAAPTPEQAAAAEQMRALIYGLK-PGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPrfDPEEL---LQLIERHRIT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 348 TSHMgVPRVWEKIMERIQEVaaqsgfiRRKMLLWAMSVTLEQNLTCPgsdlkpfttrladylvlAKVRQALgfakcqKNF 427
Cdd:PRK12406 246 HMHM-VPTMFIRLLKLPEEV-------RAKYDVSSLRHVIHAAAPCP-----------------ADVKRAM------IEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 428 YGaaPMMAETqhfflglnirlyagYGLSETSGPHFMSSP-YNYRLYSSGKLVPGCRVKLVNQDAE-----GIGEIC--LW 499
Cdd:PRK12406 295 WG--PVIYEY--------------YGSTESGAVTFATSEdALSHPGTVGKAAPGAELRFVDEDGRplpqgEIGEIYsrIA 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767983694 500 GRTIFMgYLNMEDKTCEaIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIeEAVKMELP 570
Cdd:PRK12406 359 GNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEI-EAVLHAVP 425
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
110-562 |
1.62e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 95.80 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 110 HISYSQYYLLARRAAkGFL--KLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 187
Cdd:PRK08314 35 AISYRELLEEAERLA-GYLqqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 188 VdTQKQLEKILKIWKQLPhLKAVVIYK----------EPPPNKMANVYTMEEFMELGNEVPEEALDAIID----TQQPNQ 253
Cdd:PRK08314 114 V-GSELAPKVAPAVGNLR-LRHVIVAQysdylpaepeIAVPAWLRAEPPLQALAPGGVVAWKEALAAGLAppphTAGPDD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 254 CCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFaepda 333
Cdd:PRK08314 192 LAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTP----ESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL----- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 334 lkgslvntlreveptshmgVPRvWEKimeriqEVAAQsgFIRR-KMLLW----AMSVTLeqnLTCPGsdlkpfttrLADY 408
Cdd:PRK08314 263 -------------------MPR-WDR------EAAAR--LIERyRVTHWtnipTMVVDF---LASPG---------LAER 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 409 lVLAKVRQALGfakcqknfyGAAPM---MAETQHFFLGLniRLYAGYGLSETSGPHFMSSPYNYRLYSSGklvpgcrVKL 485
Cdd:PRK08314 303 -DLSSLRYIGG---------GGAAMpeaVAERLKELTGL--DYVEGYGLTETMAQTHSNPPDRPKLQCLG-------IPT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 486 VNQDAEGI-------------GEICLWGRTIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRLKELiI 549
Cdd:PRK08314 364 FGVDARVIdpetleelppgevGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRM-I 442
|
490
....*....|...
gi 767983694 550 TAGGENVPPVPIE 562
Cdd:PRK08314 443 NASGFKVWPAEVE 455
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
111-614 |
2.35e-20 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 94.45 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDT 190
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 191 qkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealDAIidtqqpnqcCVLVYTSGTTGNPKGV 270
Cdd:cd05919 91 ----------------------------------------------------DDI---------AYLLYSSGTTGPPKGV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 271 MLSQDNITWTAR-YGSQAGDIRPaevqQEVVVSylplshiAAQIY-------DLWTGIQWGAQVCFAE--PDAlkGSLVN 340
Cdd:cd05919 110 MHAHRDPLLFADaMAREALGLTP----GDRVFS-------SAKMFfgyglgnSLWFPLAVGASAVLNPgwPTA--ERVLA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 341 TLREVEPTSHMGVPRVWEKIMeriqevaAQSGFIRRKMllwamsvtleqnltcpgSDLKPFTTRladylvlakvrqalgf 420
Cdd:cd05919 177 TLARFRPTVLYGVPTFYANLL-------DSCAGSPDAL-----------------RSLRLCVSA---------------- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 421 akcqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETsGPHFMSS-PYNYRLYSSGKLVPGCRVKLVNQDAEGI-----G 494
Cdd:cd05919 217 --------GEALPRGLGERWMEHFGGPILDGIGATEV-GHIFLSNrPGAWRLGSTGRPVPGYEIRLVDEEGHTIppgeeG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 495 EICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISN 574
Cdd:cd05919 288 DLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLI-IQHPAVAE 364
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 767983694 575 AMLIGDQRKF----LSMLLTLKCTLDPDTSdqtdnLTEQAMEFC 614
Cdd:cd05919 365 AAVVAVPESTglsrLTAFVVLKSPAAPQES-----LARDIHRHL 403
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
110-565 |
2.60e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 95.06 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 110 HISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYT-TSSPEACQYIAydccanvimv 188
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQpTPRTDLAVWAE---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 DTQKQLEKIlkiwkqlpHLKAVVIyKEPppnKMANVYTMEE----FMELGNEVPEEALDaIIDTQQpNQCCVLVYTSGTT 264
Cdd:PRK07768 99 DTLRVIGMI--------GAKAVVV-GEP---FLAAAPVLEEkgirVLTVADLLAADPID-PVETGE-DDLALMQLTSGST 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 265 GNPKGVMLSQDNITWTARYGSQAGDIrpaEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFaepdalkgslvntlre 344
Cdd:PRK07768 165 GSPKAVQITHGNLYANAEAMFVAAEF---DVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVK---------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 345 VEPTSHMGVPRVWEKIMERiqevaaqsgfiRRKmllwamSVTLEQNLTcpgsdlkpfttrladYLVLAKV--RQA----- 417
Cdd:PRK07768 226 VTPMDFLRDPLLWAELISK-----------YRG------TMTAAPNFA---------------YALLARRlrRQAkpgaf 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 418 ----LGFAKCqknfyGAAPMMAETQHFFL------GLNIR-LYAGYGLSETS----------GPHF-------------- 462
Cdd:PRK07768 274 dlssLRFALN-----GAEPIDPADVEDLLdagarfGLRPEaILPAYGMAEATlavsfspcgaGLVVdevdadllaalrra 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 463 --MSSPYNYRLYSSGKLVPGCRVKLVNQD-----AEGIGEICLWGRTIFMGYLNMeDKTCEAIDEEGWLHTGDAGRLDAD 535
Cdd:PRK07768 349 vpATKGNTRRLATLGPPLPGLEVRVVDEDgqvlpPRGVGVIELRGESVTPGYLTM-DGFIPAQDADGWLDTGDLGYLTEE 427
|
490 500 510
....*....|....*....|....*....|
gi 767983694 536 GFLYITGRLKELIITaGGENVPPVPIEEAV 565
Cdd:PRK07768 428 GEVVVCGRVKDVIIM-AGRNIYPTDIERAA 456
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
257-579 |
5.02e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 93.79 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 257 LVYTSGTTGNPKGVMLSQDNITWTAR-----YGSQAGDirpaevqqeVVVSYLPLSH-----IAAQIYDLWtgiqwGAQV 326
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSNALtlvdyWRFTPDD---------VLIHALPIFHthglfVATNVALLA-----GASM 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 327 CFA---EPDALKGSLVNTlrevepTSHMGVPRVWEKIMeriqevaAQSGFIR---RKMLLwamsvtleqnltcpgsdlkp 400
Cdd:PRK07514 227 IFLpkfDPDAVLALMPRA------TVMMGVPTFYTRLL-------QEPRLTReaaAHMRL-------------------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 401 FTTrladylvlakvrqalgfakcqknfyGAAPMMAETQHFF---LGLNI--RlyagYGLSETSgphfM--SSPYN--YRL 471
Cdd:PRK07514 274 FIS-------------------------GSAPLLAETHREFqerTGHAIleR----YGMTETN----MntSNPYDgeRRA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 472 YSSGKLVPGCRVKLVNQD------AEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLK 545
Cdd:PRK07514 321 GTVGFPLPGVSLRVTDPEtgaelpPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
330 340 350
....*....|....*....|....*....|....
gi 767983694 546 ELIITaGGENVPPVPIEEAVKmELPIISNAMLIG 579
Cdd:PRK07514 401 DLIIS-GGYNVYPKEVEGEID-ELPGVVESAVIG 432
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
54-699 |
6.13e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 94.34 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 54 APEEALWTTRADGRVRLRIDPSCPQLPYTVHRMFYEALDKYGDLIALGFKRQD--KWEHISYSQYYLLARRAAKGFLKLG 131
Cdd:PRK12582 22 KPPDISVERRADGSIVIKSRHPLGPYPRSIPHLLAKWAAEAPDRPWLAQREPGhgQWRKVTYGEAKRAVDALAQALLDLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 132 LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTTSSPE--ACQYIAYDCCANVIMVDTQKQLEKILKIwkqLPH 206
Cdd:PRK12582 102 LDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHDhaKLKHLFDLVKPRVVFAQSGAPFARALAA---LDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 207 LKAVVIYKEPPPNKMANVytmeEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITwTARYGSQ 286
Cdd:PRK12582 179 LDVTVVHVTGPGEGIASI----AFADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMC-ANIAMQE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 287 AGDIRPAEVQQEVVVSYLPLSHIAA--QIYD--LWTG----IQWGAQVcfaePdALKGSLVNTLREVEPTSHMGVPRVWE 358
Cdd:PRK12582 254 QLRPREPDPPPPVSLDWMPWNHTMGgnANFNglLWGGgtlyIDDGKPL----P-GMFEETIRNLREISPTVYGNVPAGYA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 359 KIMERIQ--EVAAQSGFIRRKMLLWAmsvtleqnltcpGSdlkpfttRLADYLvLAKVrQALGfakcqknfygaapmMAE 436
Cdd:PRK12582 329 MLAEAMEkdDALRRSFFKNLRLMAYG------------GA-------TLSDDL-YERM-QALA--------------VRT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 437 TQHfflglNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEgiGEICLWGRTIFMGYLNMEDKTCE 516
Cdd:PRK12582 374 TGH-----RIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPVGDK--YEVRVKGPNVTPGYHKDPELTAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 517 AIDEEGWLHTGDAGR-LDAD----GfLYITGRLKELIITAGGE--NVPPVPIeEAVKMELPIISNAMLIGDQRKFLSMLl 589
Cdd:PRK12582 447 AFDEEGFYRLGDAARfVDPDdpekG-LIFDGRVAEDFKLSTGTwvSVGTLRP-DAVAACSPVIHDAVVAGQDRAFIGLL- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 590 tlkCTLDPDTsdqtdnlteqamefCQRVGSRATTVSEIIeKKDEAVYQAIEEGIRRVNMNAAARPYHIQKWAILERDFSI 669
Cdd:PRK12582 524 ---AWPNPAA--------------CRQLAGDPDAAPEDV-VKHPAVLAILREGLSAHNAEAGGSSSRIARALLMTEPPSI 585
|
650 660 670
....*....|....*....|....*....|
gi 767983694 670 SGGELGPTMKLKRLTVLEKYKGIIDSFYQE 699
Cdd:PRK12582 586 DAGEITDKGYINQRAVLERRAALVERLYAE 615
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
206-565 |
1.89e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 92.52 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 206 HLKAVViykepPPNKMANVYTMEEFMELGNEVPEEALDAiidtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWT----- 280
Cdd:PRK05677 171 HVKKMV-----PAYHLPQAVKFNDALAKGAGQPVTEANP-----QADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqcr 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 281 ARYGSQAGDIRpaevqqEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCFAEPDALKGsLVNTLREVEPTSHMGVPRVWEK 359
Cdd:PRK05677 241 ALMGSNLNEGC------EILIAPLPLYHIYAFTFHCMAMMLIGNHnILISNPRDLPA-MVKELGKWKFSGFVGLNTLFVA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 360 IMERiqevaaqSGFirRKMLLWAMSVTLEQNLTcpgsdlkpfttrladyLVLAKvrqalgfAKCQKNFYGAApmmaetqh 439
Cdd:PRK05677 314 LCNN-------EAF--RKLDFSALKLTLSGGMA----------------LQLAT-------AERWKEVTGCA-------- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 440 fflglnirLYAGYGLSETSgPHFMSSPYNY-RLYSSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDK 513
Cdd:PRK05677 354 --------ICEGYGMTETS-PVVSVNPSQAiQVGTIGIPVPSTLCKVIDDDGNelplgEVGELCVKGPQVMKGYWQRPEA 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767983694 514 TCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGeNVPPVPIEEAV 565
Cdd:PRK05677 425 TDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGF-NVYPNELEDVL 475
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
257-563 |
1.90e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 90.40 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 257 LVYTSGTTGNPKGVMLSQDN-ITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALK 335
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNW----VVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 336 gSLVNTLREVEPTSHMGVPRVWEKIMeriqevaaqsgfirrkmllwamSVTLEQNLTCPgsdlkpfttrladylvlaKVR 415
Cdd:cd17635 82 -SLFKILTTNAVTTTCLVPTLLSKLV----------------------SELKSANATVP------------------SLR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 416 qALGFAkcqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMssPYNYRLY---SSGKLVPGCRVKLVNQD-AE 491
Cdd:cd17635 121 -LIGYG-------GSRAIAADVRFIEATGLTNTAQVYGLSETGTALCL--PTDDDSIeinAVGRPYPGVDVYLAATDgIA 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767983694 492 GI----GEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEE 563
Cdd:cd17635 191 GPsasfGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSE-SINCGGVKIAPDEVER 264
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
124-579 |
4.75e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 91.40 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 124 AKGFLKLGLKQAHSVAILGFNSP---EWFFsAVgtVFAGGIVTGI-YTTSSPEACQyiAYDCCANVIMV-DTQKQLEKIL 198
Cdd:PLN02860 46 AAGLLRLGLRNGDVVAIAALNSDlylEWLL-AV--ACAGGIVAPLnYRWSFEEAKS--AMLLVRPVMLVtDETCSSWYEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 199 KIWKQLPHLKAVVIYKEPPP---NKMANVYTMEEFMELGNEVPEEALdaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQD 275
Cdd:PLN02860 121 LQNDRLPSLMWQVFLESPSSsvfIFLNSFLTTEMLKQRALGTTELDY-----AWAPDDAVLICFTSGTTGRPKGVTISHS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 276 NITW-----TARYGSQAGDIrpaevqqevvvsYL---PLSHI---AAQIYDLWTGiqwGAQVCFAEPDAlkGSLVNTLRE 344
Cdd:PLN02860 196 ALIVqslakIAIVGYGEDDV------------YLhtaPLCHIgglSSALAMLMVG---ACHVLLPKFDA--KAALQAIKQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 345 VEPTSHMGVPrvweKIMERIQEVAaqsgfirRKMLLWAMSVTLEQNLTCPGSdlkpFTTRLADYLVLAKVRQALGFAkcq 424
Cdd:PLN02860 259 HNVTSMITVP----AMMADLISLT-------RKSMTWKVFPSVRKILNGGGS----LSSRLLPDAKKLFPNAKLFSA--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 425 knfYGaapmMAET--QHFFLGLNI-RLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGR 501
Cdd:PLN02860 321 ---YG----MTEAcsSLTFMTLHDpTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIGLDESSRVGRILTRGP 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767983694 502 TIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISNAMLIG 579
Cdd:PLN02860 394 HVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKT-GGENVYPEEV-EAVLSQHPGVASVVVVG 469
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
251-579 |
5.87e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 90.43 E-value: 5.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 251 PNQCCVLVYTSGTTGNPKGVMLSQDNIT-----------WTARygsqagdirpaevqqEVVVSYLPLSHIAAQIYDLWTG 319
Cdd:PRK07787 127 PDAPALIVYTSGTTGPPKGVVLSRRAIAadldalaeawqWTAD---------------DVLVHGLPLFHVHGLVLGVLGP 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 320 IQWGAQV---------CFAEPDALKGSLVntlreveptshMGVPRVWEkimeRIQEVAAQSGFIRRKMLLWAMSVTLeqn 390
Cdd:PRK07787 192 LRIGNRFvhtgrptpeAYAQALSEGGTLY-----------FGVPTVWS----RIAADPEAARALRGARLLVSGSAAL--- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 391 ltcpgsdlkPFTtrladylVLAKVRQALGFAKCQKnfYGaapmMAETqhfFLGLNIRlyagyglseTSGPHfmsspynyR 470
Cdd:PRK07787 254 ---------PVP-------VFDRLAALTGHRPVER--YG----MTET---LITLSTR---------ADGER--------R 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 471 LYSSGKLVPGCRVKLVNQ-------DAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGR 543
Cdd:PRK07787 292 PGWVGLPLAGVETRLVDEdggpvphDGETVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGR 371
|
330 340 350
....*....|....*....|....*....|....*.
gi 767983694 544 LKELIITAGGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:PRK07787 372 ESTDLIKSGGYRIGAGEIETAL-LGHPGVREAAVVG 406
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
86-579 |
6.20e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 91.11 E-value: 6.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 86 MFYEALDKY-----GDLIALGFKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGG 160
Cdd:PRK04319 44 IAYEAIDRHadggrKDKVALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 161 IVTGIYTTSSPEACQYIAYDCCANVImVDTQKQLEKilKIWKQLPHLKAVVIYKEPPPNKmANVYTMEEFMELGNEVPE- 239
Cdd:PRK04319 124 IVGPLFEAFMEEAVRDRLEDSEAKVL-ITTPALLER--KPADDLPSLKHVLLVGEDVEEG-PGTLDFNALMEQASDEFDi 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 240 EALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITW---TARYgsqAGDIRPAEvqqevvvsylplshiaaqIYdl 316
Cdd:PRK04319 200 EWTD-------REDGAILHYTSGSTGKPKGVLHVHNAMLQhyqTGKY---VLDLHEDD------------------VY-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 317 WtgiqwgaqvCFAEPDALKGS-----------LVNTLREVEPTshmgvPRVWEKIMERiQEV----AAQSGFirrKMLLW 381
Cdd:PRK04319 250 W---------CTADPGWVTGTsygifapwlngATNVIDGGRFS-----PERWYRILED-YKVtvwyTAPTAI---RMLMG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 382 AmsvtleqnltcpGSDLkpfttrLADYlVLAKVRQALGFAKcqknfygaaPMMAETQHF---FLGLniRLYAGYGLSETS 458
Cdd:PRK04319 312 A------------GDDL------VKKY-DLSSLRHILSVGE---------PLNPEVVRWgmkVFGL--PIHDNWWMTETG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 459 GpHFMSspyNY-----RLYSSGKLVPGCRVKLV-NQDAEG----IGEICL---WgRTIFMGYLNMEDKTcEAIDEEGWLH 525
Cdd:PRK04319 362 G-IMIA---NYpamdiKPGSMGKPLPGIEAAIVdDQGNELppnrMGNLAIkkgW-PSMMRGIWNNPEKY-ESYFAGDWYV 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 767983694 526 TGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:PRK04319 436 SGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVESKL-MEHPAVAEAGVIG 487
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
236-544 |
2.00e-18 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 88.46 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 236 EVPEEALDAIIDTQQP-------NQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSH 308
Cdd:cd05945 74 SSPAERIREILDAAKPalliadgDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGP----GDVFLNQAPFSF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 309 IAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWEKIMeriqevaaqsgfiRRKMLLWAMSVT 386
Cdd:cd05945 150 DLS-VMDLYPALASGATLVPVPRDATAdpKQLFRFLAEHGITVWVSTPSFAAMCL-------------LSPTFTPESLPS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 387 LEQNLTCpGsdlKPFTTRLADYLVlakvrqalgfakcqknfyGAAPmmaetqhfflglNIRLYAGYGLSET----SGPHF 462
Cdd:cd05945 216 LRHFLFC-G---EVLPHKTARALQ------------------QRFP------------DARIYNTYGPTEAtvavTYIEV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 463 MSSPY--NYRLYSsGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRL 532
Cdd:cd05945 262 TPEVLdgYDRLPI-GYAKPGAKLVILDEDGRpvppgEKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRL 340
|
330
....*....|..
gi 767983694 533 DADGFLYITGRL 544
Cdd:cd05945 341 EADGLLFYRGRL 352
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
257-565 |
3.01e-18 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 89.60 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 257 LVYTSGTTGNPKGVMLSQDNITWTARygsQAGDIRPAEvQQEVVVSYLPLSH----IAAQIYDLWTGIqwgAQVCFAEP- 331
Cdd:PRK08633 787 IIFSSGSEGEPKGVMLSHHNILSNIE---QISDVFNLR-NDDVILSSLPFFHsfglTVTLWLPLLEGI---KVVYHPDPt 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 332 DALKgslvntlreveptshmgvprvwekimerIQEVAAQsgfiRRKMLLWAMSvtleqnltcpgsdlkpftTRLADYLVL 411
Cdd:PRK08633 860 DALG----------------------------IAKLVAK----HRATILLGTP------------------TFLRLYLRN 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 412 AKVrQALGFAKCQKNFYGA---APMMAETqhFFLGLNIRLYAGYGLSETSG------PHFMSSPYNY----RLYSSGKLV 478
Cdd:PRK08633 890 KKL-HPLMFASLRLVVAGAeklKPEVADA--FEEKFGIRILEGYGATETSPvasvnlPDVLAADFKRqtgsKEGSVGMPL 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 479 PGCRVKLVNQD-----AEGI-GEICLWGRTIFMGYLNMEDKTCEAI---DEEGWLHTGDAGRLDADGFLYITGRLKEL-- 547
Cdd:PRK08633 967 PGVAVRIVDPEtfeelPPGEdGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFak 1046
|
330
....*....|....*...
gi 767983694 548 IitaGGENVPPVPIEEAV 565
Cdd:PRK08633 1047 I---GGEMVPLGAVEEEL 1061
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
57-567 |
3.06e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 88.57 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 57 EALWTTRADGRVRLRIDPScpQLPYTVHrMFYEALDKYGDLIA-------LGFKrqdKWEHISysqyyllarRAAKGFLK 129
Cdd:PRK08974 2 EKVWLNRYPADVPAEINPD--RYQSLVD-MFEQAVARYADQPAfinmgevMTFR---KLEERS---------RAFAAYLQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 130 --LGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV--DTQKQLEKIL------- 198
Cdd:PRK08974 67 ngLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIvsNFAHTLEKVVfktpvkh 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 199 ----KIWKQLPHLKA-----VVIY--KEPPPNKMANVYTMEEFMELGNEV----PEEALDAIidtqqpnqcCVLVYTSGT 263
Cdd:PRK08974 147 viltRMGDQLSTAKGtlvnfVVKYikRLVPKYHLPDAISFRSALHKGRRMqyvkPELVPEDL---------AFLQYTGGT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 264 TGNPKGVMLSQDNITwtARYGSQAGDIRPA-EVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQvcfaepdalkGSLVNTL 342
Cdd:PRK08974 218 TGVAKGAMLTHRNML--ANLEQAKAAYGPLlHPGKELVVTALPLYHIFALTVNCLLFIELGGQ----------NLLITNP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 343 REVEptshmgvprvwekimeriqevaaqsGFIRrkmllwamsvtleqnltcpgsDLK--PFTT-----RLADYLVLAKVR 415
Cdd:PRK08974 286 RDIP-------------------------GFVK---------------------ELKkyPFTAitgvnTLFNALLNNEEF 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 416 QALGFAKCQKNFYGAAPM---MAETQHFFLGLNirLYAGYGLSETSgPHFMSSPYNYRLY--SSGKLVPGCRVKLVNQDA 490
Cdd:PRK08974 320 QELDFSSLKLSVGGGMAVqqaVAERWVKLTGQY--LLEGYGLTECS-PLVSVNPYDLDYYsgSIGLPVPSTEIKLVDDDG 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 491 EGI-----GEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGeNVPPVPIEEAV 565
Cdd:PRK08974 397 NEVppgepGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGF-NVYPNEIEDVV 474
|
..
gi 767983694 566 KM 567
Cdd:PRK08974 475 ML 476
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
445-579 |
3.27e-18 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 86.31 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 445 NIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGRTIFMGYLNMEdktceAIDEEGWL 524
Cdd:cd17633 136 KANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGG-----FSNPDGWM 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 767983694 525 HTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISNAMLIG 579
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLK-AIPGIEEAIVVG 263
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
112-579 |
6.29e-17 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 83.93 E-value: 6.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 112 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYiaydccanvimvdtq 191
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEY--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 192 kqlekilkiwkQLPHLKAVVIykepppnkmanvytmeefmelgnevpeealdaIIDTQQPnqcCVLVYTSGTTGNPKGVm 271
Cdd:cd05972 67 -----------RLEAAGAKAI--------------------------------VTDAEDP---ALIYFTSGTTGLPKGV- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 272 lsqdnitwtarygsqagdirpaevqqEVVVSYlPLSHI--AAQIYDL------WTGIQWGAQVC----FAEPdALKGS-- 337
Cdd:cd05972 100 --------------------------LHTHSY-PLGHIptAAYWLGLrpddihWNIADPGWAKGawssFFGP-WLLGAtv 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 338 LVNTLREVEPtshmgvpRVWEKIMERIQevaaqsgfirrkmllwamsVTleqNLTCPGSDLKPFTTRLADYLVLAKVRQA 417
Cdd:cd05972 152 FVYEGPRFDA-------ERILELLERYG-------------------VT---SFCGPPTAYRMLIKQDLSSYKFSHLRLV 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 418 LGfakcqknfyGAAPMMAETQHFF---LGLNIRlyAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI- 493
Cdd:cd05972 203 VS---------AGEPLNPEVIEWWraaTGLPIR--DGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELp 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 494 ----GEICLWGRTI--FMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkM 567
Cdd:cd05972 272 pgeeGDIAIKLPPPglFLGYVGDPEKT-EASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS-GYRIGPFEVESAL-L 348
|
490
....*....|..
gi 767983694 568 ELPIISNAMLIG 579
Cdd:cd05972 349 EHPAVAEAAVVG 360
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
111-583 |
1.07e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 83.94 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIvtgiYTTSSP--------------EACQY 176
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAV----HVPVSPlfrehelsyelndaGAEVL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 177 IAYDCCANVIM-VDTQKQLEKILK--IWKQLPHLKAVviykePPPNKMAN----VYTMEEFMELGNEVPEEALDAIIDTQ 249
Cdd:PRK06178 135 LALDQLAPVVEqVRAETSLRHVIVtsLADVLPAEPTL-----PLPDSLRAprlaAAGAIDLLPALRACTAPVPLPPPALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 250 QPnqcCVLVYTSGTTGNPKGVMLSQDNITWTArygSQAGDIRPAEVQQEVVVSYLPLSHIAAQ----IYDLWTGI----- 320
Cdd:PRK06178 210 AL---AALNYTGGTTGMPKGCEHTQRDMVYTA---AAAYAVAVVGGEDSVFLSFLPEFWIAGEnfglLFPLFSGAtlvll 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 321 -QWGAQVCFAEPDALK----GSLVNTLREVeptshMGVPRVWEKIMERIQEVAAQSgFIRRkmllwamsvtleqnltcpg 395
Cdd:PRK06178 284 aRWDAVAFMAAVERYRvtrtVMLVDNAVEL-----MDHPRFAEYDLSSLRQVRVVS-FVKK------------------- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 396 sdLKPfttrlaDYlvlakvRQALgfakcqKNFYGAapMMAEtqhfflglnirlyAGYGLSET------------------ 457
Cdd:PRK06178 339 --LNP------DY------RQRW------RALTGS--VLAE-------------AAWGMTEThtcdtftagfqdddfdll 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 458 SGPHFMSSPynyrlyssgklVPGCRVKLVNQDAEGI------GEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGR 531
Cdd:PRK06178 384 SQPVFVGLP-----------VPGTEFKICDFETGELlplgaeGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGK 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 767983694 532 LDADGFLYITGRLKELIITAGGENVPPvpiE-EAVKMELPIISNAMLIG--DQRK 583
Cdd:PRK06178 452 IDEQGFLHYLGRRKEMLKVNGMSVFPS---EvEALLGQHPAVLGSAVVGrpDPDK 503
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
109-615 |
1.30e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 83.74 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 188
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 DTQ--KQLEKILKIW--KQLPHLKA---VVIYKE---PPPNKMA---NVYTMEEFMELGNevPEEALdaiidtQQPN--- 252
Cdd:PLN02479 124 DQEffTLAEEALKILaeKKKSSFKPpllIVIGDPtcdPKSLQYAlgkGAIEYEKFLETGD--PEFAW------KPPAdew 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 253 QCCVLVYTSGTTGNPKGVMLSQ---------DNITWTARYGSqagdirpaevqqeVVVSYLPLSHIAAQIYDLWTGIQWG 323
Cdd:PLN02479 196 QSIALGYTSGTTASPKGVVLHHrgaylmalsNALIWGMNEGA-------------VYLWTLPMFHCNGWCFTWTLAALCG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 324 AQVCfaepdalkgslvntLREVEPTShmgvprvwekimerIQEVAAQSGFIRrkmlLWAMSVTLEQNLTCPGSDLKPFTT 403
Cdd:PLN02479 263 TNIC--------------LRQVTAKA--------------IYSAIANYGVTH----FCAAPVVLNTIVNAPKSETILPLP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 404 RLADYLVLakvrqalgfakcqknfyGAAP----MMAETQHFFlglniRLYAGYGLSETSGPHFMSS--PYNYRLYSSGKL 477
Cdd:PLN02479 311 RVVHVMTA-----------------GAAPppsvLFAMSEKGF-----RVTHTYGLSETYGPSTVCAwkPEWDSLPPEEQA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 478 VPGCR------------------VKLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLY 539
Cdd:PLN02479 369 RLNARqgvryiglegldvvdtktMKPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 540 ITGRLKELIITaGGENVPPVPIEEAVKMElPIISNAMLIG--DQRKFLS--MLLTLKCtlDPDTSDQTdNLTEQAMEFCQ 615
Cdd:PLN02479 448 IKDRSKDIIIS-GGENISSLEVENVVYTH-PAVLEASVVArpDERWGESpcAFVTLKP--GVDKSDEA-ALAEDIMKFCR 522
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
249-568 |
1.50e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 82.92 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 249 QQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSH----IAAQIYDLWTGIQwga 324
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWK----TKDRILSWMPLTHdmglIAFHLAPLIAGMN--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 325 qvcfaepdalkgslvntlreveptshmgvprvwekimeriQEVAAQSGFIRRKML-LWAMSVTLEQNLTCP--GSD--LK 399
Cdd:cd05908 176 ----------------------------------------QYLMPTRLFIRRPILwLKKASEHKATIVSSPnfGYKyfLK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 400 PFTTRLADYLVLAKVRQALGfakcqknfyGAAPMMAETQHFFL------GLNIR-LYAGYGLSETS--------GPHFM- 463
Cdd:cd05908 216 TLKPEKANDWDLSSIRMILN---------GAEPIDYELCHEFLdhmskyGLKRNaILPVYGLAEASvgaslpkaQSPFKt 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 464 -------------------SSPYNYRLYSSGKLVPGCRVKLVNQDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAID 519
Cdd:cd05908 287 itlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICDEDNKIlpdgyIGHIQIRGKNVTPGYYNNPEATAKVFT 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 767983694 520 EEGWLHTGDAGrLDADGFLYITGRLKELIITaGGENVPPVPIEE-AVKME 568
Cdd:cd05908 367 DDGWLKTGDLG-FIRNGRLVITGREKDIIFV-NGQNVYPHDIERiAEELE 414
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
230-554 |
1.83e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 83.61 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 230 FMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVvvSYLPLSHI 309
Cdd:PTZ00342 282 IILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKTHL--SYLPISHI 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 310 AAQIY---DLWTGIQ---WGAQVCFAEPDAL--KGSLVntlreveptshMGVPRVWEKIMERIQEVAAQSGFIRRKMLLW 381
Cdd:PTZ00342 360 YERVIaylSFMLGGTiniWSKDINYFSKDIYnsKGNIL-----------AGVPKVFNRIYTNIMTEINNLPPLKRFLVKK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 382 AMSVTLEQNLTCPGSDLKPFTTrladylVLAKVRQALGfAKCQKNFYGAAPMMAE-TQHFFLGLNIRLYAGYGLSETSGP 460
Cdd:PTZ00342 429 ILSLRKSNNNGGFSKFLEGITH------ISSKIKDKVN-PNLEVILNGGGKLSPKiAEELSVLLNVNYYQGYGLTETTGP 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 461 HFMSSPYNYRLYS-SGKLVPGCRVKLVN------QDAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLD 533
Cdd:PTZ00342 502 IFVQHADDNNTESiGGPISPNTKYKVRTwetykaTDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQIN 581
|
330 340
....*....|....*....|.
gi 767983694 534 ADGFLYITGRLKELIITAGGE 554
Cdd:PTZ00342 582 KNGSLTFLDRSKGLVKLSQGE 602
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
111-579 |
1.94e-16 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 82.14 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCAnvimvdt 190
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGA------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 191 qkqlekilkiwkqlphlKAVVIYKEpppnkmanvytMEEFMelgnevpeealdaiidtqqpnqccVLVYTSGTTGNPKGV 270
Cdd:cd05935 75 -----------------KVAVVGSE-----------LDDLA------------------------LIPYTSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 271 MLSQDNITWTARYGSQAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCfaepdalkgslvntlreveptsh 350
Cdd:cd05935 103 MHTHFSAAANALQSAVWTGLTPSDV----ILACLPLFHVTGFVGSLNTAVYVGGTYV----------------------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 351 mgvprvwekIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTcpgSDLKPFTTRLADYLVLAKvrqalgfakcqknfyGA 430
Cdd:cd05935 156 ---------LMARWDRETALELIEKYKVTFWTNIPTMLVDLL---ATPEFKTRDLSSLKVLTG---------------GG 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 431 APMMAETQHFFLGL-NIRLYAGYGLSETSGPHFMSSPYNYRLYSSGklVPGCRVKLVNQDAEG--------IGEICLWGR 501
Cdd:cd05935 209 APMPPAVAEKLLKLtGLRFVEGYGLTETMSQTHTNPPLRPKLQCLG--IP*FGVDARVIDIETgrelppneVGEIVVRGP 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 502 TIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGEnVPPVPIeEAVKMELPIISNAMLI 578
Cdd:cd05935 287 QIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK-VWPAEV-EAKLYKHPAI*EVCVI 364
|
.
gi 767983694 579 G 579
Cdd:cd05935 365 S 365
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
256-582 |
2.66e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 80.86 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 256 VLVYTSGTTGNPKGVMLSQDNITWTA-----RYGSQAgdirpaevqQEVVVsyLPLSHIAaqiydlwtgiqwGAQVcfae 330
Cdd:PRK07824 39 LVVATSGTTGTPKGAMLTAAALTASAdathdRLGGPG---------QWLLA--LPAHHIA------------GLQV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 331 pdalkgsLV-NTLREVEPTShMGVPRVWEkIMERIQEVAAQSGFiRRKMLLWAMSvtLEQNLTCPGSdlkpfTTRLADY- 408
Cdd:PRK07824 92 -------LVrSVIAGSEPVE-LDVSAGFD-PTALPRAVAELGGG-RRYTSLVPMQ--LAKALDDPAA-----TAALAELd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 409 LVLAkvrqalgfakcqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGphfmSSPYNyrlyssGKLVPGCRVKLVNq 488
Cdd:PRK07824 155 AVLV----------------GGGPAPAPVLDAAAAAGINVVRTYGMSETSG----GCVYD------GVPLDGVRVRVED- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 489 daegiGEICLWGRTIFMGYLNMEDKtcEAIDEEGWLHTGDAGRLDaDGFLYITGRLKElIITAGGENVPPVPIEEAVkME 568
Cdd:PRK07824 208 -----GRIALGGPTLAKGYRNPVDP--DPFAEPGWFRTDDLGALD-DGVLTVLGRADD-AISTGGLTVLPQVVEAAL-AT 277
|
330
....*....|....*.
gi 767983694 569 LPIISNAMLIG--DQR 582
Cdd:PRK07824 278 HPAVADCAVFGlpDDR 293
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
112-577 |
3.05e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 82.37 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 112 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ 191
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 192 -----KQLEKILKIWKQLPHLKAVVIYK-EPPPNKMANVYTMEEFMELGNEVPEeALDAIIDTQQPNQCCVLVYTSGTTG 265
Cdd:PLN03102 121 feplaREVLHLLSSEDSNLNLPVIFIHEiDFPKRPSSEELDYECLIQRGEPTPS-LVARMFRIQDEHDPISLNYTSGTTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 266 NPKGVMLSQDNI---TWTARYGSQAGdIRPaevqqeVVVSYLPLSHIAAQIYDLWTGIQWGAQVCF---AEPDALKGSlv 339
Cdd:PLN03102 200 DPKGVVISHRGAylsTLSAIIGWEMG-TCP------VYLWTLPMFHCNGWTFTWGTAARGGTSVCMrhvTAPEIYKNI-- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 340 ntlrEVEPTSHMG-VPRVWEKIME-RIQEVAAQSGFIrrkmllwamsvtleQNLTcpGSDLKPfttrladyLVLAKVRQA 417
Cdd:PLN03102 271 ----EMHNVTHMCcVPTVFNILLKgNSLDLSPRSGPV--------------HVLT--GGSPPP--------AALVKKVQR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 418 LGFakcqknfygaapmmaETQHfflglnirlyaGYGLSETSGPHFMSS--------PYNYRLYSSGKlvPGCRV------ 483
Cdd:PLN03102 323 LGF---------------QVMH-----------AYGLTEATGPVLFCEwqdewnrlPENQQMELKAR--QGVSIlgladv 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 484 --------KLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGEN 555
Cdd:PLN03102 375 dvknketqESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGEN 452
|
490 500
....*....|....*....|..
gi 767983694 556 VPPVPIEEAVKMELPIISNAML 577
Cdd:PLN03102 453 ISSVEVENVLYKYPKVLETAVV 474
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
236-543 |
4.67e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 81.03 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 236 EVPEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDirpaevqqeVVVSY 303
Cdd:cd05930 70 SYPAERLAYILeDSGaklvltDPDDLAYVIYTSGSTGKPKGVMVEHRGLVnlllwMQEAYPLTPGD---------RVLQF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 304 LPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWekimeriqevaaqsgfirrkmllw 381
Cdd:cd05930 141 TSFSFDVS-VWEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTPSLL------------------------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 382 amSVTLEQNLTCPGSDLKpfttrladYLVLA--KVRQALgfakcQKNFYGAAPmmaetqhfflglNIRLYAGYGLSETS- 458
Cdd:cd05930 196 --RLLLQELELAALPSLR--------LVLVGgeALPPDL-----VRRWRELLP------------GARLVNLYGPTEATv 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 459 GPHFMSSPYNYRLYSS---GKLVPGCRVKLVNQD-----AEGIGEICLWGRTIFMGYLNMEDKTCEAI-----DEEGWLH 525
Cdd:cd05930 249 DATYYRVPPDDEEDGRvpiGRPIPNTRVYVLDENlrpvpPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfGPGERMY 328
|
330
....*....|....*....
gi 767983694 526 -TGDAGRLDADGFLYITGR 543
Cdd:cd05930 329 rTGDLVRWLPDGNLEFLGR 347
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
109-564 |
6.37e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 81.10 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFfsavgTVFAGGIVTGIYTT------SSPEAcQYIAYDCC 182
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFF-----EVYWAARRSGLYYTpinwhlTAAEI-AYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 183 ANVIMVDtQKQLEKILKIWKQLPHlkavviykepppnkmanvyTMEEFMELGNEVP-----EEALDAIIDTQQPNQC--C 255
Cdd:PRK08276 84 AKVLIVS-AALADTAAELAAELPA-------------------GVPLLLVVAGPVPgfrsyEEALAAQPDTPIADETagA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 256 VLVYTSGTTGNPKGVM--LSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAqiydlwtgIQWGAQVcfaepDA 333
Cdd:PRK08276 144 DMLYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAP--------LRFGMSA-----LA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 334 LKGSLV--------NTLREVE----PTSHMgVPrvwekIMeriqevaaqsgFIRrkMLlwamsvtleqnltcpgsdlkpf 401
Cdd:PRK08276 211 LGGTVVvmekfdaeEALALIEryrvTHSQL-VP-----TM-----------FVR--ML---------------------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 402 ttRLADylvlaKVRQALGFAKCQKNFYGAAP--------MMAetqhfFLGLNIRLYagYGLSETSGPHFMSS------PY 467
Cdd:PRK08276 250 --KLPE-----EVRARYDVSSLRVAIHAAAPcpvevkraMID-----WWGPIIHEY--YASSEGGGVTVITSedwlahPG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 468 nyrlySSGKLVPGcRVKLVNQDAEGI--GEIclwGrTIFM-------GYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFL 538
Cdd:PRK08276 316 -----SVGKAVLG-EVRILDEDGNELppGEI---G-TVYFemdgypfEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYL 385
|
490 500
....*....|....*....|....*.
gi 767983694 539 YITGRLKELIITaGGENVPPVPIEEA 564
Cdd:PRK08276 386 YLTDRKSDMIIS-GGVNIYPQEIENL 410
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
120-579 |
7.03e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 81.29 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 120 ARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKqLEKILK 199
Cdd:PRK07008 49 AKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTF-LPLVDA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 200 IWKQLPHLKAVVIykepppnkMANVYTMEEfmelgNEVPEEALDAIIDTQQP---------NQCCVLVYTSGTTGNPKGV 270
Cdd:PRK07008 128 LAPQCPNVKGWVA--------MTDAAHLPA-----GSTPLLCYETLVGAQDGdydwprfdeNQASSLCYTSGTTGNPKGA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 271 MLSQDNITWTArYGSQAGDIRPAEVqQEVVVSYLPLSHIAAqiydlWtGIQW-----GAQVCFAEPDaLKGSLVNTLREV 345
Cdd:PRK07008 195 LYSHRSTVLHA-YGAALPDAMGLSA-RDAVLPVVPMFHVNA-----W-GLPYsapltGAKLVLPGPD-LDGKSLYELIEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 346 EP-TSHMGVPRVWEKIMERIQEVAAQSGFIRRkmllwamsvTLEQNLTCPGSDLKPFTtrlADYLVlaKVRQALGfakcq 424
Cdd:PRK07008 266 ERvTFSAGVPTVWLGLLNHMREAGLRFSTLRR---------TVIGGSACPPAMIRTFE---DEYGV--EVIHAWG----- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 425 knfygaapmMAETQHffLGLNIRLYAGY-GLSETSGPHfmsspynyRLYSSGKLVPGCRVKLVNQ-------DAEGIGEI 496
Cdd:PRK07008 327 ---------MTEMSP--LGTLCKLKWKHsQLPLDEQRK--------LLEKQGRVIYGVDMKIVGDdgrelpwDGKAFGDL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 497 CLWGRTIFMGYLNMEDKTCeaIDeeGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEEaVKMELPIISNAM 576
Cdd:PRK07008 388 QVRGPWVIDRYFRGDASPL--VD--GWFPTGDVATIDADGFMQITDRSKD-VIKSGGEWISSIDIEN-VAVAHPAVAEAA 461
|
...
gi 767983694 577 LIG 579
Cdd:PRK07008 462 CIA 464
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
82-614 |
7.45e-16 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 81.02 E-value: 7.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 82 TVHRMFYEALDKYGDLIALGFKRQDKweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGI 161
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGL--RLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 162 VTGIYTTSSP-EACQYIAYD-CCANVIMVDTQKQLEKILkiwkqlphlkavviykepppnkmANVYTMEEFMELGNEVPE 239
Cdd:cd05923 80 PALINPRLKAaELAELIERGeMTAAVIAVDAQVMDAIFQ-----------------------SGVRVLALSDLVGLGEPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 240 EALDAIIDTQ-QPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGS-QAGDIRPAevqQEVVVSYLPLSHIAAQIYDLW 317
Cdd:cd05923 137 SAGPLIEDPPrEPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMStQAGLRHGR---HNVVLGLMPLYHVIGFFAVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 318 TGIQWGAQVCFAEPDAlKGSLVNTLREVEPTSHMGVPrvwekimeriqevaaqsgfirrkMLLWAMSVTLEQNltcpGSD 397
Cdd:cd05923 214 AALALDGTYVVVEEFD-PADALKLIEQERVTSLFATP-----------------------THLDALAAAAEFA----GLK 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 398 LKPFTTrladylvlakvrqaLGFAkcqknfyGAA---PMMAETQHFFLGLNIRLYagyGLSETsgphfMSSPYNYRLYSS 474
Cdd:cd05923 266 LSSLRH--------------VTFA-------GATmpdAVLERVNQHLPGEKVNIY---GTTEA-----MNSLYMRDARTG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 475 GKLVPG--CRVKLVN-----QDAEGIGE-----ICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITG 542
Cdd:cd05923 317 TEMRPGffSEVRIVRiggspDEALANGEegeliVAAAADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILG 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767983694 543 RLKELIITaGGENVPPVPIEEAVKMElPIISNAMLIG--DQRKFLSMLLTLKCTLDPDTSDQTDnlteqamEFC 614
Cdd:cd05923 396 RVDDMIIS-GGENIHPSEIERVLSRH-PGVTEVVVIGvaDERWGQSVTACVVPREGTLSADELD-------QFC 460
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
256-562 |
4.02e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 78.78 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 256 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSH----IAAQIYDLWTGiqwGAQVCFAEP 331
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSP----RDATVAVMPLYHghglIAALLATLASG---GAVLLPARG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 332 DALKGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSG-----FIRrkmllwamsvtleqnlTCPGsdlkPFTTRLA 406
Cdd:PRK05852 253 RFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKpaalrFIR----------------SCSA----PLTAETA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 407 dylvlakvrQALgfakcQKNFygAAPM-----MAETQHFFLGLNIRlyaGYGLSE----TSGPHFMSSPYNYRLY-SSGK 476
Cdd:PRK05852 313 ---------QAL-----QTEF--AAPVvcafgMTEATHQVTTTQIE---GIGQTEnpvvSTGLVGRSTGAQIRIVgSDGL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 477 LVPgcrvklvnqdAEGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENV 556
Cdd:PRK05852 374 PLP----------AGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKEL-INRGGEKI 441
|
....*.
gi 767983694 557 PPVPIE 562
Cdd:PRK05852 442 SPERVE 447
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
112-633 |
4.28e-15 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 78.31 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 112 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVdTQ 191
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 192 KQLEKilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtQQPNQCCVLVYTSGTTGNPKGVM 271
Cdd:cd05969 81 ELYER----------------------------------------------------TDPEDPTLLHYTSGTTGTPKGVL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 272 LSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDAlkgslvntlreveptshm 351
Cdd:cd05969 109 HVHDAMIFYYFTGKYVLDLHP----DDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF------------------ 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 352 gVPRVWEKIMERIqevaaqsgfirrKMLLWAMSVTLEQNLTcpgsdlkpfttRLADYLVLAKVRQALGFAKCqknfyGAA 431
Cdd:cd05969 167 -DAESWYGIIERV------------KVTVWYTAPTAIRMLM-----------KEGDELARKYDLSSLRFIHS-----VGE 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 432 PMMAETQHFFLG-LNIRLYAGYGLSETSGPHFMSSP-YNYRLYSSGKLVPGCRVKLVNQDAEGI-----GEICL---WgR 501
Cdd:cd05969 218 PLNPEAIRWGMEvFGVPIHDTWWQTETGSIMIANYPcMPIKPGSMGKPLPGVKAAVVDENGNELppgtkGILALkpgW-P 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 502 TIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIGDQ 581
Cdd:cd05969 297 SMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESAL-MEHPAVAEAGVIGKP 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 767983694 582 RKFLSMLLTLKCTLDPDTSdQTDNLTEQAMEFCqRVGSRATTVSEIIEKKDE 633
Cdd:cd05969 374 DPLRGEIIKAFISLKEGFE-PSDELKEEIINFV-RQKLGAHVAPREIEFVDN 423
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
250-583 |
7.22e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 78.85 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 250 QPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHiaaqiydlwtgiqwgaqvCFA 329
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSP----EDKVFNALPVFH------------------SFG 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 330 epdaLKGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFirrkmllwamsvtleqnltcpGSDlkpftTRLADYl 409
Cdd:PRK06814 849 ----LTGGLVLPLLSGVKVFLYPSPLHYRIIPELIYDTNATILF---------------------GTD-----TFLNGY- 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 410 vlAKVRQALGFAKCQKNFYGAAPMMAETQHFFL-GLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLvnQ 488
Cdd:PRK06814 898 --ARYAHPYDFRSLRYVFAGAEKVKEETRQTWMeKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRL--E 973
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 489 DAEGI---GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIEEAV 565
Cdd:PRK06814 974 PVPGIdegGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRF-AKIAGEMISLAAVEELA 1052
|
330
....*....|....*....
gi 767983694 566 KMELP-IISNAMLIGDQRK 583
Cdd:PRK06814 1053 AELWPdALHAAVSIPDARK 1071
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
255-579 |
1.21e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 75.80 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 255 CVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevvvsYL---PLSHIaaqiydlwtgiqwgaqvcfaep 331
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTV-------FLnsgPLFHI---------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 332 dalkGSLVNTLrevePTSHMG-----VPRV-WEKIMERIQEVAAQSGFIrrkmllwaMSVTLEQNLtcpgsdlKPFTTRL 405
Cdd:cd17636 54 ----GTLMFTL----ATFHAGgtnvfVRRVdAEEVLELIEAERCTHAFL--------LPPTIDQIV-------ELNADGL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 406 ADYLVLAKVRQALGFAkcqknfygaAPMMAETQHFFLGLnirlyAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKL 485
Cdd:cd17636 111 YDLSSLRSSPAAPEWN---------DMATVDTSPWGRKP-----GGYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 486 VnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRlKELIITAGGENVPP 558
Cdd:cd17636 177 L--DEDGrevpdgeVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYP 252
|
330 340
....*....|....*....|.
gi 767983694 559 VPIEEAVKmELPIISNAMLIG 579
Cdd:cd17636 253 AEVERCLR-QHPAVADAAVIG 272
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
248-567 |
2.69e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 76.21 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 248 TQQPNQCCVLVYTSGTTGNPKGVMLSQDNI--------TWTarygsQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTG 319
Cdd:PRK07059 200 KLGPDDVAFLQYTGGTTGVSKGATLLHRNIvanvlqmeAWL-----QPAFEKKPRPDQLNFVCALPLYHIFALTVCGLLG 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 320 IQWGA-QVCFAEPDALKGsLVNTLREVEPTSHMGVPRVWEKIMEriqevaaQSGFirRKMllwamsvtleqnltcpgsDL 398
Cdd:PRK07059 275 MRTGGrNILIPNPRDIPG-FIKELKKYQVHIFPAVNTLYNALLN-------NPDF--DKL------------------DF 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 399 KPFttrladylvlaKVRQALGFAkCQKNfygaapmMAETQHFFLGLNIrlYAGYGLSETSgPHFMSSPYNYRLYSSGKLV 478
Cdd:PRK07059 327 SKL-----------IVANGGGMA-VQRP-------VAERWLEMTGCPI--TEGYGLSETS-PVATCNPVDATEFSGTIGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 479 PGCRVKLVNQDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITA 551
Cdd:PRK07059 385 PLPSTEVSIRDDDGndlplgePGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
330
....*....|....*.
gi 767983694 552 GGeNVPPVPIEEAVKM 567
Cdd:PRK07059 465 GF-NVYPNEIEEVVAS 479
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
224-568 |
7.16e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 75.04 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 224 VYTMEEFMELgnevpeEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAG-DIRPAEVqqevVVS 302
Cdd:PRK09192 154 VLSHAWFKAL------PEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGlKVRPGDR----CVS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 303 YLPLSHiaaqiyDLwtgiqwGAQVCFAEPDALKGSlVNTLrevePTSHMGV-PRVWEKIMERIQEVAAQS---GF---IR 375
Cdd:PRK09192 224 WLPFYH------DM------GLVGFLLTPVATQLS-VDYL----PTRDFARrPLQWLDLISRNRGTISYSppfGYelcAR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 376 RkmllwAMSVTLEQ-NLTC-----PGSD------LKPFTTRLADylvlakvrqaLGFAkcQKNF---YG------AAPMM 434
Cdd:PRK09192 287 R-----VNSKDLAElDLSCwrvagIGADmirpdvLHQFAEAFAP----------AGFD--DKAFmpsYGlaeatlAVSFS 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 435 AETQHF-FLGLNIRLYAGYGLSETSGphfmSSPYNYRLY-SSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGY 507
Cdd:PRK09192 350 PLGSGIvVEEVDRDRLEYQGKAVAPG----AETRRVRTFvNCGKALPGHEIEIRNEAGMplperVVGHICVRGPSLMSGY 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767983694 508 LNMEDkTCEAIDEEGWLHTGDAGRLdADGFLYITGRLKELIITaGGENVPPVPIEEAVKME 568
Cdd:PRK09192 426 FRDEE-SQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIII-NGRNIWPQDIEWIAEQE 483
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
109-579 |
1.16e-13 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 73.67 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFL-KLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 187
Cdd:cd05958 9 REWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 188 VDtqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeEALDAIIDTqqpnqcCVLVYTSGTTGNP 267
Cdd:cd05958 89 CA--------------------------------------------------HALTASDDI------CILAFTSGTTGAP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 268 KGVM-LSQDNITWTARYGSQAgdIRPAEvqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQvCFAEPDALKGSLVNTLREVE 346
Cdd:cd05958 113 KATMhFHRDPLASADRYAVNV--LRLRE--DDRFVGSPPLAFTFGLGGVLLFPFGVGAS-GVLLEEATPDLLLSAIARYK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 347 PTSHMGVPRVWEKIMERIQEVAAQSGFIRRkmllwamsvtleqnLTCPGSDLKPFTTRLADYLVLAKVRQALGfakCQKN 426
Cdd:cd05958 188 PTVLFTAPTAYRAMLAHPDAAGPDLSSLRK--------------CVSAGEALPAALHRAWKEATGIPIIDGIG---STEM 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 427 FygaapmmaetqHFFLGlnirlyagyglsetsgphfmSSPYNYRLYSSGKLVPGCRVKLVnqDAEG-------IGEICLW 499
Cdd:cd05958 251 F-----------HIFIS--------------------ARPGDARPGATGKPVPGYEAKVV--DDEGnpvpdgtIGRLAVR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 500 GRTifmGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:cd05958 298 GPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVEDVL-LQHPAVAECAVVG 372
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
475-579 |
1.34e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 73.81 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 475 GKLVPGCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKtcEAIDeeGWLHTGDAGRLDADGFLYITGRLKEL 547
Cdd:PRK07788 379 GRPPKGVTVKIL--DENGnevprgvVGRIFVGNGFPFEGYTDGRDK--QIID--GLLSSGDVGYFDEDGLLFVDGRDDDM 452
|
90 100 110
....*....|....*....|....*....|..
gi 767983694 548 IITaGGENVPPVPIEEAVKmELPIISNAMLIG 579
Cdd:PRK07788 453 IVS-GGENVFPAEVEDLLA-GHPDVVEAAVIG 482
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
109-579 |
1.60e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 73.57 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFfsavgTVFAGGIVTGIYTTS-----SPEACQYIAYDCCA 183
Cdd:PRK13391 23 EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYL-----EVCWAAERSGLYYTCvnshlTPAEAAYIVDDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 184 NViMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPpnkmanvyTMEEFMELgnevpEEALDAIIDTQQPNQC--CVLVYTS 261
Cdd:PRK13391 98 RA-LITSAAKLDVARALLKQCPGVRHRLVLDGDG--------ELEGFVGY-----AEAVAGLPATPIADESlgTDMLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 262 GTTGNPKGVM--LS----QDNITWTA----RYGSQAGDIrpaevqqevvvsYL---PLSHIAAQIYDLwTGIQWGAQVCF 328
Cdd:PRK13391 164 GTTGRPKGIKrpLPeqppDTPLPLTAflqrLWGFRSDMV------------YLspaPLYHSAPQRAVM-LVIRLGGTVIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 329 AEP-DAlkgslvntlreveptshmgvprvwEKIMERIQEVAaqsgfIRRKMLLWAMSVTLeqnLTCPgsdlkpfttrlad 407
Cdd:PRK13391 231 MEHfDA------------------------EQYLALIEEYG-----VTHTQLVPTMFSRM---LKLP------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 408 ylvlAKVRQALGFAKCQKNFYGAAPMMAETQHFFL---GLNIRLYagYGLSETSGPHFMSSP-YNYRLYSSGKLVPGcrv 483
Cdd:PRK13391 266 ----EEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIdwwGPIIHEY--YAATEGLGFTACDSEeWLAHPGTVGRAMFG--- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 484 KLVNQDAEG-------IGEICLWGRTIFMgYLNMEDKTCEAIDEEG-WLHTGDAGRLDADGFLYITGRLKELIITaGGEN 555
Cdd:PRK13391 337 DLHILDDDGaelppgePGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIIS-GGVN 414
|
490 500
....*....|....*....|....
gi 767983694 556 VPPVPIEEAVkMELPIISNAMLIG 579
Cdd:PRK13391 415 IYPQEAENLL-ITHPKVADAAVFG 437
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
85-543 |
2.24e-13 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 72.73 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 85 RMFYEALDKYGDLIALgfkrQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGgivtg 164
Cdd:cd17653 1 DAFERIAAAHPDAVAV----ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAG----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 165 iyttsspeaCQYIAydccanvimVDTqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnEVPEEALDA 244
Cdd:cd17653 72 ---------AAYVP---------LDA---------------------------------------------KLPSARIQA 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 245 IIDTQQPNQC---------CVLVYTSGTTGNPKGVMLSQDNIT----WT-ARYGSQAGDiRPAEVqqevvvsylpLShIA 310
Cdd:cd17653 89 ILRTSGATLLlttdspddlAYIIFTSGSTGIPKGVMVPHRGVLnyvsQPpARLDVGPGS-RVAQV----------LS-IA 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 311 --AQIYDLWTGIQWGAQVCFAEPDalkgslvntlrevEPTSHMgvprvwekimeriqevaaqsgfirrkmllwAMSVTLe 388
Cdd:cd17653 157 fdACIGEIFSTLCNGGTLVLADPS-------------DPFAHV------------------------------ARTVDA- 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 389 qnLTCPGSDLKpfTTRLADYLVLAKVrqALGfakcqknfyGAAPMMAETQHFflGLNIRLYAGYGLSETSGPHFMSSPYN 468
Cdd:cd17653 193 --LMSTPSILS--TLSPQDFPNLKTI--FLG---------GEAVPPSLLDRW--SPGRRLYNAYGPTECTISSTMTELLP 255
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 469 YRLYSSGKLVPGCRVKLVNQD-----AEGIGEICLWGRTIFMGYLNMEDKTCEAI----DEEGWLH--TGDAGRLDADGF 537
Cdd:cd17653 256 GQPVTIGKPIPNSTCYILDADlqpvpEGVVGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGG 335
|
....*.
gi 767983694 538 LYITGR 543
Cdd:cd17653 336 LEFLGR 341
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
444-565 |
5.09e-13 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 71.56 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 444 LNIRLYAGYGLSETSGPHFMSSPYNYRL--YSSGKLVPGCRVKLVNQDaegIGEICLWGRTIFMGYLNmedktcEAIDEE 521
Cdd:PRK07445 253 LQLRLAPTYGMTETASQIATLKPDDFLAgnNSSGQVLPHAQITIPANQ---TGNITIQAQSLALGYYP------QILDSQ 323
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767983694 522 GWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAV 565
Cdd:PRK07445 324 GIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAI 366
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
111-583 |
1.79e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 70.16 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTT-SSPEACQYIAYDCCANVIMVD 189
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRyRSHEVAHILGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 190 TQKQLE--KILKIWKQ--LPHLKAVVIYKE-----PPPNKMANVYTmeefmeLGNEVPEEALDAIIDTQQPNQCCVLVYT 260
Cdd:PRK06164 116 GFKGIDfaAILAAVPPdaLPPLRAIAVVDDaadatPAPAPGARVQL------FALPDPAPPAAAGERAADPDAGALLFTT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 261 SGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDAlkGSLVN 340
Cdd:PRK06164 190 SGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAV----LLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDA--ARTAR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 341 TLREVEPTSHMGVprvwEKIMERIQEVAAQSG-FIRRKMLLWAmsvtleqnltcpgsdlkPFTTRLADYLVLAKVRQALg 419
Cdd:PRK06164 264 ALRRHRVTHTFGN----DEMLRRILDTAGERAdFPSARLFGFA-----------------SFAPALGELAALARARGVP- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 420 fakcQKNFYGAApmmaETQHFFLGlnirlyagyglsetsgpHFMSSPYNYRLYSSGKLV-PGCRVKLVNQDAEGI----- 493
Cdd:PRK06164 322 ----LTGLYGSS----EVQALVAL-----------------QPATDPVSVRIEGGGRPAsPEARVRARDPQDGALlpdge 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 494 -GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADG-FLYITgRLKElIITAGGENVPPVPIEEAVKmELPI 571
Cdd:PRK06164 377 sGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGqFVYQT-RMGD-SLRLGGFLVNPAEIEHALE-ALPG 453
|
490
....*....|..
gi 767983694 572 ISNAMLIGDQRK 583
Cdd:PRK06164 454 VAAAQVVGATRD 465
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
248-579 |
3.60e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 69.00 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 248 TQQPNQCCVLVYTSGTTGNPKGVMLSQdnitwtarygsqagdirpaevqqEVVVSYLPLSHIAAQIY----DL-WTGIQW 322
Cdd:cd05971 84 TDGSDDPALIIYTSGTTGPPKGALHAH-----------------------RVLLGHLPGVQFPFNLFprdgDLyWTPADW 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 323 gaqvcfaepdALKGSLVNTLRevePTSHMGVPRVWEKiMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGSDLKPFT 402
Cdd:cd05971 141 ----------AWIGGLLDVLL---PSLYFGVPVLAHR-MTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 403 TRL---------ADYLVLAKVRQALGFAKCQknFYGaapmMAETqHFFLGLNirlyagyglsetsgphfmSSPYNYRLYS 473
Cdd:cd05971 207 VKLraiatggesLGEELLGWAREQFGVEVNE--FYG----QTEC-NLVIGNC------------------SALFPIKPGS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 474 SGKLVPGCRVKLVNQDAE-----GIGEICLwgRT----IFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRL 544
Cdd:cd05971 262 MGKPIPGHRVAIVDDNGTplppgEVGEIAV--ELpdpvAFLGYWNNPSAT-EKKMAGDWLLTGDLGRKDSDGYFWYVGRD 338
|
330 340 350
....*....|....*....|....*....|....*
gi 767983694 545 KElIITAGGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:cd05971 339 DD-VITSSGYRIGPAEIEECL-LKHPAVLMAAVVG 371
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
445-579 |
4.02e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 69.04 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 445 NIRLYAGYGLSETSGPHFMSSPYNYRLYSS-GKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNmEDKTCEAI 518
Cdd:PRK07638 279 YAKLYEFYGASELSFVTALVDEESERRPNSvGRPFHNVQVRICNEAGEevqkgEIGTVYVKSPQFFMGYII-GGVLAREL 357
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767983694 519 DEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISNAMLIG 579
Cdd:PRK07638 358 NADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIES-VLHEHPAVDEIVVIG 416
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
67-543 |
9.50e-12 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 68.73 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 67 RVRLRIDPSCPQLPY----TVHRMFYEALDKYGDLIALGFKRQdkweHISYSQyylLARRA---AKGFLKLGLKQAHSVA 139
Cdd:COG1020 458 RQQLLAEWNATAAPYpadaTLHELFEAQAARTPDAVAVVFGDQ----SLTYAE---LNARAnrlAHHLRALGVGPGDLVG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 140 ILGFNSPEWFFSAVGTVFAGGIvtgiYT---TSSPEA-CQYIAYDCCANVIMvdTQKQLEKilkiwkQLPHLKAVVIYKE 215
Cdd:COG1020 531 VCLERSLEMVVALLAVLKAGAA----YVpldPAYPAErLAYMLEDAGARLVL--TQSALAA------RLPELGVPVLALD 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 216 PPpnkmanvytmeefmELGNEvPEEALDAIIDTQQPnqCCVLvYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDi 290
Cdd:COG1020 599 AL--------------ALAAE-PATNPPVPVTPDDL--AYVI-YTSGSTGRPKGVMVEHRALVnllawMQRRYGLGPGD- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 291 rpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVNTLREVEPTS-HMgVPRVWEKIMEriqev 367
Cdd:COG1020 660 --------RVLQFASLSFDAS-VWEIFGALLSGATLVLAPPEARRdpAALAELLARHRVTVlNL-TPSLLRALLD----- 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 368 AAQSGFIRRKMLLW---AMSVTLeqnltcpgsdlkpfttrladylvLAKVRQALGfakcqknfygaapmmaetqhfflgl 444
Cdd:COG1020 725 AAPEALPSLRLVLVggeALPPEL-----------------------VRRWRARLP------------------------- 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 445 NIRLYAGYGLSETS-----------GPHFMSSPY-----NYRLY---SSGKLVP-GCrvklvnqdaegIGEICLWGRTIF 504
Cdd:COG1020 757 GARLVNLYGPTETTvdstyyevtppDADGGSVPIgrpiaNTRVYvldAHLQPVPvGV-----------PGELYIGGAGLA 825
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 767983694 505 MGYLNMEDKTCEA-----IDEEG--WLHTGDAGRLDADGFLYITGR 543
Cdd:COG1020 826 RGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGR 871
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
473-565 |
1.06e-11 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 67.79 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 473 SSGKLVPGcRVKLVNQDAEG-----IGEICLWGRTIFMgYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKEL 547
Cdd:cd05929 298 SVGRAVLG-KVHILDEDGNEvppgeIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDM 375
|
90
....*....|....*...
gi 767983694 548 IITaGGENVPPVPIEEAV 565
Cdd:cd05929 376 IIS-GGVNIYPQEIENAL 392
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
67-311 |
2.46e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 66.82 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 67 RVRLRIDPSCPQLPYTVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSP 146
Cdd:PRK08279 23 RGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQ----SISYAELNARANRYAHWAAARGVGKGDVVALLMENRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 147 EWFFSAVGTVFAGGIVTGIYTTSSPEA---CQYIAYdccANVIMV--DTQKQLEKIlkiwkqLPHLKAVVIYKEPPPNKM 221
Cdd:PRK08279 99 EYLAAWLGLAKLGAVVALLNTQQRGAVlahSLNLVD---AKHLIVgeELVEAFEEA------RADLARPPRLWVAGGDTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 222 ANVYTMEEFMELGNEVPEEALDAiidTQ--QPNQCCVLVYTSGTTGNPKGVMLSQdnITWTARYGSQAGDIRPAEvqQEV 299
Cdd:PRK08279 170 DDPEGYEDLAAAAAGAPTTNPAS---RSgvTAKDTAFYIYTSGTTGLPKAAVMSH--MRWLKAMGGFGGLLRLTP--DDV 242
|
250
....*....|..
gi 767983694 300 VVSYLPLSHIAA 311
Cdd:PRK08279 243 LYCCLPLYHNTG 254
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
111-582 |
2.99e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 66.45 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFLKLGLK-QAHsVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTtssPEACQYIAYDCCANVI 186
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGpGDH-VGIYARNRIEYVEAMLGAFKARAVPVNVnyrYV---EDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 187 MVDTQkQLEKILKIWKQLPHLKAVVIYKEPPPNKmanvytmeefmELGNEVP-EEALDAIIDTQQPNQCC----VLVYTS 261
Cdd:PRK07798 105 VYERE-FAPRVAEVLPRLPKLRTLVVVEDGSGND-----------LLPGAVDyEDALAAGSPERDFGERSpddlYLLYTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 262 GTTGNPKGVMLSQDNItwtarYGSQAGDIRPA---EVQQEVVVSYL-------------PLSHIAAQiydlWTGiqWGAq 325
Cdd:PRK07798 173 GTTGMPKGVMWRQEDI-----FRVLLGGRDFAtgePIEDEEELAKRaaagpgmrrfpapPLMHGAGQ----WAA--FAA- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 326 vcfaepdALKGSLVNTLREVEPTSHmgvpRVWEKI-MERIQEVAaqsgfirrkMLLWAMSVTLEQNLTCPGsdlkpfTTR 404
Cdd:PRK07798 241 -------LFSGQTVVLLPDVRFDAD----EVWRTIeREKVNVIT---------IVGDAMARPLLDALEARG------PYD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 405 LADYLVLAKvrqalgfakcqknfyGAAPMMAETQHFFLGL--NIRLYAGYGLSET-SGPHFMSSPYNYRlySSGKLV-PG 480
Cdd:PRK07798 295 LSSLFAIAS---------------GGALFSPSVKEALLELlpNVVLTDSIGSSETgFGGSGTVAKGAVH--TGGPRFtIG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 481 CRVKLVNQD-------AEGIGEICLWGRtIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRlKELIIT 550
Cdd:PRK07798 358 PRTVVLDEDgnpvepgSGEIGWIARRGH-IPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGR-GSVCIN 435
|
490 500 510
....*....|....*....|....*....|....
gi 767983694 551 AGGENVPPVPIEEAVKMElPIISNAMLIG--DQR 582
Cdd:PRK07798 436 TGGEKVFPEEVEEALKAH-PDVADALVVGvpDER 468
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
249-552 |
4.64e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 66.27 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 249 QQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVcF 328
Cdd:PRK08043 362 QQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTP----NDRFMSALPLFHSFGLTVGLFTPLLTGAEV-F 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 329 AEPDALKGSLVNTLreveptshmgvprVWEkimeriqevaaqsgfiRRKMLLWAMSvtleqnltcpgsdlkpftTRLADY 408
Cdd:PRK08043 437 LYPSPLHYRIVPEL-------------VYD----------------RNCTVLFGTS------------------TFLGNY 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 409 lvlAKVRQALGFAKCQKNFYGAAPMMAET-QHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVN 487
Cdd:PRK08043 470 ---ARFANPYDFARLRYVVAGAEKLQESTkQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLS 546
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983694 488 qdAEGI---GEICLWGRTIFMGYLNMED---------KTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAG 552
Cdd:PRK08043 547 --VPGIeqgGRLQLKGPNIMNGYLRVEKpgvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
448-615 |
6.69e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 65.40 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 448 LYAGYGLSETsGPHFMSSPYNYRLY--SSGKLVPGCRVKLVNQDAEGIGEIcLWGRTIFMGYLNME---DKTCEAIdEEG 522
Cdd:PRK13383 320 LYNGYGSTEV-GIGALATPADLRDApeTVGKPVAGCPVRILDRNNRPVGPR-VTGRIFVGGELAGTrytDGGGKAV-VDG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 523 WLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKMELPIISNAML-IGDQR--KFLSMLLTLKCTLDPDT 599
Cdd:PRK13383 397 MTSTGDMGYLDNAGRLFIVGREDDMIIS-GGENVYPRAVENALAAHPAVADNAVIgVPDERfgHRLAAFVVLHPGSGVDA 475
|
170
....*....|....*.
gi 767983694 600 SDQTDNLTEQAMEFCQ 615
Cdd:PRK13383 476 AQLRDYLKDRVSRFEQ 491
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
79-579 |
8.40e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 65.03 E-value: 8.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 79 LPYTVHRMFYEALDKYGDLIALgfKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFA 158
Cdd:PRK05857 12 LPSTVLDRVFEQARQQPEAIAL--RRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 159 GGIVtgiyttsspeacqyiaydccanvIMVDTQKQLEKILKiWKQLPHLKAVVIYK------EPPPNKMANVYTMEEFME 232
Cdd:PRK05857 90 GAIA-----------------------VMADGNLPIAAIER-FCQITDPAAALVAPgskmasSAVPEALHSIPVIAVDIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 233 LGNEVPEEALDAIIDTQQPN----QCCVLVYTSGTTGNPKGVMLSqdNITWTArygsqAGDIRPAE-------VQQEVVV 301
Cdd:PRK05857 146 AVTRESEHSLDAASLAGNADqgseDPLAMIFTSGTTGEPKAVLLA--NRTFFA-----VPDILQKEglnwvtwVVGETTY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 302 SYLPLSHIAAqiydLW---TGIQWGAqVCFAepdalKGSLVNTLREVeptshmgvprvwekimeriqevaaqsgfirrkm 378
Cdd:PRK05857 219 SPLPATHIGG----LWwilTCLMHGG-LCVT-----GGENTTSLLEI--------------------------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 379 llwamSVTLEQNLTCpgsdLKP-FTTRLADYLVLAKVR-QALGFAKcqknfYGAAPMMAETQHFFLGLNIRLYAGYGLSE 456
Cdd:PRK05857 256 -----LTTNAVATTC----LVPtLLSKLVSELKSANATvPSLRLVG-----YGGSRAIAADVRFIEATGVRTAQVYGLSE 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 457 TSG-----PHFMSSPYNYRLYSSGKLVPGCRVKLVNQD-----AEGIGEIC----LWGRTI--FMGYLNMEDKTCEAIdE 520
Cdd:PRK05857 322 TGCtalclPTDDGSIVKIEAGAVGRPYPGVDVYLAATDgigptAPGAGPSAsfgtLWIKSPanMLGYWNNPERTAEVL-I 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767983694 521 EGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPP---------VP-IEEAVKMELPIISNAMLIG 579
Cdd:PRK05857 401 DGWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPdevdriaegVSgVREAACYEIPDEEFGALVG 468
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
109-579 |
1.03e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 188
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 DTQkqlekilkiwkqLPHLKAVViyKEPPPNKMANVYTMEEFMELgnevpEEALDAIID--TQQPnqC-CVLVYTSGTTG 265
Cdd:PRK13390 103 SAA------------LDGLAAKV--GADLPLRLSFGGEIDGFGSF-----EAALAGAGPrlTEQP--CgAVMLYSSGTTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 266 NPKGvmlsqdnitwtarygsqagdIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQW--GAQVCFAEPdalkgslvntLR 343
Cdd:PRK13390 162 FPKG--------------------IQPDLPGRDVDAPGDPIVAIARAFYDISESDIYysSAPIYHAAP----------LR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 344 EVEPTSHMGVPRVWEKIMEriqeVAAQSGFIRRkmllwaMSVTLEQnltcpgsdLKPftTRLADYLVL-AKVRQALGFAK 422
Cdd:PRK13390 212 WCSMVHALGGTVVLAKRFD----AQATLGHVER------YRITVTQ--------MVP--TMFVRLLKLdADVRTRYDVSS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 423 CQKNFYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSGPHFMSSP-YNYRLYSSGKLVPGcRVKLVNQD-----AEGIGE 495
Cdd:PRK13390 272 LRAVIHAAAPCPVDVKHAMIDwLGPIVYEYYSSTEAHGMTFIDSPdWLAHPGSVGRSVLG-DLHICDDDgnelpAGRIGT 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 496 ICLWGRTIFMGYLNMEDKTCEAIDEEG--WLHTGDAGRLDADGFLYITGRlKELIITAGGENVPPVPIEEAVKMElPIIS 573
Cdd:PRK13390 351 VYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADR-KSFMIISGGVNIYPQETENALTMH-PAVH 428
|
....*.
gi 767983694 574 NAMLIG 579
Cdd:PRK13390 429 DVAVIG 434
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
250-572 |
1.43e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 250 QPNQCCVLVYTSGTTGNPKGVMLSQDNIT---WTARYGSqAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 326
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVaneQLIRHGF-GIDLNP----DDVIVSWLPLYHDMGLIGGLLQPIFSGVPC 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 327 CFAEPDALkgsLVNTLREVEPTSHM-----GVPR-VWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNltcpgsDLKP 400
Cdd:PRK05691 239 VLMSPAYF---LERPLRWLEAISEYggtisGGPDfAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQD------SLER 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 401 FTTRLAdylvlakvrqALGFAkcQKNFYgAAPMMAETQHFFLG-----------LNIRLYAGYGLSETSGPHFMSSpyny 469
Cdd:PRK05691 310 FAEKFA----------ACGFD--PDSFF-ASYGLAEATLFVSGgrrgqgipaleLDAEALARNRAEPGTGSVLMSC---- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 470 rlyssGKLVPGCRVKLVN-QDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAI---DEEGWLHTGDAGRLdADGFLYI 540
Cdd:PRK05691 373 -----GRSQPGHAVLIVDpQSLEVlgdnrVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDLGFL-RDGELFV 446
|
330 340 350
....*....|....*....|....*....|..
gi 767983694 541 TGRLKELIITAgGENVPPVPIEEAVKMELPII 572
Cdd:PRK05691 447 TGRLKDMLIVR-GHNLYPQDIEKTVEREVEVV 477
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
85-543 |
8.32e-10 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 8.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 85 RMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 164
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQ----TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 165 IYTTSSPEACQYIAYDCCANVIMvdTQKQLEKilkiwkQLPHLKAVVIYKEpppnkmanvytmeefmELGNEVPEEALDA 244
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILL--TQSHLQP------PIAFIGLIDLLDE----------------DTIYHEESENLEP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 245 IIdtqQPNQCCVLVYTSGTTGNPKGVMLSQDN----ITWTARYGSQAGDIRpaevqqevVVSYLPLShIAAQIYDLWTGI 320
Cdd:cd17655 133 VS---KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlVEWANKVIYQGEHLR--------VALFASIS-FDASVTEIFASL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 321 QWGAQVCFAEPDALKG--SLVNTLREVEPTSHMGVPRVwekiMERIQEVAAQSGFIRRKMLLwamsvtleqnltcPGSDL 398
Cdd:cd17655 201 LSGNTLYIVRKETVLDgqALTQYIRQNRITIIDLTPAH----LKLLDAADDSEGLSLKHLIV-------------GGEAL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 399 KPfttrladylVLAKVRQALGFAKCQ-KNFYGAapmmAETQhffLGLNIRLYAGYGLSETSGPhfMSSPY-NYRLY---S 473
Cdd:cd17655 264 ST---------ELAKKIIELFGTNPTiTNAYGP----TETT---VDASIYQYEPETDQQVSVP--IGKPLgNTRIYildQ 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983694 474 SGKLVPgcrvklvnqdaEGI-GEICLWGRTIFMGYLNMEDKTCEA-IDE-----EGWLHTGDAGRLDADGFLYITGR 543
Cdd:cd17655 326 YGRPQP-----------VGVaGELYIGGEGVARGYLNRPELTAEKfVDDpfvpgERMYRTGDLARWLPDGNIEFLGR 391
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
257-582 |
8.70e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 61.24 E-value: 8.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 257 LVYTSGTTGNPKGVMLSQDNItwtarYGSQAG-------------DIRPAEVQQEVVVSYL--PLSHIAAQIydLWTGIQ 321
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDI-----FRMLMGgadfgtgeftpseDAHKAAAAAAGTVMFPapPLMHGTGSW--TAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 322 WGAQVCFAEPDALKGslVNTLREVEPTSHMGVPRVWEkimeriqevaaqsgfirrkmllwAMSVTLEQNLTCPGsdlkpf 401
Cdd:cd05924 81 LGGQTVVLPDDRFDP--EEVWRTIEKHKVTSMTIVGD-----------------------AMARPLIDALRDAG------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 402 TTRLADYLVLAKvrqalgfakcqknfyGAAPMMAETQHFFLGL--NIRLYAGYGLSETSgphFMSSPYN-YRLYSSGKLV 478
Cdd:cd05924 130 PYDLSSLFAISS---------------GGALLSPEVKQGLLELvpNITLVDAFGSSETG---FTGSGHSaGSGPETGPFT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 479 ---PGCRV-----KLVNQDAEGIGEICLWGRtIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRlKEL 547
Cdd:cd05924 192 ranPDTVVldddgRVVPPGSGGVGWIARRGH-IPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGR-GSV 269
|
330 340 350
....*....|....*....|....*....|....*..
gi 767983694 548 IITAGGENVPPVPIEEAVKMElPIISNAMLIG--DQR 582
Cdd:cd05924 270 CINTGGEKVFPEEVEEALKSH-PAVYDVLVVGrpDER 305
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
446-575 |
1.12e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 61.04 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 446 IRLYAGYGLSEtsgphfMSSPYNYRLYSS----GKLVPGCRVKLVNqdaegiGEICLWGRTIFMGYLnMEDKTCEAIDEE 521
Cdd:PRK09029 265 IRCWCGYGLTE------MASTVCAKRADGlagvGSPLPGREVKLVD------GEIWLRGASLALGYW-RQGQLVPLVNDE 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767983694 522 GWLHTGDAGRLDaDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISNA 575
Cdd:PRK09029 332 GWFATRDRGEWQ-NGELTILGRLDNLFFS-GGEGIQPEEI-ERVINQHPLVQQV 382
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
483-579 |
1.81e-09 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 60.54 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 483 VKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVP 557
Cdd:COG1021 365 VRIVDEDgnpvPPGeVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINR-GGEKIA 443
|
90 100
....*....|....*....|..
gi 767983694 558 PVPIEEAVkMELPIISNAMLIG 579
Cdd:COG1021 444 AEEVENLL-LAHPAVHDAAVVA 464
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
251-584 |
4.46e-09 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 59.39 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 251 PNQCCVLVYTSGTTGNPKGvmlsqdnitwtARYgSQAGDIRPAEVqqevVVSYLPLSH-----IAAQIYDLWtGIqwgAQ 325
Cdd:PRK13382 195 GRKGRVILLTSGTTGTPKG-----------ARR-SGPGGIGTLKA----ILDRTPWRAeeptvIVAPMFHAW-GF---SQ 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 326 VCFAEpdALKGSLVN--------TLREVE---PTSHMGVPRVWEKIMERIQEVAAQsgFIRRKMLLWAMSvtleqnltcp 394
Cdd:PRK13382 255 LVLAA--SLACTIVTrrrfdpeaTLDLIDrhrATGLAVVPVMFDRIMDLPAEVRNR--YSGRSLRFAAAS---------- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 395 GSDLKP-----FTTRLADYLVlakvrqalgfakcqkNFYGA--APMMAetqhfflglnirlyagyglseTSGPHFMSSPY 467
Cdd:PRK13382 321 GSRMRPdvviaFMDQFGDVIY---------------NNYNAteAGMIA---------------------TATPADLRAAP 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 468 NyrlySSGKLVPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEaideEGWLHTGDAGRLDADGFLYITG 542
Cdd:PRK13382 365 D----TAGRPAEGTEIRILDQDfrevPTGeVGTIFVRNDTQFDGYTSGSTKDFH----DGFMASGDVGYLDENGRLFVVG 436
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 767983694 543 RLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG-DQRKF 584
Cdd:PRK13382 437 RDDEMIVS-GGENVYPIEVEKTL-ATHPDVAEAAVIGvDDEQY 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
64-295 |
8.54e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.40 E-value: 8.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 64 ADGRVRLRIDPSCPQ---LPYTVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAI 140
Cdd:PRK12467 492 AEERARELVRWNAPAteyAPDCVHQLIEAQARQHPERPALVFGEQ----VLSYAELNRQANRLAHVLIAAGVGPDVLVGI 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 141 LGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDccANVIMVDTQKQLEKILKIWKQLPHLkaVVIYKEPPPNK 220
Cdd:PRK12467 568 AVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDD--SGVRLLLTQSHLLAQLPVPAGLRSL--CLDEPADLLCG 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767983694 221 MANVYtmeefmelgnevPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNIT----WTARYGSQAGDIRPAEV 295
Cdd:PRK12467 644 YSGHN------------PEVALD-------PDNLAYVIYTSGSTGQPKGVAISHGALAnyvcVIAERLQLAADDSMLMV 703
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
446-565 |
9.68e-09 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 58.28 E-value: 9.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 446 IRLYAGYGLSET-----SGPHFMSSPYnyrlySSGKLVPGCRVKLVNQDAEGI-----GEICLwgRT-------IFMGYL 508
Cdd:cd05970 327 IKLMEGFGQTETtltiaTFPWMEPKPG-----SMGKPAPGYEIDLIDREGRSCeageeGEIVI--RTskgkpvgLFGGYY 399
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767983694 509 NMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAV 565
Cdd:cd05970 400 KDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS-GYRIGPFEVESAL 454
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
122-616 |
1.15e-08 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 58.21 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 122 RAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQkqlekILKIW 201
Cdd:cd05915 36 RLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN-----LLPLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 202 KQLPHLKAVVIYKeppPNKMANVYTMEEFMELGNevPEEALDAIIDTQQPnqcCVLVYTSGTTGNPKGVMLSQDNITWTA 281
Cdd:cd05915 111 EAIRGELKTVQHF---VVMDEKAPEGYLAYEEAL--GEEADPVRVPERAA---CGMAYTTGTTGLPKGVVYSHRALVLHS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 282 RYGSQAGDIRPAEVqqEVVVSYLPLSHIAAQIYdLWTGIQWGAQ-VCFAEPDAlKGSLVNTLREVEPTSHMGVPRVWEKI 360
Cdd:cd05915 183 LAASLVDGTALSEK--DVVLPVVPMFHVNAWCL-PYAATLVGAKqVLPGPRLD-PASLVELFDGEGVTFTAGVPTVWLAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 361 MERIQEVaaqsgfirRKMLLWAMSVTleqnltcPGSDLKPFTTRLADYLVLAKVRQALGFAKCqknfYG---AAPMMAET 437
Cdd:cd05915 259 ADYLEST--------GHRLKTLRRLV-------VGGSAAPRSLIARFERMGVEVRQGYGLTET----SPvvvQNFVKSHL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 438 QHFFLGLNIRLYAGYGLS------ETSGPHFMSSPYnyrlyssgklvpgcrvklvnqDAEGIGEICLWGRTIFMGYLNME 511
Cdd:cd05915 320 ESLSEEEKLTLKAKTGLPiplvrlRVADEEGRPVPK---------------------DGKALGEVQLKGPWITGGYYGNE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 512 DKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIeEAVKMELPIISNAMLIG--DQRKFLSMLL 589
Cdd:cd05915 379 EATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKD-LIKSGGEWISSVDL-ENALMGHPKVKEAAVVAipHPKWQERPLA 456
|
490 500
....*....|....*....|....*..
gi 767983694 590 TLKCTldpdtsdQTDNLTEQAMEFCQR 616
Cdd:cd05915 457 VVVPR-------GEKPTPEELNEHLLK 476
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
109-598 |
1.45e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 57.77 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSqyyllARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQY-IAY-DCcaNVI 186
Cdd:PRK07867 33 EHIRGS-----AARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARdIAHaDC--QLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 187 MVDTqkqlekilkiwKQLPHLKAVviykePPPNKMANVYTMEEFMELGNEvPEEALDAIIDtqQPNQCCVLVYTSGTTGN 266
Cdd:PRK07867 106 LTES-----------AHAELLDGL-----DPGVRVINVDSPAWADELAAH-RDAEPPFRVA--DPDDLFMLIFTSGTSGD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 267 PKGVMLSQDNITWTARYGSQAGDIRPAEVqqeVVVSyLPLSHIAAQIYDLWTGIQWGAQvcfaepdalkgslvntlreve 346
Cdd:PRK07867 167 PKAVRCTHRKVASAGVMLAQRFGLGPDDV---CYVS-MPLFHSNAVMAGWAVALAAGAS--------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 347 ptshMGVPRVWekimeriqevaAQSGFIrrkmllwamsvtleqnltcpgSDLKPFTTRLADYL------VLAK------- 413
Cdd:PRK07867 222 ----IALRRKF-----------SASGFL---------------------PDVRRYGATYANYVgkplsyVLATperpdda 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 414 ---VRQALGfakcqkNfYGAAPMMAETQHFFlglNIRLYAGYGLSETsGPHFMSSPyNYRLYSSGKLVPGcrVKLVNQD- 489
Cdd:PRK07867 266 dnpLRIVYG------N-EGAPGDIARFARRF---GCVVVDGFGSTEG-GVAITRTP-DTPPGALGPLPPG--VAIVDPDt 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 490 -----------------AEGIGEIC-LWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITA 551
Cdd:PRK07867 332 gtecppaedadgrllnaDEAIGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDW-MRV 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 767983694 552 GGENVPPVPIEEAVkMELPIISNAML-------IGDQrKFLSMLLTLKCTLDPD 598
Cdd:PRK07867 410 DGENLGTAPIERIL-LRYPDATEVAVyavpdpvVGDQ-VMAALVLAPGAKFDPD 461
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
52-579 |
1.50e-08 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 57.97 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 52 WDAPEEAL-WTTRADGRVRLRIDPSCPQ---LPYTVHRMFYEALDKY----GDLIALGFKRQD--KWEHISYSQYYLLAR 121
Cdd:cd17634 16 WGEAGKILdWITPYQKVKNTSFAPGAPSikwFEDATLNLAANALDRHlrenGDRTAIIYEGDDtsQSRTISYRELHREVC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 122 RAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM-----------VDT 190
Cdd:cd17634 96 RFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLItadggvragrsVPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 191 QKQLEKILKIwkQLPHLKAVVIYKepppnKMANVYTMEE-----FMELGNEVPEEALDAIIDTQQPnqcCVLVYTSGTTG 265
Cdd:cd17634 176 KKNVDDALNP--NVTSVEHVIVLK-----RTGSDIDWQEgrdlwWRDLIAKASPEHQPEAMNAEDP---LFILYTSGTTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 266 NPKGVMlsQDN------ITWTARYgsqAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAE--PDALKGS 337
Cdd:cd17634 246 KPKGVL--HTTggylvyAATTMKY---VFDYGPGDI----YWCTADVGWVTGHSYLLYGPLACGATTLLYEgvPNWPTPA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 338 LVNTLREVEPTSHMGV-PRVWEKIMeriqevAAQSGFIRRKmllwamSVTLEQNLTCPGSDLKPFTTRLAdylvlakvRQ 416
Cdd:cd17634 317 RMWQVVDKHGVNILYTaPTAIRALM------AAGDDAIEGT------DRSSLRILGSVGEPINPEAYEWY--------WK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 417 ALGFAKCqknfygaaPMMAEtqhfflglnirlyagYGLSETSGphFMSSP----YNYRLYSSGKLVPGCRVKLVnqDAEG 492
Cdd:cd17634 377 KIGKEKC--------PVVDT---------------WWQTETGG--FMITPlpgaIELKAGSATRPVFGVQPAVV--DNEG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 493 -------IGEICL---W-GRTifMGYLNMEDKTCEAIDE--EGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPV 559
Cdd:cd17634 430 hpqpggtEGNLVItdpWpGQT--RTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDD-VINVAGHRLGTA 506
|
570 580
....*....|....*....|
gi 767983694 560 PIEEAVKMElPIISNAMLIG 579
Cdd:cd17634 507 EIESVLVAH-PKVAEAAVVG 525
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
230-543 |
3.19e-08 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 56.78 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 230 FMELGNEVPEEALDAIID--------TQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAevqqevvV 301
Cdd:cd05918 76 FVPLDPSHPLQRLQEILQdtgakvvlTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSE-------S 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 302 SYLPLSHIA--AQIYDLWTGIQWGAQVCFAEPDALKGSLVNTLREVEPTSHMGVPRVwekimeriqevaaqsgfirrkml 379
Cdd:cd05918 149 RVLQFASYTfdVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPSV----------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 380 lwAMSVTLEQnltCPgsDLKpfttrladYLVLA--KVRQALGFAKCQK----NFYGAA--PMMAETQHFFLGLNIRLyAG 451
Cdd:cd05918 206 --ARLLDPED---VP--SLR--------TLVLGgeALTQSDVDTWADRvrliNAYGPAecTIAATVSPVVPSTDPRN-IG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 452 YGLSETSgphFMSSPYNYrlyssGKLVP-GCrvklvnqdaegIGEICLWGRTIFMGYLNMEDKTCEA-IDEEGWLH---- 525
Cdd:cd05918 270 RPLGATC---WVVDPDNH-----DRLVPiGA-----------VGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegs 330
|
330 340
....*....|....*....|....*.
gi 767983694 526 --------TGDAGRLDADGFLYITGR 543
Cdd:cd05918 331 grgrrlyrTGDLVRYNPDGSLEYVGR 356
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
470-565 |
4.31e-08 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 56.55 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 470 RLYSSGKLVPGCRVKLVNQDAE-----GIGEIC------------LWG---RTIfMGYLNMEDktceaideeGWLHTGDA 529
Cdd:cd05967 409 KAGSPGKPVPGYQVQVLDEDGEpvgpnELGNIViklplppgclltLWKndeRFK-KLYLSKFP---------GYYDTGDA 478
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767983694 530 GRLDADGFLYITGRLKELIITAG-----GEnvppvpIEEAV 565
Cdd:cd05967 479 GYKDEDGYLFIMGRTDDVINVAGhrlstGE------MEESV 513
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
250-578 |
4.51e-08 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 55.94 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 250 QPNQCCVLVYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDIRpaevqqevvvsylpLSHIAAQIYDLWTG----- 319
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAhaahaWRREYELDSFPVR--------------LLQMASFSFDVFAGdfars 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 320 IQWGAQ--VCfaePDALK---GSLVNTLREVEPTSHMGVPRVWEKIMERIQevaaqsgfiRRKMLLWAMSVTLEQNLTCP 394
Cdd:cd17650 157 LLNGGTlvIC---PDEVKldpAALYDLILKSRITLMESTPALIRPVMAYVY---------RNGLDLSAMRLLIVGSDGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 395 GSDLKPFTTRLADYLVLAkvrqalgfakcqkNFYGAAPMMAETQHFFLGLnirlyagyGLSETSGPHFMSSPY-NYRLY- 472
Cdd:cd17650 225 AQDFKTLAARFGQGMRII-------------NSYGVTEATIDSTYYEEGR--------DPLGDSANVPIGRPLpNTAMYv 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 473 --SSGKLVPgcrvklvnqdAEGIGEICLWGRTIFMGYLNMEDKTCEAIDE------EGWLHTGDAGRLDADGFLYITGRL 544
Cdd:cd17650 284 ldERLQPQP----------VGVAGELYIGGAGVARGYLNRPELTAERFVEnpfapgERMYRTGDLARWRADGNVELLGRV 353
|
330 340 350
....*....|....*....|....*....|....*...
gi 767983694 545 KELIITAGgenvppVPIE----EAVKMELPIISNAMLI 578
Cdd:cd17650 354 DHQVKIRG------FRIElgeiESQLARHPAIDEAVVA 385
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
471-579 |
5.13e-08 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 55.80 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 471 LYSSGK-LVPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRL 544
Cdd:cd05920 307 IHTQGRpMSPDDEIRVVDEEgnpvPPGeEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRI 386
|
90 100 110
....*....|....*....|....*....|....*
gi 767983694 545 KELiITAGGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:cd05920 387 KDQ-INRGGEKIAAEEVENLL-LRHPAVHDAAVVA 419
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
109-578 |
5.16e-08 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 55.94 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMv 188
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 dTQKQLEKILKIWKQLPHLKAVVIYKEPPPNkmanvytmeefmeLGNEVPEEALDAIIdtqqpnqccvlvYTSGTTGNPK 268
Cdd:cd17656 91 -TQRHLKSKLSFNKSTILLEDPSISQEDTSN-------------IDYINNSDDLLYII------------YTSGTTGKPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 269 GVMLSQDNITWTARYG-SQAGDIRPAEVQQEVVVSYlplshiaaqiydlwtgiqwgaQVCFAEPDA--LKGSlvnTLREV 345
Cdd:cd17656 145 GVQLEHKNMVNLLHFErEKTNINFSDKVLQFATCSF---------------------DVCYQEIFStlLSGG---TLYII 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 346 EPTSHMGVPRVWEKI-MERIQEVAAQSGFIRrkmllwamsvtleqnltcpgsdlkpfttrladylVLAKVRQALG-FAKC 423
Cdd:cd17656 201 REETKRDVEQLFDLVkRHNIEVVFLPVAFLK----------------------------------FIFSEREFINrFPTC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 424 QKNFYGAAPMMAETQHF---FLGLNIRLYAGYGLSET---SGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAE-----G 492
Cdd:cd17656 247 VKHIITAGEQLVITNEFkemLHEHNVHLHNHYGPSEThvvTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQlqpqgI 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 493 IGEICLWGRTIFMGYLNMEDKTCEAI------DEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVK 566
Cdd:cd17656 327 VGELYISGASVARGYLNRQELTAEKFfpdpfdPNERMYRTGDLARYLPDGNIEFLGRADHQ-VKIRGYRIELGEI-EAQL 404
|
490
....*....|..
gi 767983694 567 MELPIISNAMLI 578
Cdd:cd17656 405 LNHPGVSEAVVL 416
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
244-578 |
6.15e-08 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 55.45 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 244 AIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAA--QIYDLWTGiq 321
Cdd:cd17649 86 GLLLTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTP----GDRELQFASFNFDGAheQLLPPLIC-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 322 wGAQVCFAePDALKGSLVNTLREVEptsHMGV------PRVWEKIMERIQEVAAqsgfiRRKMLLWAMSVTLEQnltcpg 395
Cdd:cd17649 160 -GACVVLR-PDELWASADELAEMVR---ELGVtvldlpPAYLQQLAEEADRTGD-----GRPPSLRLYIFGGEA------ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 396 sdlkpfttrladyLVLAKVRQALGFAKcqknfygaapmmaetqhfflglniRLYAGYGLSET--SGPHFMSSPYNYRLYS 473
Cdd:cd17649 224 -------------LSPELLRRWLKAPV------------------------RLFNAYGPTEAtvTPLVWKCEAGAARAGA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 474 S---GKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEAI-----DEEG--WLHTGDAGRLDADGFL 538
Cdd:cd17649 267 SmpiGRPLGGRSAYILDADLNpvpvgVTGELYIGGEGLARGYLGRPELTAERFvpdpfGAPGsrLYRTGDLARWRDDGVI 346
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767983694 539 YITGRLKELiITAGGENVPPVPIEEAVkMELPIISNAMLI 578
Cdd:cd17649 347 EYLGRVDHQ-VKIRGFRIELGEIEAAL-LEHPGVREAAVV 384
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
85-543 |
6.39e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 55.67 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 85 RMFYEALDKYGDLIALgfkrQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 164
Cdd:cd12117 1 ELFEEQAARTPDAVAV----VYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 165 IYTTSSPEACQYIAYDccANVIMVDTQKQLEKilkiwkQLPHLKAVVIYKEPPPnkmanvytmeefmelgnEVPEEALDA 244
Cdd:cd12117 77 LDPELPAERLAFMLAD--AGAKVLLTDRSLAG------RAGGLEVAVVIDEALD-----------------AGPAGNPAV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 245 IIDtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARyGSQAGDIRPaevqQEVVVSYLPLSHIAAqIYDLWTGIQWGA 324
Cdd:cd12117 132 PVS---PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK-NTNYVTLGP----DDRVLQTSPLAFDAS-TFEIWGALLNGA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 325 QVCFAEPDALKGslvntlreveptshmgvprvwekiMERIQEVAAQSGFirrkMLLWaMSVTLEQNLTcpgsDLKPFTTR 404
Cdd:cd12117 203 RLVLAPKGTLLD------------------------PDALGALIAEEGV----TVLW-LTAALFNQLA----DEDPECFA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 405 LADYLV-------LAKVRQALgfAKCQKnfygaapmmaetqhfflglnIRLYAGYGLSET---SGPHFMSSPYNYRlySS 474
Cdd:cd12117 250 GLRELLtggevvsPPHVRRVL--AACPG--------------------LRLVNGYGPTENttfTTSHVVTELDEVA--GS 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 475 ---GKLVPGCRVKLVNQD----AEGI-GEICLWGRTIFMGYLNMEDKTCEAIDEEGWL------HTGDAGRLDADGFLYI 540
Cdd:cd12117 306 ipiGRPIANTRVYVLDEDgrpvPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEF 385
|
...
gi 767983694 541 TGR 543
Cdd:cd12117 386 LGR 388
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
475-564 |
6.61e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 55.54 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 475 GKLVPGCRVKLVNQDA------EGIGEICLWGRTIFMGYLNMEdktceAIDEEGWLHTGDAGRLDADGfLYITGRLKELI 548
Cdd:PRK05851 348 GNPIPGMEVRISPGDGaagvagREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGG-LVVCGRAKELI 421
|
90
....*....|....*.
gi 767983694 549 ITAgGENVPPVPIEEA 564
Cdd:PRK05851 422 TVA-GRNIFPTEIERV 436
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
96-581 |
6.74e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 55.80 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 96 DLIALGFKRQD-KW-EHISYSQyyllARRAAKGFLKLGLKQAHSVAILGfNSPEWFFSAVGTVFAGGIVTGIYTTSSPEA 173
Cdd:PRK13388 16 DTIAVRYGDRTwTWrEVLAEAA----ARAAALIALADPDRPLHVGVLLG-NTPEMLFWLAAAALGGYVLVGLNTTRRGAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 174 -CQYIAY-DCcaNVIMVDTQ--KQLEKIlkiwkQLPHLKAVVIYKEPPPNKMAnvytmeefmELGNEVPEEALDAiiDTQ 249
Cdd:PRK13388 91 lAADIRRaDC--QLLVTDAEhrPLLDGL-----DLPGVRVLDVDTPAYAELVA---------AAGALTPHREVDA--MDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 250 qpnqcCVLVYTSGTTGNPKGVMLSQDNITW-----TARYGSQAGDirpaevqqevvVSYL--PLSHIAAqIYDLWT-GIQ 321
Cdd:PRK13388 153 -----FMLIFTSGTTGAPKAVRCSHGRLAFagralTERFGLTRDD-----------VCYVsmPLFHSNA-VMAGWApAVA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 322 WGAQVCfaepdalkgslvntlreveptshmgVPRVWekimeriqevaAQSGF---IRR----------KMLLWAMSvTLE 388
Cdd:PRK13388 216 SGAAVA-------------------------LPAKF-----------SASGFlddVRRygatyfnyvgKPLAYILA-TPE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 389 QnltcPGSDLKPfttrladylvlakVRQALGFAkcqknfygAAPM-MAETQHFFlglNIRLYAGYGLSETSG-------- 459
Cdd:PRK13388 259 R----PDDADNP-------------LRVAFGNE--------ASPRdIAEFSRRF---GCQVEDGYGSSEGAVivvrepgt 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 460 -PHFMSSPY-NYRLYSSGKLVPgCRV-------KLVNQDaEGIGEIC-LWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDA 529
Cdd:PRK13388 311 pPGSIGRGApGVAIYNPETLTE-CAVarfdahgALLNAD-EAIGELVnTAGAGFFEGYYNNPEATAERM-RHGMYWSGDL 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 767983694 530 GRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISNAML-------IGDQ 581
Cdd:PRK13388 388 AYRDADGWIYFAGRTADW-MRVDGENLSAAPI-ERILLRHPAINRVAVyavpderVGDQ 444
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
232-544 |
7.75e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 55.38 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 232 ELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEvqQEVVVS--------- 302
Cdd:cd12116 106 LLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGD--RLLAVTtyafdisll 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 303 --YLPLSHiaaqiydlwtgiqwGAQVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWekimeRIqevAAQSGFIRRKm 378
Cdd:cd12116 184 elLLPLLA--------------GARVVIAPRETQRdpEALARLIEAHSITVMQATPATW-----RM---LLDAGWQGRA- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 379 llwamSVTleqnLTCPGSDLKPfttRLADYLvLAKVRQALgfakcqkNFYG---------AAPMMAETQHFFLGLNIrly 449
Cdd:cd12116 241 -----GLT----ALCGGEALPP---DLAARL-LSRVGSLW-------NLYGptettiwstAARVTAAAGPIPIGRPL--- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 450 agyglsetsgphfmsspYNYRLY---SSGKLVPgcrvklvnqdaEG-IGEICLWGRTIFMGYLNMEDKTCEAI-----DE 520
Cdd:cd12116 298 -----------------ANTQVYvldAALRPVP-----------PGvPGELYIGGDGVAQGYLGRPALTAERFvpdpfAG 349
|
330 340
....*....|....*....|....*.
gi 767983694 521 EG--WLHTGDAGRLDADGFLYITGRL 544
Cdd:cd12116 350 PGsrLYRTGDLVRRRADGRLEYLGRA 375
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
259-579 |
9.72e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 55.42 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 259 YTSGTTGNPKGVMLSQ-DNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGiqwGAQVCFAEPDALKGS 337
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHaDPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATG---GSAVINSAPVTPEAA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 338 LVNTLReVEPTSHMGVPRVWEKIMEriqevaaqsgfirrkmllwAMSVTLEQNLTCPGSDLKPFTTRLADYLVlakvrqa 417
Cdd:PRK06060 229 AILSAR-FGPSVLYGVPNFFARVID-------------------SCSPDSFRSLRCVVSAGEALELGLAERLM------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 418 lgfakcqkNFYGAAPMMAetqhfflglnirlyaGYGLSETsGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQDAEGIG-- 494
Cdd:PRK06060 282 --------EFFGGIPILD---------------GIGSTEV-GQTFVSNRVDeWRLGTLGRVLPPYEIRVVAPDGTTAGpg 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 495 -EICLW--GRTIFMGYLNMEDKTCEaidEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPI 571
Cdd:PRK06060 338 vEGDLWvrGPAIAKGYWNRPDSPVA---NEGWLDTRDRVCIDSDGWVTYRCRADDTEVI-GGVNVDPREVERLI-IEDEA 412
|
....*...
gi 767983694 572 ISNAMLIG 579
Cdd:PRK06060 413 VAEAAVVA 420
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
257-543 |
1.08e-07 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 55.04 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 257 LVYTSGTTGNPKGVMLSQDNIT----WTARYGSQAGDIRpaevqqevVVSYLPLSHIAAQiYDLWTGIQWGAQVCFAEPD 332
Cdd:cd17651 141 VIYTSGSTGRPKGVVMPHRSLAnlvaWQARASSLGPGAR--------TLQFAGLGFDVSV-QEIFSTLCAGATLVLPPEE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 333 ALkgslvntlreveptshMGVPRVWEKIME-RIQEVAAQSGFIRRkmllWAmsvtleqnltcpgSDLKPFTTRLADylvL 411
Cdd:cd17651 212 VR----------------TDPPALAAWLDEqRISRVFLPTVALRA----LA-------------EHGRPLGVRLAA---L 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 412 AKVRQAlgfakcqknfyG-AAPMMAETQHFFLGL-NIRLYAGYGLSETsgpHFMSS------PYNYRLYSS-GKLVPGCR 482
Cdd:cd17651 256 RYLLTG-----------GeQLVLTEDLREFCAGLpGLRLHNHYGPTET---HVVTAlslpgdPAAWPAPPPiGRPIDNTR 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767983694 483 VKLVNQDAE----GI-GEICLWGRTIFMGYLNMEDKTCEAIDEEGWL------HTGDAGRLDADGFLYITGR 543
Cdd:cd17651 322 VYVLDAALRpvppGVpGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGR 393
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
256-579 |
1.56e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 54.45 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 256 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevvvsylplshiaaqiydLWtgiqwgaqvCFAEPD--- 332
Cdd:cd05973 92 VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS--------------------FW---------NAADPGway 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 333 ----ALKGSLVNTLREVEPTSHMGVPRVWeKIMER--IQEVAAQSGFIRrkmLLWAMSVTLEQNLTcpgsdlkpfttrla 406
Cdd:cd05973 143 glyyAITGPLALGHPTILLEGGFSVESTW-RVIERlgVTNLAGSPTAYR---LLMAAGAEVPARPK-------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 407 dyLVLAKVRQAlgfakcqknfygAAPMMAETQHFF---LGLNIRLYagYGLSETSGP----HFMSSPYnyRLYSSGKLVP 479
Cdd:cd05973 205 --GRLRRVSSA------------GEPLTPEVIRWFdaaLGVPIHDH--YGQTELGMVlanhHALEHPV--HAGSAGRAMP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 480 GCRVKLVNQDAEGIGE-------------ICLWgrtiFMGYLNMEDKTCEAideeGWLHTGDAGRLDADGFLYITGRLKE 546
Cdd:cd05973 267 GWRVAVLDDDGDELGPgepgrlaidiansPLMW----FRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADD 338
|
330 340 350
....*....|....*....|....*....|...
gi 767983694 547 LIITAgGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:cd05973 339 VITMS-GYRIGPFDVESAL-IEHPAVAEAAVIG 369
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
443-578 |
4.02e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 52.96 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 443 GLNIRlyAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI--GEICL-WGRT----IFMGYLNMEDKTC 515
Cdd:cd05974 225 GLTIR--DGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPAteGEVALdLGDTrpvgLMKGYAGDPDKTA 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767983694 516 EAIdEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEEAVkMELPIISNAMLI 578
Cdd:cd05974 303 HAM-RGGYYRTGDIAMRDEDGYLTYVGRADD-VFKSSDYRISPFELESVL-IEHPAVAEAAVV 362
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
109-544 |
9.93e-07 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 51.89 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 188
Cdd:cd12114 11 GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 DTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKmanvytmeefmelgnevpeealdaiidtQQPNQCCVLVYTSGTTGNPK 268
Cdd:cd12114 91 DGPDAQLDVAVFDVLILDLDALAAPAPPPPVD----------------------------VAPDDLAYVIFTSGSTGTPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 269 GVMLSQDN-----ITWTARYGSQAGDirpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDalkgslvntlR 343
Cdd:cd12114 143 GVMISHRAalntiLDINRRFAVGPDD---------RVLALSSLSFDLS-VYDIFGALSAGATLVLPDEA----------R 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 344 EVEPTShmgvprvWEKIMERIQ-----EVAAQSgfirrKMLLWAmsvtLEQNLTCPGSdlkpftTRLA----DYLVL--- 411
Cdd:cd12114 203 RRDPAH-------WAELIERHGvtlwnSVPALL-----EMLLDV----LEAAQALLPS------LRLVllsgDWIPLdlp 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 412 AKVRQALgfakcqknfygaapmmAETQHFFLGlnirlyagyGLSETS-----------GPHFMSSPYnyrlyssGKLVPG 480
Cdd:cd12114 261 ARLRALA----------------PDARLISLG---------GATEASiwsiyhpidevPPDWRSIPY-------GRPLAN 308
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767983694 481 CRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEA----IDEEGWLHTGDAGRLDADGFLYITGRL 544
Cdd:cd12114 309 QRYRVLDPRGRdcpdwVPGELWIGGRGVALGYLGDPELTAARfvthPDGERLYRTGDLGRYRPDGTLEFLGRR 381
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
50-289 |
1.02e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.65 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 50 AQWDAPEEALwttradgrvrlridPSCPQlpytVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLK 129
Cdd:PRK12316 1990 ADWDRTPEAY--------------PRGPG----VHQRIAEQAARAPEAIAVVFGDQ----HLSYAELDSRANRLAHRLRA 2047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 130 LGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMvdTQKQLEKILkiwkqlphlka 209
Cdd:PRK12316 2048 RGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL--TQRHLLERL----------- 2114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 210 vviykePPPNKMAN--VYTMEEFMELGNEVPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQ----DNITWT-AR 282
Cdd:PRK12316 2115 ------PLPAGVARlpLDRDAEWADYPDTAPAVQLA-------GENLAYVIYTSGSTGLPKGVAVSHgalvAHCQAAgER 2181
|
....*..
gi 767983694 283 YGSQAGD 289
Cdd:PRK12316 2182 YELSPAD 2188
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
493-557 |
1.41e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 51.65 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 493 IGEICLWGRTIFMGYLNMEDKTCEA--------IDE---EG------WLHTGDAGRLdADGFLYITGRLKELIITAGGEN 555
Cdd:PRK07769 418 IGEIWLHGNNIGTGYWGKPEETAATfqnilksrLSEshaEGapddalWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNH 496
|
..
gi 767983694 556 VP 557
Cdd:PRK07769 497 YP 498
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
232-553 |
1.53e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 51.31 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 232 ELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQqevvVSYLPLSHIAA 311
Cdd:cd05910 65 NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVD----LATFPLFALFG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 312 QIYDLWTGIQWGAQVCFAEPDALKgsLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRkmllwamsvtleqnL 391
Cdd:cd05910 141 PALGLTSVIPDMDPTRPARADPQK--LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRR--------------V 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 392 TCPGSDLKPFttrladylVLAKVRQALGFAKCQKNFYGAapmmaeTQhfflGLNIRLYAGYGLSETSGPhfmsSPYNYRL 471
Cdd:cd05910 205 LSAGAPVPIA--------LAARLRKMLSDEAEILTPYGA------TE----ALPVSSIGSRELLATTTA----ATSGGAG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 472 YSSGKLVPGCRVKLVNQDAE--------------GIGEICLWGRTIFMGYLNMEDKTCEA-IDEEG---WLHTGDAGRLD 533
Cdd:cd05910 263 TCVGRPIPGVRVRIIEIDDEpiaewddtlelprgEIGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDLGYLD 342
|
330 340
....*....|....*....|
gi 767983694 534 ADGFLYITGRLKELIITAGG 553
Cdd:cd05910 343 DEGRLWFCGRKAHRVITTGG 362
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
83-544 |
1.80e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.88 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 83 VHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIV 162
Cdd:PRK12316 3059 VHRLFEEQVERTPDAVALAFGEQ----RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAY 3134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 163 TGIYTTSSPEACQYIAYDCCANVIMvdTQKQLekilkiwkQLPHLKAV-VIYKEPPPNkmanvytmeefmELGNEVPEEA 241
Cdd:PRK12316 3135 VPLDPEYPEERLAYMLEDSGAQLLL--SQSHL--------RLPLAQGVqVLDLDRGDE------------NYAEANPAIR 3192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 242 LDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIAAqIYDLWTGIQ 321
Cdd:PRK12316 3193 TM-------PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGL----GVGDRVLQFTTFSFDVF-VEELFWPLM 3260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 322 WGAQVCFAEPDalKGSLVNTLREVEPTSHMGVPR-VWEKIMERIQEVAAQSGFIRRKMLlwamsvtleqnltCPGSDLKP 400
Cdd:PRK12316 3261 SGARVVLAGPE--DWRDPALLVELINSEGVDVLHaYPSMLQAFLEEEDAHRCTSLKRIV-------------CGGEALPA 3325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 401 fttrladylvlaKVRQALGFAKCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSetsgphfMSSPYNYRLYSSGKLVPg 480
Cdd:PRK12316 3326 ------------DLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRP-------IANRACYILDGSLEPVP- 3385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 481 crvklvnqdAEGIGEICLWGRTIFMGYLNMEDKTCEAI------DEEGWLHTGDAGRLDADGFLYITGRL 544
Cdd:PRK12316 3386 ---------VGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvPGERLYRTGDLARYRADGVIEYIGRV 3446
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
492-572 |
2.05e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 50.90 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 492 GIGEICLWGRTIFMGYLNMEDKT------------------CEAIDEEGWLHTGDAGrLDADGFLYITGRLKELIITaGG 553
Cdd:PRK12476 428 EVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlaegshaDGAADDGTWLRTGDLG-VYLDGELYITGRIADLIVI-DG 505
|
90
....*....|....*....
gi 767983694 554 ENVPPVPIEEAVKMELPII 572
Cdd:PRK12476 506 RNHYPQDIEATVAEASPMV 524
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
109-326 |
2.53e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 50.75 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLK-LGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYiAYDCC-ANVI 186
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLH-CFRCCgAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 187 MVDT--QKQLEKILkiwkqlPHLKA--VVIY---KEPPPNKMANVytMEEFMELGNEVPEEALDAIIDTQQPnqcCVLVY 259
Cdd:cd05938 83 VVAPelQEAVEEVL------PALRAdgVSVWylsHTSNTEGVISL--LDKVDAASDEPVPASLRAHVTIKSP---ALYIY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983694 260 TSGTTGNPKGVMLSQDNItWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 326
Cdd:cd05938 152 TSGTTGLPKAARISHLRV-LQCSGFLSLCGVT----ADDVIYITLPLYHSSGFLLGIGGCIELGATC 213
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
109-326 |
4.70e-06 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 49.66 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 109 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 188
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 189 DTqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtqqpnqcCVLVYTSGTTGNPK 268
Cdd:cd05940 82 DA----------------------------------------------------------------ALYIYTSGTTGLPK 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767983694 269 GVMLSQDNItWTARYGSQAGDIRpaeVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 326
Cdd:cd05940 98 AAIISHRRA-WRGGAFFAGSGGA---LPSDVLYTCLPLYHSTALIVGWSACLASGATL 151
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
448-579 |
6.95e-06 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 49.39 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 448 LYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI-----GEICLWGR-----TIFMGYLNMEDKTCEA 517
Cdd:cd05928 319 IYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLppgteGDIGIRVKpirpfGLFSGYVDNPEKTAAT 398
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767983694 518 IDEEGWLhTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:cd05928 399 IRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSS-GYRIGPFEVESAL-IEHPAVVESAVVS 457
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
84-598 |
1.21e-05 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 48.32 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 84 HRMFYEALDKYGDLIALGFKRQdKWehiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVT 163
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQ-SL---TYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 164 GIYTTSSPEACQYIAYDCCANVIMvdtqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeeald 243
Cdd:cd17645 77 PIDPDYPGERIAYMLADSSAKILL-------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 244 aiidtQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEvQQEVVVSYlplsHIAAQIYDLWTGIQWG 323
Cdd:cd17645 101 -----TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPAD-KSLVYASF----SFDASAWEIFPHLTAG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 324 AQVCFAePDALKGSLVNTLREVEpTSHMGVPRVWEKIMERIQEVAAQSgfirrkmllwamsvtLEQNLTcPGSDLKPFtt 403
Cdd:cd17645 171 AALHVV-PSERRLDLDALNDYFN-QEGITISFLPTGAAEQFMQLDNQS---------------LRVLLT-GGDKLKKI-- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 404 rladylvlakvrqalgfakcQKNFYgaapmmaetqhfflglniRLYAGYGLSE-----TSGPhfMSSPYNYrlYSSGKLV 478
Cdd:cd17645 231 --------------------ERKGY------------------KLVNNYGPTEntvvaTSFE--IDKPYAN--IPIGKPI 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 479 PGCRVKLVNQD----AEGI-GEICLWGRTIFMGYLNMEDKTCEA------IDEEGWLHTGDAGRLDADGFLYITGRLKEL 547
Cdd:cd17645 269 DNTRVYILDEAlqlqPIGVaGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ 348
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 767983694 548 iITAGGENVPPVPIEEAVkMELPIISNAMLI----GDQRKFLSMLLTLKCTLDPD 598
Cdd:cd17645 349 -VKIRGYRIEPGEIEPFL-MNHPLIELAAVLakedADGRKYLVAYVTAPEEIPHE 401
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
250-544 |
1.72e-05 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 48.04 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 250 QPNQCCVLVYTSGTTGNPKGVMLSQDNI-----TWTARYGSQAGDirpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGA 324
Cdd:cd17646 136 RPDNLAYVIYTSGSTGRPKGVMVTHAGIvnrllWMQDEYPLGPGD---------RVLQKTPLSFDVS-VWELFWPLVAGA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 325 QVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWEkimERIQEVAAQSGfirrkmllwamsVTLEQnLTCPGSDLKPft 402
Cdd:cd17646 206 RLVVARPGGHRdpAYLAALIREHGVTTCHFVPSMLR---VFLAEPAAGSC------------ASLRR-VFCSGEALPP-- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 403 tRLADylvlakvrqalgfakcqknfygaapmmaetqHFFLGLNIRLYAGYGLSETS--GPHFMSSPYNYRLYSS-GKLVP 479
Cdd:cd17646 268 -ELAA-------------------------------RFLALPGAELHNLYGPTEAAidVTHWPVRGPAETPSVPiGRPVP 315
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767983694 480 GCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAI-----DEEGWLH-TGDAGRLDADGFLYITGRL 544
Cdd:cd17646 316 NTRLYVL--DDALrpvpvgvPGELYLGGVQLARGYLGRPALTAERFvpdpfGPGSRMYrTGDLARWRPDGALEFLGRS 391
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
230-544 |
2.20e-05 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 47.43 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 230 FMELGNEVPEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQD---NITWTARygSQAGDIRPAEVQQEV 299
Cdd:cd17644 77 YVPLDPNYPQERLTYILeDAQisvlltQPENLAYVIYTSGSTGKPKGVMIEHQslvNLSHGLI--KEYGITSSDRVLQFA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 300 VVSYlplSHIAAQIYDLWtgiqwgaqvcfaepdaLKG-SLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQsgfirrkM 378
Cdd:cd17644 155 SIAF---DVAAEEIYVTL----------------LSGaTLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAY-------W 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 379 LLWAMSVTLEqnlTCPGsdlkPFTTRLAdylvlakvrqALGFAKCQknfygaaPMMAETQHFFLGLNIRLYAGYGLSE-- 456
Cdd:cd17644 209 HLLVLELLLS---TIDL----PSSLRLV----------IVGGEAVQ-------PELVRQWQKNVGNFIQLINVYGPTEat 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 457 -TSGPHFMSSPYNYRLYSS--GKLVPGCRVKLVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCE-------AIDEE 521
Cdd:cd17644 265 iAATVCRLTQLTERNITSVpiGRPIANTQVYILDENLQPVpvgvpGELHIGGVGLARGYLNRPELTAEkfishpfNSSES 344
|
330 340
....*....|....*....|....
gi 767983694 522 GWLH-TGDAGRLDADGFLYITGRL 544
Cdd:cd17644 345 ERLYkTGDLARYLPDGNIEYLGRI 368
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
185-579 |
3.01e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 47.08 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 185 VIMVDtQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMA-------NVYTMEEFMElGN-------EVPEEALDAIidtqq 250
Cdd:PRK05620 114 VIVAD-PRLAEQLGEILKECPCVRAVVFIGPSDADSAAahmpegiKVYSYEALLD-GRstvydwpELDETTAAAI----- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 251 pnqcCvlvYTSGTTGNPKGVMLSQDNItWTARYGSQAGD---IRPAEvqqevvvSYL---PLSHIAAqiydlW----TGI 320
Cdd:PRK05620 187 ----C---YSTGTTGAPKGVVYSHRSL-YLQSLSLRTTDslaVTHGE-------SFLccvPIYHVLS-----WgvplAAF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 321 QWGAQVCFAEPDALKGSLVNTLREVEPTSHMGVPRVWEKIMeriqevaaqSGFIR---RKMLLwamsvtleQNLTCPGSD 397
Cdd:PRK05620 247 MSGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLM---------VHYLKnppERMSL--------QEIYVGGSA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 398 LKPfttrladylVLAKVRQALgfakcqknfYGaapmmaetqhfflglnIRLYAGYGLSETSGPHFMSSP---------YN 468
Cdd:PRK05620 310 VPP---------ILIKAWEER---------YG----------------VDVVHVWGMTETSPVGTVARPpsgvsgearWA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 469 YRlYSSGKLVPGCRVKLVNqDAEGI-------GEICLWGRTIFMGYLNME----------------DKTCEAIDEEGWLH 525
Cdd:PRK05620 356 YR-VSQGRFPASLEYRIVN-DGQVMestdrneGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLR 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 767983694 526 TGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEEAVkMELPIISNAMLIG 579
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARD-VIRSGGEWIYSAQLENYI-MAAPEVVECAVIG 485
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
479-544 |
9.48e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 45.66 E-value: 9.48e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767983694 479 PGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDaDGFLYITGRL 544
Cdd:PRK04813 325 PDSPLLIIDEEGTklpdgEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGYLE-DGLLFYQGRI 397
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
238-606 |
9.56e-05 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 45.39 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 238 PEEALDAIIDTQQ-------PNQCCVLVYTSGTTGNPKGVMLSQDN----ITWtarygsqAGDIRPAEVQQEVVVSY--- 303
Cdd:cd12115 84 PPERLRFILEDAQarlvltdPDDLAYVIYTSGSTGRPKGVAIEHRNaaafLQW-------AAAAFSAEELAGVLASTsic 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 304 LPLShiaaqIYDLWTGIQWGAQVCFAE--------PDALKGSLVNTlreveptshmgVPRVwekimerIQEVAAQSGFIR 375
Cdd:cd12115 157 FDLS-----VFELFGPLATGGKVVLADnvlalpdlPAAAEVTLINT-----------VPSA-------AAELLRHDALPA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 376 rkmllwAMSVTleqNLTcpGsdlKPFTTRLADYLvlakvrqalgfakcqknfYGAAPMmaetqhfflglnIRLYAGYGLS 455
Cdd:cd12115 214 ------SVRVV---NLA--G---EPLPRDLVQRL------------------YARLQV------------ERVVNLYGPS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 456 ET---SGPHFMsSPYNYRLYSSGKLVPGCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWL- 524
Cdd:cd12115 250 EDttySTVAPV-PPGASGEVSIGRPLANTQAYVL--DRALqpvplgvPGELYIGGAGVARGYLGRPGLTAERFLPDPFGp 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 525 -----HTGDAGRLDADGFLYITGRLKELIITAGgenvppVPIE----EAVKMELPIISNA--MLIGDQ--RKFLSMLLTL 591
Cdd:cd12115 327 garlyRTGDLVRWRPDGLLEFLGRADNQVKVRG------FRIElgeiEAALRSIPGVREAvvVAIGDAagERRLVAYIVA 400
|
410
....*....|....*
gi 767983694 592 KCTLDPDTSDQTDNL 606
Cdd:cd12115 401 EPGAAGLVEDLRRHL 415
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
238-278 |
1.32e-04 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 44.99 E-value: 1.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767983694 238 PEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQDNIT 278
Cdd:cd17643 72 PVERIAFILaDSGpsllltDPDDLAYVIYTSGSTGRPKGVVVSHANVL 119
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
246-556 |
1.33e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 45.19 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 246 IDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDirPAEvqQEVVVSYLPLSHiaaqiydlwtgiQWGAQ 325
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS--PKE--DDVMMSFLPPFH------------AYGFN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 326 VCfaepdalkgSLVNTLreveptshMGVPRVW-------EKIMERIQEVAAqsgfirrkmllwamsvtleqnlTCPGSdl 398
Cdd:PRK06334 241 SC---------TLFPLL--------SGVPVVFaynplypKKIVEMIDEAKV----------------------TFLGS-- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 399 kpfTTRLADYLVLAKVRQ-----ALGFAKCQKNFYGAApMMAETQHFFLglNIRLYAGYGLSETSgP----HFMSSPYNY 469
Cdd:PRK06334 280 ---TPVFFDYILKTAKKQesclpSLRFVVIGGDAFKDS-LYQEALKTFP--HIQLRQGYGTTECS-PvitiNTVNSPKHE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 470 RLYssGKLVPGCRVKLVNQDAEG------IGEICLWGRTIFMGYLNmEDKTCEAI--DEEGWLHTGDAGRLDADGFLYIT 541
Cdd:PRK06334 353 SCV--GMPIRGMDVLIVSEETKVpvssgeTGLVLTRGTSLFSGYLG-EDFGQGFVelGGETWYVTGDLGYVDRHGELFLK 429
|
330
....*....|....*
gi 767983694 542 GRLKELiITAGGENV 556
Cdd:PRK06334 430 GRLSRF-VKIGAEMV 443
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
111-269 |
1.42e-04 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 45.17 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 111 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM--- 187
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALItad 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 188 --------VDTQKQLEKILKiwkQLPHLKAVVIY---KEPPPNKMANVYTMEEFMElgnevpeeALDAIIDTQQPNQCCV 256
Cdd:cd05968 172 gftrrgreVNLKEEADKACA---QCPTVEKVVVVrhlGNDFTPAKGRDLSYDEEKE--------TAGDGAERTESEDPLM 240
|
170
....*....|...
gi 767983694 257 LVYTSGTTGNPKG 269
Cdd:cd05968 241 IIYTSGTTGKPKG 253
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
493-566 |
1.52e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 44.93 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 493 IGEICLWGRTIFMGYLNMEDKT-----------CEAIDEEGWLHTGDAGRLDaDGFLYITGRLKELIITAgGENVPPVPI 561
Cdd:PRK05850 397 VGEIWVHGDNVAAGYWQKPEETertfgatlvdpSPGTPEGPWLRTGDLGFIS-EGELFIVGRIKDLLIVD-GRNHYPDDI 474
|
....*
gi 767983694 562 EEAVK 566
Cdd:PRK05850 475 EATIQ 479
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
83-544 |
1.82e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 45.33 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 83 VHRMFYEALDKYGDLIALGFKRQDkwehISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIV 162
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALAFGEET----LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 163 TGIYTTSSPEACQYIAYDCCANVIMvdTQKQLEKILKIWKQLphlkAVVIYKEPPPnkmanvytmeEFMELGNEVPEEAL 242
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGVQLLL--SQSHLGRKLPLAAGV----QVLDLDRPAA----------WLEGYSEENPGTEL 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 243 DaiidtqqPNQCCVLVYTSGTTGNPKGVMLS----QDNITWT-ARYGSQAGDirpaEVQQEVVVSYlplshiAAQIYDLW 317
Cdd:PRK12316 653 N-------PENLAYVIYTSGSTGKPKGAGNRhralSNRLCWMqQAYGLGVGD----TVLQKTPFSF------DVSVWEFF 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 318 TGIQWGAQVCFAEPDALK--GSLVNTL-REVEPTSHMgVPRVWEKImerIQEVAAQsgfirrkmllwamSVTLEQNLTCP 394
Cdd:PRK12316 716 WPLMSGARLVVAAPGDHRdpAKLVELInREGVDTLHF-VPSMLQAF---LQDEDVA-------------SCTSLRRIVCS 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 395 GSDLKpfttrladylvlakvrqalgfAKCQKNFYGAAPmmaetqhfflglNIRLYAGYGLSETS--GPHFMSSPYNYRLY 472
Cdd:PRK12316 779 GEALP---------------------ADAQEQVFAKLP------------QAGLYNLYGPTEAAidVTHWTCVEEGGDSV 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 473 SSGKLVPGCRVKLVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEA------IDEEGWLHTGDAGRLDADGFLYIT 541
Cdd:PRK12316 826 PIGRPIANLACYILDANLEPVpvgvlGELYLAGRGLARGYHGRPGLTAERfvpspfVAGERMYRTGDLARYRADGVIEYA 905
|
...
gi 767983694 542 GRL 544
Cdd:PRK12316 906 GRI 908
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
238-334 |
2.06e-04 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 44.17 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 238 PEEALDAIIDTQQPnqCCVL---------VYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAevqqEVVVSYLPLSH 308
Cdd:cd17652 72 PAERIAYMLADARP--ALLLttpdnlayvIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPG----SRVLQFASPSF 145
|
90 100
....*....|....*....|....*.
gi 767983694 309 IAAqIYDLWTGIQWGAQVCFAEPDAL 334
Cdd:cd17652 146 DAS-VWELLMALLAGATLVLAPAEEL 170
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
475-553 |
2.71e-04 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 44.12 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 475 GKLVPGCRVKLVNQDAE--------------GIGEICLWGRTIFMGYLNMEDKTCEA--IDEEG--WLHTGDAGRLDADG 536
Cdd:PRK09274 355 GRPVDGVEVRIIAISDApipewddalrlatgEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQG 434
|
90
....*....|....*..
gi 767983694 537 FLYITGRLKELIITAGG 553
Cdd:PRK09274 435 RLWFCGRKAHRVETAGG 451
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
240-326 |
3.36e-04 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 43.57 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 240 EALDAIIDTQQPNQCCV-------LVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQ 312
Cdd:cd05939 85 DPLLTQSSTEPPSQDDVnfrdklfYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRP----EDVVYDCLPLYHSAGG 160
|
90
....*....|....
gi 767983694 313 IYDLWTGIQWGAQV 326
Cdd:cd05939 161 IMGVGQALLHGSTV 174
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
258-276 |
6.10e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 42.96 E-value: 6.10e-04
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
250-333 |
9.38e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 42.72 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 250 QPNQCCVLVYTSGTTGNPKGVMLSQDNIT----WT-ARYGSQAGDI----RPAEVQQEVVVSYLPLshIAaqiydlwtgi 320
Cdd:PRK10252 596 QPHHTAYIIFTSGSTGRPKGVMVGQTAIVnrllWMqNHYPLTADDVvlqkTPCSFDVSVWEFFWPF--IA---------- 663
|
90
....*....|...
gi 767983694 321 qwGAQVCFAEPDA 333
Cdd:PRK10252 664 --GAKLVMAEPEA 674
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
88-295 |
1.39e-03 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 41.78 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 88 YEALD----KYGDLIALGFKRQD--KWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEwffsAVGTVFA--- 158
Cdd:cd05966 56 YNCLDrhlkERGDKVAIIWEGDEpdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPE----LVIAMLAcar 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983694 159 -GGIVTGIYTTSSPEA-CQYIAyDC-CANVIMVDTQKQLEKIL-------KIWKQLPHLKAVVIYKepppnKMANVYTME 228
Cdd:cd05966 132 iGAVHSVVFAGFSAESlADRIN-DAqCKLVITADGGYRGGKVIplkeivdEALEKCPSVEKVLVVK-----RTGGEVPMT 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767983694 229 E-----FMELGNEVPEEALDAIIDTQQPnqcCVLVYTSGTTGNPKGVMLSQ-DNITWTARYGSQAGDIRPAEV 295
Cdd:cd05966 206 EgrdlwWHDLMAKQSPECEPEWMDSEDP---LFILYTSGSTGKPKGVVHTTgGYLLYAATTFKYVFDYHPDDI 275
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
257-308 |
1.44e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 41.85 E-value: 1.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767983694 257 LVYTSGTTGNPKGVMLSQDNITWT-----ARYGSQAGDIRPAEVqqeVVVSYLPLSH 308
Cdd:PRK05850 165 LQYTSGSTRTPAGVMVSHRNVIANfeqlmSDYFGDTGGVPPPDT---TVVSWLPFYH 218
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