|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
80-651 |
0e+00 |
|
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: 920.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 80 PYQWINYDEALLRAKNFGAGMLALGAR--PKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQ 157
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 158 VVIVEDdgkaamllekaprslkiivaikpirqttlerarsrGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTT 237
Cdd:cd05927 82 IVFCDA-----------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 238 GNPKGVMLTHGNVVAGVCSVILQMGDH-RIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKP 316
Cdd:cd05927 127 GNPKGVMLTHGNIVSNVAGVFKILEILnKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIKALKP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 317 TVMPAVPRLLNRVYDKIQNDISASG-LKRGLFNMAMRAKEKEIARGVLRRNGCWDKLVFKKVHQAFGGNLRLMVVGSAPL 395
Cdd:cd05927 207 TVFPGVPRVLNRIYDKIFNKVQAKGpLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLTGSAPL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 396 AGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFA--NQNTGEVCVRGSNVF 473
Cdd:cd05927 287 SPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAkdPNPRGEVCIRGPNVF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 474 HGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSC 553
Cdd:cd05927 367 SGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKSF 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 554 IIAVVVPDTDVLKQWATENN-VRGTLSVLCNNKNVKELIMNDMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFK 632
Cdd:cd05927 447 LVAIVVPDPDVLKEWAASKGgGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLLTPTFK 526
|
570
....*....|....*....
gi 281366413 633 AKRPQLKSYFKPQLEDMYK 651
Cdd:cd05927 527 LKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
51-653 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 651.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 51 VRTLYQTFREGAYASNNGPCLGWR---ETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQG 127
Cdd:PLN02736 43 IGTLHDNFVYAVETFRDYKYLGTRirvDGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 128 CYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAML--LEKAPrSLKIIVAIKPIRQTTLERARSRGIQIFSF 205
Cdd:PLN02736 123 CSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLscLSEIP-SVRLIVVVGGADEPLPSLPSGTGVEIVTY 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 206 IDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILqmgDHRIRAGDVMVSFLPLAHMFERC 285
Cdd:PLN02736 202 SKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSL---STKFYPSDVHISYLPLAHIYERV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 286 CENGMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISASG-LKRGLFNMAMRAKEKEIARGvlr 364
Cdd:PLN02736 279 NQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGgLKERLFNAAYNAKKQALENG--- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 365 RN--GCWDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVS 442
Cdd:PLN02736 356 KNpsPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNP 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 443 CNAVKLVDVPEMEYFANQNT---GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKL 519
Cdd:PLN02736 436 ACEVKLVDVPEMNYTSEDQPyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKL 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 520 SQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVR-GTLSVLCNNKNVKELIMNDMLNW 598
Cdd:PLN02736 516 AQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAV 595
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 281366413 599 GKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMYKHL 653
Cdd:PLN02736 596 GREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
49-652 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 540.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 49 ENVRTLYQTFREGAYASNNGPCLGWRETltSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGC 128
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 129 YSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAMLLEKAPR--SLKIIVAIKPirqttleRARSRGIQIFSFI 206
Cdd:COG1022 86 LAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDElpSLRHIVVLDP-------RGLRDDPRLLSLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 207 DVEKLGAKGNHPE------VPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAH 280
Cdd:COG1022 159 ELLALGREVADPAelearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERL---PLGPGDRTLSFLPLAH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 281 MFERCCENGMYYVGGCVGfYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDIS-ASGLKRGLFNMAMR-AKEKEI 358
Cdd:COG1022 236 VFERTVSYYALAAGATVA-FAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeAGGLKRKLFRWALAvGRRYAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 359 ARGVLRRNGCW--------DKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRcALGCLVLEGYGQTECTGAITLTVQG 430
Cdd:COG1022 315 ARLAGKSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFR-ALGIPVLEGYGLTETSPVITVNRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 431 DHVPNHVGPPVSCNAVKLVDvpemeyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRII 510
Cdd:COG1022 394 DNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRIT 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 511 DRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKsCIIAVVVPDTDVLKQWATENNV-RGTLSVLCNNKNVKE 589
Cdd:COG1022 463 GRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLpYTSYAELAQDPEVRA 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366413 590 LIMN--DMLNwgkqSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMYKH 652
Cdd:COG1022 542 LIQEevDRAN----AGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
38-651 |
1.88e-165 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 488.97 E-value: 1.88e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 38 SKNGKFVsyITENVRTLYQTFREGAYASNNGPCLGWRETLTS---PYQWINYDEALLRAKNFGAGMLALGARPKQLIGIY 114
Cdd:PLN02861 31 AKDGLLD--LPADIDSPWQFFSDAVKKYPNNQMLGRRQVTDSkvgPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 115 SQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAML--LEKAPRSLKIIVAIKPIRQTTL 192
Cdd:PLN02861 109 GSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILscLPKCSSNLKTIVSFGDVSSEQK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 193 ERARSRGIQIFSFIDVEKLGAKgnHPEVPPTAE-DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSV--ILQMGDHRIRAG 269
Cdd:PLN02861 189 EEAEELGVSCFSWEEFSLMGSL--DCELPPKQKtDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTdhLLKVTDRVATEE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 270 DVMVSFLPLAHMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISASG-LKRGLFN 348
Cdd:PLN02861 267 DSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGmLRKKLFD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 349 MAMRAKEKEIARGVLRRNGC--WDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTE-CTGAIT 425
Cdd:PLN02861 347 FAYNYKLGNLRKGLKQEEASprLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFT 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 426 LTVQGDHVPNHVGPPVSCNAVKLVDVPEMEY--FANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLP 503
Cdd:PLN02861 427 SIANVFSMVGTVGVPMTTIEARLESVPEMGYdaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQP 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 504 NGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVRGTLSVLCN 583
Cdd:PLN02861 506 NGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCK 585
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281366413 584 NKNVKELIMNDMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMYK 651
Cdd:PLN02861 586 NLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
49-651 |
6.31e-165 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 487.99 E-value: 6.31e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 49 ENVRTLYQTFREGAYASNNGPCLGWRETLTSP---YQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYE 125
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRREIVDGKpgkYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 126 QGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDgKAAMLLEKAPRS---LKIIVAIKPIRQTTLERARSRGIQI 202
Cdd:PLN02614 122 EACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK-KISELFKTCPNSteyMKTVVSFGGVSREQKEEAETFGLVI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 203 FSFIDVEKLGaKGNHPEVP-PTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVI--LQMGDHRIRAGDVMVSFLPLA 279
Cdd:PLN02614 201 YAWDEFLKLG-EGKQYDLPiKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIrlLKSANAALTVKDVYLSYLPLA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 280 HMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISASG-LKRGLFNMAMRAKEKEI 358
Cdd:PLN02614 280 HIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGfLKKFVFDSAFSYKFGNM 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 359 ARGV--LRRNGCWDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTE-CTGAITLTVQGDHVPN 435
Cdd:PLN02614 360 KKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsCAGTFVSLPDELDMLG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 436 HVGPPVSCNAVKLVDVPEMEYFANQNT--GEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRR 513
Cdd:PLN02614 440 TVGPPVPNVDIRLESVPEMEYDALASTprGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRK 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 514 KHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVRGTLSVLCNNKNVKELIMN 593
Cdd:PLN02614 519 KNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILG 598
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 281366413 594 DMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMYK 651
Cdd:PLN02614 599 ELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYK 656
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
50-653 |
1.00e-163 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 484.70 E-value: 1.00e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 50 NVRTLYQTFREGA--YASNNgpCLGWRETL---TSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILY 124
Cdd:PLN02430 40 DITTAWDIFSKSVekYPDNK--MLGWRRIVdgkVGPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 125 EQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDgKAAMLLE---KAPRSLKIIVAIKPIRQTTLERARSRGIQ 201
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK-KIKELLEpdcKSAKRLKAIVSFTSVTEEESDKASQIGVK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 202 IFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMG--DHRIRAGDVMVSFLPLA 279
Cdd:PLN02430 197 TYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfEDKMTHDDVYLSFLPLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 280 HMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISA-SGLKRGLFNMAMRAKEKEI 358
Cdd:PLN02430 277 HILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQElNPRRRLIFNALYKYKLAWM 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 359 ARGVLRRNGC--WDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDH-VPN 435
Cdd:PLN02430 357 NRGYSHKKASpmADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMcMLG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 436 HVGPPVSCNAVKLVDVPEMEY--FANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRR 513
Cdd:PLN02430 437 TVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRK 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 514 KHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVRGTLSVLCNNKNVKELIMN 593
Cdd:PLN02430 516 KNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILS 595
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 594 DMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMYKHL 653
Cdd:PLN02430 596 ELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
79-635 |
1.14e-160 |
|
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: 471.31 E-value: 1.14e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 79 SPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQV 158
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 159 VIVEddgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpPTAEDLCTVCYTSGTTG 238
Cdd:cd17639 81 IFTD-----------------------------------------------------------GKPDDLACIMYTSGSTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 239 NPKGVMLTHGNVVAGVCSVILQMGDHrIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFysGDIKELTN--------D 310
Cdd:cd17639 102 NPKGVMLTHGNLVAGIAGLGDRVPEL-LGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDkskrgckgD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 311 LKMLKPTVMPAVPRLLNRVYDKIQNDISASG-LKRGLFNMAMRAKEKEIARGVLrrNGCWDKLVFKKVHQAFGGNLRLMV 389
Cdd:cd17639 179 LTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGgLKRTLFWTAYQSKLKALKEGPG--TPLLDELVFKKVRAALGGRLRYML 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 390 VGSAPLAGNVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQ--NTGEVCV 467
Cdd:cd17639 257 SGGAPLSADTQEFLN-IVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKppPRGEILI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 468 RGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYG 547
Cdd:cd17639 336 RGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYA 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 548 ESLKSCIIAVVVPDTDVLKQWATENNV-RGTLSVLCNNKNVKELIMNDMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGL 626
Cdd:cd17639 416 DPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEWTPENGL 495
|
....*....
gi 281366413 627 LTPTFKAKR 635
Cdd:cd17639 496 VTAAQKLKR 504
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
80-638 |
7.18e-144 |
|
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: 426.24 E-value: 7.18e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 80 PYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVV 159
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 160 IVEDdgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptAEDLCTVCYTSGTTGN 239
Cdd:cd05907 82 FVED------------------------------------------------------------PDDLATIIYTSGTTGR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 240 PKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAHMFERCCenGMYYV---GGCVGFYSgDIKELTNDLKMLKP 316
Cdd:cd05907 102 PKGVMLSHRNILSNALALAERL---PATEGDRHLSFLPLAHVFERRA--GLYVPllaGARIYFAS-SAETLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 317 TVMPAVPRLLNRVYDKIQNDISaSGLKRGLFnmamrakekeiargvlrrngcwdklvfkkvHQAFGGNLRLMVVGSAPLA 396
Cdd:cd05907 176 TVFLAVPRVWEKVYAAIKVKAV-PGLKRKLF------------------------------DLAVGGRLRFAASGGAPLP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 397 GNVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDvpemeyfanqnTGEVCVRGSNVFHGY 476
Cdd:cd05907 225 AELLHFFR-ALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGY 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 477 YKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKsCIIA 556
Cdd:cd05907 293 YKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRP-FLVA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 557 VVVPDTDVLKQWATENNV-RGTLSVLCNNKNVKELI--MNDMLNwgkqSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKA 633
Cdd:cd05907 372 LIVPDPEALEAWAEEHGIaYTDVAELAANPAVRAEIeaAVEAAN----ARLSRYEQIKKFLLLPEPFTIENGELTPTLKL 447
|
....*
gi 281366413 634 KRPQL 638
Cdd:cd05907 448 KRPVI 452
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
49-650 |
8.08e-134 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 408.74 E-value: 8.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 49 ENVRTLYQTFREGAYASNNGPCLGWR-----ETLTSP------------YQWINYDEALLRAKNFGAGMLALGARPKQLI 111
Cdd:PLN02387 55 EGATTLAALFEQSCKKYSDKRLLGTRklisrEFETSSdgrkfeklhlgeYEWITYGQVFERVCNFASGLVALGHNKEERV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 112 GIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDG-KAAMLLEKAPRSLKIIVAIKPIRQ- 189
Cdd:PLN02387 135 AIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQlKKLIDISSQLETVKRVIYMDDEGVd 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 190 TTLERARSRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDhrIRAG 269
Cdd:PLN02387 215 SDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPK--LGKN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 270 DVMVSFLPLAHMFERCCENGMYYVGGCVGF--------YSGDIKELTN-DLKMLKPTVMPAVPRLLNRVYDKIQNDISAS 340
Cdd:PLN02387 293 DVYLAYLPLAHILELAAESVMAAVGAAIGYgspltltdTSNKIKKGTKgDASALKPTLMTAVPAILDRVRDGVRKKVDAK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 341 G-LKRGLFNMAMRAKEKEI------ARGVLRRngCWDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLE 413
Cdd:PLN02387 373 GgLAKKLFDIAYKRRLAAIegswfgAWGLEKL--LWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQ 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 414 GYGQTE-CTGAiTLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQNT---GEVCVRGSNVFHGYYKDPEKTAEA--I 487
Cdd:PLN02387 451 GYGLTEtCAGA-TFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKPmprGEIVIGGPSVTLGYFKNQEKTDEVykV 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 488 DSEG--WHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVL 565
Cdd:PLN02387 530 DERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQAL 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 566 KQWATENNVR-GTLSVLCNNKNVKELIMNDMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKP 644
Cdd:PLN02387 610 EKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKD 689
|
....*.
gi 281366413 645 QLEDMY 650
Cdd:PLN02387 690 DLKKLY 695
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
78-520 |
5.45e-122 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 368.56 E-value: 5.45e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 78 TSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQ 157
Cdd:pfam00501 16 VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 158 VVIVEDDGKAAMLLEKAPR----SLKIIVAIKPIRQTTLerarsrgiqifsFIDVEKLGAKGNHPEVPPTAEDLCTVCYT 233
Cdd:pfam00501 96 VLITDDALKLEELLEALGKlevvKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 234 SGTTGNPKGVMLTHGNVVAGVCSV-ILQMGDHRIRAGDVMVSFLPLAHMFERC-CENGMYYVGGCVGFYSG----DIKEL 307
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIkRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGfpalDPAAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 308 TNDLKMLKPTVMPAVPRLLNRVydkiqndISASGLKRGLFnmamrakekeiargvlrrngcwdklvfkkvhqafgGNLRL 387
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNML-------LEAGAPKRALL-----------------------------------SSLRL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 388 MVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDH---VPNHVGPPVSCNAVKLVDVPEMEYFANQNTGE 464
Cdd:pfam00501 282 VLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGE 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 281366413 465 VCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLS 520
Cdd:pfam00501 362 LCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
82-635 |
4.75e-104 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 331.56 E-value: 4.75e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 82 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIV 161
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 162 edDGKA-AMLLEKAprSLKIIVAIKPIRQTTL-ERARSRGIQIFSFIDVEKLG--AKGNHPEVPPT-AEDLCTVCYTSGT 236
Cdd:PTZ00216 200 --NGKNvPNLLRLM--KSGGMPNTTIIYLDSLpASVDTEGCRLVAWTDVVAKGhsAGSHHPLNIPEnNDDLALIMYTSGT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 237 TGNPKGVMLTHGNVVAGVCSVilqmgDHRI-------RAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFysGDIKELTN 309
Cdd:PTZ00216 276 TGDPKGVMHTHGSLTAGILAL-----EDRLndligppEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 310 -------DLKMLKPTVMPAVPRllnrVYDKIQNDISAS-----GLKRGLFNMAMRAKEKEIargvlrRNGC----WDKLV 373
Cdd:PTZ00216 349 tfarphgDLTEFRPVFLIGVPR----IFDTIKKAVEAKlppvgSLKRRVFDHAYQSRLRAL------KEGKdtpyWNEKV 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 374 FKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVlEGYGQTE--CTGAITLTvqGDHVPNHVGPPVSCNAVKLVDV 451
Cdd:PTZ00216 419 FSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGMVI-QGWGLTEtvCCGGIQRT--GDLEPNAVGQLLKGVEMKLLDT 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 452 PEmeyFANQNT----GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVP 527
Cdd:PTZ00216 496 EE---YKHTDTpeprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIAL 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 528 EKIENIYTLSQYV--NQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVRGTLSVLCNNKNVKELIMNDMLNWGKQSGLK 605
Cdd:PTZ00216 573 EALEALYGQNELVvpNGVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRK 652
|
570 580 590
....*....|....*....|....*....|
gi 281366413 606 SFEQVKDIYLHPDPFSVQNGLLTPTFKAKR 635
Cdd:PTZ00216 653 SFEIVRHVRVLSDEWTPENGVLTAAMKLKR 682
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
80-636 |
1.50e-90 |
|
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: 288.87 E-value: 1.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 80 PYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVV 159
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 160 IVEDDGKaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaeDLCTVCYTSGTTGN 239
Cdd:cd17640 82 VVENDSD-----------------------------------------------------------DLATIIYTSGTTGN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 240 PKGVMLTHGNVVAGVCSvILQMGDhrIRAGDVMVSFLPLAHMFERCCEngmYYV--GGCVGFYSgDIKELTNDLKMLKPT 317
Cdd:cd17640 103 PKGVMLTHANLLHQIRS-LSDIVP--PQPGDRFLSILPIWHSYERSAE---YFIfaCGCSQAYT-SIRTLKDDLKRVKPH 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 318 VMPAVPRLLNRVYDKIQNDISASGLKRglfnmamrakeKEIARGVLrrngcwdklvfkkvhqaFGGNLRLMVVGSAPLAG 397
Cdd:cd17640 176 YIVSVPRLWESLYSGIQKQVSKSSPIK-----------QFLFLFFL-----------------SGGIFKFGISGGGALPP 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 398 NVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYY 477
Cdd:cd17640 228 HVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 478 KDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKScIIAV 557
Cdd:cd17640 307 KNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKR-LGAL 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 558 VVPDTDVLKQWATENNVR--GTLSVLCNNKNVKELIMNDMLNW-GKQSGLKSFEQVKDIYLHPDPFsVQNGLLTPTFKAK 634
Cdd:cd17640 386 IVPNFEELEKWAKESGVKlaNDRSQLLASKKVLKLYKNEIKDEiSNRPGFKSFEQIAPFALLEEPF-IENGEMTQTMKIK 464
|
..
gi 281366413 635 RP 636
Cdd:cd17640 465 RN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
81-635 |
7.68e-76 |
|
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: 251.62 E-value: 7.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 81 YQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVI 160
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 161 VeddGKaamlLEKAPrSLKIIVAIKPIRQTTLERARSRgiqifSFIDVEKLGAKGN--HPEVPPTAEDLCTVCYTSGTTG 238
Cdd:cd05932 84 V---GK----LDDWK-AMAPGVPEGLISISLPPPSAAN-----CQYQWDDLIAQHPplEERPTRFPEQLATLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 239 NPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKPTV 318
Cdd:cd05932 151 QPKGVMLTFGSFAWAAQAGIEHIG---TEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDVQRARPTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 319 MPAVPRLLNRVYDKIQNDISASGLKRglfnmamrakekeiargvLRRNGCWDKLVFKKVHQAFGGN-LRLMVVGSAPLAG 397
Cdd:cd05932 228 FFSVPRLWTKFQQGVQDKIPQQKLNL------------------LLKIPVVNSLVKRKVLKGLGLDqCRLAGCGSAPVPP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 398 NVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDvpemeyfanqnTGEVCVRGSNVFHGYY 477
Cdd:cd05932 290 ALLEWYR-SLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGYY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 478 KDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAV 557
Cdd:cd05932 358 KDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALV 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281366413 558 VVPDTDVLKQWA-TENNVRGTLSVLCNNKNvkelimndmlnwgkqSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKR 635
Cdd:cd05932 438 VLSEEARLRADAfARAELEASLRAHLARVN---------------STLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKR 501
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
81-591 |
3.73e-75 |
|
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: 251.57 E-value: 3.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 81 YQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVI 160
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 161 VEDDGKAAMLLEKAPR--SLKIIVAIKPirqttlerarsRGIQIFS---FIDVEKLGAKGN-----HPEVPPTA------ 224
Cdd:cd17641 89 AEDEEQVDKLLEIADRipSVRYVIYCDP-----------RGMRKYDdprLISFEDVVALGRaldrrDPGLYEREvaagkg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 225 EDLCTVCYTSGTTGNPKGVMLTHGNVvAGVCSVILQMGDhrIRAGDVMVSFLPLAHMFERccengMYYVG------GCVG 298
Cdd:cd17641 158 EDVAVLCTTSGTTGKPKLAMLSHGNF-LGHCAAYLAADP--LGPGDEYVSVLPLPWIGEQ-----MYSVGqalvcgFIVN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 299 FYSgDIKELTNDLKMLKPTVMPAVPRllnrVYDKIQNDIS-----ASGLKRGLFNMAMRAKEKEIARGV-LRRNGCW--- 369
Cdd:cd17641 230 FPE-EPETMMEDLREIGPTFVLLPPR----VWEGIAADVRarmmdATPFKRFMFELGMKLGLRALDRGKrGRPVSLWlrl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 370 -----DKLVFKKVHQAFG-GNLRLMVVGSAPLAGNVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSC 443
Cdd:cd17641 305 aswlaDALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 444 NAVKLvdvpemeyfanQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGE 523
Cdd:cd17641 384 TEVRI-----------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGT 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281366413 524 YIVPEKIENIYTLSQYVNQVYVYGESlKSCIIAVVVPDTDVLKQWATENNVR-GTLSVLCNNKNVKELI 591
Cdd:cd17641 453 RFSPQFIENKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELI 520
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
74-628 |
1.19e-68 |
|
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: 234.66 E-value: 1.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 74 RETLTSPyQWINYDEALLRAKNFGAGmlalgARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQ 153
Cdd:cd17632 65 FETITYA-ELWERVGAVAAAHDPEQP-----VRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 154 TDMQVVIVE----DDGKAAMLLEKAPRSLKIIVAIKPIRQTT--LERARSRGIQIFSFIDVEKLGAKGNH-------PEV 220
Cdd:cd17632 139 TEPRLLAVSaehlDLAVEAVLEGGTPPRLVVFDHRPEVDAHRaaLESARERLAAVGIPVTTLTLIAVRGRdlppaplFRP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 221 PPTAEDLCTVCYTSGTTGNPKGVMLTHGNVV-AGVCSVILQmgDHRIRAGdVMVSFLPLAHMFERCCENGMYYVGGCVGF 299
Cdd:cd17632 219 EPDDDPLALLIYTSGSTGTPKGAMYTERLVAtFWLKVSSIQ--DIRPPAS-ITLNFMPMSHIAGRISLYGTLARGGTAYF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 300 YS-GDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQndisaSGLKRGLFNMAMRAKEKEIARGVLRRngcwdklvfkkvh 378
Cdd:cd17632 296 AAaSDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQ-----AELDRRSVAGADAETLAERVKAELRE------------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 379 QAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAITLtvqgDHVPnhVGPPVScnAVKLVDVPEMEYFA 458
Cdd:cd17632 358 RVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE-AGAVIL----DGVI--VRPPVL--DYKLVDVPELGYFR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 459 NQNT---GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYT 535
Cdd:cd17632 429 TDRPhprGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFA 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 536 LSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATEnNVRGTLSvlcnnKNVKELimndmlnwGKQSGLKSFEQVKDIYL 615
Cdd:cd17632 509 ASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTA-RLRAALA-----ESLQRI--------AREAGLQSYEIPRDFLI 574
|
570
....*....|...
gi 281366413 616 HPDPFSVQNGLLT 628
Cdd:cd17632 575 ETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
84-635 |
1.00e-67 |
|
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: 228.87 E-value: 1.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 163
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 DgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaEDLCTVCYTSGTTGNPKGV 243
Cdd:cd05914 88 E------------------------------------------------------------DDVALINYTSGTTGNSKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 244 MLTHGNVVAGV--CSVILQMGdhrirAGDVMVSFLPLAHMFErCCENGMY--YVGGCVGFYSGDIKELTNDLKMLKPTVM 319
Cdd:cd05914 108 MLTYRNIVSNVdgVKEVVLLG-----KGDKILSILPLHHIYP-LTFTLLLplLNGAHVVFLDKIPSAKIIALAFAQVTPT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 320 PAVPRLLnRVYDKIQND-ISASGLKRGLFNMAMRAKEKEIArgvlrrngcwdKLVFKKVHQAFGGNLRLMVVGSAPLAGN 398
Cdd:cd05914 182 LGVPVPL-VIEKIFKMDiIPKLTLKKFKFKLAKKINNRKIR-----------KLAFKKVHEAFGGNIKEFVIGGAKINPD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 399 VLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVscnavKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYK 478
Cdd:cd05914 250 VEEFLR-TIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVI-----DGVEVRIDSPDPATGEGEIIVRGPNVMKGYYK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 479 DPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSciIAVV 558
Cdd:cd05914 324 NPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL--VALA 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366413 559 VPDTDVLKQWATennvrgtlsvlcNNKNVKELIMNDMLNWGKQSgLKSFEQVKDIYLHPDPFSVqngllTPTFKAKR 635
Cdd:cd05914 402 YIDPDFLDVKAL------------KQRNIIDAIKWEVRDKVNQK-VPNYKKISKVKIVKEEFEK-----TPKGKIKR 460
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
74-572 |
4.32e-67 |
|
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: 226.62 E-value: 4.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 74 RETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQ 153
Cdd:COG0318 15 RPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILED 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 154 TDMQVVIVeddgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaedlCTVCYT 233
Cdd:COG0318 95 SGARALVT------------------------------------------------------------------ALILYT 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 234 SGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMFerccenGMY-------YVGGCVGFYSG-DIK 305
Cdd:COG0318 109 SGTTGRPKGVMLTHRNLLANAAAIAAALG---LTPGDVVLVALPLFHVF------GLTvgllaplLAGATLVLLPRfDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 306 ELTNDLKMLKPTVMPAVPRLLNRVydkiqndisasglkrglfnmamrAKEKEIARGVLRRngcwdklvfkkvhqafggnL 385
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARL-----------------------LRHPEFARYDLSS-------------------L 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 386 RLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQ--GDHVPNHVGPPVSCNAVKLVDvPEMEYFANQNTG 463
Cdd:COG0318 218 RLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEdpGERRPGSVGRPLPGVEVRIVD-EDGRELPPGEVG 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 464 EVCVRGSNVFHGYYKDPEKTAEAIDsEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIEN-IYTLSQyVNQ 542
Cdd:COG0318 297 EIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEvLAAHPG-VAE 373
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 281366413 543 VYV-------YGESLKsciiAVVVP------DTDVLKQWATEN 572
Cdd:COG0318 374 AAVvgvpdekWGERVV----AFVVLrpgaelDAEELRAFLRER 412
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
72-650 |
2.97e-65 |
|
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: 225.70 E-value: 2.97e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 72 GWrETLTspyqWINYDEALLR-AKNFgagmLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFI 150
Cdd:cd05933 5 KW-HTLT----YKEYYEACRQaAKAF----LKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 151 IRQTDMQVVIVEDDGKAAMLLE---KAPRsLKIIVAIKpirqttlERARSRGIQIFSFIDVEKLGAkgnhpEVPPTAED- 226
Cdd:cd05933 76 AETSEANILVVENQKQLQKILQiqdKLPH-LKAIIQYK-------EPLKEKEPNLYSWDEFMELGR-----SIPDEQLDa 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 227 ---------LCTVCYTSGTTGNPKGVMLTHGNVV----AGVCSVILQMGDHRiraGDVMVSFLPLAH----MFErcceng 289
Cdd:cd05933 143 iissqkpnqCCTLIYTSGTTGMPKGVMLSHDNITwtakAASQHMDLRPATVG---QESVVSYLPLSHiaaqILD------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 290 MY---YVGGCVGFYSGD-IK-ELTNDLKMLKPTVMPAVPRllnrVYDKIQNDI-----SASGLKRGLFNMAMRA------ 353
Cdd:cd05933 214 IWlpiKVGGQVYFAQPDaLKgTLVKTLREVRPTAFMGVPR----VWEKIQEKMkavgaKSGTLKRKIASWAKGVgletnl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 354 KEKEIARGVLRRNGCWDKLVFKKVHQAFG-GNLRLMVVGSAPLAGNVLTFMrCALGCLVLEGYGQTECTGAITLTVQGDH 432
Cdd:cd05933 290 KLMGGESPSPLFYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 433 VPNHVGPPVSCNAVKLVdvpemeyfaNQNT---GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRI 509
Cdd:cd05933 369 RLLSCGKALPGCKTKIH---------NPDAdgiGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYI 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 510 IDRRKHIFKLSQGEYIVPEKIEN-IYTLSQYVNQVYVYGESLK--SCIIAV---VVPDT----DVLKQWATENNVRG--- 576
Cdd:cd05933 440 TGRIKELIITAGGENVPPVPIEDaVKKELPIISNAMLIGDKRKflSMLLTLkceVNPETgeplDELTEEAIEFCRKLgsq 519
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281366413 577 --TLSVLCNNKN--VKELImNDMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMY 650
Cdd:cd05933 520 atRVSEIAGGKDpkVYEAI-EEGIKRVNKKAISNAQKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
226-572 |
3.82e-55 |
|
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: 190.96 E-value: 3.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 226 DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVIlqmGDHRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFYSGDIK 305
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALA---ASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 306 ELT-NDLKMLKPTVMPAVPRLLNRvydkiqndisasglkrglfnmamrakekeiargvLRRNGCWDKLVFKkvhqafggN 384
Cdd:cd04433 78 EAAlELIEREKVTILLGVPTLLAR----------------------------------LLKAPESAGYDLS--------S 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 385 LRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHV--PNHVGPPVSCNAVKLVDvPEMEYFANQNT 462
Cdd:cd04433 116 LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVD-PDGGELPPGEI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 463 GEVCVRGSNVFHGYYKDPEKTAEAiDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIENIytLSQY--V 540
Cdd:cd04433 195 GELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAV--LLGHpgV 270
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 281366413 541 NQVYVYG---ESLKSCIIAVVVP------DTDVLKQWATEN 572
Cdd:cd04433 271 AEAAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
84-571 |
4.09e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 195.89 E-value: 4.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 163
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 D-GKAAMLLEKAPRSLKIIVAIKPirqttlERARSRGIQIFSFIDVEKLGAKGN-HPEVppTAEDLCTVCYTSGTTGNPK 241
Cdd:PRK07656 111 LfLGVDYSATTRLPALEHVVICET------EEDDPHTEKMKTFTDFLAAGDPAErAPEV--DPDDVADILFTSGTTGRPK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 242 GVMLTHGNV---VAGVCSvILQmgdhrIRAGDVMVSFLPLAHMFercCengmYYVGGCVGFYSG---------DIKELTN 309
Cdd:PRK07656 183 GAMLTHRQLlsnAADWAE-YLG-----LTEGDRYLAANPFFHVF---G----YKAGVNAPLMRGatilplpvfDPDEVFR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 310 DLKMLKPTVMPAVPRLLNRvydkiqndisasglkrgLFNMAMRAKEKeiargvLRrngcwdklvfkkvhqafggNLRLMV 389
Cdd:PRK07656 250 LIETERITVLPGPPTMYNS-----------------LLQHPDRSAED------LS-------------------SLRLAV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 390 VGSAPLAGNVLTFMRCALGC-LVLEGYGQTECTGAITLTVQGD---HVPNHVGPPVSCNAVKLVDVPEMEYFANQnTGEV 465
Cdd:PRK07656 288 TGAASMPVALLERFESELGVdIVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVNELGEEVPVGE-VGEL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 466 CVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV 545
Cdd:PRK07656 367 LVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAV 445
|
490 500 510
....*....|....*....|....*....|....*
gi 281366413 546 YG---ESLKSCIIAVVVP------DTDVLKQWATE 571
Cdd:PRK07656 446 IGvpdERLGEVGKAYVVLkpgaelTEEELIAYCRE 480
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
82-560 |
1.48e-53 |
|
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: 190.47 E-value: 1.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 82 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIirqtdmqvviV 161
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHI----------L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 162 EDDGKAAMllekaprslkiivaikpirqttlerarsrgIQIFSFIDVEKLGAKGNhPEVPPTAEDLCTVCYTSGTTGNPK 241
Cdd:cd05936 93 NDSGAKAL------------------------------IVAVSFTDLLAAGAPLG-ERVALTPEDVAVLQYTSGTTGVPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 242 GVMLTHGNVVAGVCSVILQMGDhRIRAGDVMVSFLPLAHMF-ERCCENGMYYVGGC-VGFYSGDIKELTNDLKMLKPTVM 319
Cdd:cd05936 142 GAMLTHRNLVANALQIKAWLED-LLEGDDVVLAALPLFHVFgLTVALLLPLALGATiVLIPRFRPIGVLKEIRKHRVTIF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 320 PAVPRllnrvydkiqndisasglkrgLFNMAMRAKEKEiargvlrrngcwdKLVFKkvhqafggNLRLMVVGSAPLAGNV 399
Cdd:cd05936 221 PGVPT---------------------MYIALLNAPEFK-------------KRDFS--------SLRLCISGGAPLPVEV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 400 LTFMRCALGCLVLEGYGQTECTGAITLT-VQGDHVPNHVGPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVF 473
Cdd:cd05936 259 AERFEELTGVPIVEGYGLTETSPVVAVNpLDGPRKPGSIGIPLPGTEVKIVDddgeeLPPGE------VGELWVRGPQVM 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 474 HGYYKDPEKTAEAIDsEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV-------Y 546
Cdd:cd05936 333 KGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVvgvpdpyS 410
|
490
....*....|....
gi 281366413 547 GESLKsciiAVVVP 560
Cdd:cd05936 411 GEAVK----AFVVL 420
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
193-652 |
1.24e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 190.70 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 193 ERARSRGIQIFSFIDVeklgAKGNHPEVPPTAED---LCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVIlqmgDHRIRAG 269
Cdd:PTZ00342 273 EKAKKLGISIILFDDM----TKNKTTNYKIQNEDpdfITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLC----KHSIFKK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 270 ---DVMVSFLPLAHMFERCCENGMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISA-SGLKRG 345
Cdd:PTZ00342 345 ynpKTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNlPPLKRF 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 346 LFN--MAMRAKEKeiargvlrrNGCWDKL------VFKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQ 417
Cdd:PTZ00342 425 LVKkiLSLRKSNN---------NGGFSKFlegithISSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 418 TECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMeYFANQNT--GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHT 495
Cdd:PTZ00342 496 TETTGPIFVQHADDNNTESIGGPISPNTKYKVRTWET-YKATDTLpkGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKT 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 496 GDVGMWLPNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKSCIIAVVVPDTDVLKQWATENNVR 575
Cdd:PTZ00342 575 GDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNML 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 576 GTLSVlcNNKNVKELIMND--------------MLNWGKQSGLKSFEQVKDIYLHPDPFSVQNgLLTPTFKAKRPQL--- 638
Cdd:PTZ00342 655 ESTGI--NEKNYLEKLTDEtinnniyvdyvkgkMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVfkd 731
|
490
....*....|....
gi 281366413 639 KSYFKPQLEDMYKH 652
Cdd:PTZ00342 732 YAFFIDQVKKIYKN 745
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
84-533 |
2.04e-49 |
|
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: 179.72 E-value: 2.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 163
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 DGkaamlLEKAPRSLKIIVAIKPIRQTTLERARSRGIQIFSFidvEKLGAKGNHPEVPP--TAEDLCTVCYTSGTTGNPK 241
Cdd:cd05911 91 DG-----LEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLS---PTLGEEDEDLPPPLkdGKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 242 GVMLTHGNVVAGVCSVILQMGDHrIRAGDVMVSFLPLAHMFerccenGM-----YYVGGCVG-----FYSGDIKELTNDL 311
Cdd:cd05911 163 GVCLSHRNLIANLSQVQTFLYGN-DGSNDVILGFLPLYHIY------GLfttlaSLLNGATViimpkFDSELFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 312 KMlkpTVMPAVPRLLNRvydkiqndisasglkrgLFNMAMRAKEKeiargvlrrngcwdkLvfkkvhqafgGNLRLMVVG 391
Cdd:cd05911 236 KI---TFLYLVPPIAAA-----------------LAKSPLLDKYD---------------L----------SSLRVILSG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 392 SAPLAGNVLTFMRCALG-CLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQNTGEVCVRGS 470
Cdd:cd05911 271 GAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGP 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366413 471 NVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPEKIENI 533
Cdd:cd05911 351 QVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV 412
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
53-548 |
3.73e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 179.61 E-value: 3.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 53 TLYQTFREGA-YASNngpclgwRETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSF 131
Cdd:PRK06187 7 TIGRILRHGArKHPD-------KEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 132 SLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDD--GKAAMLLEKAPRSLKIIVAIKPIRQTTLERARSrgiqiFSfidvE 209
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGE-----YE----E 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 210 KLGAKGNHPEVPPTAE-DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAHMFERccen 288
Cdd:PRK06187 151 LLAAASDTFDFPDIDEnDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWL---KLSRDDVYLVIVPMFHVHAW---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 289 GMYYVGgcvgFYSG---------DIKELTNDLKMLKPTVMPAVPRLLNrvydkiqndisasglkrglfnMAMRAKekeIA 359
Cdd:PRK06187 224 GLPYLA----LMAGakqviprrfDPENLLDLIETERVTFFFAVPTIWQ---------------------MLLKAP---RA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 360 RGVlrrngcwdklvfkkvhqAFGGnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNH--- 436
Cdd:PRK06187 276 YFV-----------------DFSS-LRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGQwtk 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 437 ---VGPPVSCNAVKLVDvPEMEYFANQN--TGEVCVRGSNVFHGYYKDPEKTAEAIDSeGWHHTGDVGMWLPNGTLRIID 511
Cdd:PRK06187 338 rrsAGRPLPGVEARIVD-DDGDELPPDGgeVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITD 415
|
490 500 510
....*....|....*....|....*....|....*....
gi 281366413 512 RRKHIFKlSQGEYIVPEKIENIytLSQY--VNQVYVYGE 548
Cdd:PRK06187 416 RIKDVII-SGGENIYPRELEDA--LYGHpaVAEVAVIGV 451
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
83-572 |
6.30e-46 |
|
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: 170.19 E-value: 6.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 83 WINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVE 162
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 163 DDGKAAmLLEKAPRSLKIIVAIkpirqtTLERARSRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKG 242
Cdd:cd05926 94 KGELGP-ASRAASKLGLAILEL------ALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 243 VMLTHGNVVAGVCSVIlqmGDHRIRAGDVMVSFLPLAHMfercceNGM-------YYVGGCV----GFysgDIKELTNDL 311
Cdd:cd05926 167 VPLTHRNLAASATNIT---NTYKLTPDDRTLVVMPLFHV------HGLvasllstLAAGGSVvlppRF---SASTFWPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 312 KMLKPTVMPAVPRLLnrvydKIqndisasglkrgLFNMAMRAKEKEIARgvlrrngcwdklvfkkvhqafggnLRLMVVG 391
Cdd:cd05926 235 RDYNATWYTAVPTIH-----QI------------LLNRPEPNPESPPPK------------------------LRFIRSC 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 392 SAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLT--VQGDHVPNHVGPPVscnAVKLVDVPEM-EYFANQNTGEVCVR 468
Cdd:cd05926 274 SASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKPV---GVEVRILDEDgEILPPGVVGEICLR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 469 GSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVYV--- 545
Cdd:cd05926 351 GPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEAVAfgv 429
|
490 500 510
....*....|....*....|....*....|....*..
gi 281366413 546 ----YGESlkscIIAVVVP------DTDVLKQWATEN 572
Cdd:cd05926 430 pdekYGEE----VAAAVVLregasvTEEELRAFCRKH 462
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
92-561 |
3.52e-40 |
|
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: 152.76 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 92 RAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIveddgkaamll 171
Cdd:cd17631 29 RVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF----------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 172 ekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaEDLCTVCYTSGTTGNPKGVMLTHGNVV 251
Cdd:cd17631 98 -----------------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 252 AGVCSVILQMGdhrIRAGDVMVSFLPLAHmferCCENGMY-----YVGGCV----GFysgDIKELTNDLKMLKPTVMPAV 322
Cdd:cd17631 125 WNAVNALAALD---LGPDDVLLVVAPLFH----IGGLGVFtlptlLRGGTVvilrKF---DPETVLDLIERHRVTSFFLV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 323 PRLLNRVYDkiqndisasglkrglfnmamrakekeiargvlrrngcwdklvfkkvHQAFGG----NLRLMVVGSAPLAGN 398
Cdd:cd17631 195 PTMIQALLQ----------------------------------------------HPRFATtdlsSLRAVIYGGAPMPER 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 399 VLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHV--PNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGY 476
Cdd:cd17631 229 LLRALQ-ARGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGPHVMAGY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 477 YKDPEKTAEAIDsEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIEN-IYTLSQyVNQVYV-------YGE 548
Cdd:cd17631 307 WNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDvLYEHPA-VAEVAVigvpdekWGE 383
|
490
....*....|...
gi 281366413 549 SlkscIIAVVVPD 561
Cdd:cd17631 384 A----VVAVVVPR 392
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
84-547 |
1.39e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 142.05 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVed 163
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 dgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaeDLCTVCYTSGTTGNPKGV 243
Cdd:cd05934 82 --------------------------------------------------------------DPASILYTSGTTGPPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 244 MLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMfeRCCENGMY---YVGGCV---------GFYSgDIKE----L 307
Cdd:cd05934 100 VITHANLTFAGYYSARRFG---LGEDDVYLTVLPLFHI--NAQAVSVLaalSVGATLvllprfsasRFWS-DVRRygatV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 308 TNDLKMLKPTVMPAVPRllnrvydkiQNDisasglkrglfnmamrakekeiargvlRRNgcwdklvfkkvhqafggnlRL 387
Cdd:cd05934 174 TNYLGAMLSYLLAQPPS---------PDD---------------------------RAH-------------------RL 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 388 MVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCV 467
Cdd:cd05934 199 RAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEPGELVI 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 468 R---GSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVY 544
Cdd:cd05934 278 RglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVREAA 355
|
...
gi 281366413 545 VYG 547
Cdd:cd05934 356 VVA 358
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
84-518 |
2.04e-36 |
|
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: 143.14 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVed 163
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 dgkAAMLLEKAPRSLKIIVaikpirqtTLERARSRGIQIFSFIDVEKLGAKgnhPEVPPTAEDLCTVCYTSGTTGNPKGV 243
Cdd:cd05904 111 ---TAELAEKLASLALPVV--------LLDSAEFDSLSFSDLLFEADEAEP---PVVVIKQDDVAALLYSSGTTGRSKGV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 244 MLTHGNVVAGVCSVILQMGDHRIRaGDVMVSFLPLAHMFERC-CENGMYYVGGCV----GFysgDIKELTNDLKMLKPTV 318
Cdd:cd05904 177 MLTHRNLIAMVAQFVAGEGSNSDS-EDVFLCVLPMFHIYGLSsFALGLLRLGATVvvmpRF---DLEELLAAIERYKVTH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 319 MPAVPRLLnrvydkiqndisasglkrglfnMAMRAKEKEiargvlrrngcwDKLVFKKVHQafggnlrlMVVGSAPLAGN 398
Cdd:cd05904 253 LPVVPPIV----------------------LALVKSPIV------------DKYDLSSLRQ--------IMSGAAPLGKE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 399 VL-TFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGppvSC-----NA-VKLVDvPE--MEYFANQnTGEVCVRG 469
Cdd:cd05904 291 LIeAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAKYG---SVgrlvpNVeAKIVD-PEtgESLPPNQ-TGELWIRG 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 281366413 470 SNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFK 518
Cdd:cd05904 366 PSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIK 414
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
99-547 |
5.01e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 139.91 E-value: 5.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 99 GMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKA----AMLLEKA 174
Cdd:PRK12583 61 GLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTsdyhAMLQELL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 175 PR-SLKIIVAIKPIRQTTLERARSRGIQ----IFSFIDVEKLG-----AKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVM 244
Cdd:PRK12583 141 PGlAEGQPGALACERLPELRGVVSLAPApppgFLAWHELQARGetvsrEALAERQASLDRDDPINIQYTSGTTGFPKGAT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 245 LTHGNVV--AGVCSVILQMGDHriragDVMVSFLPLAHMFerccengmyyvgGCVgfysgdikeLTNDLKMLKPTVMpav 322
Cdd:PRK12583 221 LSHHNILnnGYFVAESLGLTEH-----DRLCVPVPLYHCF------------GMV---------LANLGCMTVGACL--- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 323 prllnrVYDKIQNDISASglkrglfnmaMRAKEKEIARGVlrrNGCWDKLVFKKVHQAFG----GNLRLMVVGSAP---- 394
Cdd:PRK12583 272 ------VYPNEAFDPLAT----------LQAVEEERCTAL---YGVPTMFIAELDHPQRGnfdlSSLRTGIMAGAPcpie 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 395 LAGNVLTFMRCALgclVLEGYGQTECTGAITLTVQGDHVPNH---VGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSN 471
Cdd:PRK12583 333 VMRRVMDEMHMAE---VQIAYGMTETSPVSLQTTAADDLERRvetVGRTQPHLEVKVVD-PDGATVPRGEIGELCTRGYS 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281366413 472 VFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYG 547
Cdd:PRK12583 409 VMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
226-571 |
5.86e-35 |
|
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: 137.81 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 226 DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAHMfercceNGMY-------YVGGCVG 298
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAW---RWTEDDVLLHVLPLHHV------HGLVnallcplFAGASVE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 299 FYSGDIKELTNDLKMLKP-TVMPAVPRllnrVYDKIQNDISASglkrglfnmamrAKEKEIARGVLRRNgcwdklvfkkv 377
Cdd:cd05941 161 FLPKFDPKEVAISRLMPSiTVFMGVPT----IYTRLLQYYEAH------------FTDPQFARAAAAER----------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 378 hqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYF 457
Cdd:cd05941 214 -------LRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 458 ANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRK-HIFKlSQGEYIVPEKIENiyTL 536
Cdd:cd05941 287 PRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIER--VL 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 281366413 537 SQY--VNQVYVYGESLKS---CIIAVVVP-------DTDVLKQWATE 571
Cdd:cd05941 364 LAHpgVSECAVIGVPDPDwgeRVVAVVVLragaaalSLEELKEWAKQ 410
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
225-555 |
9.38e-34 |
|
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: 132.40 E-value: 9.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 225 EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDhriRAGDVMvsflplahmferCCENGMYYVGGCVGfysGDI 304
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGL---TEQDRL------------CIPVPLFHCFGSVL---GVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 305 KELTNDLKMLKP------------------TVMPAVP----RLLNRVyDKIQNDISAsglkrglfnmamrakekeIARGV 362
Cdd:cd05917 64 ACLTHGATMVFPspsfdplavleaiekekcTALHGVPtmfiAELEHP-DFDKFDLSS------------------LRTGI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 363 LRRNGCWDKLVfKKVHQAFggNLRLMVVGsaplagnvltfmrcalgclvlegYGQTECTGAITLTVQGDHVP---NHVGP 439
Cdd:cd05917 125 MAGAPCPPELM-KRVIEVM--NMKDVTIA-----------------------YGMTETSPVSTQTRTDDSIEkrvNTVGR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 440 PVSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkL 519
Cdd:cd05917 179 IMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-I 257
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 281366413 520 SQGEYIVPEKIEN-IYTLsQYVNQVYV-------YGESLKSCII 555
Cdd:cd05917 258 RGGENIYPREIEEfLHTH-PKVSDVQVvgvpderYGEEVCAWIR 300
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
98-572 |
1.92e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 132.43 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 98 AGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVV---PLYDT---LGP--DACAfiirqtdmQVVIVEDdgKAAM 169
Cdd:PRK05605 72 AGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLYTAhelEHPfeDHGA--------RVAIVWD--KVAP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 170 LLEKAPR--------SLKIIVAIKPIRQTTLE----RARSRGIQIFS----FIDVEKL--------GAKGNHPEvpPTAE 225
Cdd:PRK05605 142 TVERLRRttpletivSVNMIAAMPLLQRLALRlpipALRKARAALTGpapgTVPWETLvdaaiggdGSDVSHPR--PTPD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 226 DLCTVCYTSGTTGNPKGVMLTHGNVVAGvcsviLQMGDH---RIRAGD-VMVSFLPLAHMF--ERCCENGMYYVGGCVGF 299
Cdd:PRK05605 220 DVALILYTSGTTGKPKGAQLTHRNLFAN-----AAQGKAwvpGLGDGPeRVLAALPMFHAYglTLCLTLAVSIGGELVLL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 300 YSGDIKELTNDLKMLKPTVMPAVPRLlnrvYDKI-----QNDISASGLkRGLFNMAMRAKEKEIARgvlrrngcWDKLVf 374
Cdd:PRK05605 295 PAPDIDLILDAMKKHPPTWLPGVPPL----YEKIaeaaeERGVDLSGV-RNAFSGAMALPVSTVEL--------WEKLT- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 375 kkvhqafGGNLrlmvvgsaplagnvltfmrcalgclvLEGYGQTECTGAITLTVQGDHV-PNHVGPPVSCNAVKLVDvPE 453
Cdd:PRK05605 361 -------GGLL--------------------------VEGYGLTETSPIIVGNPMSDDRrPGYVGVPFPDTEVRIVD-PE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 454 --MEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIE 531
Cdd:PRK05605 407 dpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVE 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 281366413 532 NIYTLSQYVNQVYVYG-------ESLKSCIIAV--VVPDTDVLKQWATEN 572
Cdd:PRK05605 485 EVLREHPGVEDAAVVGlpredgsEEVVAAVVLEpgAALDPEGLRAYCREH 534
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
51-650 |
8.37e-32 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 132.67 E-value: 8.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 51 VRTLYQTFREGAYASNNGPCLGWRETLTSPyQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYS 130
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGES-EWLTYGTVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVACAL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 131 FSLVVVPLYDTlgPDACAFIIRQTDMQVViVEDDGKAAMLLEKAPRSLKIIVAIKPIRQTTLER-ARSRGIQIFSFIDVE 209
Cdd:PTZ00297 505 YGFTTLPLVGK--GSTMRTLIDEHKIKVV-FADRNSVAAILTCRSRKLETVVYTHSFYDEDDHAvARDLNITLIPYEFVE 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 210 KlgaKGNHPEVPP----TAEDLCTVCY---TSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIRAGDVMVSFLPLAHMF 282
Cdd:PTZ00297 582 Q---KGRLCPVPLkehvTTDTVFTYVVdntTSASGDGLAVVRVTHADVLRDISTLVMTGVLPSSFKKHLMVHFTPFAMLF 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 283 ERCCENGMYYVGGCVGfySGDIKELTNDLKMLKPTVMPAVPRLLNrvydkiqndISASGLKRG----------LFNMAMR 352
Cdd:PTZ00297 659 NRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSLFS---------TSRLQLSRAnerysavyswLFERAFQ 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 353 AKEKEIarGVLRRNGCWDKLVFKKVHQ-AFGGNLRLMVVGSA------PLAGNVLTfmrCALGCLVLEGYgqTECTGAIT 425
Cdd:PTZ00297 728 LRSRLI--NIHRRDSSLLRFIFFRATQeLLGGCVEKIVLCVSeestsfSLLEHISV---CYVPCLREVFF--LPSEGVFC 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 426 LtvqgDHVPnhvGPPVScnavklVDVPEMEYFANQNT-GEVCV--RGsnvfhgyykDPEKTAEAidsegwhhtgdVGMWL 502
Cdd:PTZ00297 801 V----DGTP---APSLQ------VDLEPFDEPSDGAGiGQLVLakKG---------EPRRTLPI-----------AAQWK 847
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 503 PNGTLRIIDRRKHIFKLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLKScIIAVVVPDTDVLK-QW--ATENNVRGTLS 579
Cdd:PTZ00297 848 RDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWrqSHCMGEGGGPA 926
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366413 580 VLCNNKNVKE----LIMNDMLNWGKQSGLKSFEQVKDIYLHPDPFSVQNGLLTPTFKAKRPQLKSYFKPQLEDMY 650
Cdd:PTZ00297 927 RQLGWTELVAyassLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
209-555 |
1.77e-31 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 129.33 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 209 EKLGAKGNHPEVPPTaeDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIraGDVM-VSFLPLAHMFER--- 284
Cdd:PLN02330 170 DRAGDTSDNEEILQT--DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMI--GQVVtLGLIPFFHIYGItgi 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 285 CCENgMYYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRL-LNRVYDKIQNDISASGLKrglfnmamrakekeiargvl 363
Cdd:PLN02330 246 CCAT-LRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIiLNLVKNPIVEEFDLSKLK-------------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 364 rrngcwdklvfkkvhqafggnLRLMVVGSAPLAGNVLT-FMRCALGCLVLEGYGQTECTgAITLTV------QGDHVPNH 436
Cdd:PLN02330 305 ---------------------LQAIMTAAAPLAPELLTaFEAKFPGVQVQEAYGLTEHS-CITLTHgdpekgHGIAKKNS 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 437 VGPPVSCNAVKLVDvPEMEYFANQNT-GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKH 515
Cdd:PLN02330 363 VGFILPNLEVKFID-PDTGRSLPKNTpGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKE 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 281366413 516 IFKLsQGEYIVPEKIENIYTLSQYVNQVYVY-------GESLKSCII 555
Cdd:PLN02330 442 LIKY-KGFQVAPAELEAILLTHPSVEDAAVVplpdeeaGEIPAACVV 487
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
201-533 |
3.61e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 128.40 E-value: 3.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 201 QIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHR------IRAG-DVMV 273
Cdd:PRK12492 183 QAVPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGpdgqplMKEGqEVMI 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 274 SFLPLAHMFErccengmyYVGGCVGFY-SGDIKEL-TNdlkmlkptvmpavPRLLNRVYDKIQN-DISAS-GLKRgLFNM 349
Cdd:PRK12492 263 APLPLYHIYA--------FTANCMCMMvSGNHNVLiTN-------------PRDIPGFIKELGKwRFSALlGLNT-LFVA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 350 AMRAKEkeiargvlrrngcwdklvFKKVHQAfggNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQ 429
Cdd:PRK12492 321 LMDHPG------------------FKDLDFS---ALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPY 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 430 GDHVP-NHVGPPVSCNAVKLVDVPEMEYFANQNtGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLR 508
Cdd:PRK12492 380 GELARlGTVGIPVPGTALKVIDDDGNELPLGER-GELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVR 458
|
330 340
....*....|....*....|....*
gi 281366413 509 IIDRRKHIFKLSqGEYIVPEKIENI 533
Cdd:PRK12492 459 IVDRKKDLIIVS-GFNVYPNEIEDV 482
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
86-562 |
1.60e-30 |
|
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: 124.80 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 86 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRqtdmqvvivedDG 165
Cdd:cd05903 4 YSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILR-----------RA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 166 KAAMLLekAPRSLKiivaikpirqttlerarsrgiqifsfidveklgaKGNHPEVPptaEDLCTVCYTSGTTGNPKGVML 245
Cdd:cd05903 73 KAKVFV--VPERFR----------------------------------QFDPAAMP---DAVALLLFTSGTTGEPKGVMH 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 246 THGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMferccengmyyvggcVGFYSGdikeltndlkMLKPTVMPAvPRL 325
Cdd:cd05903 114 SHNTLSASIRQYAERLG---LGPGDVFLVASPMAHQ---------------TGFVYG----------FTLPLLLGA-PVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 326 LNRVYDkiqndisasglkrglfnmAMRAKEkeiargVLRRNGC---------WDKLVfkkVHQAFGG----NLRLMVVGS 392
Cdd:cd05903 165 LQDIWD------------------PDKALA------LMREHGVtfmmgatpfLTDLL---NAVEEAGeplsRLRTFVCGG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 393 APLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDhvPNHV----GPPVSCNAVKLVDVPEMEYFANQnTGEVCVR 468
Cdd:cd05903 218 ATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAP--EDRRlytdGRPLPGVEIKVVDDTGATLAPGV-EGELLSR 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 469 GSNVFHGYYKDPEKTAEAiDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYG- 547
Cdd:cd05903 295 GPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAl 372
|
490
....*....|....*..
gi 281366413 548 --ESLKSCIIAVVVPDT 562
Cdd:cd05903 373 pdERLGERACAVVVTKS 389
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
87-560 |
2.98e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 125.43 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 87 DEALLRAknfGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDgk 166
Cdd:PRK08316 43 DAAVNRV---AAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPA-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 167 aamLLEKAPRSLkiivAIKPIRQTTLERARSRGIQIFSFIDVEKLGAKGN--HPEVPPTAEDLCTVCYTSGTTGNPKGVM 244
Cdd:PRK08316 118 ---LAPTAEAAL----ALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSvaEPDVELADDDLAQILYTSGTESLPKGAM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 245 LTHGNVVAGVCSVILqmgDHRIRAGDVMVSFLPLAHMFERCCENGMY-YVGGcvgfysgdikelTNdlkmlkpTVM--PA 321
Cdd:PRK08316 191 LTHRALIAEYVSCIV---AGDMSADDIPLHALPLYHCAQLDVFLGPYlYVGA------------TN-------VILdaPD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 322 VPRLLNRVydkiqndisasglkrglfnmamrakEKEIAR----------GVLRrngcwdklvfkkvHQAFG----GNLRL 387
Cdd:PRK08316 249 PELILRTI-------------------------EAERITsffapptvwiSLLR-------------HPDFDtrdlSSLRK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 388 MVVGSAPLAGNVLTFMRCAL-GCLVLEGYGQTECtgAITLTVQG--DHV--PNHVGPPVSCNAVKLVDvPEMEYFANQNT 462
Cdd:PRK08316 291 GYYGASIMPVEVLKELRERLpGLRFYNCYGQTEI--APLATVLGpeEHLrrPGSAGRPVLNVETRVVD-DDGNDVAPGEV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 463 GEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIEN-IYTLSQyVN 541
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIK-TGGENVASREVEEaLYTHPA-VA 444
|
490 500
....*....|....*....|....*.
gi 281366413 542 QVYVYG-------ESlkscIIAVVVP 560
Cdd:PRK08316 445 EVAVIGlpdpkwiEA----VTAVVVP 466
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
201-535 |
1.79e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 123.33 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 201 QIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIRAGDVMVSFLPLAH 280
Cdd:PRK05677 183 QAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIAPLPLYH 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 281 MFerccengmyyvggCVGFYSGDIKELTN-DLKMLKPTVMPAVPRLLNRvydkiQNDISASGLKRgLFNmamrakekeia 359
Cdd:PRK05677 263 IY-------------AFTFHCMAMMLIGNhNILISNPRDLPAMVKELGK-----WKFSGFVGLNT-LFV----------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 360 rgVLRRNGCWDKLVFKKvhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGP 439
Cdd:PRK05677 313 --ALCNNEAFRKLDFSA--------LKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 440 PVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKL 519
Cdd:PRK05677 383 PVPSTLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILV 461
|
330
....*....|....*.
gi 281366413 520 SqGEYIVPEKIENIYT 535
Cdd:PRK05677 462 S-GFNVYPNELEDVLA 476
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
141-533 |
1.95e-29 |
|
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: 122.44 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 141 TLGPDACAFIIRQTDMQVVIVeddgkAAMLLEKApRSLKIIVAIKPIRQTTLERARSR-----GIQIFSFIDVEKLGAKG 215
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLT-----SKQFIEKL-KLHHLFDVEYDARIVYLEDLRAKiskadKCKAFLAGKFPPKWLLR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 216 NHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGV--CSVILqmgdhRIRAGDVMVSFLPLAHMFerccengmyyv 293
Cdd:cd05909 138 IFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeqITAIF-----DPNPEDVVFGALPFFHSF----------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 294 ggcvGFYSGDIKELTNDLKML---KPTVMPAVPRLlnrVYD-KIQNDISASGLKRGLFNmamRAKEKEIARgvlrrngcw 369
Cdd:cd05909 202 ----GLTGCLWLPLLSGIKVVfhpNPLDYKKIPEL---IYDkKATILLGTPTFLRGYAR---AAHPEDFSS--------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 370 dklvfkkvhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITL-TVQGDHVPNHVGPPVSCNAVKL 448
Cdd:cd05909 263 ---------------LRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVnTPQSPNKEGTVGRPLPGMEVKI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 449 VDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPE 528
Cdd:cd05909 328 VSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLE 405
|
....*
gi 281366413 529 KIENI 533
Cdd:cd05909 406 AIEDI 410
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
208-531 |
3.52e-29 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 121.91 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 208 VEKLGAKG-------------NHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGvcSVILQmgDH-RIRAGDVMV 273
Cdd:PRK07514 126 VETLDADGtgslleaaaaapdDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSN--ALTLV--DYwRFTPDDVLI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 274 SFLPLAH---MFERCceNGMYYVGGCVGFYSG-DIKELTNdlKMLKPTVMPAVP----RLLnrvydkiQNDisasGLKRg 345
Cdd:PRK07514 202 HALPIFHthgLFVAT--NVALLAGASMIFLPKfDPDAVLA--LMPRATVMMGVPtfytRLL-------QEP----RLTR- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 346 lfnmamrakekEIARgvlrrngcwdklvfkkvhqafggNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAIT 425
Cdd:PRK07514 266 -----------EAAA-----------------------HMRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 426 LT-VQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPN 504
Cdd:PRK07514 311 SNpYDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDER 390
|
330 340
....*....|....*....|....*..
gi 281366413 505 GTLRIIDRRKHIFkLSQGEYIVPEKIE 531
Cdd:PRK07514 391 GYVHIVGRGKDLI-ISGGYNVYPKEVE 416
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
218-556 |
1.18e-28 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 120.93 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 218 PEVppTAEDLCTVCYTSGTTGNPKGVMLTHGNVVA------GVCSVILQMGDhriragDVMVSFLPLAHMFERCCeNGMY 291
Cdd:PRK08974 201 PEL--VPEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleqakAAYGPLLHPGK------ELVVTALPLYHIFALTV-NCLL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 292 YV--GGCVGFYSG--DIKELTNDLKMLKPTVMPAVprllnrvydkiqndisasglkRGLFNMAMRAKEkeiargvlrrng 367
Cdd:PRK08974 272 FIelGGQNLLITNprDIPGFVKELKKYPFTAITGV---------------------NTLFNALLNNEE------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 368 cwdklvFKKVHqaFGgNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLT-VQGDHVPNHVGPPVSCNAV 446
Cdd:PRK08974 319 ------FQELD--FS-SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNpYDLDYYSGSIGLPVPSTEI 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 447 KLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIV 526
Cdd:PRK08974 390 KLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVS-GFNVY 466
|
330 340 350
....*....|....*....|....*....|....*..
gi 281366413 527 PEKIENIYTLSQYVNQVY-------VYGESLKSCIIA 556
Cdd:PRK08974 467 PNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
220-533 |
7.04e-28 |
|
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: 118.01 E-value: 7.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 220 VPPTA---EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIRAGDVMVSFLPLAHMFerccenGMYYVGG- 295
Cdd:cd17642 176 KPPSFdrdEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHGF------GMFTTLGy 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 296 -CVGF-----YSGDIKELTNDLKMLKPTVMPAVPRLlnrvydkiqndisasglkrglfnMAMRAKEKEIARGVLrrngcw 369
Cdd:cd17642 250 lICGFrvvlmYKFEEELFLRSLQDYKVQSALLVPTL-----------------------FAFFAKSTLVDKYDL------ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 370 dklvfkkvhqafgGNLRLMVVGSAPLAGNV---------LTFMRcalgclvlEGYGQTECTGAITLTVQGDHVPNHVGPP 440
Cdd:cd17642 301 -------------SNLHEIASGGAPLSKEVgeavakrfkLPGIR--------QGYGLTETTSAILITPEGDDKPGAVGKV 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 441 VSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLs 520
Cdd:cd17642 360 VPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY- 438
|
330
....*....|...
gi 281366413 521 QGEYIVPEKIENI 533
Cdd:cd17642 439 KGYQVPPAELESI 451
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
168-531 |
8.17e-28 |
|
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: 116.21 E-value: 8.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 168 AMLLEKAprSLKIIVAIKPIRQTTLERARSRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTH 247
Cdd:TIGR01733 65 AFILEDA--GARLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTH 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 248 GNVVAgvcsVILQMGDHRI-RAGDVMVSFLPLAH------MFerccenGMYYVGGCVGFYSGDikeltndlkMLKPTvmp 320
Cdd:TIGR01733 143 RSLVN----LLAWLARRYGlDPDDRVLQFASLSFdasveeIF------GALLAGATLVVPPED---------EERDD--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 321 avPRLLNRVYDkiQNDISASGLKRGLFNMAMRAKEKEIARgvlrrngcwdklvfkkvhqafggnLRLMVV-GSAPLAGNV 399
Cdd:TIGR01733 201 --AALLAALIA--EHPVTVLNLTPSLLALLAAALPPALAS------------------------LRLVILgGEALTPALV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 400 LTFMRCALGCLVLEGYGQTECTGAITLTVQGDH-----VPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFH 474
Cdd:TIGR01733 253 DRWRARGPGARLINLYGPTETTVWSTATLVDPDdapreSPVPIGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVAR 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366413 475 GYYKDPEKTAEAI--------DSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIE 531
Cdd:TIGR01733 332 GYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIR-GYRIELGEIE 395
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
102-564 |
1.25e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 117.39 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 102 ALGARPKQLIGIYSQNRPE-WILYEQGCYSfSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDD---GKAAMLLEKAPrS 177
Cdd:PRK06188 56 ALGLGTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALHPLGSLDDHAYVLEDAGISTLIVDPApfvERALALLARVP-S 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 178 LKIIVAIKPirqttLERARSRGIQIFSFidveklgakGNHPEVPPTA-EDLCTVCYTSGTTGNPKGVMLTHGNVVAgvcS 256
Cdd:PRK06188 134 LKHVLTLGP-----VPDGVDLLAAAAKF---------GPAPLVAAALpPDIAGLAYTGGTTGKPKGVMGTHRSIAT---M 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 257 VILQMGDHRIRAGDVMVSFLPLAHMfercceNGMYYV-----GGCV----GFYSGD----IKELTNDLKMLKPTVMPAV- 322
Cdd:PRK06188 197 AQIQLAEWEWPADPRFLMCTPLSHA------GGAFFLptllrGGTVivlaKFDPAEvlraIEEQRITATFLVPTMIYALl 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 323 --PRLLNRvydkiqnDISAsglkrglfnmamrakekeiargvlrrngcwdklvfkkvhqafggnLRLMVVGSAPLAGNVL 400
Cdd:PRK06188 271 dhPDLRTR-------DLSS---------------------------------------------LETVYYGASPMSPVRL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 401 TFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHV------GPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFH 474
Cdd:PRK06188 299 AEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-EDGREVAQGEVGEICVRGPLVMD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 475 GYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV-------YG 547
Cdd:PRK06188 378 GYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWG 455
|
490
....*....|....*..
gi 281366413 548 ESLKsciiAVVVPDTDV 564
Cdd:PRK06188 456 EAVT----AVVVLRPGA 468
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
226-547 |
1.50e-27 |
|
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: 113.75 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 226 DLCTVCYTSGTTGNPKGVMLTHGNVVaGVCSVILQMGDhrIRAGDVMVSFLPLAHMFerccengmyyvggcvGFYSGDIK 305
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL-RAAAAWADCAD--LTEDDRYLIINPFFHTF---------------GYKAGIVA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 306 ELTNDLKMLkPTVMPAVPRLLNRVY-DKIQNDISASGLKRGLFNMAMRAKEKEiargvlrrngcwdklvfkkvhqafgGN 384
Cdd:cd17638 63 CLLTGATVV-PVAVFDVDAILEAIErERITVLPGPPTLFQSLLDHPGRKKFDL-------------------------SS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 385 LRLMVVGSAPLAGNVLTFMRCALGC-LVLEGYGQTECtGAITLTVQGDH---VPNHVGPPVSCNAVKLVDvpemeyfanq 460
Cdd:cd17638 117 LRAAVTGAATVPVELVRRMRSELGFeTVLTAYGLTEA-GVATMCRPGDDaetVATTCGRACPGFEVRIAD---------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 461 nTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYV 540
Cdd:cd17638 186 -DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHPGV 263
|
....*..
gi 281366413 541 NQVYVYG 547
Cdd:cd17638 264 AQVAVIG 270
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
205-561 |
1.62e-27 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 117.29 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 205 FIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGV--CSVILQMGDHRIRAGDVMVSFLPLAHMF 282
Cdd:PRK08751 188 FREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqAHQWLAGTGKLEEGCEVVITALPLYHIF 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 283 ErCCENGMYY--VGGCVGFYSG--DIKELTNDLKMLKPTVMPAVPRLLNrvydkiqndisasglkrglfnmamrakekei 358
Cdd:PRK08751 268 A-LTANGLVFmkIGGCNHLISNprDMPGFVKELKKTRFTAFTGVNTLFN------------------------------- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 359 arGVLRRNGcWDKLVFKKVHQAFGGNlrlMVVGSAplagnVLTFMRCALGCLVLEGYGQTE-----CTGAITLtvqgDHV 433
Cdd:PRK08751 316 --GLLNTPG-FDQIDFSSLKMTLGGG---MAVQRS-----VAERWKQVTGLTLVEAYGLTEtspaaCINPLTL----KEY 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 434 PNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRR 513
Cdd:PRK08751 381 NGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRK 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 281366413 514 KHIFKLSqGEYIVPEKIENIYTLSQYVNQVyvygeslksciIAVVVPD 561
Cdd:PRK08751 460 KDMILVS-GFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPD 495
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
221-512 |
1.16e-26 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 116.18 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 221 PPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGvcsvILQMGD-HRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGF 299
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDvFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 300 YSGDIKELTNDLKML---KPTVMPAVPRLLnRVYdkiqndisasglkrglfnmamrakekeiargvLRRngcwdklvfKK 376
Cdd:PRK08633 854 YHPDPTDALGIAKLVakhRATILLGTPTFL-RLY--------------------------------LRN---------KK 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 377 VHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITL----------TVQGDHVPNHVGPPVSCNAV 446
Cdd:PRK08633 892 LHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVnlpdvlaadfKRQTGSKEGSVGMPLPGVAV 971
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281366413 447 KLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI---DSEGWHHTGDVGMWLPNGTLRIIDR 512
Cdd:PRK08633 972 RIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
74-555 |
1.26e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 114.52 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 74 RETLTSPYQWI--NYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVV---PLYDT--Lgpda 146
Cdd:PRK08315 32 REALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVtinPAYRLseL---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 147 cAFIIRQTDMQVVIVEDDGK----AAMLLEKAPRsLKIIV--AIKPIRQTTLER------ARSRGIqiFSFIDVEKLGAK 214
Cdd:PRK08315 108 -EYALNQSGCKALIAADGFKdsdyVAMLYELAPE-LATCEpgQLQSARLPELRRviflgdEKHPGM--LNFDELLALGRA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 215 GNHPEVPPTAEDL-----CTVCYTSGTTGNPKGVMLTHGNVVAGVCSVilqmGDH-RIRAGDVMVSFLPLAHMFerccen 288
Cdd:PRK08315 184 VDDAELAARQATLdpddpINIQYTSGTTGFPKGATLTHRNILNNGYFI----GEAmKLTEEDRLCIPVPLYHCF------ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 289 gmyyvgGCVgfySGDIKELTNDLKMLKP-------TVMPAV---------------------PRLLNrvYDkiqndisAS 340
Cdd:PRK08315 254 ------GMV---LGNLACVTHGATMVYPgegfdplATLAAVeeerctalygvptmfiaeldhPDFAR--FD-------LS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 341 GLKRGLfnMAmrakekeiarG------VLRRngcwdklVFKKVHqafggnlrlmvvgsaplagnvltfMRcalgcLVLEG 414
Cdd:PRK08315 316 SLRTGI--MA----------GspcpieVMKR-------VIDKMH------------------------MS-----EVTIA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 415 YGQTECTGAITLTVQGDHVPNHVG------PPVScnaVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAID 488
Cdd:PRK08315 348 YGMTETSPVSTQTRTDDPLEKRVTtvgralPHLE---VKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAID 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366413 489 SEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIEN-IYTLSQyVNQVYV-------YGESLKSCII 555
Cdd:PRK08315 425 ADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEfLYTHPK-IQDVQVvgvpdekYGEEVCAWII 497
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
222-560 |
1.40e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 114.38 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 222 PTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMferccengmyyvggcVGFYS 301
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG---LGADDVILMASPMAHQ---------------TGFMY 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 302 GdikeltndlkMLKPTVMPAvprllNRVYDKIQNDISASGLKR--GL-FNMAMRAKEKEIARGVlrrngcwdKLVFKKVH 378
Cdd:PRK13295 256 G----------LMMPVMLGA-----TAVLQDIWDPARAAELIRteGVtFTMASTPFLTDLTRAV--------KESGRPVS 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 379 QafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECtGAITLTVQGD---HVPNHVGPPVSCNAVKLVDVPEME 455
Cdd:PRK13295 313 S-----LRTFLCAGAPIPGALVERARAALGAKIVSAWGMTEN-GAVTLTKLDDpdeRASTTDGCPLPGVEVRVVDADGAP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 456 YFANQnTGEVCVRGSNVFHGYYKDPEKTAEaiDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYT 535
Cdd:PRK13295 387 LPAGQ-IGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLY 462
|
330 340
....*....|....*....|....*...
gi 281366413 536 LSQYVNQVYVYG---ESLKSCIIAVVVP 560
Cdd:PRK13295 463 RHPAIAQVAIVAypdERLGERACAFVVP 490
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
72-512 |
2.73e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 113.67 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 72 GWRETLTspyqwinYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWI---LyeqGCYSFSLVVVPLYDTLGPDACA 148
Cdd:COG0365 35 GEERTLT-------YAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAViamL---ACARIGAVHSPVFPGFGAEALA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 149 FIIRQTDMQVVIVEDDG-----------KAAMLLEKAPRSLKIIVAikpirQTTLERARSRGiqifsFIDVEKL--GAKG 215
Cdd:COG0365 105 DRIEDAEAKVLITADGGlrggkvidlkeKVDEALEELPSLEHVIVV-----GRTGADVPMEG-----DLDWDELlaAASA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 216 NHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdHRIRAGDVMVSFLPLA----HMfercceNGMY 291
Cdd:COG0365 175 EFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV--LDLKPGDVFWCTADIGwatgHS------YIVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 292 ---YVGGCVGFYSGdiKELTND----LKML---KPTVMPAVPrllnrvydkiqndisasglkrGLFNMAMRAKEKEIARG 361
Cdd:COG0365 247 gplLNGATVVLYEG--RPDFPDpgrlWELIekyGVTVFFTAP---------------------TAIRALMKAGDEPLKKY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 362 VLRRngcwdklvfkkvhqafggnLRLMV-VGSaPLagNVLTFMRC--ALGCLVLEGYGQTECTGAITLTVQGDHV-PNHV 437
Cdd:COG0365 304 DLSS-------------------LRLLGsAGE-PL--NPEVWEWWyeAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSM 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 438 GPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSN--VFHGYYKDPEKTAEAI--DSEGWHHTGDVGMWLPNGTLR 508
Cdd:COG0365 362 GKPVPGYDVAVVDedgnpVPPGE------EGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFW 435
|
....
gi 281366413 509 IIDR 512
Cdd:COG0365 436 ILGR 439
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
206-564 |
3.96e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 112.01 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 206 IDVEkLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVcsvilqmgDHRIRA-----GDVMVSFLPLAH 280
Cdd:PRK07787 110 VPVR-LHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADL--------DALAEAwqwtaDDVLVHGLPLFH 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 281 mferccengmyyVGGCVgfysgdikeltndLKMLKPTvmpavpRLLNRVYD--KIQNDISASGLKRG---LF---NMAMR 352
Cdd:PRK07787 181 ------------VHGLV-------------LGVLGPL------RIGNRFVHtgRPTPEAYAQALSEGgtlYFgvpTVWSR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 353 -AKEKEIARgvlrrngcwdklvfkkvhqAFGGnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTgaITLTVQ-- 429
Cdd:PRK07787 230 iAADPEAAR-------------------ALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETL--ITLSTRad 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 430 GDHVPNHVGPPVSCNAVKLVDVPEMEYFANQNT-GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLR 508
Cdd:PRK07787 288 GERRPGWVGLPLAGVETRLVDEDGGPVPHDGETvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHR 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366413 509 IIDRRKH--I----FKLSQGEyivpekIENIYTLSQYVNQVYVYGE---SLKSCIIAVVVPDTDV 564
Cdd:PRK07787 368 IVGRESTdlIksggYRIGAGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVGADDV 426
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
84-532 |
6.71e-26 |
|
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: 111.03 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVed 163
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 dgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnHPEVpptaEDLCTVCYTSGTTGNPKGV 243
Cdd:cd05935 80 -----------------------------------------------------GSEL----DDLALIPYTSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 244 MLTHGNVVAGVC-SVILQMGDHriraGDVMVSFLPLAHMFERCCE-NGMYYVGGCVGFYSGDIKELTNDL-KMLKPTVMP 320
Cdd:cd05935 103 MHTHFSAAANALqSAVWTGLTP----SDVILACLPLFHVTGFVGSlNTAVYVGGTYVLMARWDRETALELiEKYKVTFWT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 321 AVPRLLNRVYDKIQNdisasglkrglfnmamrakekeiargvlrRNGCWDKLVfkkvhqAFGGnlrlmvvGSAPLAGNVL 400
Cdd:cd05935 179 NIPTMLVDLLATPEF-----------------------------KTRDLSSLK------VLTG-------GGAPMPPAVA 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 401 TFMRCALGCLVLEGYGQTEctgaitlTVQGDHVPNHVGPPVSCNAV-------KLVDVPEMEYFANQNTGEVCVRGSNVF 473
Cdd:cd05935 217 EKLLKLTGLRFVEGYGLTE-------TMSQTHTNPPLRPKLQCLGIp*fgvdaRVIDIETGRELPPNEVGEIVVRGPQIF 289
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366413 474 HGYYKDPEKTAEA---IDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIEN 532
Cdd:cd05935 290 KGYWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEA 350
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
72-567 |
2.36e-25 |
|
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: 110.60 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 72 GWREtltspyqwINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSF---SLVVVPLYDTLGPD--A 146
Cdd:cd05921 22 GWRR--------VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAgvpAAPVSPAYSLMSQDlaK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 147 CAFIIRQTDMQVVIVEDdgkaamllekAPRSLKIIVAIKPIRQTTL-ERARSRGIQIFSFIDVEKLGAKGNHPEVPP--T 223
Cdd:cd05921 94 LKHLFELLKPGLVFAQD----------AAPFARALAAIFPLGTPLVvSRNAVAGRGAISFAELAATPPTAAVDAAFAavG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 224 AEDLCTVCYTSGTTGNPKGVMLTHGNVvagvCSVILQMGDHRIRAGD---VMVSFLPLAHMFERCCENGMYYVGGcvGFY 300
Cdd:cd05921 164 PDTVAKFLFTSGSTGLPKAVINTQRML----CANQAMLEQTYPFFGEeppVLVDWLPWNHTFGGNHNFNLVLYNG--GTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 301 --------SGDIKELTNDLKMLKPTVMPAVPRllnrvydkiqndisasglkrGlFNMAMRAKEKEIArgvLRRNgcwdkl 372
Cdd:cd05921 238 yiddgkpmPGGFEETLRNLREISPTVYFNVPA--------------------G-WEMLVAALEKDEA---LRRR------ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 373 vfkkvhqaFGGNLRLMVVGSAPLAGNV------LTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAV 446
Cdd:cd05921 288 --------FFKRLKLMFYAGAGLSQDVwdrlqaLAVATVGERIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 447 KLVdvpemeyfANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWL----PNGTLRIIDRRKHIFKLSQG 522
Cdd:cd05921 360 KLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFDGRVAEDFKLASG 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 281366413 523 EYIV--PEKIENIYTLSQYVNQVYVYGESlKSCIIAVVVPDTDVLKQ 567
Cdd:cd05921 432 TWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLACRR 477
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
225-534 |
3.01e-25 |
|
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: 108.59 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 225 EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAH------MFErccenGMYYvGGCVG 298
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLG---LTEDDNWLCALPLFHisglsiLMR-----SVIY-GMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 299 FYSG-DIKELTNDLKMLKPTVMPAVPRLLNRVydkiqndisasglkrglfnmamrakekeiargvlrrngcwdklvFKKV 377
Cdd:cd05912 148 LVDKfDAEQVLHLINSGKVTIISVVPTMLQRL--------------------------------------------LEIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 378 HQAFGGNLRLMVVGSAPLAGNVLTfmRCA-LGCLVLEGYGQTE-CTGAITLTVQGDHV-PNHVGPPVSCNAVKLVDVPEM 454
Cdd:cd05912 184 GEGYPNNLRCILLGGGPAPKPLLE--QCKeKGIPVYQSYGMTEtCSQIVTLSPEDALNkIGSAGKPLFPVELKIEDDGQP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 455 EYfanqNTGEVCVRGSNVFHGYYKDPEKTAEAIDSeGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIY 534
Cdd:cd05912 262 PY----EVGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 335
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
223-571 |
3.51e-25 |
|
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: 108.77 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 223 TAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAH------MFerccenGMYYVGGC 296
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP---LTPGDRVLQFTSFSFdvsvweIF------GALLAGAT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 297 VGFYS----GDIKELTNDLKMLKPTVMPAVPRLLNRVydkiqndisASGLKRGLFNmamrakekeiargvlrrngcwdkl 372
Cdd:cd05930 162 LVVLPeevrKDPEALADLLAEEGITVLHLTPSLLRLL---------LQELELAALP------------------------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 373 vfkkvhqafggNLRLMVVGSAPLAGNVLTFMRCALGCLVLE-GYGQTECTGAITLTV------QGDHVPnhVGPPVSCNA 445
Cdd:cd05930 209 -----------SLRLVLVGGEALPPDLVRRWRELLPGARLVnLYGPTEATVDATYYRvppddeEDGRVP--IGRPIPNTR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 446 VKLVDvpemeyfANQN------TGEVCVRGSNVFHGYYKDPEKTAE---AIDSEGW---HHTGDVGMWLPNGTLRIIDRR 513
Cdd:cd05930 276 VYVLD-------ENLRpvppgvPGELYIGGAGLARGYLNRPELTAErfvPNPFGPGermYRTGDLVRWLPDGNLEFLGRI 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366413 514 KHIFKLSqGEYIVPEKIENIYTLSQYVNQVYV--YGESLKS-CIIAVVVP------DTDVLKQWATE 571
Cdd:cd05930 349 DDQVKIR-GYRIELGEIEAALLAHPGVREAAVvaREDGDGEkRLVAYVVPdeggelDEEELRAHLAE 414
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
103-547 |
5.62e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 108.79 E-value: 5.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 103 LGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAMLLEKAPRSLKiiv 182
Cdd:PRK06839 48 LNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQ--- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 183 aiKPIRQTTLERARSRGIQIFsfidveklgakgnhpeVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMG 262
Cdd:PRK06839 125 --RVISITSLKEIEDRKIDNF----------------VEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAID 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 263 dhrIRAGDVMVSFLPLAHmferccengmyyVGGcVGFYSgdikeltndlkmlKPTVMPAVPRLLNRVYDKIQndisasgl 342
Cdd:PRK06839 187 ---LTMHDRSIVLLPLFH------------IGG-IGLFA-------------FPTLFAGGVIIVPRKFEPTK-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 343 krglfnmAMRAKEKE---IARGVlrrngcwdklvfKKVHQAFG----------GNLRLMVVGSAPLAgnvLTFMRCAL-- 407
Cdd:PRK06839 230 -------ALSMIEKHkvtVVMGV------------PTIHQALIncskfettnlQSVRWFYNGGAPCP---EELMREFIdr 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 408 GCLVLEGYGQTECTGAITLTVQGD--HVPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAE 485
Cdd:PRK06839 288 GFLFGQGFGMTETSPTVFMLSEEDarRKVGSIGKPVLFCDYELID-ENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366413 486 AIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYG 547
Cdd:PRK06839 367 TI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
83-533 |
6.12e-25 |
|
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: 108.93 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 83 WINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEwiLYE--QGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVI 160
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPA--MYElhFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 161 VEddgkaamllekaprslkiivaikpirqttlerarsrgiQIFSFIDVEKLGaKGNHPEVPPTAE-DLCTVCYTSGTTGN 239
Cdd:cd12118 107 VD--------------------------------------REFEYEDLLAEG-DPDFEWIPPADEwDPIALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 240 PKGVMLTH-GNVVAGVCSVIL-QMGDHriragDVMVSFLPLAHMFERCCENGMYYVGGC-VGFYSGDIKELTNDLKMLKP 316
Cdd:cd12118 148 PKGVVYHHrGAYLNALANILEwEMKQH-----PVYLWTLPMFHCNGWCFPWTVAAVGGTnVCLRKVDAKAIYDLIEKHKV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 317 TVMPAVPRLLNRVYDkiqndisasglkrglfnmAMRAKEKEIARGVlrrngcwdklvfkkvhqafggnlRLMVVGSAPLA 396
Cdd:cd12118 223 THFCGAPTVLNMLAN------------------APPSDARPLPHRV-----------------------HVMTAGAPPPA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 397 gNVLTFMRcALGCLVLEGYGQTECTGAITLTV-------------------QGdhVPNHVGPPVSC-NAVKLVDVPemey 456
Cdd:cd12118 262 -AVLAKME-ELGFDVTHVYGLTETYGPATVCAwkpewdelpteerarlkarQG--VRYVGLEEVDVlDPETMKPVP---- 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281366413 457 fANQNT-GEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENI 533
Cdd:cd12118 334 -RDGKTiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGV 408
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
221-562 |
8.60e-25 |
|
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: 107.78 E-value: 8.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 221 PPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVagvcSVILQMGDH-RIRAGDVMVSFLPLAhmFERCCenGMYYVGGCVG- 298
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVL----NYVSQPPARlDVGPGSRVAQVLSIA--FDACI--GEIFSTLCNGg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 299 --FYSGDIKELTNDLKMLkpTVMPAVPRLLnrvydkiqndisasglkrglfnmamrakekeiarGVLRRNGcwdklvFKk 376
Cdd:cd17653 173 tlVLADPSDPFAHVARTV--DALMSTPSIL----------------------------------STLSPQD------FP- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 377 vhqafggNLRLMVVGSAPLAGNVLTfmRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEY 456
Cdd:cd17653 210 -------NLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 457 FANQnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHH------TGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPEKI 530
Cdd:cd17653 281 PEGV-VGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEI 358
|
330 340 350
....*....|....*....|....*....|....*
gi 281366413 531 EN-IYTLSQYVNQVY--VYGESLksciIAVVVPDT 562
Cdd:cd17653 359 EEvVLQSQPEVTQAAaiVVNGRL----VAFVTPET 389
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
218-518 |
1.94e-24 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 107.76 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 218 PEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAgvcSVILQM-GDH---RIRAGDVMVSFLPLAHMFercCENGMYYV 293
Cdd:PLN02246 172 PEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVT---SVAQQVdGENpnlYFHSDDVILCVLPMFHIY---SLNSVLLC 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 294 GGCVG--------FYSGDIKELTNDLKMlkpTVMPAVPRLLnrvydkiqndisasglkrglfnMAMrAKEKEIARGVLrr 365
Cdd:PLN02246 246 GLRVGaailimpkFEIGALLELIQRHKV---TIAPFVPPIV----------------------LAI-AKSPVVEKYDL-- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 366 ngcwdklvfkkvhqafgGNLRLMVVGSAPLAGNVLTFMRCALGCLVL-EGYGQTECTGAITLTVQGDHVPNHVGPPvSC- 443
Cdd:PLN02246 298 -----------------SSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEAGPVLAMCLAFAKEPFPVKSG-SCg 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 444 ----NA-VKLVDvPE--MEYFANQnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHI 516
Cdd:PLN02246 360 tvvrNAeLKIVD-PEtgASLPRNQ-PGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKEL 437
|
..
gi 281366413 517 FK 518
Cdd:PLN02246 438 IK 439
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
218-531 |
3.19e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 107.43 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 218 PEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVV---AGVCSVILQMGDHriragDVMVSFLPlahmferccengMYYVG 294
Cdd:PRK06178 202 PLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVytaAAAYAVAVVGGED-----SVFLSFLP------------EFWIA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 295 GcvgfysgdikeltNDLKMLKPTVMPAVPRLLNRvYDkiqndisASGlkrglfnmAMRAKEKeiaRGVLRRNGCWDKLVF 374
Cdd:PRK06178 265 G-------------ENFGLLFPLFSGATLVLLAR-WD-------AVA--------FMAAVER---YRVTRTVMLVDNAVE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 375 KKVHQAFGG-NLR-LMVVGsaplagnVLTFMR----------CAL-GCLVLEG-YGQTECTGAITLTV--QGDHV----- 433
Cdd:PRK06178 313 LMDHPRFAEyDLSsLRQVR-------VVSFVKklnpdyrqrwRALtGSVLAEAaWGMTETHTCDTFTAgfQDDDFdllsq 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 434 PNHVGPPVSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRR 513
Cdd:PRK06178 386 PVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRR 464
|
330
....*....|....*...
gi 281366413 514 KHIFKLSqGEYIVPEKIE 531
Cdd:PRK06178 465 KEMLKVN-GMSVFPSEVE 481
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
204-533 |
2.16e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 104.72 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 204 SFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIRAGDV----MVSFLPLA 279
Cdd:PRK07059 183 RFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPdqlnFVCALPLY 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 280 HMFER--CCENGMYyVGGCVGFYSG--DIKELTNDLKMLKPTVMPAVPRLLNrvydkiqndisasglkrGLFNmamrake 355
Cdd:PRK07059 263 HIFALtvCGLLGMR-TGGRNILIPNprDIPGFIKELKKYQVHIFPAVNTLYN-----------------ALLN------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 356 keiargvlrrNGCWDKLVFKKVHQAFGGNlrlMVVgSAPLAGNVLTFMrcalGCLVLEGYGQTECTGAITLT-VQGDHVP 434
Cdd:PRK07059 318 ----------NPDFDKLDFSKLIVANGGG---MAV-QRPVAERWLEMT----GCPITEGYGLSETSPVATCNpVDATEFS 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 435 NHVGPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRI 509
Cdd:PRK07059 380 GTIGLPLPSTEVSIRDddgndLPLGE------PGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKI 453
|
330 340
....*....|....*....|....
gi 281366413 510 IDRRKHIFKLSqGEYIVPEKIENI 533
Cdd:PRK07059 454 VDRKKDMILVS-GFNVYPNEIEEV 476
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
98-532 |
2.36e-23 |
|
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: 103.67 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 98 AGMLALGARPKQLIGIYSQNRPEWI-LYEQ----GCySFSLVVVPLYDTLGPdacafiirqTDMQVVIVEDDGKAAMLLE 172
Cdd:cd05922 8 SALLEAGGVRGERVVLILPNRFTYIeLSFAvayaGG-RLGLVFVPLNPTLKE---------SVLRYLVADAGGRIVLADA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 173 KAPRSLKIIVAIKPIRQTtlerarsrgiqifsFIDVEKL-GAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVV 251
Cdd:cd05922 78 GAADRLRDALPASPDPGT--------------VLDADGIrAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 252 AGVCSVILQMGdhrIRAGDVMVSFLPLAHMFERCCENGMYYVGGCV----GFYSGDikELTNDLKMLKPTVMPAVP---R 324
Cdd:cd05922 144 ANARSIAEYLG---ITADDRALTVLPLSYDYGLSVLNTHLLRGATLvltnDGVLDD--AFWEDLREHGATGLAGVPstyA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 325 LLNRVydkIQNDISASGLkRGLFNMAMRAKEKEIARgvLRrngcwDKLVfkkvhqafGGNLRLMvvgsaplagnvltfmr 404
Cdd:cd05922 219 MLTRL---GFDPAKLPSL-RYLTQAGGRLPQETIAR--LR-----ELLP--------GAQVYVM---------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 405 calgclvlegYGQTECTGAITlTVQGDHV---PNHVGPPVSCNAVKLVDVPEMEYfANQNTGEVCVRGSNVFHGYYKDPE 481
Cdd:cd05922 264 ----------YGQTEATRRMT-YLPPERIlekPGSIGLAIPGGEFEILDDDGTPT-PPGEPGEIVHRGPNVMKGYWNDPP 331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 281366413 482 KTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIEN 532
Cdd:cd05922 332 YRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEA 381
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
52-525 |
4.28e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 103.97 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 52 RTLYQTFREGAYASNNGPCLGWRETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSF 131
Cdd:PRK12582 49 RSIPHLLAKWAAEAPDRPWLAQREPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 132 SLVVVPL---YDTLGPD-----ACAFIIRQtdmQVVIVEDdgkaAMLLEKAPRSLK-----IIVAIKPIRqttlerarsr 198
Cdd:PRK12582 129 GVPAAPVspaYSLMSHDhaklkHLFDLVKP---RVVFAQS----GAPFARALAALDlldvtVVHVTGPGE---------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 199 GIQIFSFIDvekLGAKGNHPEVPPTAEDLC--TVC---YTSGTTGNPKGVMLTHGNvvagVCSVILQMGDHRIRAGD--- 270
Cdd:PRK12582 192 GIASIAFAD---LAATPPTAAVAAAIAAITpdTVAkylFTSGSTGMPKAVINTQRM----MCANIAMQEQLRPREPDppp 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 271 -VMVSFLPLAHMFE-RCCENGMYYVGGCvgFY-------SGDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDisasg 341
Cdd:PRK12582 265 pVSLDWMPWNHTMGgNANFNGLLWGGGT--LYiddgkplPGMFEETIRNLREISPTVYGNVPAGYAMLAEAMEKD----- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 342 lkrglfnmamrakekeiarGVLRRNgcwdklVFKkvhqafggNLRLMVVGSAPLAGNVLTFMRcALGC-------LVLEG 414
Cdd:PRK12582 338 -------------------DALRRS------FFK--------NLRLMAYGGATLSDDLYERMQ-ALAVrttghriPFYTG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 415 YGQTEcTGAITLTVQGD-HVPNHVGPPVSCNAVKLVDVPEmeyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWH 493
Cdd:PRK12582 384 YGATE-TAPTTTGTHWDtERVGLIGLPLPGVELKLAPVGD--------KYEVRVKGPNVTPGYHKDPELTAAAFDEEGFY 454
|
490 500 510
....*....|....*....|....*....|....*.
gi 281366413 494 HTGDVGMWL----PNGTLRIIDRRKHIFKLSQGEYI 525
Cdd:PRK12582 455 RLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGTWV 490
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
72-569 |
5.55e-23 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 103.81 E-value: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 72 GWREtltspyqwINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPL---YDTLGPD--A 146
Cdd:PRK08180 66 GWRR--------LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSQDfgK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 147 CAFIIRQTDMQVVIVEDDGK-AAMLLEKAPRSLKIIVAikpirqttleRARSRGIQIFSFidvEKLGAKGNHPEVPP--- 222
Cdd:PRK08180 138 LRHVLELLTPGLVFADDGAAfARALAAVVPADVEVVAV----------RGAVPGRAATPF---AALLATPPTAAVDAaha 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 223 --TAEDLCTVCYTSGTTGNPKGVMLTHGNVvagvCSVILQMGDHRIRAGD---VMVSFLPLAHMFerccenG-------M 290
Cdd:PRK08180 205 avGPDTIAKFLFTSGSTGLPKAVINTHRML----CANQQMLAQTFPFLAEeppVLVDWLPWNHTF------GgnhnlgiV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 291 YYVGGCvgFY-------SGDIKELTNDLKMLKPTVMPAVPRLlnrvydkiqndisasglkrglFNMAMRAKEKEIArgvL 363
Cdd:PRK08180 275 LYNGGT--LYiddgkptPGGFDETLRNLREISPTVYFNVPKG---------------------WEMLVPALERDAA---L 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 364 RRNgcwdklvfkkvhqaFGGNLRLMVVGSAPLAGNVLT-FMRCA---LGCLV--LEGYGQTECTGAITLTvqgdHVPN-- 435
Cdd:PRK08180 329 RRR--------------FFSRLKLLFYAGAALSQDVWDrLDRVAeatCGERIrmMTGLGMTETAPSATFT----TGPLsr 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 436 --HVGPPVSCNAVKLVDvpemeyfaNQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWL----PNGTLRI 509
Cdd:PRK08180 391 agNIGLPAPGCEVKLVP--------VGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMF 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366413 510 IDRRKHIFKLSQGEYI-V-PEKIENIYTLSQYVNQVYVYGESLKsCIIAVVVPDTDVLKQWA 569
Cdd:PRK08180 463 DGRIAEDFKLSSGTWVsVgPLRARAVSAGAPLVQDVVITGHDRD-EIGLLVFPNLDACRRLA 523
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
86-564 |
1.10e-22 |
|
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: 101.89 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 86 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLYDTLGPDACAFIIRqtdmqvv 159
Cdd:cd12117 25 YAELNERANRLARRLRAAGVGPGDVVGVLAERSPELvvallaVLKAGAAY------VPLDPELPAERLAFMLA------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 160 ivedDGKAAMLLEKAPrslkiivaikpirqttlERARSRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGN 239
Cdd:cd12117 92 ----DAGAKVLLTDRS-----------------LAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 240 PKGVMLTHGNVVAGVCSvilqmGDHR-IRAGDVMVSFLPL---AHMFErccengmYYV----GGCVgfysgdikELTNDL 311
Cdd:cd12117 151 PKGVAVTHRGVVRLVKN-----TNYVtLGPDDRVLQTSPLafdASTFE-------IWGallnGARL--------VLAPKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 312 KMLKPTVMPAVPRllnrvydkiQNDISASGLKRGLFNMAMRAKEkeiargvlrrngcwdklvfkkvhQAFGGnLRLMVVG 391
Cdd:cd12117 211 TLLDPDALGALIA---------EEGVTVLWLTAALFNQLADEDP-----------------------ECFAG-LRELLTG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 392 ----SAPLAGNVLTfmRCALGCLVlEGYGQTECTGAIT------LTVQGDHVPnhVGPPVSCNAVKLVD-----VPEMEy 456
Cdd:cd12117 258 gevvSPPHVRRVLA--ACPGLRLV-NGYGPTENTTFTTshvvteLDEVAGSIP--IGRPIANTRVYVLDedgrpVPPGV- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 457 fanqnTGEVCVRGSNVFHGYYKDPEKTAE------AIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPEKI 530
Cdd:cd12117 332 -----PGELYVGGDGLALGYLNRPALTAErfvadpFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEI 405
|
490 500 510
....*....|....*....|....*....|....*....
gi 281366413 531 ENiyTLSQY--VNQVYVY---GESLKSCIIAVVVPDTDV 564
Cdd:cd12117 406 EA--ALRAHpgVREAVVVvreDAGGDKRLVAYVVAEGAL 442
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
84-572 |
1.14e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 102.35 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFgAGML--ALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIV 161
Cdd:PRK08314 36 ISYRELLEEAERL-AGYLqqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 162 EDD--GKAAMLLEKAPRSLKII------------VAIKPIRQTTLERARSRGIQIFSFIDVekLGAKGNHPEVPPTAEDL 227
Cdd:PRK08314 115 GSElaPKVAPAVGNLRLRHVIVaqysdylpaepeIAVPAWLRAEPPLQALAPGGVVAWKEA--LAAGLAPPPHTAGPDDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 228 CTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHrirAGDVMVSFLPLAH---MfeRCCENGMYYVGGCVgfysgdi 304
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNST---PESVVLAVLPLFHvtgM--VHSMNAPIYAGATV------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 305 keltndlkmlkptVMpaVPRLlnrvydkiqndisasglkrglfnmamrakEKEIARGVLRRNGC--W--------DKLVF 374
Cdd:PRK08314 261 -------------VL--MPRW-----------------------------DREAAARLIERYRVthWtniptmvvDFLAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 375 KKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAitltvqgdhvPNHVGPP----VSCNAVKLVD 450
Cdd:PRK08314 297 PGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMA----------QTHSNPPdrpkLQCLGIPTFG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 451 V------PEM-EYFANQNTGEVCVRGSNVFHGYYKDPEKTAEA---IDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLS 520
Cdd:PRK08314 366 VdarvidPETlEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINAS 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366413 521 qGEYIVPEKIENIYTLSQYVNQVYVY-------GESLKsciiAVVVPD--------TDVLKQWATEN 572
Cdd:PRK08314 446 -GFKVWPAEVENLLYKHPAIQEACVIatpdprrGETVK----AVVVLRpeargkttEEEIIAWAREH 507
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
78-547 |
1.64e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 101.68 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 78 TSPYQWINYDEALLRAKNFgagMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQ 157
Cdd:PRK08008 35 VRRYSYLELNEEINRTANL---FYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 158 VVIVEddgkaamllekaPRSLKIIVAIKPIRQTTLER---ARSRGIQIFSFIDVEKLgaKGNHP----EVPP-TAEDLCT 229
Cdd:PRK08008 112 LLVTS------------AQFYPMYRQIQQEDATPLRHiclTRVALPADDGVSSFTQL--KAQQPatlcYAPPlSTDDTAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 230 VCYTSGTTGNPKGVMLTHGNvvagvcsviLQMGDH------RIRAGDVMVSFLPLAHM-FErcCENGM--YYVGGC---V 297
Cdd:PRK08008 178 ILFTSGTTSRPKGVVITHYN---------LRFAGYysawqcALRDDDVYLTVMPAFHIdCQ--CTAAMaaFSAGATfvlL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 298 GFYS-----GDIKE----LTNDLKMLKPTVM--PAVPRLLNRVydkiqndisasgLKRGLFNMAMRAKEKE--IARgvlr 364
Cdd:PRK08008 247 EKYSarafwGQVCKyratITECIPMMIRTLMvqPPSANDRQHC------------LREVMFYLNLSDQEKDafEER---- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 365 rngcwdklvfkkvhqaFGgnLRLMvvgsaplagnvltfmrcalgclvlEGYGQTECTGAITLTVQGD--HVPNhVGPPVS 442
Cdd:PRK08008 311 ----------------FG--VRLL------------------------TSYGMTETIVGIIGDRPGDkrRWPS-IGRPGF 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 443 CNAVKLVDVPEMEYFANQnTGEVCVRG---SNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKL 519
Cdd:PRK08008 348 CYEAEIRDDHNRPLPAGE-IGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKR 426
|
490 500
....*....|....*....|....*...
gi 281366413 520 SqGEYIVPEKIENIYTLSQYVNQVYVYG 547
Cdd:PRK08008 427 G-GENVSCVELENIIATHPKIQDIVVVG 453
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
142-547 |
6.69e-22 |
|
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: 99.63 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 142 LGPDACAFIIRQTDMQVVIVEDDgkaamllekaprSLKIIVAIKPiRQTTLER----------ARSRGIQIFSFidvEKL 211
Cdd:cd12119 84 LFPEQIAYIINHAEDRVVFVDRD------------FLPLLEAIAP-RLPTVEHvvvmtddaamPEPAGVGVLAY---EEL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 212 GAKGNHPEVPPTAE--DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQ--MGdhrIRAGDVMVSFLPLAHMfercce 287
Cdd:cd12119 148 LAAESPEYDWPDFDenTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTdgLG---LSESDVVLPVVPMFHV------ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 288 N--GMYYVGGCVG---FYSG---DIKELTNDLKMLKPTVMPAVPR----LLNRVyDKIQNDISAsglkrglfnmamrake 355
Cdd:cd12119 219 NawGLPYAAAMVGaklVLPGpylDPASLAELIEREGVTFAAGVPTvwqgLLDHL-EANGRDLSS---------------- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 356 keiargvlrrngcwdklvfkkvhqafggnLRLMVV-GSAPLAGNVLTFMRcaLGCLVLEGYGQTE-----CTGAITLTVQ 429
Cdd:cd12119 282 -----------------------------LRRVVIgGSAVPRSLIEAFEE--RGVRVIHAWGMTEtsplgTVARPPSEHS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 430 GDHVPNHV------GPPVSCNAVKLVDvPEMEYFAN--QNTGEVCVRGSNVFHGYYKDPEkTAEAIDSEGWHHTGDVGMW 501
Cdd:cd12119 331 NLSEDEQLalrakqGRPVPGVELRIVD-DDGRELPWdgKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATI 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 281366413 502 LPNGTLRIIDRRKHIFKlSQGEYIVPEKIENIYTLSQYVNQVYVYG 547
Cdd:cd12119 409 DEDGYLTITDRSKDVIK-SGGEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
117-575 |
7.75e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 99.85 E-value: 7.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 117 NRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED--DGKAAMLLEKAPRSLKIIVAIKPIRQTTL-- 192
Cdd:PRK07786 76 NRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAalAPVATAVRDIVPLLSTVVVAGGSSDDSVLgy 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 193 ERARSRGIQIFSFIDVeklgakgnhPEVPPTAedlctVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRirAGDVM 272
Cdd:PRK07786 156 EDLLAEAGPAHAPVDI---------PNDSPAL-----IMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADI--NSDVG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 273 VSFLPLAHmferccengmyyvggcvgfysgdIKELTNDLKML---KPTVMPAVprllnrvydkiqndisasglkrGLFNM 349
Cdd:PRK07786 220 FVGVPLFH-----------------------IAGIGSMLPGLllgAPTVIYPL----------------------GAFDP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 350 A--MRAKEKEIARGVLRRNGCWDKLVfkKVHQAFGGNLRLMVV--GSAPLAGNVLTFMRCAL-GCLVLEGYGQTECTgAI 424
Cdd:PRK07786 255 GqlLDVLEAEKVTGIFLVPAQWQAVC--AEQQARPRDLALRVLswGAAPASDTLLRQMAATFpEAQILAAFGQTEMS-PV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 425 TLTVQGDHVPNH---VGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSeGWHHTGDVGMW 501
Cdd:PRK07786 332 TCMLLGEDAIRKlgsVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 502 LPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYG---ESLKSCIIAVVVPDTDV-------LKQWATE 571
Cdd:PRK07786 410 DEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGradEKWGEVPVAVAAVRNDDaaltledLAEFLTD 488
|
....
gi 281366413 572 NNVR 575
Cdd:PRK07786 489 RLAR 492
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
84-560 |
1.08e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 99.19 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLyDTLGPDACAFI-IRQTDMQVVIVE 162
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPL-DPALPIAEQRVrSQAAGARVVLID 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 163 DDGKAAMLLEKApRSLKIIVAIKPirqttlERARSRGIQIFSFIDVEKLGAKGNHPEvpPTAEDLCTVCYTSGTTGNPKG 242
Cdd:PRK05852 123 ADGPHDRAEPTT-RWWPLTVNVGG------DSGPSGGTLSVHLDAATEPTPATSTPE--GLRPDDAMIMFTGGTTGLPKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 243 VMLTHGNVVAGVCSVIlqmGDHRIRAGDVMVSFLPLAHMferccengmyyvggcvgfySGDIKELTNDLKMLKPTVMPAV 322
Cdd:PRK05852 194 VPWTHANIASSVRAII---TGYRLSPRDATVAVMPLYHG-------------------HGLIAALLATLASGGAVLLPAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 323 PRLLNRVYdkiQNDISASGlkrGLFNMAMRAkekeIARGVLRRNgcwDKLVFKKVHQAfggnLRLMVVGSAPLAGNVLTF 402
Cdd:PRK05852 252 GRFSAHTF---WDDIKAVG---ATWYTAVPT----IHQILLERA---ATEPSGRKPAA----LRFIRSCSAPLTAETAQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 403 MRCALGCLVLEGYGQTECTGAITLT-VQG---DHVPN-HVGPPVSCNAVKLVDV-PEMEYFANQNTGEVCVRGSNVFHGY 476
Cdd:PRK05852 315 LQTEFAAPVVCAFGMTEATHQVTTTqIEGigqTENPVvSTGLVGRSTGAQIRIVgSDGLPLPAGAVGEVWLRGTTVVRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 477 YKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVYV-------YGES 549
Cdd:PRK05852 395 LGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVfgvpdqlYGEA 472
|
490
....*....|.
gi 281366413 550 lkscIIAVVVP 560
Cdd:PRK05852 473 ----VAAVIVP 479
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
226-579 |
1.35e-21 |
|
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: 96.25 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 226 DLCTVCYTSGTTGNPKGVMLTHGNVVA---GVCSVI-LQMGDHRIRAgdvmvsfLPLahmferccengmYYVGGCV---- 297
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLAsaaGLHSRLgFGGGDSWLLS-------LPL------------YHVGGLAilvr 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 298 GFYSGDIKELTN-------DLKMLKPTVMPAVPRLLNRVYDkiqNDISASGLKRglfnmamrakekeiargvlrrngcwd 370
Cdd:cd17630 62 SLLAGAELVLLErnqalaeDLAPPGVTHVSLVPTQLQRLLD---SGQGPAALKS-------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 371 klvfkkvhqafggnLRLMVVGSAPLAgNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVD 450
Cdd:cd17630 113 --------------LRAVLLGGAPIP-PELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 451 vpemeyfanqnTGEVCVRGSNVFHGYYKDPEKtaEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKI 530
Cdd:cd17630 178 -----------DGEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEI 243
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 281366413 531 ENIYTLSQYVNQVYVYG---ESLKSCIIAVVV----PDTDVLKQWatennVRGTLS 579
Cdd:cd17630 244 EAALAAHPAVRDAFVVGvpdEELGQRPVAVIVgrgpADPAELRAW-----LKDKLA 294
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
219-547 |
1.56e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 98.95 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 219 EVPPTAE-DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCsvilqMGDHRI----RAGDVMVSFLPLAHMFERCCENGMYYV 293
Cdd:PRK06710 199 EVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTL-----MGVQWLynckEGEEVVLGVLPFFHVYGMTAVMNLSIM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 294 GG--CVGFYSGDIKELTNDLKMLKPTVMPAVPRLLnrvydkiqndisasglkRGLFNMAMrAKEKEIArgvlrrngcwdk 371
Cdd:PRK06710 274 QGykMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIY-----------------IALLNSPL-LKEYDIS------------ 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 372 lvfkkvhqafggNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAITLT--VQGDHVPNHVGPPVSCNAVKLV 449
Cdd:PRK06710 324 ------------SIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTE-SSPVTHSnfLWEKRVPGSIGVPWPDTEAMIM 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 450 DVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAeAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEK 529
Cdd:PRK06710 391 SLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPRE 468
|
330
....*....|....*...
gi 281366413 530 IENIYTLSQYVNQVYVYG 547
Cdd:PRK06710 469 VEEVLYEHEKVQEVVTIG 486
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
226-571 |
2.92e-21 |
|
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: 96.93 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 226 DLCTVCYTSGTTGNPKGVMLTHGNVVAGVcSVILQMGDhrIRAGDVMVSFLPLAhmFERCcengMYYVGGCVGfySG--- 302
Cdd:cd05945 98 DNAYIIFTSGSTGRPKGVQISHDNLVSFT-NWMLSDFP--LGPGDVFLNQAPFS--FDLS----VMDLYPALA--SGatl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 303 ---------DIKELTNDLKMLKPTVMPAVPRLLNRVydkiqndisasgLKRGLFNmamrakekeiargvlrrngcwdklv 373
Cdd:cd05945 167 vpvprdataDPKQLFRFLAEHGITVWVSTPSFAAMC------------LLSPTFT------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 374 fkkvhQAFGGNLRLMVvgsapLAGNVLT------FMRCALGCLVLEGYGQTECTGAITLTV-------QGDHVPnhVGPP 440
Cdd:cd05945 210 -----PESLPSLRHFL-----FCGEVLPhktaraLQQRFPDARIYNTYGPTEATVAVTYIEvtpevldGYDRLP--IGYA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 441 VSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEA---IDSEGWHHTGDVGMWLPNGTLRIIDR 512
Cdd:cd05945 278 KPGAKLVILDedgrpVPPGE------KGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRLEADGLLFYRGR 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281366413 513 RKHIFKLsQGEYIVPEKIENIYTLSQYVNQ---VYVYGESLKSCIIAVVVPDTDV----LKQWATE 571
Cdd:cd05945 352 LDFQVKL-NGYRIELEEIEAALRQVPGVKEavvVPKYKGEKVTELIAFVVPKPGAeaglTKAIKAE 416
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
84-564 |
3.58e-21 |
|
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: 97.55 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 163
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 DGKAamLLEKAPRSLKIIVAIKPIRQTTLERARSRGIQIFSFIDVEKLG-AKGNHPEVPPtaeDLCTVCYTSGTTGNPKG 242
Cdd:TIGR03098 106 ERLD--LLHPALPGCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGdADPPHPVIDS---DMAAILYTSGSTGRPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 243 VMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVgfysgdikeltndlkMLKPTVMPav 322
Cdd:TIGR03098 181 VVLSHRNLVAGAQSVATYL---ENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATV---------------VLHDYLLP-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 323 prllnrvydkiqNDIsasglkrglfnmaMRAKEKEIARGVLRRNGCWDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLTF 402
Cdd:TIGR03098 241 ------------RDV-------------LKALEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 403 MRCALG-CLVLEGYGQTECTGAITLTVQG-DHVPNHVGPPVScNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDP 480
Cdd:TIGR03098 296 LRSFLPnARLFLMYGLTEAFRSTYLPPEEvDRRPDSIGKAIP-NAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 481 EKTAEAIDSEGWHH-----------TGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVYVYG-- 547
Cdd:TIGR03098 375 EKTAERFRPLPPFPgelhlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVAYATGLVAEAVAFGvp 453
|
490
....*....|....*...
gi 281366413 548 -ESLKSCIIAVVVPDTDV 564
Cdd:TIGR03098 454 dPTLGQAIVLVVTPPGGE 471
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
219-533 |
5.43e-21 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 97.13 E-value: 5.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 219 EVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHmferccengmyyvggCVG 298
Cdd:PRK06087 181 AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLN---LTWQDVFMMPAPLGH---------------ATG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 299 FYSGDIkeltndLKMLkptvmpavprllnrvydkiqndISASGLKRGLFNmamrakeKEIARGVLRRNGC---------- 368
Cdd:PRK06087 243 FLHGVT------APFL----------------------IGARSVLLDIFT-------PDACLALLEQQRCtcmlgatpfi 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 369 WDKLVFKKVHQAFGGNLRLMVVGSAPLAGNVLtfmRCAL--GCLVLEGYGQTECtgaitltvqgdhVPNHVGPPVSCNA- 445
Cdd:PRK06087 288 YDLLNLLEKQPADLSALRFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTES------------SPHAVVNLDDPLSr 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 446 -------------VKLVDVPEMEyFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDR 512
Cdd:PRK06087 353 fmhtdgyaaagveIKVVDEARKT-LPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGR 431
|
330 340
....*....|....*....|.
gi 281366413 513 RKHIFkLSQGEYIVPEKIENI 533
Cdd:PRK06087 432 KKDII-VRGGENISSREVEDI 451
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
232-568 |
5.70e-21 |
|
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: 94.64 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 232 YTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMFERCCENGMYYVGGC-VGFYSGDIKELTND 310
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMG---LTEADVYLNMLPLFHIAGLNLALATFHAGGAnVVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 311 LKMLKPTVMPAVPRLLNRVYDKIQ-NDISASGLKrglfnmamrakekeiargvlrrngcwdklvfkkvhqafggnlrlMV 389
Cdd:cd17637 84 IEEEKVTLMGSFPPILSNLLDAAEkSGVDLSSLR--------------------------------------------HV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 390 VG-SAPlaGNVLTFMRCALGCLvLEGYGQTECTGAITLTVQGDHvPNHVGPPVSCNAVKLVD-----VPEMEyfanqnTG 463
Cdd:cd17637 120 LGlDAP--ETIQRFEETTGATF-WSLYGQTETSGLVTLSPYRER-PGSAGRPGPLVRVRIVDdndrpVPAGE------TG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 464 EVCVRGSNVFHGYYKDPEKTAEAIDsEGWHHTGDVGMWLPNGTLRIIDRR--KHIFKlSQGEYIVPEKIENIYTLSQYVN 541
Cdd:cd17637 190 EIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHPAIA 267
|
330 340
....*....|....*....|....*..
gi 281366413 542 QVYVYGeslksciiavvVPDTdvlkQW 568
Cdd:cd17637 268 EVCVIG-----------VPDP----KW 279
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
87-531 |
9.44e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 96.03 E-value: 9.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 87 DEALLRAknfgAGML-ALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVvIVEDDG 165
Cdd:PRK09088 29 DALVGRL----AAVLrRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL-LLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 166 KAAmllekaprslkiivaikpirqttlerARSRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLctVCYTSGTTGNPKGVML 245
Cdd:PRK09088 104 VAA--------------------------GRTDVEDLAAFIASADALEPADTPSIPPERVSL--ILFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 246 THGNV--VAGVCSVILQMGDHRiragdvmvSFLplahmfercCENGMYYVGGCVgfysgdikelTNdlkmLKPTVM---- 319
Cdd:PRK09088 156 SERNLqqTAHNFGVLGRVDAHS--------SFL---------CDAPMFHIIGLI----------TS----VRPVLAvggs 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 320 --------PAvpRLLNRVYDKiqndisASGLKR--GLFNMAMRakekeiargvLRRNGCWDKlvfkkvhqAFGGNLRLMV 389
Cdd:PRK09088 205 ilvsngfePK--RTLGRLGDP------ALGITHyfCVPQMAQA----------FRAQPGFDA--------AALRHLTALF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 390 VGSAP-LAGNVLTFMrcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVG------PPVScnaVKLVDVPEMEYFANQnT 462
Cdd:PRK09088 259 TGGAPhAAEDILGWL--DDGIPMVDGFGMSEAGTVFGMSVDCDVIRAKAGaagiptPTVQ---TRVVDDQGNDCPAGV-P 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281366413 463 GEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIE 531
Cdd:PRK09088 333 GELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE 400
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
82-547 |
2.07e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 94.95 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 82 QWINYDEALLRAKNfGAGML-ALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVI 160
Cdd:PRK06145 26 QEISYAEFHQRILQ-AAGMLhARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 161 VEDDgkaamllekaprsLKIIVAIKPIRQTTLERARSrgiqifsfiDVEKLGAKGNH-PEVPPTAE-DLCTVCYTSGTTG 238
Cdd:PRK06145 105 VDEE-------------FDAIVALETPKIVIDAAAQA---------DSRRLAQGGLEiPPQAAVAPtDLVRLMYTSGTTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 239 NPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLahmferccengmYYVGGCvgfysgdikeltnDLkmlkptv 318
Cdd:PRK06145 163 RPKGVMHSYGNLHWKSIDHVIALG---LTASERLLVVGPL------------YHVGAF-------------DL------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 319 mPAVPRLLNRVYDKIQNDISASGlkrglfnmAMRAKEKEiargvlRRNGCW---------------DKLVFKKVHQAFGG 383
Cdd:PRK06145 208 -PGIAVLWVGGTLRIHREFDPEA--------VLAAIERH------RLTCAWmapvmlsrvltvpdrDRFDLDSLAWCIGG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 384 nlrlmvvGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPN--HVGPPVSCNAVKLVDVPEMEYFANQN 461
Cdd:PRK06145 273 -------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKigSTGRALAHVEIRIADGAGRWLPPNMK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 462 tGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIEN-IYTLSQyV 540
Cdd:PRK06145 346 -GEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERvIYELPE-V 421
|
....*..
gi 281366413 541 NQVYVYG 547
Cdd:PRK06145 422 AEAAVIG 428
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
82-513 |
2.55e-20 |
|
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: 96.08 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 82 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLyDTLGPDA-CAFIIRQT 154
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMvvallaVLKAGAAY------VPL-DPAYPAErLAYMLEDA 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 155 DMQVVIVEDDgkaamllekaprslkiivaikpirqtTLERARSRGIQIFSfIDVEKLGAKGNH-PEVPPTAEDLCTVCYT 233
Cdd:COG1020 573 GARLVLTQSA--------------------------LAARLPELGVPVLA-LDALALAAEPATnPPVPVTPDDLAYVIYT 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 234 SGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVM---------VS----FLPLAHmferccengmyyvGGCVGFY 300
Cdd:COG1020 626 SGSTGRPKGVMVEHRALVNLLAWMQRRYG---LGPGDRVlqfaslsfdASvweiFGALLS-------------GATLVLA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 301 S----GDIKELTNDLKMLKPTVMPAVPrllnrvydkiqndisasglkrGLFNMAMRAkekeiARGVLRRngcwdklvfkk 376
Cdd:COG1020 690 PpearRDPAALAELLARHRVTVLNLTP---------------------SLLRALLDA-----APEALPS----------- 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 377 vhqafggnLRLMVVGSAPLAGNVLT-FMRCALGCLVLEGYGQTECTGAITLTV------QGDHVPnhVGPPVSCNAVKLV 449
Cdd:COG1020 733 --------LRLVLVGGEALPPELVRrWRARLPGARLVNLYGPTETTVDSTYYEvtppdaDGGSVP--IGRPIANTRVYVL 802
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366413 450 DvpemeyfANQN------TGEVCVRGSNVFHGYYKDPEKTAEA-------IDSEGWHHTGDVGMWLPNGTLRIIDRR 513
Cdd:COG1020 803 D-------AHLQpvpvgvPGELYIGGAGLARGYLNRPELTAERfvadpfgFPGARLYRTGDLARWLPDGNLEFLGRA 872
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
92-572 |
2.68e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 94.64 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 92 RAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAmll 171
Cdd:PRK03640 36 AVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDDFEAK--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 172 ekaprslkiIVAIKPIRQTTLERARSRGIQIFSFIDVEklgakgnhpevpptaeDLCTVCYTSGTTGNPKGVMLTHGNVV 251
Cdd:PRK03640 113 ---------LIPGISVKFAELMNGPKEEAEIQEEFDLD----------------EVATIMYTSGTTGKPKGVIQTYGNHW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 252 AGVCSVILQMGdhrIRAGDVMVSFLPLAH------MFErcceNGMYyvGGCVGFYSG-DIKELTNDLKMLKPTVMPAVPR 324
Cdd:PRK03640 168 WSAVGSALNLG---LTEDDCWLAAVPIFHisglsiLMR----SVIY--GMRVVLVEKfDAEKINKLLQTGGVTIISVVST 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 325 LLNRVYDKIQNDisasglkrglfnmamrakekeiargvlrrngcwdklvfkkvhqAFGGNLRLMVVGSAPLAGNVLTfmR 404
Cdd:PRK03640 239 MLQRLLERLGEG-------------------------------------------TYPSSFRCMLLGGGPAPKPLLE--Q 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 405 CAL-GCLVLEGYGQTE-CTGAITLTVQgDHVPNH--VGPPVSCNAVKLVDvpEMEYFANQNTGEVCVRGSNVFHGYYKDP 480
Cdd:PRK03640 274 CKEkGIPVYQSYGMTEtASQIVTLSPE-DALTKLgsAGKPLFPCELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNRE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 481 EKTAEAIDSeGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYGESLK---SCIIAV 557
Cdd:PRK03640 351 DATRETFQD-GWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDkwgQVPVAF 428
|
490
....*....|....*....
gi 281366413 558 VVPDTDV----LKQWATEN 572
Cdd:PRK03640 429 VVKSGEVteeeLRHFCEEK 447
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
75-564 |
2.28e-19 |
|
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: 91.92 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 75 ETLTspYQWINydealLRAKNFGAGMLALGARPKQLIGIYSQNrPEWILYEQGCYSFSLVVVPLYDTLGPdacafiiRQT 154
Cdd:cd05931 23 ETLT--YAELD-----RRARAIAARLQAVGKPGDRVLLLAPPG-LDFVAAFLGCLYAGAIAVPLPPPTPG-------RHA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 155 DMQVVIVEDDGKAAMLLEKAPRSLkiivaikpIRQTTLERARSRGIQIFsFIDVEKLGAKGNHPEVPPTAEDLCTVCYTS 234
Cdd:cd05931 88 ERLAAILADAGPRVVLTTAAALAA--------VRAFAASRPAAGTPRLL-VVDLLPDTSAADWPPPSPDPDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 235 GTTGNPKGVMLTHGNVVAGVCSVILQMGDhriRAGDVMVSFLPLAH-MferccenGMY-------YVGGCVGFYSgdike 306
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIRRAYGL---DPGDVVVSWLPLYHdM-------GLIgglltplYSGGPSVLMS----- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 307 lTND--------LKML---KPTVMPAvPrllNRVYDKIQNDISASGLK-------RGLFNMAMRakekeIARGVLRRngc 368
Cdd:cd05931 224 -PAAflrrplrwLRLIsryRATISAA-P---NFAYDLCVRRVRDEDLEgldlsswRVALNGAEP-----VRPATLRR--- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 369 wdklvFkkvHQAFGG-NLR--------------LMVVGSAPLAG-NVLTFMRCALGCLVLEGYGQTEctGAITLTVqgdh 432
Cdd:cd05931 291 -----F---AEAFAPfGFRpeafrpsyglaeatLFVSGGPPGTGpVVLRVDRDALAGRAVAVAADDP--AARELVS---- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 433 vpnhVGPPVSCNAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAE------AIDSEGWHHTGDVGMwLPNGT 506
Cdd:cd05931 357 ----CGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLGF-LHDGE 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 281366413 507 LRIIDRRKHIFKLSqGEYIVPEKIEniYTLSQyvnqvyVYGESLKSCIIAVVVPDTDV 564
Cdd:cd05931 432 LYITGRLKDLIIVR-GRNHYPQDIE--ATAEE------AHPALRPGCVAAFSVPDDGE 480
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
218-533 |
2.36e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 91.83 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 218 PEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGV-CSVILQMGDHRIRAGD-VMVSFLPLAHMFerccenGM-YYVG 294
Cdd:PLN02574 191 PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVeLFVRFEASQYEYPGSDnVYLAALPMFHIY------GLsLFVV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 295 GCVGFYSG-------DIKELTNDLKMLKPTVMPAVPRLLnrvydkiqndisasglkrglfnMAMRAKEKEIARGVLrrng 367
Cdd:PLN02574 265 GLLSLGSTivvmrrfDASDMVKVIDRFKVTHFPVVPPIL----------------------MALTKKAKGVCGEVL---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 368 cwdklvfkkvhqafgGNLRLMVVGSAPLAGNVLT-FMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNH--VGPPVSCN 444
Cdd:PLN02574 319 ---------------KSLKQVSCGAAPLSGKFIQdFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYssVGLLAPNM 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 445 AVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEY 524
Cdd:PLN02574 384 QAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQ 462
|
....*....
gi 281366413 525 IVPEKIENI 533
Cdd:PLN02574 463 IAPADLEAV 471
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
84-568 |
2.77e-19 |
|
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: 91.66 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 163
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 D--GKAAMLLEKAPRSLKIIVAIKPIRQTTLERARSRGIQIFSfidvEKLGAKGNHPEvpptaeDLCTVCYTSGTTGNPK 241
Cdd:cd05959 110 ElaPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEA----EQLKPAATHAD------DPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 242 GVMLTHGNVVAgVCSV----ILqmgdhRIRAGDVMVSFLPLahMFERCCENGMYY---VGGCVGFYSGDIKELT--NDLK 312
Cdd:cd05959 180 GVVHLHADIYW-TAELyarnVL-----GIREDDVCFSAAKL--FFAYGLGNSLTFplsVGATTVLMPERPTPAAvfKRIR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 313 MLKPTVMPAVPRLLNrvydkiqndisasglkrglfnmAMRAKEKEIARGVLRrngcwdklvfkkvhqafggnLRLMVVGS 392
Cdd:cd05959 252 RYRPTVFFGVPTLYA----------------------AMLAAPNLPSRDLSS--------------------LRLCVSAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 393 APLAGNVLTFMRCALGCLVLEGYGQTEcTGAITLT-VQGDHVPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSN 471
Cdd:cd05959 290 EALPAEVGERWKARFGLDILDGIGSTE-MLHIFLSnRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 472 VFHGYYKDPEKTAEAIDSEgWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENiyTLSQY--VNQVYVYGES 549
Cdd:cd05959 368 SATMYWNNRDKTRDTFQGE-WTRTGDKYVRDDDGFYTYAGRADDMLKVS-GIWVSPFEVES--ALVQHpaVLEAAVVGVE 443
|
490 500 510
....*....|....*....|....*....|.
gi 281366413 550 LKSCII---AVVVP---------DTDVLKQW 568
Cdd:cd05959 444 DEDGLTkpkAFVVLrpgyedseaLEEELKEF 474
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
85-567 |
8.00e-19 |
|
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: 89.32 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 85 NYDEaLLRAKNFGAGMLA-LGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPdacafiirqtdmqvvived 163
Cdd:cd05972 2 SFRE-LKRESAKAANVLAkLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGP------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 dgkaamllekaprslkiivaiKPIRQTtLERARSRGIQIfsfidveklgakgnhpevppTAEDLCTVCYTSGTTGNPKGV 243
Cdd:cd05972 62 ---------------------KDIEYR-LEAAGAKAIVT--------------------DAEDPALIYFTSGTTGLPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 244 MLTHGNVVAgvcsVILQMGD-HRIRAGDVMVS--------------FLPLAHmferccengmyyvGGCVGFYSG---DIK 305
Cdd:cd05972 100 LHTHSYPLG----HIPTAAYwLGLRPDDIHWNiadpgwakgawssfFGPWLL-------------GATVFVYEGprfDAE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 306 ELTNDLKMLKPTVM---PAVPRLLnrvydkIQNDISAsglkrglfnmamrakekeiargvlrrngcwdklvFKKVHqafg 382
Cdd:cd05972 163 RILELLERYGVTSFcgpPTAYRML------IKQDLSS----------------------------------YKFSH---- 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 383 gnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVD-----VPEMEyf 457
Cdd:cd05972 199 --LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDddgreLPPGE-- 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 458 anqnTGEVCVRGSNV--FHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIENiyT 535
Cdd:cd05972 275 ----EGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVES--A 346
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 281366413 536 LSQY--VNQVYV-------YGESLKsciiAVVV-----PDTDVLKQ 567
Cdd:cd05972 347 LLEHpaVAEAAVvgspdpvRGEVVK----AFVVltsgyEPSEELAE 388
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
84-556 |
8.63e-19 |
|
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: 89.88 E-value: 8.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 163
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 DGKAAmllekaprslkiivaikpirqttlERARSRGIQIFSFIDVEKLGAKGNH----PEVPPTAEDLCTVCYTSGTTGN 239
Cdd:cd05923 109 DAQVM------------------------DAIFQSGVRVLALSDLVGLGEPESAgpliEDPPREPEQPAFVFYTSGTTGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 240 PKGVMLTHGNVVAGVCSVILQMGdHRIRAGDVMVSFLPLAH-------MFERCCENGMYYVggCVGFYSGDIKELTNDLK 312
Cdd:cd05923 165 PKGAVIPQRAAESRVLFMSTQAG-LRHGRHNVVLGLMPLYHvigffavLVAALALDGTYVV--VEEFDPADALKLIEQER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 313 MlkpTVMPAVPRLlnrvYDKIQNDISASGLKrglfnmaMRAKEKEIARGVLRRNGcwdklVFKKVHQAFGGnlrlmvvgs 392
Cdd:cd05923 242 V---TSLFATPTH----LDALAAAAEFAGLK-------LSSLRHVTFAGATMPDA-----VLERVNQHLPG--------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 393 aplagnvltfmrcalgcLVLEGYGQTEctgAITLTVQGDHVPNHVGPPVSCNAVKLVDVPE--MEYFANQNTGEVCVR-- 468
Cdd:cd05923 294 -----------------EKVNIYGTTE---AMNSLYMRDARTGTEMRPGFFSEVRIVRIGGspDEALANGEEGELIVAaa 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 469 GSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV--- 545
Cdd:cd05923 354 ADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVigv 431
|
490
....*....|....*
gi 281366413 546 ----YGESLKSCIIA 556
Cdd:cd05923 432 aderWGQSVTACVVP 446
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
69-564 |
1.08e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 89.74 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 69 PCLGWRETLTSpyqWinyDEALLRAKNFGAGMLAL--GARPKQlIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDA 146
Cdd:PRK07867 20 RGLYFEDSFTS---W---REHIRGSAARAAALRARldPTRPPH-VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 147 CAFIIRQTDMQVVIVEDdgKAAMLLEKAPRSLKIIVAIKPirQTTLERARSRGIQIfsfidveklgakgnhPEVPPTAED 226
Cdd:PRK07867 93 LARDIAHADCQLVLTES--AHAELLDGLDPGVRVINVDSP--AWADELAAHRDAEP---------------PFRVADPDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 227 LCTVCYTSGTTGNPKGVMLTHGNVV-AGVcsvilQMGDHR-IRAGDVMVSFLPLAHmferccENGMYyVGGCVGFYSGdi 304
Cdd:PRK07867 154 LFMLIFTSGTSGDPKAVRCTHRKVAsAGV-----MLAQRFgLGPDDVCYVSMPLFH------SNAVM-AGWAVALAAG-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 305 keltndlkmlkptvmpavprllnrvydkiqndisASglkrglfnMAMRAKEKeiARGVL---RRNGC-WDKLVFKKVHQA 380
Cdd:PRK07867 220 ----------------------------------AS--------IALRRKFS--ASGFLpdvRRYGAtYANYVGKPLSYV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 381 FG---------GNLRlMVVGSAPLAGNVLTFMRcALGCLVLEGYGQTEctGAITLTVQGDHVPNHVGPPVScnAVKLVDV 451
Cdd:PRK07867 256 LAtperpddadNPLR-IVYGNEGAPGDIARFAR-RFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPP--GVAIVDP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 452 ------PEMEY------FANQNTGE-VCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTL----RIIDRRK 514
Cdd:PRK07867 330 dtgtecPPAEDadgrllNADEAIGElVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAyfagRLGDWMR 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 281366413 515 hifklSQGEYIVPEKIENIytLSQY--VNQVYVYGeslksciiavvVPDTDV 564
Cdd:PRK07867 409 -----VDGENLGTAPIERI--LLRYpdATEVAVYA-----------VPDPVV 442
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
226-560 |
3.90e-18 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 88.15 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 226 DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVIL--QMGdhrirAGDVMVSFLPLAHMFERCCENGMYYVGG---CVGFY 300
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIgwEMG-----TCPVYLWTLPMFHCNGWTFTWGTAARGGtsvCMRHV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 301 SGdiKELTNDLKMLKPTVMPAVPRLLNRVYDKIQNDISasglkrglfnmamrakekeiargvlrrngcwdklvfkkvHQA 380
Cdd:PLN03102 262 TA--PEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLS---------------------------------------PRS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 381 fgGNLRLMVVGSAPLAGNVLTFMRcaLGCLVLEGYGQTECTGAITLTVQGDH---VPNH------VGPPVSCNAVKLVDV 451
Cdd:PLN03102 301 --GPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPVLFCEWQDEwnrLPENqqmelkARQGVSILGLADVDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 452 PEMEYFAN-----QNTGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIV 526
Cdd:PLN03102 377 KNKETQESvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENIS 454
|
330 340 350
....*....|....*....|....*....|....
gi 281366413 527 PEKIENIytlsqyvnqVYVYGESLKSCIIAVVVP 560
Cdd:PLN03102 455 SVEVENV---------LYKYPKVLETAVVAMPHP 479
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
223-513 |
1.21e-17 |
|
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: 86.06 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 223 TAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMG-DHRIR-------AGDVMV--SFLPLAHmferccengmyy 292
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGlTSESRvlqfasyTFDVSIleIFTTLAA------------ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 293 vGGCVGFYS-----GDIKELTNDLK----MLKPTVMpavpRLLNRvydkiqndisasglkrglfnmamrakekeiargvl 363
Cdd:cd05918 172 -GGCLCIPSeedrlNDLAGFINRLRvtwaFLTPSVA----RLLDP----------------------------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 364 rrngcwdKLVFkkvhqafggNLRLMVVGSAPLAGNVLTfmRCALGCLVLEGYGQTECTGAITLTVQGDHV-PNHVGPPVS 442
Cdd:cd05918 212 -------EDVP---------SLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVPSTdPRNIGRPLG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 443 CNAVkLVDvPEmeyfaNQN-------TGEVCVRGSNVFHGYYKDPEKTAEA-IDSEGWHH------------TGDVGMWL 502
Cdd:cd05918 274 ATCW-VVD-PD-----NHDrlvpigaVGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYN 346
|
330
....*....|.
gi 281366413 503 PNGTLRIIDRR 513
Cdd:cd05918 347 PDGSLEYVGRK 357
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
142-574 |
2.24e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 85.67 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 142 LGPDACAFIIRQTDMQVVIVED------DGKAAMLLEKAPRSLK----IIVAIKPIRQTTLERARSRGIqifsfIDVEKL 211
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMVDQefftlaEEALKILAEKKKSSFKppllIVIGDPTCDPKSLQYALGKGA-----IEYEKF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 212 GAKGNhPEV---PPTAE-DLCTVCYTSGTTGNPKGVMLTH--GNVVAGVCSVILQMGDhriraGDVMVSFLPLAHmferc 285
Cdd:PLN02479 179 LETGD-PEFawkPPADEwQSIALGYTSGTTASPKGVVLHHrgAYLMALSNALIWGMNE-----GAVYLWTLPMFH----- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 286 CeNGMYYVGGCVGFYSGDI-------KELTNDLKMLKPTVMPAVPRLLNrvydkiqndisasglkrglfnMAMRAKEKEI 358
Cdd:PLN02479 248 C-NGWCFTWTLAALCGTNIclrqvtaKAIYSAIANYGVTHFCAAPVVLN---------------------TIVNAPKSET 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 359 ARGVLRrngcwdklvfkKVHqafggnlrLMVVGSAPLAgNVLTFMRcALGCLVLEGYGQTECTGAITLTV---QGDHVPN 435
Cdd:PLN02479 306 ILPLPR-----------VVH--------VMTAGAAPPP-SVLFAMS-EKGFRVTHTYGLSETYGPSTVCAwkpEWDSLPP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 436 HVGPPVSC---------NAVKLVDVPEMEYFANQNT--GEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPN 504
Cdd:PLN02479 365 EEQARLNArqgvryiglEGLDVVDTKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPD 443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366413 505 GTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV-------YGESlkSCIIAVVVPDTDVLKQWATENNV 574
Cdd:PLN02479 444 GYIEIKDRSKDII-ISGGENISSLEVENVVYTHPAVLEASVvarpderWGES--PCAFVTLKPGVDKSDEAALAEDI 517
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
52-514 |
2.31e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 85.78 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 52 RTLYQTFREGAYASNNGPCL-------GWRETLTspyqwINYDEaLLRAKNFGAGML-ALGARPKQLIGIYSQNRPEWIl 123
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPALsflldadPLDRPET-----WTYAE-LLADVTRTANLLhSLGVGPGDVVAFLLPNLPETH- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 124 yeqgcysFSL-------VVVPLYDTLGPDACAFIIRQTDMQVVIV--EDDG-----KAAMLLEKAPrSLKIIVAIKPIRQ 189
Cdd:PRK07529 98 -------FALwggeaagIANPINPLLEPEQIAELLRAAGAKVLVTlgPFPGtdiwqKVAEVLAALP-ELRTVVEVDLARY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 190 TTLER-------ARSRGIQIFSFiDVEKLGAKGNHPEV--PPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQ 260
Cdd:PRK07529 170 LPGPKrlavpliRRKAHARILDF-DAELARQPGDRLFSgrPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 261 MGdhrIRAGDVMVSFLPLAHMFErCCENGMYYV--GGCVGF-----YSGD--IKELTNDLKMLKPTVMPAVPR----LLN 327
Cdd:PRK07529 249 LG---LGPGDTVFCGLPLFHVNA-LLVTGLAPLarGAHVVLatpqgYRGPgvIANFWKIVERYRINFLSGVPTvyaaLLQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 328 RVYDKiqNDISAsglkrglfnmamrakekeiargvlrrngcwdklvfkkvhqafggnLRLMVVGSAPLAGNVL-TFMRcA 406
Cdd:PRK07529 325 VPVDG--HDISS---------------------------------------------LRYALCGAAPLPVEVFrRFEA-A 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 407 LGCLVLEGYGQTECTGAITLT-VQGDHVPNHVGPPVSCNAVKLVDV-PEMEYF---ANQNTGEVCVRGSNVFHGYYkDPE 481
Cdd:PRK07529 357 TGVRIVEGYGLTEATCVSSVNpPDGERRIGSVGLRLPYQRVRVVILdDAGRYLrdcAVDEVGVLCIAGPNVFSGYL-EAA 435
|
490 500 510
....*....|....*....|....*....|...
gi 281366413 482 KTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRK 514
Cdd:PRK07529 436 HNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
82-564 |
2.45e-17 |
|
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: 85.04 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 82 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIV 161
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 162 EDDgkaamLLEKAPRSLKIIVaikpirqttlerarsrgiqifsfIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPK 241
Cdd:cd12116 91 DDA-----LPDRLPAGLPVLL-----------------------LALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 242 GVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVS-------------FLPLAHmferccengmyyvGGCVGFYSGDIKELT 308
Cdd:cd12116 143 GVVVSHRNLVNFLHSMRERLG---LGPGDRLLAvttyafdisllelLLPLLA-------------GARVVIAPRETQRDP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 309 NDLKML----KPTVMPAVPRLLnrvydkiqndisasglkRGLFNMAMRAKEkeiargvlrrngcwdklvfkkvhqafggN 384
Cdd:cd12116 207 EALARLieahSITVMQATPATW-----------------RMLLDAGWQGRA----------------------------G 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 385 LRLMVVGSA---PLAGNVltfmrCALGCLVLEGYGQTECT--GAITLtVQGDHVPNHVGPPVSCNAVKLVD-----VPEM 454
Cdd:cd12116 242 LTALCGGEAlppDLAARL-----LSRVGSLWNLYGPTETTiwSTAAR-VTAAAGPIPIGRPLANTQVYVLDaalrpVPPG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 455 EyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAI-------DSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVP 527
Cdd:cd12116 316 V------PGELYIGGDGVAQGYLGRPALTAERFvpdpfagPGSRLYRTGDLVRRRADGRLEYLGRADGQVKI-RGHRIEL 388
|
490 500 510
....*....|....*....|....*....|....*....
gi 281366413 528 EKIENIYTLSQYVNQ--VYVYGESLKSCIIAVVVPDTDV 564
Cdd:cd12116 389 GEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLKAGA 427
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
209-514 |
2.55e-17 |
|
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: 85.41 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 209 EKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILqmgDHRIRAGDVMVSFLPLAHmferccen 288
Cdd:cd05906 151 ELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ---HNGLTPQDVFLNWVPLDH-------- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 289 gmyyVGGCVGFYSGDIkeltnDLKMLK---PTV-MPAVPRLLNRVYDKIQNDISASGlkrglfNMA---MRAKEKEIARG 361
Cdd:cd05906 220 ----VGGLVELHLRAV-----YLGCQQvhvPTEeILADPLRWLDLIDRYRVTITWAP------NFAfalLNDLLEEIEDG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 362 vlrrngCWDKlvfkkvhqafgGNLRLMVVGSAPL---AGNVLTFM--RCALGCLVLE-GYGQTE-CTGAI------TLTV 428
Cdd:cd05906 285 ------TWDL-----------SSLRYLVNAGEAVvakTIRRLLRLlePYGLPPDAIRpAFGMTEtCSGVIysrsfpTYDH 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 429 QGDHVPNHVGPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGmWLP 503
Cdd:cd05906 348 SQALEFVSLGRPIPGVSMRIVDdegqlLPEGE------VGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLD 420
|
330
....*....|.
gi 281366413 504 NGTLRIIDRRK 514
Cdd:cd05906 421 NGNLTITGRTK 431
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
219-571 |
2.63e-17 |
|
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: 85.07 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 219 EVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVV--------AGVCSVILQMGDHRIRAGDVMVS--FLPLAhmfercCEN 288
Cdd:cd17655 131 EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVnlvewankVIYQGEHLRVALFASISFDASVTeiFASLL------SGN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 289 GMYYVGgcvgfysgdikeltndlkmlKPTVMPAVPrlLNRVYDkiQNDISASGLKRGLFNMAMRAKEKEiargvlrrngc 368
Cdd:cd17655 205 TLYIVR--------------------KETVLDGQA--LTQYIR--QNRITIIDLTPAHLKLLDAADDSE----------- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 369 wdklvfkkvhqafGGNLRLMVVG----SAPLAGNVLTFMRcaLGCLVLEGYGQTECTGAITL------TVQGDHVPnhVG 438
Cdd:cd17655 250 -------------GLSLKHLIVGgealSTELAKKIIELFG--TNPTITNAYGPTETTVDASIyqyepeTDQQVSVP--IG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 439 PPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEA------IDSEGWHHTGDVGMWLPNGTL 507
Cdd:cd17655 313 KPLGNTRIYILDqygrpQPVGV------AGELYIGGEGVARGYLNRPELTAEKfvddpfVPGERMYRTGDLARWLPDGNI 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281366413 508 RIIDRRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYVY---GESLKSCIIAVVVPDTDV----LKQWATE 571
Cdd:cd17655 387 EFLGRIDHQVKI-RGYRIELGEIEARLLQHPDIKEAVVIarkDEQGQNYLCAYIVSEKELpvaqLREFLAR 456
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
142-525 |
3.20e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 85.38 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 142 LGPDACAFIIRQTDMQVVIVE----DDGKAAMLLEKAPRSLKIIVAIKPirqttlerarSRGIQIFSFIDVEKLGAKGNh 217
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDtefaEVAREALALLPGPKPLVIDVDDPE----------YPGGRFIGALDYEAFLASGD- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 218 PE---VPPTAE-DLCTVCYTSGTTGNPKGVMLTH--------GNVVAGvcsvilQMGDHriragDVMVSFLPLAHmferc 285
Cdd:PRK08162 171 PDfawTLPADEwDAIALNYTSGTTGNPKGVVYHHrgaylnalSNILAW------GMPKH-----PVYLWTLPMFH----- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 286 CeNG------MYYVGG---CV-GFYSGDIKELTNDLKMlkpTVMPAVPRLLNrvydkiqndisasglkrGLFNMAMRAKE 355
Cdd:PRK08162 235 C-NGwcfpwtVAARAGtnvCLrKVDPKLIFDLIREHGV---THYCGAPIVLS-----------------ALINAPAEWRA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 356 KeIARGVlrrngcwdklvfkkvhqafggnlRLMVVGSAPLAGnVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDH--- 432
Cdd:PRK08162 294 G-IDHPV-----------------------HAMVAGAAPPAA-VIAKME-EIGFDLTHVYGLTETYGPATVCAWQPEwda 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 433 --------------VPNHVgppvsCNAVKLVDVPEMEYFAN--QNTGEVCVRGSNVFHGYYKDPEKTAEAIDSeGWHHTG 496
Cdd:PRK08162 348 lplderaqlkarqgVRYPL-----QEGVTVLDPDTMQPVPAdgETIGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTG 421
|
410 420
....*....|....*....|....*....
gi 281366413 497 DVGMWLPNGTLRIIDRRKHIFkLSQGEYI 525
Cdd:PRK08162 422 DLAVLHPDGYIKIKDRSKDII-ISGGENI 449
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
197-639 |
4.61e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 84.85 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 197 SRGIQIFSFIDVE---KLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMV 273
Cdd:PLN02860 141 SVFIFLNSFLTTEmlkQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVG---YGEDDVYL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 274 SFLPLAHMFERCCENGMYYVGGC-VGFYSGDIKELTNDLKMLKPTVMPAVPRLLNrvydkiqnDISASGlkrglfNMAMR 352
Cdd:PLN02860 218 HTAPLCHIGGLSSALAMLMVGAChVLLPKFDAKAALQAIKQHNVTSMITVPAMMA--------DLISLT------RKSMT 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 353 AKEKEIARGVLRRNGCWDKLVFKKVHQAFGgNLRLMVVGSAPLAGNVLTFMRCalgclvlegYGQTECTGAITLTVQGDH 432
Cdd:PLN02860 284 WKVFPSVRKILNGGGSLSSRLLPDAKKLFP-NAKLFSAYGMTEACSSLTFMTL---------HDPTLESPKQTLQTVNQT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 433 VPNHVGPPVSCNAVKlvDVPEMEYFANQN----TGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLR 508
Cdd:PLN02860 354 KSSSVHQPQGVCVGK--PAPHVELKIGLDessrVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLW 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 509 IIDRRKHIFKlSQGEYIVPEKIENIytLSQY--VNQVYVYG---ESLKSCIIAVVvpdtdVLKQ-WATENNvrgtlsVLC 582
Cdd:PLN02860 432 LIGRSNDRIK-TGGENVYPEEVEAV--LSQHpgVASVVVVGvpdSRLTEMVVACV-----RLRDgWIWSDN------EKE 497
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 281366413 583 NNKNVKELIMNDMLNWGKQSGLKSFEQVKDIYLHPDPFSvqnglLTPTFKAKRPQLK 639
Cdd:PLN02860 498 NAKKNLTLSSETLRHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
414-560 |
7.22e-17 |
|
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: 82.35 E-value: 7.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 414 GYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAID 488
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDedgreVPDGE------VGEIVARGPTVMAGYWNRPEVNARRTR 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 489 SeGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIENiyTLSQY--VNQVYV-------YGESLKsciiAVVV 559
Cdd:cd17636 216 G-GWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIYPAEVER--CLRQHpaVADAAVigvpdprWAQSVK----AIVV 287
|
.
gi 281366413 560 P 560
Cdd:cd17636 288 L 288
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
82-546 |
1.15e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 83.65 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 82 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPL-YDTLGPDaCAFIIRQTDMQVVI 160
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPInTALRGPQ-LEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 161 VEDDGKAAM-LLEKAPRSLKIIVAIKPIRQTTLERArsrgiqiFSFIDVEKLGAKGnhPEVPPTAEDLCTVCYTSGTTGN 239
Cdd:PRK06155 124 VEAALLAALeAADPGDLPLPAVWLLDAPASVSVPAG-------WSTAPLPPLDAPA--PAAAVQPGDTAAILYTSGTTGP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 240 PKGVMLTHGNV-VAGVCSViLQMGdhrIRAGDVMVSFLPLAH-----MFERCCENGMYYV-----------------GGC 296
Cdd:PRK06155 195 SKGVCCPHAQFyWWGRNSA-EDLE---IGADDVLYTTLPLFHtnalnAFFQALLAGATYVleprfsasgfwpavrrhGAT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 297 VGFYSGDIkeltndlkmlkptvmpaVPRLLNRvyDKIQNDiSASGLKRGLfnmamrakekeiARGVLRRngcwdklvfkk 376
Cdd:PRK06155 271 VTYLLGAM-----------------VSILLSQ--PARESD-RAHRVRVAL------------GPGVPAA----------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 377 VHQAFggnlrlmvvgsaplagnvltFMRCalGCLVLEGYGQTEcTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEY 456
Cdd:PRK06155 308 LHAAF--------------------RERF--GVDLLDGYGSTE-TNFVIAVTHGSQRPGSMGRLAPGFEARVVDEHDQEL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 457 FANQnTGEVCVRGSNVF---HGYYKDPEKTAEAIDSEgWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIENI 533
Cdd:PRK06155 365 PDGE-PGELLLRADEPFafaTGYFGMPEKTVEAWRNL-WFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV 441
|
490
....*....|...
gi 281366413 534 YTLSQYVNQVYVY 546
Cdd:PRK06155 442 LLSHPAVAAAAVF 454
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
84-531 |
1.52e-16 |
|
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: 82.51 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 163
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 DgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptaeDLCTVCYTSGTTGNPKGV 243
Cdd:cd05919 91 D-------------------------------------------------------------DIAYLLYSSGTTGPPKGV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 244 MLTHGNVVAGV---CSVILqmgdhRIRAGDVMVSflpLAHM-FERCCENGMY---YVGGCVGFYSG--DIKELTNDLKML 314
Cdd:cd05919 110 MHAHRDPLLFAdamAREAL-----GLTPGDRVFS---SAKMfFGYGLGNSLWfplAVGASAVLNPGwpTAERVLATLARF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 315 KPTVMPAVPRLLNRVYDkiQNDISASglkrglfnmAMRAkekeiargvlrrngcwdklvfkkvhqafggnLRLMVVGSAP 394
Cdd:cd05919 182 RPTVLYGVPTFYANLLD--SCAGSPD---------ALRS-------------------------------LRLCVSAGEA 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 395 LAGNVLTFMRCALGCLVLEGYGQTEcTGAITLTVQ-GDHVPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVF 473
Cdd:cd05919 220 LPRGLGERWMEHFGGPILDGIGATE-VGHIFLSNRpGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGDLLVRGPSAA 297
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 281366413 474 HGYYKDPEKTaEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIE 531
Cdd:cd05919 298 VGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVE 353
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
84-531 |
2.25e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 82.48 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 163
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 DGK----AAMLLEKAP---RSLKIIVAIKPIRQTTLERARSRGIQIFSFIDVEKLGAKGnhpeVPPTAEDLCTVCYT-SG 235
Cdd:PRK06164 116 GFKgidfAAILAAVPPdalPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAAG----ERAADPDAGALLFTtSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 236 TTGNPKGVM------LTHGNVVAGVCSVilqmgdhriRAGDVMVSFLPLAHMFerccenGMyyvGGCVGFYSGDIkeltn 309
Cdd:PRK06164 192 TTSGPKLVLhrqatlLRHARAIARAYGY---------DPGAVLLAALPFCGVF------GF---STLLGALAGGA----- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 310 dlkmlkPTVMPAV---PRLLNRVYD-KIQNDISASGLKRGLFNMAMRAKekeiARGVLRRNGcwdklvFKKVHQAFGGNL 385
Cdd:PRK06164 249 ------PLVCEPVfdaARTARALRRhRVTHTFGNDEMLRRILDTAGERA----DFPSARLFG------FASFAPALGELA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 386 RLMVVGSAPLAGNvltfmrcalgclvlegYGQTE-----CTGAITLTVQGDHVPNhvGPPVSCNA-VKLVDVPEMEYFAN 459
Cdd:PRK06164 313 ALARARGVPLTGL----------------YGSSEvqalvALQPATDPVSVRIEGG--GRPASPEArVRARDPQDGALLPD 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366413 460 QNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIE 531
Cdd:PRK06164 375 GESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIE 445
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
86-532 |
9.68e-16 |
|
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: 80.17 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 86 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVedDG 165
Cdd:cd05971 9 FKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--DG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 166 kaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevpptAEDLCTVCYTSGTTGNPKGVMl 245
Cdd:cd05971 87 ----------------------------------------------------------SDDPALIIYTSGTTGPPKGAL- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 246 tHGnvvagvcsvilqmgdHRIRAGDVMVSFLPLaHMFERCcENGMY------YVGGCVGfysgdikeltndlkMLKPTVM 319
Cdd:cd05971 108 -HA---------------HRVLLGHLPGVQFPF-NLFPRD-GDLYWtpadwaWIGGLLD--------------VLLPSLY 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 320 PAVPRLLNRV--YDK-------IQNDISASGLKRGLFNMaMRAKEKEIARgvlrrngcwdklvfkkvhqaFGGNLRLMVV 390
Cdd:cd05971 156 FGVPVLAHRMtkFDPkaaldlmSRYGVTTAFLPPTALKM-MRQQGEQLKH--------------------AQVKLRAIAT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 391 GSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAIT-LTVQGDHVPNHVGPPVSCNAVKLVDVPEMEYFANQnTGEVCVR- 468
Cdd:cd05971 215 GGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGnCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGE-VGEIAVEl 293
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366413 469 -GSNVFHGYYKDPEKTAEAIDSeGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIEN 532
Cdd:cd05971 294 pDPVAFLGYWNNPSATEKKMAG-DWLLTGDLGRKDSDGYFWYVGRDDDVIT-SSGYRIGPAEIEE 356
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
98-561 |
1.10e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 80.47 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 98 AGMLALGARPKQLIGIYSQNRPEwiLYEQGCYSFSL--VVVPLYDTLGPDACAFIIRQTDMQVVIVEDD--GKAAMLLEK 173
Cdd:PRK07470 47 AALAARGVRKGDRILVHSRNCNQ--MFESMFAAFRLgaVWVPTNFRQTPDEVAYLAEASGARAMICHADfpEHAAAVRAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 174 APrSLKIIVAIKPIRQTTlerarsrgiqifsfiDVEKLGAKGNHPEVPPTA---EDLCTVCYTSGTTGNPKGVMLTHGN- 249
Cdd:PRK07470 125 SP-DLTHVVAIGGARAGL---------------DYEALVARHLGARVANAAvdhDDPCWFFFTSGTTGRPKAAVLTHGQm 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 250 --VVAG-VCSVILQMGDHriragDVMVSFLPLAHmferccengmyyvggcvgfySGDIKELTNDLKMLKpTVMPAVPRL- 325
Cdd:PRK07470 189 afVITNhLADLMPGTTEQ-----DASLVVAPLSH--------------------GAGIHQLCQVARGAA-TVLLPSERFd 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 326 LNRVYDKIQndisasglKRGLFNM-------AMRAKEKEIARgvlrrngcWDklvfkkvHqafgGNLRLMVVGSAPLAGN 398
Cdd:PRK07470 243 PAEVWALVE--------RHRVTNLftvptilKMLVEHPAVDR--------YD-------H----SSLRYVIYAGAPMYRA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 399 VLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHvGPPV---SCN------AVKLVDVPEMEYFANQnTGEVCVRG 469
Cdd:PRK07470 296 DQKRALAKLGKVLVQYFGLGEVTGNITVLPPALHDAED-GPDArigTCGfertgmEVQIQDDEGRELPPGE-TGEICVIG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 470 SNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYGes 549
Cdd:PRK07470 374 PAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-- 449
|
490
....*....|..
gi 281366413 550 lksciiavvVPD 561
Cdd:PRK07470 450 ---------VPD 452
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
225-576 |
2.62e-15 |
|
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: 77.69 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 225 EDLCTVCYTSGTTGNPKGVMLTHGNVVAgvCSVILQMGDHRIRAGDVMVSFLPLAHMFE----RCCengMYYVGGCVGFy 300
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFA--VPDILQKEGLNWVVGDVTYLPLPATHIGGlwwiLTC---LIHGGLCVTG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 301 sGDIKELTNDLKML---KPTVMPAVPRLLNRVYDKIQNDISASglkrglfnmamrakekeiargvlrrngcwdklvfkkv 377
Cdd:cd17635 75 -GENTTYKSLFKILttnAVTTTCLVPTLLSKLVSELKSANATV------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 378 hqafgGNLRLMVVGSA-PLAGNVLTFMRCALgCLVLEGYGQTECTGAITLTVQGDHVP-NHVGPPVSCNAVKLVDVPEME 455
Cdd:cd17635 117 -----PSLRLIGYGGSrAIAADVRFIEATGL-TNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 456 YFANQNtGEVCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYT 535
Cdd:cd17635 191 GPSASF-GTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAE 267
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 281366413 536 LSQYVNQVYVYgeSLKSCIIAVVVPDTDVLKQWATENNVRG 576
Cdd:cd17635 268 GVSGVQECACY--EISDEEFGELVGLAVVASAELDENAIRA 306
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
167-532 |
9.58e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 77.25 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 167 AAMLLEKAPRSLKIIVAIKP---IRQTTLERARSRGiqifsfidveklgAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGV 243
Cdd:PRK09274 126 ARRLFGWGKPSVRRLVTVGGrllWGGTTLATLLRDG-------------AAAPFPMADLAPDDMAAILFTSGSTGTPKGV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 244 MLTHGNVVAgvcsVILQMGDHR-IRAGDVMVSFLPLAHMFERCCenGMYYVggcvgfysgdIKELtnDLKmlKP-TVMPA 321
Cdd:PRK09274 193 VYTHGMFEA----QIEALREDYgIEPGEIDLPTFPLFALFGPAL--GMTSV----------IPDM--DPT--RPaTVDPA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 322 vprllnRVYDKIQndisasglKRGLFNMA-----MRakekeiargVLRRNGCWDKLVFkkvhqafgGNLRLMVVGSAPLA 396
Cdd:PRK09274 253 ------KLFAAIE--------RYGVTNLFgspalLE---------RLGRYGEANGIKL--------PSLRRVISAGAPVP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 397 GNVLTFMRCAL--GCLVLEGYGQTEC------TGAITLTVQGDHVPNH----VGPPVSCNAVKLVDV---P-----EMEY 456
Cdd:PRK09274 302 IAVIERFRAMLppDAEILTPYGATEAlpissiESREILFATRAATDNGagicVGRPVDGVEVRIIAIsdaPipewdDALR 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 457 FANQNTGEVCVRGSNVFHGYYKDPEKTAEA--IDSEG--WHHTGDVGmWL-PNGTLRIIDRRKHIFKLSQGEY--IVPEK 529
Cdd:PRK09274 382 LATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLytIPCER 460
|
...
gi 281366413 530 IEN 532
Cdd:PRK09274 461 IFN 463
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
218-545 |
1.75e-14 |
|
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: 76.16 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 218 PEVPPTAEDLCTVCYTSGTTGNPKGVMLTHgnvvAGVCSVILQM-GDHRIRAGDVM---------VS----FLPLAhmfe 283
Cdd:cd17646 131 PLVPPRPDNLAYVIYTSGSTGRPKGVMVTH----AGIVNRLLWMqDEYPLGPGDRVlqktplsfdVSvwelFWPLV---- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 284 rccengmyyVGGCVGFYS----GDIKELTNDLKMLKPTVMPAVPRLLnrvydkiqndisasglkrglfnmamrakekEIA 359
Cdd:cd17646 203 ---------AGARLVVARpgghRDPAYLAALIREHGVTTCHFVPSML------------------------------RVF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 360 RGVLRRNGCwdklvfkkvhqafgGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITL-TVQGDHVPNHV- 437
Cdd:cd17646 244 LAEPAAGSC--------------ASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVp 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 438 -GPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI------DSEGWHHTGDVGMWLPNGTLRII 510
Cdd:cd17646 310 iGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFvpdpfgPGSRMYRTGDLARWRPDGALEFL 388
|
330 340 350
....*....|....*....|....*....|....*
gi 281366413 511 DRRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYV 545
Cdd:cd17646 389 GRSDDQVKI-RGFRVEPGEIEAALAAHPAVTHAVV 422
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
218-531 |
2.62e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.13 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 218 PEVPPtaEDLCTVCYTSGTTGNPKGVMLTHGNVVAGvcSVILQMGdHRIRAG--DVMVSFLPLAHmferccenGMYYVGG 295
Cdd:PRK05691 161 PALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVAN--EQLIRHG-FGIDLNpdDVIVSWLPLYH--------DMGLIGG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 296 CV-GFYSGdikeltndlkmlKPTVMPAVPRLLNRVYDKIQNDISASGLKRGLFNMAMRAKEKEIARGVLRRngcwdkLVF 374
Cdd:PRK05691 228 LLqPIFSG------------VPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALER------LDL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 375 KKVHQAFGG-------NLRLMVVGSAPLAGNVLTFMRCalgclvlegYGQTECTGAITLTVQGDHVP-----------NH 436
Cdd:PRK05691 290 SRWRVAYSGsepirqdSLERFAEKFAACGFDPDSFFAS---------YGLAEATLFVSGGRRGQGIPaleldaealarNR 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 437 V----GPPV-SC------NAVKLVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI---DSEGWHHTGDVGmWL 502
Cdd:PRK05691 361 AepgtGSVLmSCgrsqpgHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDLG-FL 439
|
330 340
....*....|....*....|....*....
gi 281366413 503 PNGTLRIIDRRKHIFkLSQGEYIVPEKIE 531
Cdd:PRK05691 440 RDGELFVTGRLKDML-IVRGHNLYPQDIE 467
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
196-531 |
2.97e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 75.80 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 196 RSRGIQIfsfIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVilqmgdhRIRAG-----D 270
Cdd:PRK07768 126 EEKGIRV---LTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAM-------FVAAEfdvetD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 271 VMVSFLPLAH-MferccenGMyyVGG-CVGFYSGdikeltNDLKMLKPTVMPAVPRLLNRVYDKIQNDISASglkrGLFN 348
Cdd:PRK07768 196 VMVSWLPLFHdM-------GM--VGFlTVPMYFG------AELVKVTPMDFLRDPLLWAELISKYRGTMTAA----PNFA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 349 MAMRAKekeiargVLRRngcwdklvfkkvhQAFGGN-----LRLMVVGSAPL----------AGNVLTFMRCALGClvle 413
Cdd:PRK07768 257 YALLAR-------RLRR-------------QAKPGAfdlssLRFALNGAEPIdpadvedlldAGARFGLRPEAILP---- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 414 GYGQTECTGAIT-----------------LTVQGDHVPNH---------VGPPVSCNAVKLVD-----VPEMEyfanqnT 462
Cdd:PRK07768 313 AYGMAEATLAVSfspcgaglvvdevdadlLAALRRAVPATkgntrrlatLGPPLPGLEVRVVDedgqvLPPRG------V 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281366413 463 GEVCVRGSNVFHGyYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIE 531
Cdd:PRK07768 387 GVIELRGESVTPG-YLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
75-567 |
5.64e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 74.66 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 75 ETLTspYQWINYDEALLRAKNFGAGMlalgaRPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQT 154
Cdd:PRK13390 23 EQVS--YRQLDDDSAALARVLYDAGL-----RTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 155 DMQVVIVED--DGKAAMLleKAPRSLKIivaikpirqttlerarSRGIQIFSFIDVEK-LGAKGnhpevPPTAEDLC--T 229
Cdd:PRK13390 96 GARVLVASAalDGLAAKV--GADLPLRL----------------SFGGEIDGFGSFEAaLAGAG-----PRLTEQPCgaV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 230 VCYTSGTTGNPKGVM--LTHGNVVA-GVCSVILQMGDHRIRAGDVMVSFLPLAHMFE-RCCenGMYY-VGGCVGFYSG-D 303
Cdd:PRK13390 153 MLYSSGTTGFPKGIQpdLPGRDVDApGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWC--SMVHaLGGTVVLAKRfD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 304 IKELTNDLKMLKPTVMPAVPRLLNRVYdKIQNDIsasglkRGLFNMAmrakekeiargvlrrngcwdklvfkkvhqafgg 383
Cdd:PRK13390 231 AQATLGHVERYRITVTQMVPTMFVRLL-KLDADV------RTRYDVS--------------------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 384 NLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGaITLTVQGDHV--PNHVGPPVsCNAVKLVDVPEMEYFANQn 461
Cdd:PRK13390 271 SLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHG-MTFIDSPDWLahPGSVGRSV-LGDLHICDDDGNELPAGR- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 462 TGEVCVRGSNVFHGYYKDPEKTAEAIDSEG--WHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQY 539
Cdd:PRK13390 348 IGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPA 426
|
490 500
....*....|....*....|....*...
gi 281366413 540 VNQVYVYGeslksciiavvVPDTDVLKQ 567
Cdd:PRK13390 427 VHDVAVIG-----------VPDPEMGEQ 443
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
233-571 |
6.24e-14 |
|
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: 74.67 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 233 TSGTTGNPKGVMLTHGNVV------AGVCsvilqmgdhRIRAGDVMVSFLPLAHMFERCCEN--GMYYVGGCVGFYSGDI 304
Cdd:cd05920 147 SGGTTGTPKLIPRTHNDYAynvrasAEVC---------GLDQDTVYLAVLPAAHNFPLACPGvlGTLLAGGRVVLAPDPS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 305 KELTNDL-KMLKPTVMPAVPRLLNRVYDkiqndiSASGLKRGLfnmamrakekeiargvlrrngcwdklvfkkvhqafgG 383
Cdd:cd05920 218 PDAAFPLiEREGVTVTALVPALVSLWLD------AAASRRADL------------------------------------S 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 384 NLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEctGAITLTVQGDhvPNHV-----GPPVSC-NAVKLVD-----VP 452
Cdd:cd05920 256 SLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE--GLLNYTRLDD--PDEViihtqGRPMSPdDEIRVVDeegnpVP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 453 EMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIEN 532
Cdd:cd05920 332 PGE------EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 281366413 533 IYTLSQYVNQVYV-------YGEslKSCiiAVVV-----PDTDVLKQWATE 571
Cdd:cd05920 405 LLLRHPAVHDAAVvampdelLGE--RSC--AFVVlrdppPSAAQLRRFLRE 451
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
77-531 |
9.44e-14 |
|
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: 73.92 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 77 LTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLyDTLGPDA-CAFIIRQTD 155
Cdd:cd17651 14 LVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPL-DPAYPAErLAFMLADAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 156 MQVVIVEDDgkaamLLEKAPRSLKIIVAIKPIRQTTLERARsrgiqifsfidveklgakgnhPEVPPTAEDLCTVCYTSG 235
Cdd:cd17651 93 PVLVLTHPA-----LAGELAVELVAVTLLDQPGAAAGADAE---------------------PDPALDADDLAYVIYTSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 236 TTGNPKGVMLTHGNVV-----------AGVCSVILQMgdhrirAG---DVMVS--FLPLAHmferccengmyyvGGCVGF 299
Cdd:cd17651 147 STGRPKGVVMPHRSLAnlvawqarassLGPGARTLQF------AGlgfDVSVQeiFSTLCA-------------GATLVL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 300 YSGDIKeltNDLkmlkptvmPAVPRLLNRvydkiqNDISASGLKrglfNMAMRAKEKEIARgvlrrngcwdklvfkkvHQ 379
Cdd:cd17651 208 PPEEVR---TDP--------PALAAWLDE------QRISRVFLP----TVALRALAEHGRP-----------------LG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 380 AFGGNLRLMVVGSAPLAGNVLT--FMRCALGCLVLEGYGQTECTGAITLTVQGDHV----PNHVGPPVSCNAVKLVD--- 450
Cdd:cd17651 250 VRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAawpaPPPIGRPIDNTRVYVLDaal 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 451 --VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGW------HHTGDVGMWLPNGTLRIIDRRKHIFKLSqG 522
Cdd:cd17651 330 rpVPPGV------PGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGRADDQVKIR-G 402
|
....*....
gi 281366413 523 EYIVPEKIE 531
Cdd:cd17651 403 FRIELGEIE 411
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
134-531 |
9.46e-14 |
|
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: 74.07 E-value: 9.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 134 VVVPLYDTLGPDACAFIIRQTDMQVVIVEDDGKAAMLLEKAPRSLKiivaikpirqTTLERARSRGIQIFSFIDVEKLGA 213
Cdd:cd05970 98 IAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAAPECP----------SKPKLVWVGDPVPEGWIDFRKLIK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 214 KGNHPEVPPTA------EDLCTVCYTSGTTGNPKgvMLTH------GNVVAGvcsvilqMGDHRIRAGDVMVSFLPLAhm 281
Cdd:cd05970 168 NASPDFERPTAnsypcgEDILLVYFSSGTTGMPK--MVEHdftyplGHIVTA-------KYWQNVREGGLHLTVADTG-- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 282 FERCCENGMY--YVGGCVGFysgdikelTNDLKMLKPTVM---------------PAVPRLLnrvydkIQNDISASGLKr 344
Cdd:cd05970 237 WGKAVWGKIYgqWIAGAAVF--------VYDYDKFDPKALleklskygvttfcapPTIYRFL------IREDLSRYDLS- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 345 glfnmamrakekeiargvlrrngcwdklvfkkvhqafggNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAI 424
Cdd:cd05970 302 ---------------------------------------SLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 425 TLTVQGDHVPNHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSN-----VFHGYYKDPEKTAEAIdSEGWHHTGDVG 499
Cdd:cd05970 343 ATFPWMEPKPGSMGKPAPGYEIDLID-REGRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAA 420
|
410 420 430
....*....|....*....|....*....|..
gi 281366413 500 MWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIE 531
Cdd:cd05970 421 WMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVE 451
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
219-533 |
9.89e-14 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 74.36 E-value: 9.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 219 EVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVcSVILQMGDHRIRagDVMVSFLPLAHMFerccengmyyvGGCVG 298
Cdd:PRK08043 359 QVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANV-EQIKTIADFTPN--DRFMSALPLFHSF-----------GLTVG 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 299 FYSgdiKELTNDLKMLKPTVM--PAVPRLlnrVYDkiQNDISASGLKRGLFNMAMRAKEKEIARgvlrrngcwdklvfkk 376
Cdd:PRK08043 425 LFT---PLLTGAEVFLYPSPLhyRIVPEL---VYD--RNCTVLFGTSTFLGNYARFANPYDFAR---------------- 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 377 vhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEMEy 456
Cdd:PRK08043 481 --------LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE- 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 457 fanqNTGEVCVRGSNVFHGYYK--DP-------EKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVP 527
Cdd:PRK08043 552 ----QGGRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSL 626
|
....*.
gi 281366413 528 EKIENI 533
Cdd:PRK08043 627 EMVEQL 632
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
225-571 |
1.01e-13 |
|
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: 73.66 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 225 EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCS------------VILQMGDhriragdvmVSFLPLAHMFERCCENG--M 290
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAwrreyeldsfpvRLLQMAS---------FSFDVFAGDFARSLLNGgtL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 291 YYVGGCVGFysgDIKELTNDLKMLKPTVMPAVPRLLNRVYDKIQndisasglkrglfnmamrakekeiargvlrrngcWD 370
Cdd:cd17650 164 VICPDEVKL---DPAALYDLILKSRITLMESTPALIRPVMAYVY----------------------------------RN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 371 KLVFKkvhqafggNLRLMVVGS--------APLAGNVLTFMRcalgclVLEGYGQTECT-------GAITLTVQGDHVPn 435
Cdd:cd17650 207 GLDLS--------AMRLLIVGSdgckaqdfKTLAARFGQGMR------IINSYGVTEATidstyyeEGRDPLGDSANVP- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 436 hVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI------DSEGWHHTGDVGMWLPNGTLRI 509
Cdd:cd17650 272 -IGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFvenpfaPGERMYRTGDLARWRADGNVEL 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281366413 510 IDRRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYVY------GE-SLKSCIIAVVVPDTDVLKQWATE 571
Cdd:cd17650 350 LGRVDHQVKI-RGFRIELGEIESQLARHPAIDEAVVAvredkgGEaRLCAYVVAAATLNTAELRAFLAK 417
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
221-531 |
1.04e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 74.27 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 221 PPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGvCSVILQMGDHrIRAGDVMVSFLPLAH-MferccengmyyvgGCVGF 299
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMAN-LRAISHDGLK-VRPGDRCVSWLPFYHdM-------------GLVGF 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 300 YsgdIKELTNDLKM-LKPTVMPAV-PRLLNRVYDKIQNDISAS---GLKRglfnMAMRAKEKEIARGVL---RRNGCWDK 371
Cdd:PRK09192 237 L---LTPVATQLSVdYLPTRDFARrPLQWLDLISRNRGTISYSppfGYEL----CARRVNSKDLAELDLscwRVAGIGAD 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 372 LVFKKVHQAFGGNLrlmvvgsAPLAGNVLTFMRCalgclvlegYGQTECT----------GAITLTV-------QGDHVP 434
Cdd:PRK09192 310 MIRPDVLHQFAEAF-------APAGFDDKAFMPS---------YGLAEATlavsfsplgsGIVVEEVdrdrleyQGKAVA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 435 NHV-----------GPPVSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEkTAEAIDSEGWHHTGDV 498
Cdd:PRK09192 374 PGAetrrvrtfvncGKALPGHEIEIRNeagmpLPERV------VGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDL 446
|
330 340 350
....*....|....*....|....*....|...
gi 281366413 499 GmWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIE 531
Cdd:PRK09192 447 G-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
92-531 |
1.09e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 74.15 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 92 RAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED--DGKAAM 169
Cdd:PRK07798 37 RANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYERefAPRVAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 170 LLEKAPRsLKIIVAIkpirqttlerARSRGIQIFSF-IDVEKLGAKG--NHPEVPPTAEDLcTVCYTSGTTGNPKGVMLT 246
Cdd:PRK07798 117 VLPRLPK-LRTLVVV----------EDGSGNDLLPGaVDYEDALAAGspERDFGERSPDDL-YLLYTGGTTGMPKGVMWR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 247 HGNVVAgvcsVILQMGDH--------------RIRAGDVMVSFL--PLAHMFERCCENGMYYVGGCVGFYsgDIKELTND 310
Cdd:PRK07798 185 QEDIFR----VLLGGRDFatgepiedeeelakRAAAGPGMRRFPapPLMHGAGQWAAFAALFSGQTVVLL--PDVRFDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 311 lkmlkpTVMPAVPRllNRVydkiqNDISASGlkrglfnMAMrakekeiARGV---LRRNGCWDklvfkkvhqafGGNLRL 387
Cdd:PRK07798 259 ------EVWRTIER--EKV-----NVITIVG-------DAM-------ARPLldaLEARGPYD-----------LSSLFA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 388 MVVGSAPLAGNV-LTFMRCALGCLVLEGYGQTEcTGAITLTVQGDHVPNHVGPPVSCNA-VKLVDvpEMEYFANQNTGEV 465
Cdd:PRK07798 301 IASGGALFSPSVkEALLELLPNVVLTDSIGSSE-TGFGGSGTVAKGAVHTGGPRFTIGPrTVVLD--EDGNPVEPGSGEI 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281366413 466 CV--RGSNVFHGYYKDPEKTAEA---IDSEGWHHTGDVGMWLPNGTLRIIDRRkhifklSQ-----GEYIVPEKIE 531
Cdd:PRK07798 378 GWiaRRGHIPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGRG------SVcintgGEKVFPEEVE 447
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
52-566 |
1.40e-13 |
|
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: 73.64 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 52 RTLYQTFREGAYASNNgpclgwRETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCysF 131
Cdd:COG1021 25 ETLGDLLRRRAERHPD------RIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFAL--F 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 132 SLVVVPLYdtlgpdacA----------FIIRQTDMQVVIVED-------DGKAAMLLEKAPrSLKIIVAikpirqttLER 194
Cdd:COG1021 97 RAGAIPVF--------AlpahrraeisHFAEQSEAVAYIIPDrhrgfdyRALARELQAEVP-SLRHVLV--------VGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 195 ARSrgiqifsFIDVEKLGAKGNHPEVP-PTAEDLCTVCYTSGTTGNPKGVMLTHG----NVV--AGVCsvilqmgdhRIR 267
Cdd:COG1021 160 AGE-------FTSLDALLAAPADLSEPrPDPDDVAFFQLSGGTTGLPKLIPRTHDdylySVRasAEIC---------GLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 268 AGDVMVSFLPLAHMFERCCEN--GMYYVGGCVgfysgdikeltndlkmlkptVMPAVPRLlNRVYDKI-QNDISASGLKR 344
Cdd:COG1021 224 ADTVYLAALPAAHNFPLSSPGvlGVLYAGGTV--------------------VLAPDPSP-DTAFPLIeRERVTVTALVP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 345 GLFNMAMRAKEKEIARGvlrrngcwdklvfkkvhqafgGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEctGAI 424
Cdd:COG1021 283 PLALLWLDAAERSRYDL---------------------SSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE--GLV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 425 TLTVQGD---HVPNHVGPPVSC-NAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHT 495
Cdd:COG1021 340 NYTRLDDpeeVILTTQGRPISPdDEVRIVDedgnpVPPGE------VGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRT 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 496 GDVGMWLPNGTLRIIDRRK-HIFKlsQGEYIVPEKIENIytLSQY--VNQVYV-------YGEslKSCiiAVVVPDTDVL 565
Cdd:COG1021 414 GDLVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVENL--LLAHpaVHDAAVvampdeyLGE--RSC--AFVVPRGEPL 485
|
.
gi 281366413 566 K 566
Cdd:COG1021 486 T 486
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
225-531 |
1.74e-13 |
|
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: 73.17 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 225 EDLCTVCYTSGTTGNPKGVMLTHGNVVAgVCSVIlqMGDHRIRAGDVMVSFLPLAhmFERCCENGM--YYVGGCVgfysg 302
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAA-HCQAT--AERYGLTPGDRELQFASFN--FDGAHEQLLppLICGACV----- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 303 dikeltndlkmlkptVMPAVPRLL--NRVYDKIQND-ISASGLKRGLFNMAMRAKEKEIARGVLRrngcwdklvfkkvhq 379
Cdd:cd17649 164 ---------------VLRPDELWAsaDELAEMVRELgVTVLDLPPAYLQQLAEEADRTGDGRPPS--------------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 380 afggnLRLMVVGSAPLAGNVLTfMRCALGCLVLEGYGQTECTgaITLTV---------QGDHVPnhVGPPVSCNAVKLVD 450
Cdd:cd17649 214 -----LRLYIFGGEALSPELLR-RWLKAPVRLFNAYGPTEAT--VTPLVwkceagaarAGASMP--IGRPLGGRSAYILD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 451 vPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI-----DSEG--WHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGE 523
Cdd:cd17649 284 -ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpdpfGAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGF 361
|
....*...
gi 281366413 524 YIVPEKIE 531
Cdd:cd17649 362 RIELGEIE 369
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
74-578 |
2.08e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.04 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 74 RETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLYDTLGPDAC 147
Cdd:PRK12467 528 RPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMvvgllaVLKAGGAY------VPLDPEYPQDRL 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 148 AFIIRQTDMQVVIVEDDGKAAMLLEKAPRSLKIIVAIKPIRqttlerarsrgiqifsfidveklGAKGNHPEVPPTAEDL 227
Cdd:PRK12467 602 AYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPADLLC-----------------------GYSGHNPEVALDPDNL 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 228 CTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAhmFERCCEngMYYVGGCVGfysgdikel 307
Cdd:PRK12467 659 AYVIYTSGSTGQPKGVAISHGALANYVCVIAERL---QLAADDSMLMVSTFA--FDLGVT--ELFGALASG--------- 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 308 tNDLKMLKPTVMPAVPRLLNRVYDKiqnDISASGLKRGLFNMAMRAKEKEIARGvlrrngcwdklvfkkvhqafggnLRL 387
Cdd:PRK12467 723 -ATLHLLPPDCARDAEAFAALMADQ---GVTVLKIVPSHLQALLQASRVALPRP-----------------------QRA 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 388 MVVGSAPLAGNVLTFMR-CALGCLVLEGYGQTECT-GAITLTVQGDHVPNH---VGPPVSCNAVKLVDvPEMEYFANQNT 462
Cdd:PRK12467 776 LVCGGEALQVDLLARVRaLGPGARLINHYGPTETTvGVSTYELSDEERDFGnvpIGQPLANLGLYILD-HYLNPVPVGVV 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 463 GEVCVRGSNVFHGYYKDPEKTAE-------AIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPEKIENIYT 535
Cdd:PRK12467 855 GELYIGGAGLARGYHRRPALTAErfvpdpfGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLL 933
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 281366413 536 LSQYVNQ--VYVYGESLKSCIIAVVVPDT--DVLKQWATENNVRGTL 578
Cdd:PRK12467 934 AQPGVREavVLAQPGDAGLQLVAYLVPAAvaDGAEHQATRDELKAQL 980
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-533 |
3.24e-13 |
|
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: 71.36 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 226 DLCTVCYTSGTTGNPKGVMLTHGNVVA-GVCSVILQMGDhrirAGDVMVSFLPLAHMFERCCENG-MYYVGGCVGFYS-- 301
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYnAWMLALNSLFD----PDDVLLCGLPLFHVNGSVVTLLtPLASGAHVVLAGpa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 302 -----GDIKELTNDLKMLKPTVMPAVPRLLNRVYDK-IQNDISAsglkrglfnmamrakekeiargvlrrngcwdklvfk 375
Cdd:cd05944 79 gyrnpGLFDNFWKLVERYRITSLSTVPTVYAALLQVpVNADISS------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 376 kvhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTV-QGDHVPNHVGPPVSCNAVKLVDV-PE 453
Cdd:cd05944 123 ---------LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPpDGPKRPGSVGLRLPYARVRIKVLdGV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 454 MEYF---ANQNTGEVCVRGSNVFHGYYKDpEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKI 530
Cdd:cd05944 194 GRLLrdcAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALI 271
|
...
gi 281366413 531 ENI 533
Cdd:cd05944 272 EEA 274
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
224-533 |
5.06e-13 |
|
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: 71.75 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 224 AEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMgdhRIRAGDVMVSFLPLAHMFerccengmyyvgGCVGFYsgd 303
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST---EWKTKDRILSWMPLTHDM------------GLIAFH--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 304 ikeLTNDLKMLKPTVMPAV-----PRL-LNRVYDKIQNDISASGLKRGLFnmAMRAKEKEIARgvlrrngcWDKlvfkkv 377
Cdd:cd05908 167 ---LAPLIAGMNQYLMPTRlfirrPILwLKKASEHKATIVSSPNFGYKYF--LKTLKPEKAND--------WDL------ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 378 hqafgGNLRLMVVGSAPLAGNVL-TFM-RCALGCL----VLEGYGQTECTGAITLTVQGDH--VPNH------------- 436
Cdd:cd05908 228 -----SSIRMILNGAEPIDYELChEFLdHMSKYGLkrnaILPVYGLAEASVGASLPKAQSPfkTITLgrrhvthgepepe 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 437 -------------VGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMwLP 503
Cdd:cd05908 303 vdkkdsecltfveVGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGF-IR 380
|
330 340 350
....*....|....*....|....*....|
gi 281366413 504 NGTLRIIDRRKHIFkLSQGEYIVPEKIENI 533
Cdd:cd05908 381 NGRLVITGREKDII-FVNGQNVYPHDIERI 409
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
225-533 |
1.45e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 70.62 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 225 EDLCTVCYTSGTTGNPKGVMLTHGNVVAG--VCsviLQMGDHRirAGDVMVSFLPLAHMFE-RCCENGMYYVGGCVGF-- 299
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLANqrAC---LKFFSPK--EDDVMMSFLPPFHAYGfNSCTLFPLLSGVPVVFay 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 300 ---YSGDIKELTNDLKMlkpTVMPAVPRLLNRVydkiqndisasgLKRglfnmamrAKEKEIARGvlrrngcwdklvfkk 376
Cdd:PRK06334 258 nplYPKKIVEMIDEAKV---TFLGSTPVFFDYI------------LKT--------AKKQESCLP--------------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 377 vhqafggNLRLMVVGSAPL-----AGNVLTFMRCALgclvLEGYGQTECTGAITLTVQGDhvPNH---VGPPVSCNAVKL 448
Cdd:PRK06334 300 -------SLRFVVIGGDAFkdslyQEALKTFPHIQL----RQGYGTTECSPVITINTVNS--PKHescVGMPIRGMDVLI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 449 VDVPEMEYFANQNTGEVCVRGSNVFHGYY-KDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVP 527
Cdd:PRK06334 367 VSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSL 445
|
....*.
gi 281366413 528 EKIENI 533
Cdd:PRK06334 446 EALESI 451
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
203-545 |
1.59e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 69.90 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 203 FSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVA---GVCSVIlqmgdhRIRAGDVMVSFLPLA 279
Cdd:PRK09029 113 FSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLAsaeGVLSLM------PFTAQDSWLLSLPLF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 280 HMfercceNGM------YYVGGCVGFysGDIKELTNDLKM-----LKPTvmpAVPRLLnrvydkiQNDISASGLKRGLFN 348
Cdd:PRK09029 187 HV------SGQgivwrwLYAGATLVV--RDKQPLEQALAGcthasLVPT---QLWRLL-------DNRSEPLSLKAVLLG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 349 MAM-------RAKEKEIArgvlrrngCWdklvfkkvhqafggnlrlmvvgsaplagnvltfmrcalgClvleGYGQTECt 421
Cdd:PRK09029 249 GAAipvelteQAEQQGIR--------CW---------------------------------------C----GYGLTEM- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 422 gAITLT-VQGDHVPNhVGPPVSCNAVKLVDvpemeyfanqntGEVCVRGSNVFHGYYKDPEKTAeAIDSEGWHHTGDVGM 500
Cdd:PRK09029 277 -ASTVCaKRADGLAG-VGSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQLVP-LVNDEGWFATRDRGE 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 281366413 501 WLpNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYV 545
Cdd:PRK09029 342 WQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
61-561 |
3.32e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 66.20 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 61 GAYASNNGPCLGWRETltsPYQWINY-DEALLRAKNFGAgmLALGARPKQlIGIYSQNRPEWILYEQGCYSFSLVVVPLY 139
Cdd:PRK13388 10 RDRAGDDTIAVRYGDR---TWTWREVlAEAAARAAALIA--LADPDRPLH-VGVLLGNTPEMLFWLAAAALGGYVLVGLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 140 DTLGPDACAFIIRQTDMQVVIVEDDGKAamLLEkaprslkiivaikpirqtTLERARSRgiqifsFIDV------EKLGA 213
Cdd:PRK13388 84 TTRRGAALAADIRRADCQLLVTDAEHRP--LLD------------------GLDLPGVR------VLDVdtpayaELVAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 214 KGN-HPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRiraGDVMVSFLPLAHmferccENGMYY 292
Cdd:PRK13388 138 AGAlTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTR---DDVCYVSMPLFH------SNAVMA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 293 -------VGGCV---------GFYSgdikeltnDLKMLKPTVMPAVPRLLNRVY------DKIQNDisasgLKRGLFNma 350
Cdd:PRK13388 209 gwapavaSGAAValpakfsasGFLD--------DVRRYGATYFNYVGKPLAYILatperpDDADNP-----LRVAFGN-- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 351 mRAKEKEIARgVLRRngcwdklvfkkvhqafggnlrlmvvgsaplagnvltfmrcaLGCLVLEGYGQTEctGAITLTVQG 430
Cdd:PRK13388 274 -EASPRDIAE-FSRR-----------------------------------------FGCQVEDGYGSSE--GAVIVVREP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 431 DHVPNHVGPP----VSCNAVKLVDVPEMEYFAN-------QNTGE-VCVRGSNVFHGYYKDPEKTAEAIdSEGWHHTGDV 498
Cdd:PRK13388 309 GTPPGSIGRGapgvAIYNPETLTECAVARFDAHgallnadEAIGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDL 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366413 499 GMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVYVYGeslksciiavvVPD 561
Cdd:PRK13388 388 AYRDADGWIYFAGRTADWMRVD-GENLSAAPIERILLRHPAINRVAVYA-----------VPD 438
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
103-547 |
6.12e-11 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 65.19 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 103 LGARPKQLIGIYSQNRPEW--ILYEQGCysFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVE--DDGKAAMLLEKAPrSL 178
Cdd:PRK05620 59 LGITGDQRVGSMMYNCAEHleVLFAVAC--MGAVFNPLNKQLMNDQIVHIINHAEDEVIVADprLAEQLGEILKECP-CV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 179 KIIVAIKPIRQTTLERARSRGIQIFSFidvEKL----GAKGNHPEVPPTaeDLCTVCYTSGTTGNPKGVMLTHGnvvagv 254
Cdd:PRK05620 136 RAVVFIGPSDADSAAAHMPEGIKVYSY---EALldgrSTVYDWPELDET--TAAAICYSTGTTGAPKGVVYSHR------ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 255 cSVILQ-MGdhrIRAGDVM-----VSFLplahmferCCENGMYYVGGCV---GFYSGdikeltndlkmlKPTVMPAvprl 325
Cdd:PRK05620 205 -SLYLQsLS---LRTTDSLavthgESFL--------CCVPIYHVLSWGVplaAFMSG------------TPLVFPG---- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 326 lnrvydkiqNDISASGLKRgLFNMAMrakeKEIARGVlrrNGCWDKLVfkkVHQAFGG----NLRLMVVGSAPLAGNVLT 401
Cdd:PRK05620 257 ---------PDLSAPTLAK-IIATAM----PRVAHGV---PTLWIQLM---VHYLKNPpermSLQEIYVGGSAVPPILIK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 402 FMRCALGCLVLEGYGQTEcTGAITlTVQgdHVPNHVGP-------------PVSCNaVKLVDVPEMEYFANQNTGEVCVR 468
Cdd:PRK05620 317 AWEERYGVDVVHVWGMTE-TSPVG-TVA--RPPSGVSGearwayrvsqgrfPASLE-YRIVNDGQVMESTDRNEGEIQVR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 469 GSNVFHGYYKDP----------------EKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIEN 532
Cdd:PRK05620 392 GNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLEN 470
|
490
....*....|....*
gi 281366413 533 IYTLSQYVNQVYVYG 547
Cdd:PRK05620 471 YIMAAPEVVECAVIG 485
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
385-532 |
9.04e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 64.63 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 385 LRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEctGAITLTVQGD---HVPNHVGPPVSCN-AVKLVD-----VPEME 455
Cdd:PRK10946 302 LKLLQVGGARLSETLARRIPAELGCQLQQVFGMAE--GLVNYTRLDDsdeRIFTTQGRPMSPDdEVWVADadgnpLPQGE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 456 yfanqnTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKhifklSQ----GEYIVPEKIE 531
Cdd:PRK10946 380 ------VGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREK-----DQinrgGEKIAAEEIE 448
|
.
gi 281366413 532 N 532
Cdd:PRK10946 449 N 449
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
228-533 |
9.48e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 64.77 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 228 CTVCYTSGTTGNPKGVMLTH-GNVVAgvcSVILQMGDHR-IRAGDVMVSFLPLAHmferccEN--GMYYVGGCVGfysgd 303
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHrSNVLH---ALMANNGDALgTSAADTMLPVVPLFH------ANswGIAFSAPSMG----- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 304 ikeltndLKMlkptVMPAVPRLLNRVYDKIQND-ISASGLKRGLFNMAMRAKEKEIArgvlrrngcwdKLVFKKvhqafg 382
Cdd:PRK06018 246 -------TKL----VMPGAKLDGASVYELLDTEkVTFTAGVPTVWLMLLQYMEKEGL-----------KLPHLK------ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 383 gnlrlMVV--GSAPLAGNVLTFMRcaLGCLVLEGYGQTECTGAITLTVQGDHVPNHVG------------PPVSCNaVKL 448
Cdd:PRK06018 298 -----MVVcgGSAMPRSMIKAFED--MGVEVRHAWGMTEMSPLGTLAALKPPFSKLPGdarldvlqkqgyPPFGVE-MKI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 449 VD-----VPemeyFANQNTGEVCVRGSNVFHGYYKdpeKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGE 523
Cdd:PRK06018 370 TDdagkeLP----WDGKTFGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGE 441
|
330
....*....|
gi 281366413 524 YIVPEKIENI 533
Cdd:PRK06018 442 WISSIDLENL 451
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
213-571 |
2.76e-10 |
|
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: 63.17 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 213 AKGNHPEVPPTAEDLCT-VCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIRAGDVMVSFLPLAHMF-ERCCENGM 290
Cdd:cd05929 112 AEGGSPETPIEDEAAGWkMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAApFRWSMTAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 291 YYVGGCVGFYSGDIKELTNDLKMLKPTVMPAVPRLLNR---VYDKIQNDISASGLKRgLFNMA--MRAKEKEIargvlrr 365
Cdd:cd05929 192 FMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRllkLPEAVRNAYDLSSLKR-VIHAAapCPPWVKEQ------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 366 ngcWDKLVFKKVHQAFGGNlrlmvvgsaplagnvltfmrcalgclvlEGYGQTECTGAITLTvqgdHvPNHVGPPVScNA 445
Cdd:cd05929 264 ---WIDWGGPIIWEYYGGT----------------------------EGQGLTIINGEEWLT----H-PGSVGRAVL-GK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 446 VKLVDvPEMEYFANQNTGEVCVRGSNVFHgYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYI 525
Cdd:cd05929 307 VHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNI 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 281366413 526 VPEKIENIYTLSQYVNQVYVYG---ESLKSCIIAVV--VPDTDVLKQWATE 571
Cdd:cd05929 384 YPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVqpAPGADAGTALAEE 434
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
86-302 |
3.54e-10 |
|
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: 62.89 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 86 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED-- 163
Cdd:cd05968 94 YGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgf 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 --DGKAAMLLEKA-------PRSLKIIVaikpIRQTTLERARSRGIQIFSFIDVEKLGAKGNHPEvpptAEDLCTVCYTS 234
Cdd:cd05968 174 trRGREVNLKEEAdkacaqcPTVEKVVV----VRHLGNDFTPAKGRDLSYDEEKETAGDGAERTE----SEDPLMIIYTS 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281366413 235 GTTGNPKGVMLTH-GNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFYSG 302
Cdd:cd05968 246 GTTGKPKGTVHVHaGFPLKAAQDMYFQFD---LKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDG 311
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
224-549 |
4.37e-10 |
|
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: 62.49 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 224 AEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDhrIRAGDVM----VSFLPLAH-MFERCCENGMYYVggcvg 298
Cdd:cd17656 127 SDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNI--NFSDKVLqfatCSFDVCYQeIFSTLLSGGTLYI----- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 299 fysgdikeLTNDLKMlkptvmpAVPRLLNRVYdkiQNDISASGLKRGLFNMAmrAKEKEIARGVlrrngcwdklvFKKVH 378
Cdd:cd17656 200 --------IREETKR-------DVEQLFDLVK---RHNIEVVFLPVAFLKFI--FSEREFINRF-----------PTCVK 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 379 QAFGGNLRLMVVgsaplagNVLTFMRCALGCLVLEGYGQTECTGAITLTVQ-GDHVPNH--VGPPVSCNAVKLVDvpemE 455
Cdd:cd17656 249 HIITAGEQLVIT-------NEFKEMLHEHNVHLHNHYGPSETHVVTTYTINpEAEIPELppIGKPISNTWIYILD----Q 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 456 YFANQ---NTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGW------HHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIV 526
Cdd:cd17656 318 EQQLQpqgIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIE 396
|
330 340
....*....|....*....|....*..
gi 281366413 527 PEKIE----NIYTLSQYVnqVYVYGES 549
Cdd:cd17656 397 LGEIEaqllNHPGVSEAV--VLDKADD 421
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
37-561 |
5.38e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 37 ESKNGKFVSYITEnvRTLYQTFREGAYASNNGPCLGWREtltspyQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQ 116
Cdd:PRK12316 3044 EAWNATAAEYPLE--RGVHRLFEEQVERTPDAVALAFGE------QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVE 3115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 117 NRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIrqtdmqvvivEDDGKAAMLlekaprslkiivaikpiRQTTLERAR 196
Cdd:PRK12316 3116 RSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYML----------EDSGAQLLL-----------------SQSHLRLPL 3168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 197 SRGIQIFsFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFL 276
Cdd:PRK12316 3169 AQGVQVL-DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG---LGVGDRVLQFT 3244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 277 PLAhmferccengmyyvggcvgfYSGDIKELTNDLkMLKPTVMPAVPRLLNRVyDKIQNDISASGLKRGLFNMAMRAKek 356
Cdd:PRK12316 3245 TFS--------------------FDVFVEELFWPL-MSGARVVLAGPEDWRDP-ALLVELINSEGVDVLHAYPSMLQA-- 3300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 357 eiargvlrrngcwdklVFKKVHQAFGGNLRLMVVGSAPLAGNVLTfmRCALGCLVLEGYGQTECTGAITLTVQGDHVPNH 436
Cdd:PRK12316 3301 ----------------FLEEEDAHRCTSLKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDA 3362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 437 --VGPPVSCNAVKLVDVpEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI------DSEGWHHTGDVGMWLPNGTLR 508
Cdd:PRK12316 3363 vpIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvPGERLYRTGDLARYRADGVIE 3441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 281366413 509 IIDRRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYVYGESLKScIIAVVVPD 561
Cdd:PRK12316 3442 YIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPE 3492
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
218-564 |
5.67e-10 |
|
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: 61.90 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 218 PEVPPTAEDLCTVCYTSGTTGNPKGVMLTHgnvvAGVCSVILQMGDH-RIRAGDVMVSFLPLAH------MFerccenGM 290
Cdd:cd12114 119 PPVDVAPDDLAYVIFTSGSTGTPKGVMISH----RAALNTILDINRRfAVGPDDRVLALSSLSFdlsvydIF------GA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 291 YYVGGCVGFYSGDIKELTNDLKML----KPTVMPAVPRLLNRVYDKIQndiSASGLKRGLfnmamrakekeiaRGVLRrN 366
Cdd:cd12114 189 LSAGATLVLPDEARRRDPAHWAELierhGVTLWNSVPALLEMLLDVLE---AAQALLPSL-------------RLVLL-S 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 367 GCWDKLVFKKVHQAFGGNLRLMvvgsaplagnvltfmrcALGclvlegyGQTEctGAITLTVQG-DHVPNHV-----GPP 440
Cdd:cd12114 252 GDWIPLDLPARLRALAPDARLI-----------------SLG-------GATE--ASIWSIYHPiDEVPPDWrsipyGRP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 441 VSCNAVKLVD-----VPEMEyfanqnTGEVCVRGSNVFHGYYKDPEKTAEA----IDSEGWHHTGDVGMWLPNGTLRIID 511
Cdd:cd12114 306 LANQRYRVLDprgrdCPDWV------PGELWIGGRGVALGYLGDPELTAARfvthPDGERLYRTGDLGRYRPDGTLEFLG 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 281366413 512 RRKHIFKLsQGEYIVPEKIENIYTLSQYVNQ--VYVYGESLKSCIIAVVVPDTDV 564
Cdd:cd12114 380 RRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDG 433
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
84-560 |
6.44e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 61.84 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPE-----WILYEQGCYSfslvvVPLYDTLGPDACAFIIRQTDMQV 158
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEffevyWAARRSGLYY-----TPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 159 VIVEDDGKAAM--LLEKAPRSLKIIVAIkpirqttlerarsrGIQIFSFIDVEKLGAKgnHPEVPPTAEDL-CTVCYTSG 235
Cdd:PRK08276 87 LIVSAALADTAaeLAAELPAGVPLLLVV--------------AGPVPGFRSYEEALAA--QPDTPIADETAgADMLYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 236 TTGNPKGVM--LTHGNV--VAGVCSVILQMGDHrIRAGDVMVSFLPLAHmferccengmyyvgGCVGFYSGDIKELTNDL 311
Cdd:PRK08276 151 TTGRPKGIKrpLPGLDPdeAPGMMLALLGFGMY-GGPDSVYLSPAPLYH--------------TAPLRFGMSALALGGTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 312 ---------KML------KPTVMPAVP----RLLnRVYDKIQN--DISAsglkrglfnmamrakekeiargvlrrngcwd 370
Cdd:PRK08276 216 vvmekfdaeEALalieryRVTHSQLVPtmfvRML-KLPEEVRAryDVSS------------------------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 371 klvfkkvhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQG--DHvPNHVGPPVSCnAVKL 448
Cdd:PRK08276 264 --------------LRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTVITSEDwlAH-PGSVGKAVLG-EVRI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 449 VD-----VPEME----YFAnqntgevcvRGSNVFHgYYKDPEKTAEAIDSEGWHHTGDVGmWL-PNGTLRIIDRRKHIFk 518
Cdd:PRK08276 328 LDedgneLPPGEigtvYFE---------MDGYPFE-YHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI- 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 281366413 519 LSQGEYIVPEKIENIYTLSQYVNQVYV-------YGESLKsciiAVVVP 560
Cdd:PRK08276 396 ISGGVNIYPQEIENLLVTHPKVADVAVfgvpdeeMGERVK----AVVQP 440
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
84-560 |
6.80e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 62.02 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 163
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 D--GKAAMLLEKAPRSLKIIVAIKPirqTTLERarsrgiqifsFIDVEKlgAKGNHPEVPPTAEDLCT-VCYTSGTTGNP 240
Cdd:PRK13391 105 AklDVARALLKQCPGVRHRLVLDGD---GELEG----------FVGYAE--AVAGLPATPIADESLGTdMLYSSGTTGRP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 241 KGVM--LTHGNVVAGVCSVILQMGDHRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCV----GFYSGDIKELTNDLK-- 312
Cdd:PRK13391 170 KGIKrpLPEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVivmeHFDAEQYLALIEEYGvt 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 313 --MLKPTVMPAVPRLLNRVYDKIqnDISAsglkrglfnmamrakekeiargvlrrngcwdklvfkkvhqafggnLRLMVV 390
Cdd:PRK13391 250 htQLVPTMFSRMLKLPEEVRDKY--DLSS---------------------------------------------LEVAIH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 391 GSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQG--DHvPNHVGPPVsCNAVKLVDvPEMEYFANQNTGEVCVR 468
Cdd:PRK13391 283 AAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEwlAH-PGTVGRAM-FGDLHILD-DDGAELPPGEPGTIWFE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 469 GSNVFHgYYKDPEKTAEAIDSEG-WHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVYVYG 547
Cdd:PRK13391 360 GGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG 437
|
490
....*....|....*.
gi 281366413 548 ---ESLKSCIIAVVVP 560
Cdd:PRK13391 438 vpnEDLGEEVKAVVQP 453
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
222-524 |
1.07e-09 |
|
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: 60.94 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 222 PTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAHMFERCCenGMYYVGGCVGFY- 300
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYG---IRPGEVDLATFPLFALFGPAL--GLTSVIPDMDPTr 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 301 --SGDIKELTNDLKMLKPTVMPAVPRLLNRVYDK-IQNDISASGLKRGLfnmamrakekeiargvlrrngcwdklvfkkv 377
Cdd:cd05910 157 paRADPQKLVGAIRQYGVSIVFGSPALLERVARYcAQHGITLPSLRRVL------------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 378 hqAFGgnlrlmvvgsAPLAGNVLTFMRCAL--GCLVLEGYGQTEC--TGAIT----LTVQGDHVPNH----VGPPVSCNA 445
Cdd:cd05910 206 --SAG----------APVPIALAARLRKMLsdEAEILTPYGATEAlpVSSIGsrelLATTTAATSGGagtcVGRPIPGVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 446 VKLVDVPEMEYFANQNT--------GEVCVRGSNVFHGYYKDPEKTAEA-IDSEG---WHHTGDVGMWLPNGTLRIIDRR 513
Cdd:cd05910 274 VRIIEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDLGYLDDEGRLWFCGRK 353
|
330
....*....|.
gi 281366413 514 KHIFKLSQGEY 524
Cdd:cd05910 354 AHRVITTGGTL 364
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
218-533 |
1.37e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 61.52 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 218 PEVPPT---AEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRiraGDVMVSFLPLAHMFerccengmyyvg 294
Cdd:PRK06814 783 PLVYFCnrdPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSP---EDKVFNALPVFHSF------------ 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 295 gcvGFYSGDIKELTNDLKM-LKPTvmP----AVPRLlnrVYDK-----IQNDISASGLKRGLFNMAMRAkekeiargvlr 364
Cdd:PRK06814 848 ---GLTGGLVLPLLSGVKVfLYPS--PlhyrIIPEL---IYDTnatilFGTDTFLNGYARYAHPYDFRS----------- 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 365 rngcwdklvfkkvhqafggnLRLMVVGSAPL-AGNVLTFMRcALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSC 443
Cdd:PRK06814 909 --------------------LRYVFAGAEKVkEETRQTWME-KFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPG 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 444 NAVKLVDVPEMEyfanqNTGEVCVRGSNVFHGYYKdPEK--TAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSq 521
Cdd:PRK06814 968 IEYRLEPVPGID-----EGGRLFVRGPNVMLGYLR-AENpgVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA- 1039
|
330
....*....|..
gi 281366413 522 GEYIVPEKIENI 533
Cdd:PRK06814 1040 GEMISLAAVEEL 1051
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-568 |
1.54e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.51 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 52 RTLYQTFREGAYASNNGPCLGWREtltspyQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYE 125
Cdd:PRK12316 511 RGVHRLFEEQVERTPEAPALAFGE------ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMvvallaILKA 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 126 QGCYsfslvvVPLYDTLGPDACAFIIRQTDMQVVIVEddgkaAMLLEKAPRSlkiivaikpirqttlerarsRGIQIFSF 205
Cdd:PRK12316 585 GGAY------VPLDPEYPAERLAYMLEDSGVQLLLSQ-----SHLGRKLPLA--------------------AGVQVLDL 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 206 --IDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSV--ILQMGDHRIRAGDVMVSFLPLAHM 281
Cdd:PRK12316 634 drPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMqqAYGLGVGDTVLQKTPFSFDVSVWE 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 282 FERCCENGMYYVGGCVGFYSgDIKELTNDLKMLKPTVMPAVPRLLNrvydkiqndisasglkrglfnmAMRAKEKEIARG 361
Cdd:PRK12316 714 FFWPLMSGARLVVAAPGDHR-DPAKLVELINREGVDTLHFVPSMLQ----------------------AFLQDEDVASCT 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 362 VLRRNGCwdklvfkkVHQAFGGNLRLMVVGSAPLAGnvltfmrcalgclVLEGYGQTECTGAIT----LTVQGDHVPnhV 437
Cdd:PRK12316 771 SLRRIVC--------SGEALPADAQEQVFAKLPQAG-------------LYNLYGPTEAAIDVThwtcVEEGGDSVP--I 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 438 GPPVSCNAVKLVDVpEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEA------IDSEGWHHTGDVGMWLPNGTLRIID 511
Cdd:PRK12316 828 GRPIANLACYILDA-NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERfvpspfVAGERMYRTGDLARYRADGVIEYAG 906
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366413 512 RRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYVYGESLKScIIAVVVPDT------DVLKQW 568
Cdd:PRK12316 907 RIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQ-LVGYVVLESeggdwrEALKAH 967
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
223-535 |
1.61e-09 |
|
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: 60.34 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 223 TAEDLCTVCYTSGTTGNPKGVMLTHgnvvAGVCSVILQMGDH-RIRAGDVMVSFLPL---AHMFERC---CENGMYYVGG 295
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTH----RGLANLAAAQIAAfDVGPGSRVLQFASPsfdASVWELLmalLAGATLVLAP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 296 CVGFYSGDikELTNDLKMLKPTVMPAVPRLLNRVydkiqndiSASGLKrglfnmamrakekeiargvlrrngcwdklvfk 375
Cdd:cd17652 167 AEELLPGE--PLADLLREHRITHVTLPPAALAAL--------PPDDLP-------------------------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 376 kvhqafgGNLRLMVVGSAPLAGNVltfMRCALGCLVLEGYGQTECTGAITL---TVQGDHVPnhVGPPVSCNAVKLVDvP 452
Cdd:cd17652 205 -------DLRTLVVAGEACPAELV---DRWAPGRRMINAYGPTETTVCATMagpLPGGGVPP--IGRPVPGTRVYVLD-A 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 453 EMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAE-------AIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYI 525
Cdd:cd17652 272 RLRPVPPGVPGELYIAGAGLARGYLNRPGLTAErfvadpfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKI-RGFRI 350
|
330
....*....|
gi 281366413 526 VPEKIENIYT 535
Cdd:cd17652 351 ELGEVEAALT 360
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
223-531 |
4.98e-09 |
|
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: 58.86 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 223 TAEDLCTVCYTSGTTGNPKGVMLTHGNVVAgvcsvILQMGDH--RIRAGDVMVSF-------------LPLAHmfercce 287
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLA-----LFAATQRwfGFNEDDVWTLFhsyafdfsvweiwGALLH------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 288 ngmyyvGGCVGFYSGDIKELTNDLKML----KPTVMPAVPrllnrvydkiqndiSAsglkrglFNMAMRAkekeiargvL 363
Cdd:cd17643 159 ------GGRLVVVPYEVARSPEDFARLlrdeGVTVLNQTP--------------SA-------FYQLVEA---------A 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 364 RRNGCWDKlvfkkvhqafggNLRLMVVGSAPLAGNVLT--FMRCALGC-LVLEGYGQTECTGAITLT-VQGDHVPNH--- 436
Cdd:cd17643 203 DRDGRDPL------------ALRYVIFGGEALEAAMLRpwAGRFGLDRpQLVNMYGITETTVHVTFRpLDAADLPAAaas 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 437 -VGPPVSCNAVKLVDvpemeyfANQN------TGEVCVRGSNVFHGYYKDPEKTAE-------AIDSEGWHHTGDVGMWL 502
Cdd:cd17643 271 pIGRPLPGLRVYVLD-------ADGRpvppgvVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRL 343
|
330 340
....*....|....*....|....*....
gi 281366413 503 PNGTLRIIDRRKHIFKLSqGEYIVPEKIE 531
Cdd:cd17643 344 PDGELEYLGRADEQVKIR-GFRIELGEIE 371
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
223-531 |
5.13e-09 |
|
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: 59.03 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 223 TAEDLCTVCYTSGTTGNPKGVMLTHGNVVAgVCSV----ILqmgdhRIRAGDVMVSFLPLAHMFERcceNGM----YYVG 294
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLA-SADRyavnVL-----RLREDDRFVGSPPLAFTFGL---GGVllfpFGVG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 295 G-CVGFYSGDIKELTNDLKMLKPTVMPAVPrllnrvydkiqndisasglkrglfnMAMRAkekeiargvlrrngcwdKLV 373
Cdd:cd05958 166 AsGVLLEEATPDLLLSAIARYKPTVLFTAP-------------------------TAYRA-----------------MLA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 374 FKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTgAITLTVQGDHV-PNHVGPPVSCNAVKLVD-- 450
Cdd:cd05958 204 HPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMF-HIFISARPGDArPGATGKPVPGYEAKVVDde 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 451 ---VPEMEyfanqnTGEVCVRGSNvfhGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVP 527
Cdd:cd05958 283 gnpVPDGT------IGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAP 352
|
....
gi 281366413 528 EKIE 531
Cdd:cd05958 353 PEVE 356
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
224-533 |
6.00e-09 |
|
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: 58.73 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 224 AEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVM--VSFLPLA-HMFErcCENGMYYVGGCVGFY 300
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIG---LKPGDVHwnISSPGWAkHAWS--CFFAPWNAGATVFLF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 301 SG---DIKELTNDLKMLKPTVM---PAVPRLLnrvydkIQNDISASGLKrglfnmamrakekeiargvlrrngcwdklvf 374
Cdd:cd05974 159 NYarfDAKRVLAALVRYGVTTLcapPTVWRML------IQQDLASFDVK------------------------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 375 kkvhqafggnLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTECTGAITLTVQGDHVPNHVGPPVSCNAVKLVDVPEM 454
Cdd:cd05974 202 ----------LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 455 EyfanQNTGEVCV-----RGSNVFHGYYKDPEKTAEAIdSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqgEY-IVPE 528
Cdd:cd05974 272 P----ATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSS--DYrISPF 344
|
....*
gi 281366413 529 KIENI 533
Cdd:cd05974 345 ELESV 349
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
85-533 |
7.20e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 58.56 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 85 NYDEALLRAKNFGAGMLALGARPKQLIGIYSQN--RPEWILYeqGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVe 162
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNgyRHLEAYY--GVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLF- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 163 dDGKAAMLLEK-APR--SLKIIVAIkpirqTTLERARSRGIQIFSFIDVekLGAKGNHPEVPPTAEDL-CTVCYTSGTTG 238
Cdd:PRK07008 118 -DLTFLPLVDAlAPQcpNVKGWVAM-----TDAAHLPAGSTPLLCYETL--VGAQDGDYDWPRFDENQaSSLCYTSGTTG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 239 NPKGVMLTHGNVVAGVCSVIL--QMGdhrIRAGDVMVSFLPLAHMfercceN--GMYYVGGCVG---FYSG---DIKELT 308
Cdd:PRK07008 190 NPKGALYSHRSTVLHAYGAALpdAMG---LSARDAVLPVVPMFHV------NawGLPYSAPLTGaklVLPGpdlDGKSLY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 309 NDLKMLKPTVMPAVPRllnrVYDKIQNDISASGLKRGLFNmamrakekeiargvlrrngcwdklvfkkvhqafggnlRLM 388
Cdd:PRK07008 261 ELIEAERVTFSAGVPT----VWLGLLNHMREAGLRFSTLR-------------------------------------RTV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 389 VVGSA-PLAgnVLTFMRCALGCLVLEGYGQTECT--GAI-TLTVQGDHVP----NHV----GPPVSCNAVKLVDVPEMEY 456
Cdd:PRK07008 300 IGGSAcPPA--MIRTFEDEYGVEVIHAWGMTEMSplGTLcKLKWKHSQLPldeqRKLlekqGRVIYGVDMKIVGDDGREL 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281366413 457 -FANQNTGEVCVRGSNVFHGYYKDpeKTAEAIDseGWHHTGDVGMWLPNGTLRIIDRRKHIFKlSQGEYIVPEKIENI 533
Cdd:PRK07008 378 pWDGKAFGDLQVRGPWVIDRYFRG--DASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIENV 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-562 |
7.32e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.20 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 82 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLyDTLGP-DACAFIIRQT 154
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELvvallaVLKAGGAY------VPL-DPNYPaERLAYMLEDS 2099
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 155 DMQVVIVEDDGKAAMLLEKAPRSLkiivaikpirqtTLERarsrgiqifsfiDVEKLGAKGNHPEVPPTAEDLCTVCYTS 234
Cdd:PRK12316 2100 GAALLLTQRHLLERLPLPAGVARL------------PLDR------------DAEWADYPDTAPAVQLAGENLAYVIYTS 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 235 GTTGNPKGVMLTHGNVVAGvCSVILQMgdHRIRAGDVMVSFLPLAhmFErccengmyyvggcvGFYSGDIKELTNDLKML 314
Cdd:PRK12316 2156 GSTGLPKGVAVSHGALVAH-CQAAGER--YELSPADCELQFMSFS--FD--------------GAHEQWFHPLLNGARVL 2216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 315 kptVMPAVPRLLNRVYDKIQNdisaSGLKRGLFNMAMRAKEKEIArgvlRRNGCwdklvfkkvhqafGGNLRLMVVGSAP 394
Cdd:PRK12316 2217 ---IRDDELWDPEQLYDEMER----HGVTILDFPPVYLQQLAEHA----ERDGR-------------PPAVRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 395 LAGNVLTFMRCALGCLVL-EGYGQTECTGAITLTVQGDHVPNH-----VGPPVSCNAVKLVDVpEMEYFANQNTGEVCVR 468
Cdd:PRK12316 2273 VPAASLRLAWEALRPVYLfNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRALGNRRAYILDA-DLNLLAPGMAGELYLG 2351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 469 GSNVFHGYYKDPEKTAE-----AIDSEG--WHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPEKIENIYTLSQYVN 541
Cdd:PRK12316 2352 GEGLARGYLNRPGLTAErfvpdPFSASGerLYRTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVR 2430
|
490 500
....*....|....*....|...
gi 281366413 542 QVYVYGESLKSC--IIAVVVPDT 562
Cdd:PRK12316 2431 EAVVVAQDGASGkqLVAYVVPDD 2453
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
77-531 |
7.41e-09 |
|
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: 58.48 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 77 LTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYEQGCYsfslvvVPLYDTLGPDACAFI 150
Cdd:cd12115 18 LVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLvvallaVLKAGAAY------VPLDPAYPPERLRFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 151 IRQTDMQVVIVeddgkaamllekaprslkiivaikpirqttlerarsrgiqifsfidveklgakgnhpevppTAEDLCTV 230
Cdd:cd12115 92 LEDAQARLVLT-------------------------------------------------------------DPDDLAYV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 231 CYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRIRAgdVMVS------------FLPLAHmferccengmyyvGGCVg 298
Cdd:cd12115 111 IYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAG--VLAStsicfdlsvfelFGPLAT-------------GGKV- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 299 fysgdikELTNDLKMLkptvmPAVPR-----LLNRVYDKIQNDISASGLKRGL--FNMAMRAKEKEIARGVlrrngcWDK 371
Cdd:cd12115 175 -------VLADNVLAL-----PDLPAaaevtLINTVPSAAAELLRHDALPASVrvVNLAGEPLPRDLVQRL------YAR 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 372 LVFKKVHqafggNLrlmvvgsaplagnvltfmrcalgclvlegYGQTECTGAITLTV--QGDHVPNHVGPPVSCNAVKLV 449
Cdd:cd12115 237 LQVERVV-----NL-----------------------------YGPSEDTTYSTVAPvpPGASGEVSIGRPLANTQAYVL 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 450 DvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWH------HTGDVGMWLPNGTLRIIDRRKHIFKLsQGE 523
Cdd:cd12115 283 D-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGF 360
|
....*...
gi 281366413 524 YIVPEKIE 531
Cdd:cd12115 361 RIELGEIE 368
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
86-531 |
7.75e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 58.56 E-value: 7.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 86 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDg 165
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHAD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 166 kaamLLEKA----PRSLKIIVAIKP--IRQTTLERARSRGIQIFSfIDVEKLGAKGNHPEVPPTAEDlCTVCYTSGTTGN 239
Cdd:PRK12406 93 ----LLHGLasalPAGVTVLSVPTPpeIAAAYRISPALLTPPAGA-IDWEGWLAQQEPYDGPPVPQP-QSMIYTSGTTGH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 240 PKGVML---THGNVVAGVCSVILQMGDHR-IRAgdVMVSflPLAHmferCCENGMYYVGGCVG--------FysgDIKEL 307
Cdd:PRK12406 167 PKGVRRaapTPEQAAAAEQMRALIYGLKPgIRA--LLTG--PLYH----SAPNAYGLRAGRLGgvlvlqprF---DPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 308 TNDLKMLKPTVMPAVPRLLNRVydkiqndisasglkrglfnmaMRAKEKEIARGVLrrngcwdklvfkkvhqafgGNLRL 387
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRL---------------------LKLPEEVRAKYDV-------------------SSLRH 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 388 MVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAITLTVQGDHV--PNHVGPPVSCNAVKLVD-----VPEMEyfanq 460
Cdd:PRK12406 276 VIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALshPGTVGKAAPGAELRFVDedgrpLPQGE----- 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366413 461 nTGEVCVR--GSNVFhGYYKDPEKTAEaIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIE 531
Cdd:PRK12406 350 -IGEIYSRiaGNPDF-TYHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIE 418
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
224-532 |
1.96e-08 |
|
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: 57.18 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 224 AEDLCTVCYTSGTTGNPKGVMLTHGNVVaGVCSVilqmgdHRiragdvmvsflplaHMFERCCE-NGMYYVGgcVGFYSG 302
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLV-NLCEW------HR--------------PYFGVTPAdKSLVYAS--FSFDAS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 303 DIKELTNDLKMLKPTVMPAVPRL----LNRVYDkiQNDISASGLKRGLFNMAMRAKEKeiargvlrrngcwdklvfkkvh 378
Cdd:cd17645 160 AWEIFPHLTAGAALHVVPSERRLdldaLNDYFN--QEGITISFLPTGAAEQFMQLDNQ---------------------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 379 qafggNLRLMVVGsaplaGNVLTFMRcALGCLVLEGYGQTECTGAIT-LTVQGDHVPNHVGPPVSCNAVKLVDvpemEYF 457
Cdd:cd17645 216 -----SLRVLLTG-----GDKLKKIE-RKGYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD----EAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 458 ANQN---TGEVCVRGSNVFHGYYKDPEKTAEA------IDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLsQGEYIVPE 528
Cdd:cd17645 281 QLQPigvAGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPG 359
|
....
gi 281366413 529 KIEN 532
Cdd:cd17645 360 EIEP 363
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
385-532 |
3.71e-08 |
|
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: 56.32 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 385 LRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTEcTGAITLTVQGDHV-PNHVGPPVSCNAVKLVDV------PEMEyf 457
Cdd:cd05928 293 LQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTE-TGLICANFKGMKIkPGSMGKASPPYDVQIIDDngnvlpPGTE-- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 458 anqntGEVCVRGSNV-----FHGYYKDPEKTAEAIDSEGWhHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIEN 532
Cdd:cd05928 370 -----GDIGIRVKPIrpfglFSGYVDNPEKTAATIRGDFY-LTGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVES 442
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
73-248 |
5.37e-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: 56.05 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 73 WRETLTSPYQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIR 152
Cdd:cd17634 74 YEGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRII 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 153 QTDMQVVIVEDDG-KAAMLLEKAPRSLKIIVAIKPIRQTTLERARSR---GIQIFSFIDVEKLGAKGN--HPEVPPTAED 226
Cdd:cd17634 154 DSSSRLLITADGGvRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGsdiDWQEGRDLWWRDLIAKASpeHQPEAMNAED 233
|
170 180
....*....|....*....|..
gi 281366413 227 LCTVCYTSGTTGNPKGVMLTHG 248
Cdd:cd17634 234 PLFILYTSGTTGKPKGVLHTTG 255
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-519 |
2.10e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.58 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 52 RTLYQTFREGAYASNNGPCLGWREtltspyQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYE 125
Cdd:PRK12316 4551 RCVHQLVAERARMTPDAVAVVFDE------EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMmvgllaVLKA 4624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 126 QGCYsfslvvVPLYDTLGPDACAFIIrqtdmqvvivEDDGkAAMLLEKApRSLKIIVAIKPIRQTTLERARsrgiqifsf 205
Cdd:PRK12316 4625 GGAY------VPLDPEYPRERLAYMM----------EDSG-AALLLTQS-HLLQRLPIPDGLASLALDRDE--------- 4677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 206 idvEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSvilqMGD-HRIRAGDVMVSFLPLAhmfer 284
Cdd:PRK12316 4678 ---DWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHA----TGErYELTPDDRVLQFMSFS----- 4745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 285 ccengmyYVGGCVGFYSGdikeLTNDLKMLKPTVMPAVPRLLNRVYDKiqNDISASGLKRGLFNMAMRAKEKEIARGVLR 364
Cdd:PRK12316 4746 -------FDGSHEGLYHP----LINGASVVIRDDSLWDPERLYAEIHE--HRVTVLVFPPVYLQQLAEHAERDGEPPSLR 4812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 365 rngcwdklvfkkvHQAFGGNlrLMVVGSAPLAgnvltfMRCALGCLVLEGYGQTECTGAITLTVQGDHVPN-----HVGP 439
Cdd:PRK12316 4813 -------------VYCFGGE--AVAQASYDLA------WRALKPVYLFNGYGPTETTVTVLLWKARDGDACgaaymPIGT 4871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 440 PVSCNAVKLVDVpEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAE-----AIDSEG--WHHTGDVGMWLPNGTLRIIDR 512
Cdd:PRK12316 4872 PLGNRSGYVLDG-QLNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGR 4950
|
....*..
gi 281366413 513 RKHIFKL 519
Cdd:PRK12316 4951 VDHQVKI 4957
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
176-560 |
2.19e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 53.75 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 176 RSLKIIVAIKP-----IRQTTLERArsrGIQIFSFIDVEKLGAKGNHPEV--PPTAEDLCTVCYTSGTTGNPKGVMLTHG 248
Cdd:PRK04813 90 RIEMIIEVAKPsliiaTEELPLEIL---GIPVITLDELKDIFATGNPYDFdhAVKGDDNYYIIFTSGTTGKPKGVQISHD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 249 NVVAGVCSVIlqmGDHRIRAGDVMVSFLPlahmferccengmyyvggcvgfYSGDI-------------------KELTN 309
Cdd:PRK04813 167 NLVSFTNWML---EDFALPEGPQFLNQAP----------------------YSFDLsvmdlyptlasggtlvalpKDMTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 310 DLKMLKPTvMPAVPR-------------LLNRVYDKIQNdisaSGLKRGLFnmamrakekeiargvlrrngCWDKL---V 373
Cdd:PRK04813 222 NFKQLFET-LPQLPInvwvstpsfadmcLLDPSFNEEHL----PNLTHFLF--------------------CGEELphkT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 374 FKKVHQAFggnlrlmvvgsaPLAgnvltfmrcalgcLVLEGYGQTECTGAIT-------LTVQGDHVPnhVGPPVSCNAV 446
Cdd:PRK04813 277 AKKLLERF------------PSA-------------TIYNTYGPTEATVAVTsieitdeMLDQYKRLP--IGYAKPDSPL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 447 KLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEA---IDSEGWHHTGDVGMwLPNGTLRIIDRRKHIFKLSqGE 523
Cdd:PRK04813 330 LIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGY-LEDGLLFYQGRIDFQIKLN-GY 406
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 281366413 524 YIVPEKIENIYTLSQYVNQ---VYVYGESLKSCIIAVVVP 560
Cdd:PRK04813 407 RIELEEIEQNLRQSSYVESavvVPYNKDHKVQYLIAYVVP 446
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
92-533 |
2.24e-07 |
|
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: 53.97 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 92 RAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDgkaamLL 171
Cdd:cd05915 33 RARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN-----LL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 172 EKAPRSLKIIVAI--KPIRQTTLERarsrgiqifsFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGN 249
Cdd:cd05915 108 PLVEAIRGELKTVqhFVVMDEKAPE----------GYLAYEEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 250 VVAGVCSVILqMGDHRIRAGDVMVSFLPLAHMFERCCENGMYYVGGCVGFysgdIKELTNDlkmlkptvmpavprllNRV 329
Cdd:cd05915 178 LVLHSLAASL-VDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVL----PGPRLDP----------------ASL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 330 YDKI-QNDISASGLKRGLFNMAMRAKEKeiargvlrrngcwdklvfkkVHQAFGGNLRLMVVGSAPlaGNVLTFMRCALG 408
Cdd:cd05915 237 VELFdGEGVTFTAGVPTVWLALADYLES--------------------TGHRLKTLRRLVVGGSAA--PRSLIARFERMG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 409 CLVLEGYGQTECTGAIT----------------LTVQGDHVPNHVGppvscNAVKLVDVPEMEYFANQNTGEV-CVRGSN 471
Cdd:cd05915 295 VEVRQGYGLTETSPVVVqnfvkshleslseeekLTLKAKTGLPIPL-----VRLRVADEEGRPVPKDGKALGEvQLKGPW 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366413 472 VFHGYYKDPEKTAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENI 533
Cdd:cd05915 370 ITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GEWISSVDLENA 430
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-519 |
2.93e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 54.01 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 82 QWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWI------LYEQGCYsfslvvVPLYDTLGPDACAFIIRQTD 155
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIvallavLKAGGAY------VPLDPEYPRERLAYMIEDSG 3192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 156 MQVVIVEddgkaAMLLEKAPRSlkiivaikpirqttlerarsRGIQIFSFIDVEKLGAKGNHPEVPPTAEDLCTVCYTSG 235
Cdd:PRK12467 3193 VKLLLTQ-----AHLLEQLPAP--------------------AGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSG 3247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 236 TTGNPKGVMLTHGnVVAGVCSVILQMgdHRIRAGDVMVSFLPLAhmFERCCEN--GMYYVGGCVGFYSGDIkeltndlkm 313
Cdd:PRK12467 3248 STGKPKGVGVRHG-ALANHLCWIAEA--YELDANDRVLLFMSFS--FDGAQERflWTLICGGCLVVRDNDL--------- 3313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 314 lkptvmpavprllnRVYDKIQNDISASGLKRGLFNMAMRAKEKEIARGvlrrngcwdklvfkkvhqAFGGNLRLMVVGSA 393
Cdd:PRK12467 3314 --------------WDPEELWQAIHAHRISIACFPPAYLQQFAEDAGG------------------ADCASLDIYVFGGE 3361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 394 PLAGNVLTFMRCALGCLVL-EGYGQTECTGAITL-TVQGDHVPNH----VGPPVSCNAVKLVDvPEMEYFANQNTGEVCV 467
Cdd:PRK12467 3362 AVPPAAFEQVKRKLKPRGLtNGYGPTEAVVTVTLwKCGGDAVCEApyapIGRPVAGRSIYVLD-GQLNPVPVGVAGELYI 3440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 281366413 468 RGSNVFHGYYKDPEKTAE-----AIDSEG--WHHTGDVGMWLPNGTLRIIDRRKHIFKL 519
Cdd:PRK12467 3441 GGVGLARGYHQRPSLTAErfvadPFSGSGgrLYRTGDLARYRADGVIEYLGRIDHQVKI 3499
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
204-539 |
3.06e-07 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 53.17 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 204 SFIdVEKLGAKGnhpeVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhRIRAGDVMVSFLPlAHMFE 283
Cdd:cd17648 78 QFI-LEDTGARV----VITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYF--GRDNGDEAVLFFS-NYVFD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 284 RCCENgMyyvggCVGFYSGdikeltNDLKMLKPTVMPAVPRLlnrvYDKIQND----ISASGLKRGLFNMAMRAKEKeia 359
Cdd:cd17648 150 FFVEQ-M-----TLALLNG------QKLVVPPDEMRFDPDRF----YAYINREkvtyLSGTPSVLQQYDLARLPHLK--- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 360 rgvlrrngcwdklvfkkvhqafggnlRLMVVGSApLAGNVLTFMRCALGCLVLEGYGQTECTgaITLTVQ----GDHVPN 435
Cdd:cd17648 211 --------------------------RVDAAGEE-FTAPVFEKLRSRFAGLIINAYGPTETT--VTNHKRffpgDQRFDK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 436 HVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAE-------AIDSEGW-------HHTGDVGMW 501
Cdd:cd17648 262 SLGRPVRNTKCYVLN-DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfQTEQERArgrnarlYKTGDLVRW 340
|
330 340 350
....*....|....*....|....*....|....*...
gi 281366413 502 LPNGTLRIIDRRKHIFKLsQGEYIVPEKIENiyTLSQY 539
Cdd:cd17648 341 LPSGELEYLGRNDFQVKI-RGQRIEPGEVEA--ALASY 375
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
84-280 |
3.18e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 53.34 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVED 163
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 DGKAAmlLEKAPRSLKIivaikPIRQTTLERARsrGIQIFSFIDVEKLGAkgNHPEVPP------TAEDLCTVCYTSGTT 237
Cdd:PRK08279 143 ELVEA--FEEARADLAR-----PPRLWVAGGDT--LDDPEGYEDLAAAAA--GAPTTNPasrsgvTAKDTAFYIYTSGTT 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 281366413 238 GNPKGVMLTH------GNVVAGVCsvilqmgdhRIRAGDVMVSFLPLAH 280
Cdd:PRK08279 212 GLPKAAVMSHmrwlkaMGGFGGLL---------RLTPDDVLYCCLPLYH 251
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
86-547 |
6.83e-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: 52.14 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 86 YDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLVVVPLYDTLGPDACAFIIRQTDMQVVIVEDDG 165
Cdd:cd05973 3 FGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 166 KAamllekaprslkiivaikpirqttlerarsrgiqifsfidveKLgakgnhpevpptAEDLCTVCYTSGTTGNPKGVML 245
Cdd:cd05973 83 RH------------------------------------------KL------------DSDPFVMMFTSGTTGLPKGVPV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 246 THGNVVAGVCSVILQMGdhrIRAGDVmvsflplahmFERCCENGMYYvggcvGFYSGdikeLTNDLKMLKPTVMPAVPRL 325
Cdd:cd05973 109 PLRALAAFGAYLRDAVD---LRPEDS----------FWNAADPGWAY-----GLYYA----ITGPLALGHPTILLEGGFS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 326 LNRVYDKIQndisasglKRGLFNMAMrakekeiARGVLRrngcwdKLVFKKVHQAFGGNLRLMVVGSA--PLAGNVLTFM 403
Cdd:cd05973 167 VESTWRVIE--------RLGVTNLAG-------SPTAYR------LLMAAGAEVPARPKGRLRRVSSAgePLTPEVIRWF 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 404 RCALGCLVLEGYGQTEcTGAITLTVQGDHVPNHVGP---PVSCNAVKLVDVPEMEYFANQnTGEVCVRGSNV----FHGY 476
Cdd:cd05973 226 DAALGVPIHDHYGQTE-LGMVLANHHALEHPVHAGSagrAMPGWRVAVLDDDGDELGPGE-PGRLAIDIANSplmwFRGY 303
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281366413 477 YKDPEKTAEAidseGWHHTGDVGMWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENIYTLSQYVNQVYVYG 547
Cdd:cd05973 304 QLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAVAEAAVIG 369
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
52-255 |
1.00e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 52.47 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 52 RTLYQTFREGAYASNNGPCLGWREtltspyQWINYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEW------ILYE 125
Cdd:PRK12467 1574 RLVHQLIEDQAAATPEAVALVFGE------QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMvvgllaILKA 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 126 QGCYsfslvvVPLYDTLGPDACAFIIRQTDMQVVIVEddgkaAMLLEKAPrslkiivAIKPIRQTTLErarsrgiQIFSF 205
Cdd:PRK12467 1648 GGAY------VPLDPEYPRERLAYMIEDSGIELLLTQ-----SHLQARLP-------LPDGLRSLVLD-------QEDDW 1702
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 281366413 206 IDveklGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVC 255
Cdd:PRK12467 1703 LE----GYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLC 1748
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
217-564 |
3.22e-06 |
|
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: 50.39 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 217 HPEVPPTAEDLCTVCYTSGTTGNPKGVML-THGNVVAGVCSVI----LQMGDHRIRAGDV-------MVSFLPLAHmfer 284
Cdd:cd05967 222 VDCVPVAATDPLYILYTSGTTGKPKGVVRdNGGHAVALNWSMRniygIKPGDVWWAASDVgwvvghsYIVYGPLLH---- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 285 ccenGMYYVggcvgFYSGdikeltndlkmlKPTVMPAvPRLLNRVYDKIQndisasglKRGLFN--MAMRAKEKEIARGv 362
Cdd:cd05967 298 ----GATTV-----LYEG------------KPVGTPD-PGAFWRVIEKYQ--------VNALFTapTAIRAIRKEDPDG- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 363 lrrngcwdklvfKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCLVLEGYGQTE--------CTGAITLTVQgdhvP 434
Cdd:cd05967 347 ------------KYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTEtgwpitanPVGLEPLPIK----A 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 435 NHVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRG---SNVFHGYYKDPE--KTAEAIDSEGWHHTGDVGMWLPNGTLRI 509
Cdd:cd05967 411 GSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLplpPGCLLTLWKNDErfKKLYLSKFPGYYDTGDAGYKDEDGYLFI 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366413 510 IDRRKHIF-----KLSQGEyivpekIENIYTLSQYVNQVYVYG--ESLKSCI-IAVVVPDTDV 564
Cdd:cd05967 490 MGRTDDVInvaghRLSTGE------MEESVLSHPAVAECAVVGvrDELKGQVpLGLVVLKEGV 546
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
225-545 |
3.36e-06 |
|
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: 50.13 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 225 EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAhmFERCCENgMYyvggcVGFYSGdi 304
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYG---ITSSDRVLQFASIA--FDVAAEE-IY-----VTLLSG-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 305 keltNDLKMLKPTVMPAVPRLLnrvyDKI-QNDISASGLKRGLFNMAMRAKEKEIARGVlrrngcwdklvfkkvhqafgG 383
Cdd:cd17644 173 ----ATLVLRPEEMRSSLEDFV----QYIqQWQLTVLSLPPAYWHLLVLELLLSTIDLP--------------------S 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 384 NLRLMVVGSAPLAGNVLTFMRCALGCLV--LEGYGQTECTGAITL-------TVQGDHVPnhVGPPVSCNAVKLVD---- 450
Cdd:cd17644 225 SLRLVIVGGEAVQPELVRQWQKNVGNFIqlINVYGPTEATIAATVcrltqltERNITSVP--IGRPIANTQVYILDenlq 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 451 -VPEmeyfanQNTGEVCVRGSNVFHGYYKDPEKTAEAIDSEGWHH--------TGDVGMWLPNGTLRIIDRRKHIFKLsQ 521
Cdd:cd17644 303 pVPV------GVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-R 375
|
330 340
....*....|....*....|....
gi 281366413 522 GEYIVPEKIENIYTLSQYVNQVYV 545
Cdd:cd17644 376 GFRIELGEIEAVLSQHNDVKTAVV 399
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
164-278 |
4.93e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.04 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 164 DGKAAMLLEKAPRSLKIIVAIkpirqttlERARSRGIQIFSFIDVEK-LGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKG 242
Cdd:PRK10252 544 DDRLKMMLEDARPSLLITTAD--------QLPRFADVPDLTSLCYNApLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKG 615
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 281366413 243 VMLTHGNVVagvcSVILQMGDH-RIRAGDVM---------VS----FLPL 278
Cdd:PRK10252 616 VMVGQTAIV----NRLLWMQNHyPLTADDVVlqktpcsfdVSvwefFWPF 661
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
222-558 |
5.02e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 49.30 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 222 PTAEDLcTVCYTSGTTGNPKGVMLTHG----------NVVAGVCSVILQMGDHRIRAGD-VMVSFLPLAHmferccenGM 290
Cdd:cd05924 1 RSADDL-YILYTGGTTGMPKGVMWRQEdifrmlmggaDFGTGEFTPSEDAHKAAAAAAGtVMFPAPPLMH--------GT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 291 YYVGGCVGFYSGDiKELTNDLKMLKPTVMPAVPRllNRVydkiqNDISASGLKrglfnMAMRAKEKeiargvLRRNGCWD 370
Cdd:cd05924 72 GSWTAFGGLLGGQ-TVVLPDDRFDPEEVWRTIEK--HKV-----TSMTIVGDA-----MARPLIDA------LRDAGPYD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 371 KlvfkkvhqafgGNLRLMVVGSAPLAGNVLT-FMRCALGCLVLEGYGQTECTGAITLTVQGDhvPNHVGPPVSCNA-VKL 448
Cdd:cd05924 133 L-----------SSLFAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFTGSGHSAGS--GPETGPFTRANPdTVV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 449 VD-----VPEmeyfANQNTGEVCVRGsNVFHGYYKDPEKTAEA---IDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFKlS 520
Cdd:cd05924 200 LDddgrvVPP----GSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCIN-T 273
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 281366413 521 QGEYIVPEKIENIYTLSQYVNQVYVYG---ESLKSCIIAVV 558
Cdd:cd05924 274 GGEKVFPEEVEEALKSHPAVYDVLVVGrpdERWGQEVVAVV 314
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
207-519 |
1.15e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.01 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 207 DVEKLGAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVI--LQMGDHRIRAG------DVMV-SFLP 277
Cdd:PRK05691 3851 EVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVpyLALSEADVIAQtasqsfDISVwQFLA 3930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 278 lAHMFerccengmyyvGGCVGFYSGDI----KELTNDLKMLKPTVMPAVPRLLNRvydkiqndisasglkrglfnmaMRA 353
Cdd:PRK05691 3931 -APLF-----------GARVEIVPNAIahdpQGLLAHVQAQGITVLESVPSLIQG----------------------MLA 3976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 354 KEkeiargvlrrngcwdklvfkkvHQAFGGnLRLMV-VGSA---PLAGNVLtfMRCALGCLVlEGYGQTECTGAITL--- 426
Cdd:PRK05691 3977 ED----------------------RQALDG-LRWMLpTGEAmppELARQWL--QRYPQIGLV-NAYGPAECSDDVAFfrv 4030
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 427 ---TVQGDHVPnhVGPPVSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKTAEAI-------DSEGWHHTG 496
Cdd:PRK05691 4031 dlaSTRGSYLP--IGSPTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTG 4107
|
330 340
....*....|....*....|...
gi 281366413 497 DVGMWLPNGTLRIIDRRKHIFKL 519
Cdd:PRK05691 4108 DLARRRSDGVLEYVGRIDHQVKI 4130
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
194-533 |
1.81e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 47.84 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 194 RARSRGIQIFsfiDVEKLGAKGNHPEVPPTA-EDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGDHRirAGDVM 272
Cdd:PRK05851 123 RAVDSSVTVH---DLATAAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDA--ATDVG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 273 VSFLPLAHmferccENGMYYVggCVGFYSGdiKELtndlkMLKPT-VMPAVP-RLLNRvydkiqndISASGlkrglfnmA 350
Cdd:PRK05851 198 CSWLPLYH------DMGLAFL--LTAALAG--APL-----WLAPTtAFSASPfRWLSW--------LSDSR--------A 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 351 MRAKEKEIARGVLRRNGcwdklvfKKVHQAFGGNLRLMVVGSAPLAGNVLTFMRCALGCL------VLEGYGQTECTGAI 424
Cdd:PRK05851 247 TLTAAPNFAYNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFgfdagaAAPSYGLAESTCAV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 425 TLTVQG-----DHVPNHVGPPVSCNAVKLVDVPEMEY----------FANQNTGEVCVRGSNVFHGYYKDPektaeAIDS 489
Cdd:PRK05851 320 TVPVPGiglrvDEVTTDDGSGARRHAVLGNPIPGMEVrispgdgaagVAGREIGEIEIRGASMMSGYLGQA-----PIDP 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 281366413 490 EGWHHTGDVGmWLPNGTLRIIDRRKHIFKLSqGEYIVPEKIENI 533
Cdd:PRK05851 395 DDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
226-549 |
1.86e-05 |
|
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: 47.01 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 226 DLCTVCYTSGTTGNPKGVMLTHGNVVAgvcSVILQMGDHRIRAGDVMVSFLPLAH-MFERCCENGMYYVGGCVGFYSGDI 304
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIE---SFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 305 KELTNDLKMLKPTVMPAVPRLLNRVYdKIQNDISAsglkrglfnmamrakekeiARGVLRRNGCWDKLVFKKVHQAFggn 384
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALA-RTLEPESK-------------------IKSIFSSGQKLFESTKKKLKNIF--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 385 lrlmvvgsaPLAgNVLTFmrcalgclvlegYGQTECTGAITLTVQGDHVPNHVGPPvsCNAVKLvdvpEMEYFANQNTGE 464
Cdd:cd17633 135 ---------PKA-NLIEF------------YGTSELSFITYNFNQESRPPNSVGRP--FPNVEI----EIRNADGGEIGK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 465 VCVRGSNVFHGYYKdpektAEAIDSEGWHHTGDVGMWLPNGTLRIIDRRKHIFkLSQGEYIVPEKIENIYTLSQYVNQVY 544
Cdd:cd17633 187 IFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAI 260
|
....*
gi 281366413 545 VYGES 549
Cdd:cd17633 261 VVGIP 265
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
415-568 |
1.89e-05 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 47.68 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 415 YGQTECTGAI-TLT----VQGDhvpNHVGPPVSCNAVKLVdvpemeyfaNQNTGEVCVRGSNVFHGYYkdPEKtaeaIDS 489
Cdd:PRK07445 261 YGMTETASQIaTLKpddfLAGN---NSSGQVLPHAQITIP---------ANQTGNITIQAQSLALGYY--PQI----LDS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 490 EGWHHTGDVGMWLPNGTLRIIDR--RKHIfklSQGEYIVPEKIENIYTLSQYVNQVYVYGesLKSC-----IIAVVVPDT 562
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRnsQKII---TGGENVYPAEVEAAILATGLVQDVCVLG--LPDPhwgevVTAIYVPKD 397
|
170
....*....|.
gi 281366413 563 DV-----LKQW 568
Cdd:PRK07445 398 PSisleeLKTA 408
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
226-563 |
2.66e-05 |
|
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: 46.96 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 226 DLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVilqMGDHRIRAGDVMVSFLPLAHMFER-CCENGMYYVGGCV------- 297
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF---AGSGGALPSDVLYTCLPLYHSTALiVGWSACLASGATLvirkkfs 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 298 --GFYSGDIKEltndlkmlKPTVMPAVPRLLnrvydkiqndisasglkRGLFNmamrAKEKEIARGvlrrngcwdklvfK 375
Cdd:cd05940 159 asNFWDDIRKY--------QATIFQYIGELC-----------------RYLLN----QPPKPTERK-------------H 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 376 KVHQAFGGNLRLMVVGSAPLAGNVLTfmrcalgclVLEGYGQTECT-GAITLtvqgDHVPNHVG------PPVSCNAVKL 448
Cdd:cd05940 197 KVRMIFGNGLRPDIWEEFKERFGVPR---------IAEFYAATEGNsGFINF----FGKPGAIGrnpsllRKVAPLALVK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 449 VDVPEMEYFANQN----------TGEVCVRGSNV--FHGYYkDPEKTAEAI------DSEGWHHTGDVGMWLPNGTLRII 510
Cdd:cd05940 264 YDLESGEPIRDAEgrcikvprgePGLLISRINPLepFDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFV 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 281366413 511 DRRKHIFKLsQGEYIVPEKIENIYTLSQYVNQVYVYGeslksciiaVVVPDTD 563
Cdd:cd05940 343 DRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYG---------VQVPGTD 385
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
74-572 |
3.25e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 47.06 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 74 RETLTspyqWINYDEallRAKNFGAGMLALGARPKQLIGIYSQNRPEWILyeqgcysfSLVV-------VPLYDT--LGP 144
Cdd:PRK13382 66 LGTLT----WRELDE---RSDALAAALQALPIGEPRVVGIMCRNHRGFVE--------ALLAanrigadILLLNTsfAGP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 145 DACAFIIRQtdmQVVIVEDDGKAAMLLEKA----PRSLKIIVAIKPIRQTTlerarsrgiqifsfidVEKLGAKGNHPEV 220
Cdd:PRK13382 131 ALAEVVTRE---GVDTVIYDEEFSATVDRAladcPQATRIVAWTDEDHDLT----------------VEVLIAAHAGQRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 221 PPTAEDLCTVCYTSGTTGNPKGVMLThGNVVAGVCSVILQmgdhRI--RAGDVMVSFLPLAHMFerccengmyyvggcvG 298
Cdd:PRK13382 192 EPTGRKGRVILLTSGTTGTPKGARRS-GPGGIGTLKAILD----RTpwRAEEPTVIVAPMFHAW---------------G 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 299 F----YSGDIK-----------ELTNDL-KMLKPTVMPAVPRLLNRVYDkIQNDISASGLKRGLfnmamrakekeiargv 362
Cdd:PRK13382 252 FsqlvLAASLActivtrrrfdpEATLDLiDRHRATGLAVVPVMFDRIMD-LPAEVRNRYSGRSL---------------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 363 lrrngcwdklvfkKVHQAFGGNLRLMVVgsaplagnvLTFMRcALGCLVLEGYGQTEcTGAITLTVQGD--HVPNHVGPP 440
Cdd:PRK13382 315 -------------RFAAASGSRMRPDVV---------IAFMD-QFGDVIYNNYNATE-AGMIATATPADlrAAPDTAGRP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 441 VSCNAVKLVDvPEMEYFANQNTGEVCVRGSNVFHGYykDPEKTAEAIDseGWHHTGDVGMWLPNGTLRIIDRRKHIFkLS 520
Cdd:PRK13382 371 AEGTEIRILD-QDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHD--GFMASGDVGYLDENGRLFVVGRDDEMI-VS 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281366413 521 QGEYIVPEKIENIYTLSQYVNQVYVYG---ESLKSCIIAVVVPDTDV------LKQWATEN 572
Cdd:PRK13382 445 GGENVYPIEVEKTLATHPDVAEAAVIGvddEQYGQRLAAFVVLKPGAsatpetLKQHVRDN 505
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
219-280 |
6.84e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 45.88 E-value: 6.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366413 219 EVPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAGVCSVILQMGdhrIRAGDVMVSFLPLAH 280
Cdd:PRK07769 174 PPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALE---GQEGDRGVSWLPFFH 232
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
232-280 |
1.09e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 45.32 E-value: 1.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 281366413 232 YTSGTTGNPKGVMLTHGNVVAGVCSVILQ-MGDH--RIRAGDVMVSFLPLAH 280
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANFEQLMSDyFGDTggVPPPDTTVVSWLPFYH 218
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
220-298 |
1.53e-04 |
|
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: 44.97 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 220 VPPTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAgvCSVILQM-GdhrIRAGDVMVSFLPLAHMferccENGMYYVGGCVG 298
Cdd:cd05938 139 AHVTIKSPALYIYTSGTTGLPKAARISHLRVLQ--CSGFLSLcG---VTADDVIYITLPLYHS-----SGFLLGIGGCIE 208
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
84-248 |
2.23e-04 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 44.16 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 84 INYDEALLRAKNFGAGMLALGARPKQLIGIYSQNRPEWILYEQGCYSFSLV--VVplYDTLGPDACAFIIRQTDMQVVIV 161
Cdd:TIGR02188 89 ITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIhsVV--FGGFSAEALADRINDAGAKLVIT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 162 EDD----GKAAML-------LEKAPRSLK-IIVaikpIRQTtlerarsrGIQIFSFI---DV--EKLGAKGNhPEVPPT- 223
Cdd:TIGR02188 167 ADEglrgGKVIPLkaivdeaLEKCPVSVEhVLV----VRRT--------GNPVVPWVegrDVwwHDLMAKAS-AYCEPEp 233
|
170 180
....*....|....*....|....*..
gi 281366413 224 --AEDLCTVCYTSGTTGNPKGVMLTHG 248
Cdd:TIGR02188 234 mdSEDPLFILYTSGSTGKPKGVLHTTG 260
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
134-252 |
3.72e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 43.73 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 134 VVVPLYDTLGPDACAFIIRQTDMQVVIVEDDgkaamLLEKAPR----SLKIIVAIKpirqttlerarSRGIQIFSFIDVE 209
Cdd:PRK04319 124 IVGPLFEAFMEEAVRDRLEDSEAKVLITTPA-----LLERKPAddlpSLKHVLLVG-----------EDVEEGPGTLDFN 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 281366413 210 KLGAKGN-HPEVPPT-AEDLCTVCYTSGTTGNPKGVMLTHGNVVA 252
Cdd:PRK04319 188 ALMEQASdEFDIEWTdREDGAILHYTSGSTGKPKGVLHVHNAMLQ 232
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
220-515 |
4.63e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 43.19 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 220 VPPTAEDLCTVCYTSGTTGNPKGVMLTHgnvvAGVCSVILQMgdhrIRAGDVM------VSFLPLAH-------MFERCC 286
Cdd:PRK12476 188 VELDTDDVSHLQYTSGSTRPPVGVEITH----RAVGTNLVQM----ILSIDLLdrnthgVSWLPLYHdmglsmiGFPAVY 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 287 engmyyvGGCVGFYSGD---------IKELTNDLKMLKptVMPAVPrllNRVYD-KIQNDISASGLKRGLFNMAMRAKEK 356
Cdd:PRK12476 260 -------GGHSTLMSPTafvrrpqrwIKALSEGSRTGR--VVTAAP---NFAYEwAAQRGLPAEGDDIDLSNVVLIIGSE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 357 EIARGVLRrngcwdklVFKKVHQAFG------------GNLRLMVVGSAPLA-GNVLTFMRCALGclvlEGYGqtectga 423
Cdd:PRK12476 328 PVSIDAVT--------TFNKAFAPYGlprtafkpsygiAEATLFVATIAPDAePSVVYLDREQLG----AGRA------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366413 424 itLTVQGDHvPNHVgPPVSCNAVK------LVDVPEMEYFANQNTGEVCVRGSNVFHGYYKDPEKT-------------- 483
Cdd:PRK12476 389 --VRVAADA-PNAV-AHVSCGQVArsqwavIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlae 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 281366413 484 ----AEAIDSEGWHHTGDVGMWLpNGTL----RI-----IDRRKH 515
Cdd:PRK12476 465 gshaDGAADDGTWLRTGDLGVYL-DGELyitgRIadlivIDGRNH 508
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
214-248 |
9.58e-04 |
|
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: 42.16 E-value: 9.58e-04
10 20 30
....*....|....*....|....*....|....*...
gi 281366413 214 KGNHPEVPPT---AEDLCTVCYTSGTTGNPKGVMLTHG 248
Cdd:cd05966 217 AKQSPECEPEwmdSEDPLFILYTSGSTGKPKGVVHTTG 254
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
222-253 |
1.06e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 41.95 E-value: 1.06e-03
10 20 30
....*....|....*....|....*....|..
gi 281366413 222 PTAEDLCTVCYTSGTTGNPKGVMLTHGNVVAG 253
Cdd:PRK07824 32 PIDDDVALVVATSGTTGTPKGAMLTAAALTAS 63
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
212-248 |
1.73e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 41.66 E-value: 1.73e-03
10 20 30
....*....|....*....|....*....|....*..
gi 281366413 212 GAKGNHPEVPPTAEDLCTVCYTSGTTGNPKGVMLTHG 248
Cdd:PRK00174 232 GASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTG 268
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
218-280 |
3.91e-03 |
|
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: 40.10 E-value: 3.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366413 218 PEVPPTAED------LCTVcYTSGTTGNPKGVMLTHGN---VVAGVCSVIlqmgdhRIRAGDVMVSFLPLAH 280
Cdd:cd05939 92 STEPPSQDDvnfrdkLFYI-YTSGTTGLPKAAVIVHSRyyrIAAGAYYAF------GMRPEDVVYDCLPLYH 156
|
|
| |
