|
Name |
Accession |
Description |
Interval |
E-value |
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
20-532 |
3.47e-141 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 420.28 E-value: 3.47e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 20 LPPPTQVLTFDE--ALSASLARPLTFRPVPKDVR--SVATLVYTSGTTNKPKGVVLRHSNLLHQVNynsftdspskepAY 95
Cdd:COG1022 148 LRDDPRLLSLDEllALGREVADPAELEARRAAVKpdDLATIIYTSGTTGRPKGVMLTHRNLLSNAR------------AL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 96 NPVL----GDVLVSVLPCWHIFERTAEYWMFSKGIHVVYS-NVKNFKADLAKHQPQFIVAVPRLLETIYRGVLQKFAAEK 170
Cdd:COG1022 216 LERLplgpGDRTLSFLPLAHVFERTVSYYALAAGATVAFAeSPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 171 GAKKKIIEFFTRVGSAWVKAwrvarglVLRSRAPNPIERllalvlalvlsPLAAVGDKLVWSKVRAGLGGRIKVLVAGGS 250
Cdd:COG1022 296 GLKRKLFRWALAVGRRYARA-------RLAGKSPSLLLR-----------LKHALADKLVFSKLREALGGRLRFAVSGGA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 251 SMPLVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIvdpesgarlpeGQPGLVLMRGPQMMA 330
Cdd:COG1022 358 ALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKI-----------AEDGEILVRGPNVMK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 331 GYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVLSNGENVEPQPIEDVVCAnSALVDQVMCVGQDEKV 410
Cdd:COG1022 427 GYYKNPEATAEAFDADGWLHTGDIGELDE-DGFLRITGRKKDLIVTSGGKNVAPQPIENALKA-SPLIEQAVVVGDGRPF 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 411 LGMLVVPNVRALARaglvdrgLAERvaellggqvltNGIAGSRAEleeveaSLREKKEVKKALLADIARAMgKSFRETER 490
Cdd:COG1022 505 LAALIVPDFEALGE-------WAEE-----------NGLPYTSYA------ELAQDPEVRALIQEEVDRAN-AGLSRAEQ 559
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 585104306 491 VGAVEVVLEPFNMANGFLTQTLKVKRNVVSGHYAQEIEQMYR 532
Cdd:COG1022 560 IKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
52-519 |
4.25e-133 |
|
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: 394.80 E-value: 4.25e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 52 SVATLVYTSGTTNKPKGVVLRHSNLLHQV-NYNSFTDspskepaynPVLGDVLVSVLPCWHIFERTAEYWMFSKGIHVVY 130
Cdd:cd17640 89 DLATIIYTSGTTGNPKGVMLTHANLLHQIrSLSDIVP---------PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 131 SNVKNFKADLAKHQPQFIVAVPRLLETIYRGVLQKFAAEKGAKKKIIEFFTrvgsawvkawrvarglvlrsrapnpierl 210
Cdd:cd17640 160 TSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFL----------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 211 lalvlalvlsplaavgdklvwskvragLGGRIKVLVAGGSSMPLVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLA 290
Cdd:cd17640 211 ---------------------------SGGIFKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 291 GSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRA 370
Cdd:cd17640 264 GSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTC-GGELVLTGRA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 371 KDTIVLSNGENVEPQPIEDvVCANSALVDQVMCVGQDEKVLGMLVVPNVRALARAglvdrgLAERvaellgGQVLTNGIA 450
Cdd:cd17640 343 KDTIVLSNGENVEPQPIEE-ALMRSPFIEQIMVVGQDQKRLGALIVPNFEELEKW------AKES------GVKLANDRS 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585104306 451 GSRAELEEVEAslrEKKEVKKALladiarAMGKSFRETERVGAVEVVLEPFnMANGFLTQTLKVKRNVV 519
Cdd:cd17640 410 QLLASKKVLKL---YKNEIKDEI------SNRPGFKSFEQIAPFALLEEPF-IENGEMTQTMKIKRNVV 468
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
53-519 |
2.02e-84 |
|
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: 269.08 E-value: 2.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 53 VATLVYTSGTTNKPKGVVLRHSNLLHQVnYNSFTdspskepAYNPVLGDVLVSVLPCWHIFE-RTAEYWMFSKGIHVVY- 130
Cdd:cd05907 89 LATIIYTSGTTGRPKGVMLSHRNILSNA-LALAE-------RLPATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFa 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 131 SNVKNFKADLAKHQPQFIVAVPRLLETIYRGVLQKfaAEKGAKKKIIEFftrvgsawvkawrvarglvlrsrapnpierl 210
Cdd:cd05907 161 SSAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVK--AVPGLKRKLFDL------------------------------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 211 lalvlalvlsplaavgdklvwskvraGLGGRIKVLVAGGSSMPLVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLA 290
Cdd:cd05907 208 --------------------------AVGGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 291 GSVGRTARDTEVKIVDpesgarlpegqPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRA 370
Cdd:cd05907 262 GTVGKPLPGVEVRIAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDE-DGFLHITGRK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 371 KDTIVLSNGENVEPQPIEDVVcANSALVDQVMCVGQDEKVLGMLVVPNVRALARAGLVDRGLAERVAELlggqvltngia 450
Cdd:cd05907 330 KDLIITSGGKNISPEPIENAL-KASPLISQAVVIGDGRPFLVALIVPDPEALEAWAEEHGIAYTDVAEL----------- 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585104306 451 gsrAELEEVEASLREkkEVkKALLADIARAmgksfretERVGAVEVVLEPFNMANGFLTQTLKVKRNVV 519
Cdd:cd05907 398 ---AANPAVRAEIEA--AV-EAANARLSRY--------EQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
45-532 |
9.72e-78 |
|
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: 254.06 E-value: 9.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 45 PVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVNynSFTDSPSKEPAYNPVlgDVLVSVLPCWHIFERTAEYWMFSK 124
Cdd:cd05927 108 PPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVA--GVFKILEILNKINPT--DVYISYLPLAHIFERVVEALFLYH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 125 GIHV-VYS-NVKNFKADLAKHQPQFIVAVPRLLETIYRGVLQKFAAEKGAKKKIIEFFTRVGSAWVKawrvaRGLVLRSR 202
Cdd:cd05927 184 GAKIgFYSgDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELR-----SGVVRASP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 203 apnpierllalvlalvlsplaaVGDKLVWSKVRAGLGGRIKVLVAGGSSMPLVLEDFfelLRT----PVIVGYGMTETSP 278
Cdd:cd05927 259 ----------------------FWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEF---LRValgcPVLEGYGQTECTA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 279 VITNRVAEKNLAGSVGRTARDTEVKIVD-PESG--ARLPEGQpGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLG 355
Cdd:cd05927 314 GATLTLPGDTSVGHVGGPLPCAEVKLVDvPEMNydAKDPNPR-GEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIG 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 356 RIHPlTKHLIITGRAKDTIVLSNGENVEPQPIEDVVcANSALVDQVMCVGQDEKV-LGMLVVPNVRALARaglvdrglae 434
Cdd:cd05927 393 EWLP-NGTLKIIDRKKNIFKLSQGEYVAPEKIENIY-ARSPFVAQIFVYGDSLKSfLVAIVVPDPDVLKE---------- 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 435 rvaellggqvltngIAGSRAELEEVEASLREKKEVKKALLADIaRAMGK-----SFretERVGAVEVVLEPFNMANGFLT 509
Cdd:cd05927 461 --------------WAASKGGGTGSFEELCKNPEVKKAILEDL-VRLGKenglkGF---EQVKAIHLEPEPFSVENGLLT 522
|
490 500
....*....|....*....|...
gi 585104306 510 QTLKVKRNVVSGHYAQEIEQMYR 532
Cdd:cd05927 523 PTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
15-532 |
2.46e-65 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 223.82 E-value: 2.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 15 AELANLPPPT--QVLTFDEALSASLARPLTFRPvPKDvRSVATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSFTDSpske 92
Cdd:PLN02736 185 EPLPSLPSGTgvEIVTYSKLLAQGRSSPQPFRP-PKP-EDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK---- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 93 paYNPvlGDVLVSVLPCWHIFERTAEYWMFSKGIHVVYSNVKNFKA--DLAKHQPQFIVAVPRLLETIYRGVLQKFAAEK 170
Cdd:PLN02736 259 --FYP--SDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLmdDLAALRPTIFCSVPRLYNRIYDGITNAVKESG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 171 GAKKKIIEfftrvgsawvKAWRVARGLVLRSRAPNPIerllalvlalvlsplaavGDKLVWSKVRAGLGGRIKVLVAGGS 250
Cdd:PLN02736 335 GLKERLFN----------AAYNAKKQALENGKNPSPM------------------WDRLVFNKIKAKLGGRVRFMSSGAS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 251 smPLVlEDFFELLRT----PVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVD-PESGARlPEGQP---GLVL 322
Cdd:PLN02736 387 --PLS-PDVMEFLRIcfggRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvPEMNYT-SEDQPyprGEIC 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 323 MRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPLTKhLIITGRAKDTIVLSNGENVEPQPIEDVVcANSALVDQVM 402
Cdd:PLN02736 463 VRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGR-LKIIDRKKNIFKLAQGEYIAPEKIENVY-AKCKFVAQCF 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 403 cvgqdekVLGMLVVPNVRALAragLVDrglaervAELLGGQVLTNGIAGSraELEEVEASLRekkeVKKALLADIaRAMG 482
Cdd:PLN02736 541 -------VYGDSLNSSLVAVV---VVD-------PEVLKAWAASEGIKYE--DLKQLCNDPR----VRAAVLADM-DAVG 596
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 585104306 483 K--SFRETERVGAVEVVLEPFNMANGFLTQTLKVKRNVVSGHYAQEIEQMYR 532
Cdd:PLN02736 597 ReaQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
45-519 |
2.10e-61 |
|
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: 210.15 E-value: 2.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 45 PVPKDVrsvATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSFTDSPSKEPAynpvlgDVLVSVLPCWHIFERTAEYWMFSK 124
Cdd:cd17639 85 GKPDDL---ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD------DRYLAYLPLAHIFELAAENVCLYR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 125 GIHVVYSNVK--------NFKADLAKHQPQFIVAVPRLLETIYRGVLQKFAAEKGAKKKIIEFftrvgSAWVKAWRVARG 196
Cdd:cd17639 156 GGTIGYGSPRtltdkskrGCKGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWT-----AYQSKLKALKEG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 197 lvlrsrapnpierllalvlalvlsPLAAVGDKLVWSKVRAGLGGRIKVLVAGGSSMPLVLEDFFELLRTPVIVGYGMTET 276
Cdd:cd17639 231 ------------------------PGTPLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTET 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 277 SPVITNRVAEKNLAGSVGRTARDTEVKIVDPESGARLPEGQP--GLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDL 354
Cdd:cd17639 287 CAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 355 GRIHPlTKHLIITGRAKDTIVLSNGENVEPQPIEDVVCANSaLVDQVmCVGQDE---KVLGmLVVPNvralaraglvdRG 431
Cdd:cd17639 367 GEFHP-DGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNP-LVNNI-CVYADPdksYPVA-IVVPN-----------EK 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 432 LAERVAELLGgqvltngiaGSRAELEEveasLREKKEVKKAL---LADIARAMG-KSFretERVGAVEVVLEPFNMANGF 507
Cdd:cd17639 432 HLTKLAEKHG---------VINSEWEE----LCEDKKLQKAVlksLAETARAAGlEKF---EIPQGVVLLDEEWTPENGL 495
|
490
....*....|..
gi 585104306 508 LTQTLKVKRNVV 519
Cdd:cd17639 496 VTAAQKLKRKEI 507
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
53-417 |
2.63e-57 |
|
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: 198.05 E-value: 2.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 53 VATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSFTDsPSKEpaynpvlGDVLVSVLPCWHIFERTAEYWM-FSKGIHVVY- 130
Cdd:cd05914 91 VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVV-LLGK-------GDKILSILPLHHIYPLTFTLLLpLLNGAHVVFl 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 131 SNVKNFKAD-LAKHQPQFIVAVPRLLETIyrgvlqkfaaekgaKKKIIEFFTRVGSAWVKaWRVARGLVLRSRApnpier 209
Cdd:cd05914 163 DKIPSAKIIaLAFAQVTPTLGVPVPLVIE--------------KIFKMDIIPKLTLKKFK-FKLAKKINNRKIR------ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 210 llalvlalvlsplaavgdKLVWSKVRAGLGGRIKVLVAGGSSMPLVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNL 289
Cdd:cd05914 222 ------------------KLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 290 AGSVGRTARDTEVKIVDPEsgarlPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGR 369
Cdd:cd05914 284 LGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDA-EGYLYIRGR 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 585104306 370 AKDTIVLSNGENVEPQPIEDVVCANSALVDQVmcVGQDEKVLGMLVVP 417
Cdd:cd05914 358 KKEMIVLSSGKNIYPEEIEAKINNMPFVLESL--VVVQEKKLVALAYI 403
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
34-377 |
6.20e-54 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 187.90 E-value: 6.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 34 SASLARPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVnynsFTDSPSKEPAYNPVLGDVLVSVLPCWHIF 113
Cdd:pfam00501 138 EAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANV----LSIKRVRPRGFGLGPDDRVLSTLPLFHDF 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 114 ERTAE-YWMFSKGIHVVYS------NVKNFKADLAKHQPQFIVAVPRLLETIyrgvlqkfaaekgakkkiiefftrvgsa 186
Cdd:pfam00501 214 GLSLGlLGPLLAGATVVLPpgfpalDPAALLELIERYKVTVLYGVPTLLNML---------------------------- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 187 wvkawrvarglvLRSRAPNPIerllalvlalvlsplaavgdklvwskvragLGGRIKVLVAGGSSMPLVLEDFF-ELLRT 265
Cdd:pfam00501 266 ------------LEAGAPKRA------------------------------LLSSLRLVLSGGAPLPPELARRFrELFGG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 266 PVIVGYGMTETSPVITNRV---AEKNLAGSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAV 342
Cdd:pfam00501 304 ALVNGYGLTETTGVVTTPLpldEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEA 383
|
330 340 350
....*....|....*....|....*....|....*
gi 585104306 343 LDQEGFLDTGDLGRIHPLTkHLIITGRAKDTIVLS 377
Cdd:pfam00501 384 FDEDGWYRTGDLGRRDEDG-YLEIVGRKKDQIKLG 417
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
27-531 |
8.92e-53 |
|
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: 188.72 E-value: 8.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 27 LTFDEALSASLARPLTFRPvpkdvRSVATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSfTDSPSKEPaynPVLGDVLVSV 106
Cdd:cd05933 131 LGRSIPDEQLDAIISSQKP-----NQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAAS-QHMDLRPA---TVGQESVVSY 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 107 LPCWHIFERTAEYWM-FSKGIHVVYSNVKNFKADLAKH----QPQFIVAVPRLLETIYRGVLQKFAAEKGAKKKIIefft 181
Cdd:cd05933 202 LPLSHIAAQILDIWLpIKVGGQVYFAQPDALKGTLVKTlrevRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIA---- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 182 rvgsawvkAWrvARGLVLrsrapnpiERLLALVLALVLSPLAA-VGDKLVWSKVRAGLG-GRIKVLVAGGSSMPLVLEDF 259
Cdd:cd05933 278 --------SW--AKGVGL--------ETNLKLMGGESPSPLFYrLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEF 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 260 FELLRTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDPESgarlpEGQpGLVLMRGPQMMAGYKSNAEAS 339
Cdd:cd05933 340 FLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDA-----DGI-GEICFWGRHVFMGYLNMEDKT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 340 KAVLDQEGFLDTGDLGRIHPLtKHLIITGRAKDTIVLSNGENVEPQPIEDVVCANSALVDQVMCVGQDEKVLGMLVVPNV 419
Cdd:cd05933 414 EEAIDEDGWLHSGDLGKLDED-GFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGDKRKFLSMLLTLKC 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 420 RALARAGLVDRGLAERVAELLGGqvltngiAGSRAELEEVEASLREKKeVKKALLADIARAMGKSFRETERVGAVEVVLE 499
Cdd:cd05933 493 EVNPETGEPLDELTEEAIEFCRK-------LGSQATRVSEIAGGKDPK-VYEAIEEGIKRVNKKAISNAQKIQKWVILEK 564
|
490 500 510
....*....|....*....|....*....|..
gi 585104306 500 PFNMANGFLTQTLKVKRNVVSGHYAQEIEQMY 531
Cdd:cd05933 565 DFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
42-532 |
5.69e-52 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 187.72 E-value: 5.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 42 TFRPVPKDVrsvATLVYTSGTTNKPKGVVLRHSNLLHQVN-----YNSFTDSPSKEpaynpvlgDVLVSVLPCWHIFERT 116
Cdd:PLN02430 214 TNPPKPLDI---CTIMYTSGTSGDPKGVVLTHEAVATFVRgvdlfMEQFEDKMTHD--------DVYLSFLPLAHILDRM 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 117 AEYWMFSKGIHVVY--SNVKNFKADLAKHQPQFIVAVPRLLETIYRGVLQKFAAEKGAKKKIIEFFTRVGSAWVKawrva 194
Cdd:PLN02430 283 IEEYFFRKGASVGYyhGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMN----- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 195 RGLVLRSrapnpierllalvlalvLSPLAavgDKLVWSKVRAGLGGRIKVLVAGGSSMPLVLEDFfelLRTP----VIVG 270
Cdd:PLN02430 358 RGYSHKK-----------------ASPMA---DFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEF---LRVTscafVVQG 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 271 YGMTET-SPVITNRVAEKNLAGSVGRTARDTEVKIVD-PESGARlPEGQP--GLVLMRGPQMMAGYKSNAEASKAVLdQE 346
Cdd:PLN02430 415 YGLTETlGPTTLGFPDEMCMLGTVGAPAVYNELRLEEvPEMGYD-PLGEPprGEICVRGKCLFSGYYKNPELTEEVM-KD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 347 GFLDTGDLGRIHPlTKHLIITGRAKDTIVLSNGENVEPQPIEDVVcANSALVDQVMCVGQDEK-VLGMLVVPNVRALara 425
Cdd:PLN02430 493 GWFHTGDIGEILP-NGVLKIIDRKKNLIKLSQGEYVALEYLENVY-GQNPIVEDIWVYGDSFKsMLVAVVVPNEENT--- 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 426 glvdrglaERVAELlggqvltNGIAGSRAELEEVEaslrekkEVKKALLADIARAMGKS-FRETERVGAVEVVLEPFNMA 504
Cdd:PLN02430 568 --------NKWAKD-------NGFTGSFEELCSLP-------ELKEHILSELKSTAEKNkLRGFEYIKGVILETKPFDVE 625
|
490 500
....*....|....*....|....*...
gi 585104306 505 NGFLTQTLKVKRNVVSGHYAQEIEQMYR 532
Cdd:PLN02430 626 RDLVTATLKKRRNNLLKYYQVEIDEMYR 653
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
22-523 |
3.55e-51 |
|
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: 182.67 E-value: 3.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 22 PPTQVLTFDEALSASLAR--PLTFRPVPKDvRSVATLVYTSGTTNKPKGVVLrhsnllhqvNYNSFTDSPS---KEPAYN 96
Cdd:cd05932 107 PPPSAANCQYQWDDLIAQhpPLEERPTRFP-EQLATLIYTSGTTGQPKGVML---------TFGSFAWAAQagiEHIGTE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 97 PvlGDVLVSVLPCWHIFERTA-EYWMFSKGIHVVYS-NVKNFKADLAKHQPQFIVAVPRLLETIYRGVLQKFAAEKgakk 174
Cdd:cd05932 177 E--NDRMLSYLPLAHVTERVFvEGGSLYGGVLVAFAeSLDTFVEDVQRARPTLFFSVPRLWTKFQQGVQDKIPQQK---- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 175 kiiefftrvgsawvkawrvargLVLRSRAPnpierllalvlalvlsplaaVGDKLVWSKVRAGLG-GRIKVLVAGGSSMP 253
Cdd:cd05932 251 ----------------------LNLLLKIP--------------------VVNSLVKRKVLKGLGlDQCRLAGCGSAPVP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 254 LVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIvdpesgarlpeGQPGLVLMRGPQMMAGYK 333
Cdd:cd05932 289 PALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI-----------SEDGEILVRSPALMMGYY 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 334 SNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVLSNGENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLGM 413
Cdd:cd05932 358 KDPEATAEAFTADGFLRTGDKGELDA-DGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDR-VEMVCVIGSGLPAPLA 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 414 LVVPNVRALARAGLVDRglaervaellggqvltngiagsraelEEVEASLRekkevkkALLADIARAMGKSfretERVGA 493
Cdd:cd05932 436 LVVLSEEARLRADAFAR--------------------------AELEASLR-------AHLARVNSTLDSH----EQLAG 478
|
490 500 510
....*....|....*....|....*....|
gi 585104306 494 VEVVLEPFNMANGFLTQTLKVKRNVVSGHY 523
Cdd:cd05932 479 IVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
53-438 |
5.17e-50 |
|
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: 178.08 E-value: 5.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 53 VATLVYTSGTTNKPKGVVLRHSNLLHqvNYNSFTDSPSKEPaynpvlGDVLVSVLPCWHIFERTAEYWM-FSKGIHVVYs 131
Cdd:COG0318 102 TALILYTSGTTGRPKGVMLTHRNLLA--NAAAIAAALGLTP------GDVVLVALPLFHVFGLTVGLLApLLAGATLVL- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 132 nVKNFKAD-----LAKHQPQFIVAVPrlleTIYRGVLQKFAAEKGAkkkiiefftrvgsawvkawrvarglvLRSrapnp 206
Cdd:COG0318 173 -LPRFDPErvlelIERERVTVLFGVP----TMLARLLRHPEFARYD--------------------------LSS----- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 207 ierllalvlalvlsplaavgdklvwskvraglggrIKVLVAGGSSMPL-VLEDFFELLRTPVIVGYGMTETSPVITNRVA 285
Cdd:COG0318 217 -----------------------------------LRLVVSGGAPLPPeLLERFEERFGVRIVEGYGLTETSPVVTVNPE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 286 EKNLA--GSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDqEGFLDTGDLGRIHPlTKH 363
Cdd:COG0318 262 DPGERrpGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDE-DGY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 364 LIITGRAKDTIVlSNGENVEPQPIEDVVCANSAlVDQVMCVGQD-----EKVLGMLVVPNVRALARAGLVDRgLAERVAE 438
Cdd:COG0318 339 LYIVGRKKDMII-SGGENVYPAEVEEVLAAHPG-VAEAAVVGVPdekwgERVVAFVVLRPGAELDAEELRAF-LRERLAR 415
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
26-405 |
4.67e-46 |
|
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: 167.74 E-value: 4.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 26 VLTFDEALSASLARPLTFRPVPKDVrsvATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSFTDSPSKEPaynpvlGDVLVS 105
Cdd:cd05936 103 AVSFTDLLAAGAPLGERVALTPEDV---AVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEG------DDVVLA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 106 VLPCWHIFERTAEY-WMFSKGIHVVYsnVKNFK-----ADLAKHQPQFIVAVPrlleTIYRGVLQKFAAEKGAKKkiief 179
Cdd:cd05936 174 ALPLFHVFGLTVALlLPLALGATIVL--IPRFRpigvlKEIRKHRVTIFPGVP----TMYIALLNAPEFKKRDFS----- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 180 ftrvgsawvkawrvarglvlrsrapnpierllalvlalvlsplaavgdklvwskvraglggRIKVLVAGGSSMPL-VLED 258
Cdd:cd05936 243 -------------------------------------------------------------SLRLCISGGAPLPVeVAER 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 259 FFELLRTPVIVGYGMTETSPVIT-NRVAEKNLAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAE 337
Cdd:cd05936 262 FEELTGVPIVEGYGLTETSPVVAvNPLDGPRKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPE 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585104306 338 ASKAVLDqEGFLDTGDLGRIHPlTKHLIITGRAKDTIvLSNGENVEPQPIEDVVCANSAlVDQVMCVG 405
Cdd:cd05936 341 ETAEAFV-DGWLRTGDIGYMDE-DGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPA-VAEAAVVG 404
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
16-437 |
1.32e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 164.97 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 16 ELANLPPPTQVLTFDEALSAslaRPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNL-LH--QVNY-NSFTDSpsk 91
Cdd:PRK06187 135 DGPAAPLAPEVGEYEELLAA---ASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLfLHslAVCAwLKLSRD--- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 92 epaynpvlgDVLVSVLPCWHIFERTAEYWMFSKGIHVVYsnVKNFKAD-----LAKHQPQFIVAVPrlleTIYRGVLqkf 166
Cdd:PRK06187 209 ---------DVYLVIVPMFHVHAWGLPYLALMAGAKQVI--PRRFDPEnlldlIETERVTFFFAVP----TIWQMLL--- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 167 aaekgakkkiiefftrvgsawvkawrvarglvlrsRAPNPIERLLalvlalvlsplaavgdklvwskvraglgGRIKVLV 246
Cdd:PRK06187 271 -----------------------------------KAPRAYFVDF----------------------------SSLRLVI 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 247 AGGSSMPLVL-EDFFELLRTPVIVGYGMTETSPVIT-NR-----VAEKNLAGSVGRTARDTEVKIVDPEsGARLP--EGQ 317
Cdd:PRK06187 288 YGGAALPPALlREFKEKFGIDLVQGYGMTETSPVVSvLPpedqlPGQWTKRRSAGRPLPGVEARIVDDD-GDELPpdGGE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 318 PGLVLMRGPQMMAGYKSNAEASKAVLDqEGFLDTGDLGRIHPLtKHLIITGRAKDTIVlSNGENVEPQPIEDVVCANSAl 397
Cdd:PRK06187 367 VGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDED-GYLYITDRIKDVII-SGGENIYPRELEDALYGHPA- 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 585104306 398 VDQVMCVGQ-----DEKVLGMLVV-PNVRALARAglVDRGLAERVA 437
Cdd:PRK06187 443 VAEVAVIGVpdekwGERPVAVVVLkPGATLDAKE--LRAFLRGRLA 486
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
45-532 |
1.45e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 167.46 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 45 PVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVNynsftdspSKEPAYNPVLG-----DVLVSVLPCWHIFERTAEY 119
Cdd:PTZ00216 258 NIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGIL--------ALEDRLNDLIGppeedETYCSYLPLAHIMEFGVTN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 120 WMFSKGIHVVYSNVKNF-------KADLAKHQPQFIVAVPRLLETIYRGVLQKFAAEKGAKKKIIEfftrvgsawvKAWR 192
Cdd:PTZ00216 330 IFLARGALIGFGSPRTLtdtfarpHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFD----------HAYQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 193 varglvlrsrapnpierllalvlalvlSPLAAVGD--------KLVWSKVRAGLGGRIKVLVAGGSSMPLVLEDFFELLR 264
Cdd:PTZ00216 400 ---------------------------SRLRALKEgkdtpywnEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVF 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 265 TPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDPESGARLPEGQP-GLVLMRGPQMMAGYKSNAEASKAVL 343
Cdd:PTZ00216 453 GMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKHTDTPEPrGEILLRGPFLFKGYYKQEELTREVL 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 344 DQEGFLDTGDLGRIHPLTKhLIITGRAKDTIVLSNGENVEPQPIEDVVCANSALVDQVMCVgqdekvlgmLVVPN---VR 420
Cdd:PTZ00216 533 DEDGWFHTGDVGSIAANGT-LRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPNGVCV---------LVHPArsyIC 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 421 ALAragLVDRGLAERVAEllggqvlTNGIAGSRAELeeveasLREKKEVKKAL--LADIARAMG-KSFretERVGAVEVV 497
Cdd:PTZ00216 603 ALV---LTDEAKAMAFAK-------EHGIEGEYPAI------LKDPEFQKKATesLQETARAAGrKSF---EIVRHVRVL 663
|
490 500 510
....*....|....*....|....*....|....*
gi 585104306 498 LEPFNMANGFLTQTLKVKRNVVSGHYAQEIEQMYR 532
Cdd:PTZ00216 664 SDEWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
53-442 |
7.87e-42 |
|
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: 152.82 E-value: 7.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 53 VATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSFTDSPSKepaynpvlGDVLVSVLPCWHIFERTAEYWMFSKGIHVV--- 129
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTE--------GDVFLSTLPLFHIGGLFGLLGALLAGGTVVllp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 130 YSNVKNFKADLAKHQPQFIVAVPRLLETIyrgvlqkfaaekgakkkiiefftrvgsawVKAWRVaRGLVLRSrapnpier 209
Cdd:cd04433 74 KFDPEAALELIEREKVTILLGVPTLLARL-----------------------------LKAPES-AGYDLSS-------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 210 llalvlalvlsplaavgdklvwskvraglggrIKVLVAGGSSMPLVLEDFFELLRTPVIV-GYGMTETSPVIT--NRVAE 286
Cdd:cd04433 116 --------------------------------LRALVSGGAPLPPELLERFEEAPGIKLVnGYGLTETGGTVAtgPPDDD 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 287 KNLAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVlDQEGFLDTGDLGRIHPlTKHLII 366
Cdd:cd04433 164 ARKPGSVGRPVPGVEVRIVDPD-GGELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDE-DGYLYI 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585104306 367 TGRAKDTIVlSNGENVEPQPIEDVVcANSALVDQVMCVGQDEKVLGMLVVPNVRALARAGLVDRGLAERVAELLGG 442
Cdd:cd04433 241 VGRLKDMIK-SGGENVYPAEVEAVL-LGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
45-531 |
8.60e-40 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 153.73 E-value: 8.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 45 PVPKDVrsvATLVYTSGTTNKPKGVVLRHSNLLHQVNyNSFTDSPSKEPaynpvlGDVLVSVLPCWHIFERTAEYWMFSK 124
Cdd:PLN02387 247 PSPNDI---AVIMYTSGSTGLPKGVMMTHGNIVATVA-GVMTVVPKLGK------NDVYLAYLPLAHILELAAESVMAAV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 125 GIHVVY---------SN--VKNFKADLAKHQPQFIVAVPRLLETIYRGVLQKFAAEKGAKKKIIEF-FTRVGSAWVKAWR 192
Cdd:PLN02387 317 GAAIGYgspltltdtSNkiKKGTKGDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIaYKRRLAAIEGSWF 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 193 VARGLvlrsrapnpiERLlalvlalvlsplaaVGDKLVWSKVRAGLGGRIKVLVAGGSSMPLVLEDFFEL-LRTPVIVGY 271
Cdd:PLN02387 397 GAWGL----------EKL--------------LWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINIcLGAPIGQGY 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 272 GMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDPESGARLPEGQP---GLVLMRGPQMMAGYKSNAEASKAV--LDQE 346
Cdd:PLN02387 453 GLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKPmprGEIVIGGPSVTLGYFKNQEKTDEVykVDER 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 347 G--FLDTGDLGRIHPlTKHLIITGRAKDTIVLSNGENVEPQPIEDVVCAnSALVDQVM---------CVGqdekvlgmLV 415
Cdd:PLN02387 533 GmrWFYTGDIGQFHP-DGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSV-SPYVDNIMvhadpfhsyCVA--------LV 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 416 VPNVRALaraglvdRGLAERVaellggqvltnGIAGSRAeleeveASLREKKEVKKALLADIARAmGKSFR--ETERVGA 493
Cdd:PLN02387 603 VPSQQAL-------EKWAKKA-----------GIDYSNF------AELCEKEEAVKEVQQSLSKA-AKAARleKFEIPAK 657
|
490 500 510
....*....|....*....|....*....|....*...
gi 585104306 494 VEVVLEPFNMANGFLTQTLKVKRNVVSGHYAQEIEQMY 531
Cdd:PLN02387 658 IKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
47-532 |
2.11e-37 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 146.53 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 47 PKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVnynSFTDSPSKEPAYNPVLGDVLVSVLPCWHIFERTAEYWMFSKGI 126
Cdd:PLN02861 216 PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEV---LSTDHLLKVTDRVATEEDSYFSYLPLAHVYDQVIETYCISKGA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 127 HVVY--SNVKNFKADLAKHQPQFIVAVPRLLETIYRGVLQKFAAEKGAKKKIIEFftrvgSAWVKAWRVARGLVLRSRAP 204
Cdd:PLN02861 293 SIGFwqGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDF-----AYNYKLGNLRKGLKQEEASP 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 205 npierllalvlalvlsplaaVGDKLVWSKVRAGLGGRIKVLVAGGSSMPLVLEDFFELLRTPVIV-GYGMTET-SPVITN 282
Cdd:PLN02861 368 --------------------RLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSqGYGLTEScGGCFTS 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 283 RVAEKNLAGSVGRTARDTEVKIVD-PESG----ARLPEGQpglVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRI 357
Cdd:PLN02861 428 IANVFSMVGTVGVPMTTIEARLESvPEMGydalSDVPRGE---ICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEW 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 358 HPLTKHLIITgRAKDTIVLSNGENVEPQPIEDVVcANSALVDQVMCVGQD-EKVLGMLVVPNVRALaraglvdrglaERV 436
Cdd:PLN02861 504 QPNGAMKIID-RKKNIFKLSQGEYVAVENLENTY-SRCPLIASIWVYGNSfESFLVAVVVPDRQAL-----------EDW 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 437 AEllggqvlTNGIAGSRAELEEveaSLREKKEVKKALladiaRAMGKSF--RETERVGAVEVVLEPFNMANGFLTQTLKV 514
Cdd:PLN02861 571 AA-------NNNKTGDFKSLCK---NLKARKYILDEL-----NSTGKKLqlRGFEMLKAIHLEPNPFDIERDLITPTFKL 635
|
490
....*....|....*...
gi 585104306 515 KRNVVSGHYAQEIEQMYR 532
Cdd:PLN02861 636 KRPQLLKYYKDCIDQLYS 653
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
17-399 |
2.38e-36 |
|
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: 141.20 E-value: 2.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 17 LANLPPPTQVLTFDEALSASLAR----------PLTFRPVPKDVRS--VATLVYTSGTTNKPKGVVLRHSNL---LHQVN 81
Cdd:cd05911 100 AKELGPKDKIIVLDDKPDGVLSIedllsptlgeEDEDLPPPLKDGKddTAAILYSSGTTGLPKGVCLSHRNLianLSQVQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 82 YNSFTDSPSKepaynpvlgDVLVSVLPCWHIFERTAEYWMFSKGIHVVYSN---VKNFKADLAKHQPQFIVAVPRLLETI 158
Cdd:cd05911 180 TFLYGNDGSN---------DVILGFLPLYHIYGLFTTLASLLNGATVIIMPkfdSELFLDLIEKYKITFLYLVPPIAAAL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 159 yrgvlqkfaaekgAKKKIIEFFTrvgsawvkawrvarglvLRSrapnpierllalvlalvlsplaavgdklvwskvragl 238
Cdd:cd05911 251 -------------AKSPLLDKYD-----------------LSS------------------------------------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 239 ggrIKVLVAGGSSMPLVLEDFFE--LLRTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDPESGARLPEG 316
Cdd:cd05911 264 ---LRVILSGGAPLSKELQELLAkrFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 317 QPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVLsNGENVEPQPIEDVVCANSA 396
Cdd:cd05911 341 EPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDE-DGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPG 418
|
...
gi 585104306 397 LVD 399
Cdd:cd05911 419 VAD 421
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
52-523 |
9.19e-36 |
|
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: 140.64 E-value: 9.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 52 SVATLVYTSGTTNKPKGVVLRHSNLL-HQVNYNSFTdspSKEPaynpvlGDVLVSVLPCWHIFERtaeywMFSKGIHVVY 130
Cdd:cd17641 159 DVAVLCTTSGTTGKPKLAMLSHGNFLgHCAAYLAAD---PLGP------GDEYVSVLPLPWIGEQ-----MYSVGQALVC 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 131 SNVKNF-------KADLAKHQPQFIVAVPRLLETIYRGVLQKFAaekgakkkiiefftrvGSAWVKAWRVARGLVLRSRA 203
Cdd:cd17641 225 GFIVNFpeepetmMEDLREIGPTFVLLPPRVWEGIAADVRARMM----------------DATPFKRFMFELGMKLGLRA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 204 PNPIERLLALVLALVLSplAAVGDKLVWSKVRAGLG-GRIKVLVAGGSSM-PLVLeDFFELLRTPVIVGYGMTETSPVIT 281
Cdd:cd17641 289 LDRGKRGRPVSLWLRLA--SWLADALLFRPLRDRLGfSRLRSAATGGAALgPDTF-RFFHAIGVPLKQLYGQTELAGAYT 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 282 NRVAEKNLAGSVGRTARDTEVKIVDpesgarlpegqPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlT 361
Cdd:cd17641 366 VHRDGDVDPDTVGVPFPGTEVRIDE-----------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKE-N 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 362 KHLIITGRAKDTIVLSNGENVEPQPIEDVVcANSALVDQVMCVGQDEKVLGMLV---VPNV------RALARAGLVDRGL 432
Cdd:cd17641 434 GHLVVIDRAKDVGTTSDGTRFSPQFIENKL-KFSPYIAEAVVLGAGRPYLTAFIcidYAIVgkwaeqRGIAFTTYTDLAS 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 433 AERVAELLggqvltngiagsRAELEEVEASLREKKEVKKALLAdiaramgksFREtervgavevvLEPfnmANGFLTQTL 512
Cdd:cd17641 513 RPEVYELI------------RKEVEKVNASLPEAQRIRRFLLL---------YKE----------LDA---DDGELTRTR 558
|
490
....*....|.
gi 585104306 513 KVKRNVVSGHY 523
Cdd:cd17641 559 KVRRGVIAEKY 569
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
26-399 |
1.18e-35 |
|
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: 139.29 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 26 VLTFDEALSASLA-------RPLTFRPVPKDVRS-VATLVYTSGTTNKPKGVVLRHSNLLHQVN-YNSFTDSpskepayN 96
Cdd:cd05904 125 VVLLDSAEFDSLSfsdllfeADEAEPPVVVIKQDdVAALLYSSGTTGRSKGVMLTHRNLIAMVAqFVAGEGS-------N 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 97 PVLGDVLVSVLPCWHIFertaeywmfskGIHVvysnvknfkadlakhqpqFIVAVPRLLETIYrgVLQKFAAEkgakkki 176
Cdd:cd05904 198 SDSEDVFLCVLPMFHIY-----------GLSS------------------FALGLLRLGATVV--VMPRFDLE------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 177 iEFFtrvgsAWVKAWRVARGLVlrsrAPnPIerllalvlalvlsPLA----AVGDKLVWSKVRAglggrikvLVAGGSsm 252
Cdd:cd05904 240 -ELL-----AAIERYKVTHLPV----VP-PI-------------VLAlvksPIVDKYDLSSLRQ--------IMSGAA-- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 253 PL---VLEDFFELLRTPVIV-GYGMTETSPVIT---NRVAEKNLAGSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRG 325
Cdd:cd05904 286 PLgkeLIEAFRAKFPNVDLGqGYGMTESTGVVAmcfAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRG 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585104306 326 PQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHpLTKHLIITGRAKDTIVLsNGENVEPQPIEDVVCANSALVD 399
Cdd:cd05904 366 PSIMKGYLNNPEATAATIDKEGWLHTGDLCYID-EDGYLFIVDRLKELIKY-KGFQVAPAELEALLLSHPEILD 437
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
48-532 |
1.02e-34 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 138.61 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 48 KDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVN-----YNSFTDSPSKEpaynpvlgDVLVSVLPCWHIFERTAEYWMF 122
Cdd:PLN02614 220 KKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAgvirlLKSANAALTVK--------DVYLSYLPLAHIFDRVIEECFI 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 123 SKGIHVVY--SNVKNFKADLAKHQPQFIVAVPRLLETIYRGVLQKFAAEKGAKKKIIEfftrvgsawvKAWRVARGLVLR 200
Cdd:PLN02614 292 QHGAAIGFwrGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFD----------SAFSYKFGNMKK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 201 SRApnpierllalvlALVLSPLAavgDKLVWSKVRAGLGGRIKVLVAGGSSMPLVLEDFFELLR-TPVIVGYGMTET-SP 278
Cdd:PLN02614 362 GQS------------HVEASPLC---DKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVAcCHVLQGYGLTEScAG 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 279 VITNRVAEKNLAGSVGRTARDTEVKI-----VDPESGARLPEGQpglVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGD 353
Cdd:PLN02614 427 TFVSLPDELDMLGTVGPPVPNVDIRLesvpeMEYDALASTPRGE---ICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 354 LGRIHPlTKHLIITGRAKDTIVLSNGENVEPQPIEDVVcANSALVDQVMCVGQD-EKVLGMLVVPNVRALARaglvdrgl 432
Cdd:PLN02614 503 VGEWQP-NGSMKIIDRKKNIFKLSQGEYVAVENIENIY-GEVQAVDSVWVYGNSfESFLVAIANPNQQILER-------- 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 433 aervaellggQVLTNGIAGSRaeleeveASLREKKEVKKALLADIAR-AMGKSFRETERVGAVEVVLEPFNMANGFLTQT 511
Cdd:PLN02614 573 ----------WAAENGVSGDY-------NALCQNEKAKEFILGELVKmAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPT 635
|
490 500
....*....|....*....|.
gi 585104306 512 LKVKRNVVSGHYAQEIEQMYR 532
Cdd:PLN02614 636 FKKKRPQLLKYYQSVIDEMYK 656
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
18-412 |
1.85e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 136.19 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 18 ANLPPPTQVLTFDEALsASLARPLTFRPVPKDvrSVATLVYTSGTTNKPKGVVLRHSNLLHqvNYNSFTDSPSKEPaynp 97
Cdd:PRK07656 136 EDDPHTEKMKTFTDFL-AAGDPAERAPEVDPD--DVADILFTSGTTGRPKGAMLTHRQLLS--NAADWAEYLGLTE---- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 98 vlGDVLVSVLPCWHIFERTAEyWM--FSKG----IHVVYSNVKNFKAdLAKHQPQFIVAVPrlleTIYRGVLQkfaAEKG 171
Cdd:PRK07656 207 --GDRYLAANPFFHVFGYKAG-VNapLMRGatilPLPVFDPDEVFRL-IETERITVLPGPP----TMYNSLLQ---HPDR 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 172 AKKKIiefftrvgsawvkawrvarglvlrsrapnpierllalvlalvlsplaavgdklvwSKVRAGlggrikvlVAGGSS 251
Cdd:PRK07656 276 SAEDL-------------------------------------------------------SSLRLA--------VTGAAS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 252 MPLVL-EDFFELLRTP-VIVGYGMTETSPVIT-NRVAE--KNLAGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGP 326
Cdd:PRK07656 293 MPVALlERFESELGVDiVLTGYGLSEASGVTTfNRLDDdrKTVAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 327 QMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIvLSNGENVEPQPIEDVVCANSAlVDQVMCVGQ 406
Cdd:PRK07656 372 NVMKGYYDDPEATAAAIDADGWLHTGDLGRLDE-EGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPA-VAEAAVIGV 448
|
....*.
gi 585104306 407 DEKVLG 412
Cdd:PRK07656 449 PDERLG 454
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
50-409 |
2.13e-33 |
|
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: 131.96 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 50 VRSVATLVYTSGTTNKPKGVVLRHSNLLHQVnYNSFTDSPSKEpaynpvlGDVLVSVLPCWHIFErtAEYWMFS---KGI 126
Cdd:cd17631 97 FDDLALLMYTSGTTGRPKGAMLTHRNLLWNA-VNALAALDLGP-------DDVLLVVAPLFHIGG--LGVFTLPtllRGG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 127 HVVYsnVKNFKAD-----LAKHQPQFIVAVPrlleTIYRGVLQkfaaekgakkkiiefftrvgsawvkawrvarglvlrs 201
Cdd:cd17631 167 TVVI--LRKFDPEtvldlIERHRVTSFFLVP----TMIQALLQ------------------------------------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 202 rapnpierllalvlalvlSPLAAVGDklvWSKVRAGLGGrikvlvagGSSMPLVLEDFFELLRTPVIVGYGMTETSPVIT 281
Cdd:cd17631 204 ------------------HPRFATTD---LSSLRAVIYG--------GAPMPERLLRALQARGVKFVQGYGMTETSPGVT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 282 NRVAEKNLA--GSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHP 359
Cdd:cd17631 255 FLSPEDHRRklGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDE 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 585104306 360 lTKHLIITGRAKDTIVlSNGENVEPQPIEDVVCANSAlVDQVMCVG-QDEK 409
Cdd:cd17631 333 -DGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPA-VAEVAVIGvPDEK 380
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
29-391 |
8.12e-32 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 128.98 E-value: 8.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 29 FDEALSAslARPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSFTdspsKEPAY-NPVLGDVLVSV- 106
Cdd:PRK07059 184 FNDALAE--GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAW----LQPAFeKKPRPDQLNFVc 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 107 -LPCWHIFERTAEYW--MFSKGIHVVYSN---VKNFKADLAKHQPQFIVAVprllETIYRGVLQKfaaekgakkkiIEFf 180
Cdd:PRK07059 258 aLPLYHIFALTVCGLlgMRTGGRNILIPNprdIPGFIKELKKYQVHIFPAV----NTLYNALLNN-----------PDF- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 181 trvgsawvkawrvarglvlrsrapnpierllalvlalvlsplaavgDKLVWSKVRAGLGGRIKVLVAggssmplVLEDFF 260
Cdd:PRK07059 322 ----------------------------------------------DKLDFSKLIVANGGGMAVQRP-------VAERWL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 261 ELLRTPVIVGYGMTETSPVIT-NRVAEKNLAGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAEAS 339
Cdd:PRK07059 349 EMTGCPITEGYGLSETSPVATcNPVDATEFSGTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDET 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 585104306 340 KAVLDQEGFLDTGDLGRIHP--LTKhliITGRAKDTIVLSnGENVEPQPIEDVV 391
Cdd:PRK07059 428 AKVMTADGFFRTGDVGVMDErgYTK---IVDRKKDMILVS-GFNVYPNEIEEVV 477
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
21-392 |
1.07e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 125.88 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 21 PPPTQVLTFDEALSASLARPLTFRPVPK-DVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVnynsftdspSKEPAYNPVL 99
Cdd:PRK05605 188 GPAPGTVPWETLVDAAIGGDGSDVSHPRpTPDDVALILYTSGTTGKPKGAQLTHRNLFANA---------AQGKAWVPGL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 100 GD---VLVSVLPCWHIFERT--AEYWMFSKGIHVVYSNvknFKADLA-----KHQPQFIVAVPrlleTIYRGVLQkfAAE 169
Cdd:PRK05605 259 GDgpeRVLAALPMFHAYGLTlcLTLAVSIGGELVLLPA---PDIDLIldamkKHPPTWLPGVP----PLYEKIAE--AAE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 170 KgakkkiiefftrvgsawvkawrvaRGLVLRSrapnpierllalvlalvlsplaavgdklvwskvraglggrIKVLVAGG 249
Cdd:PRK05605 330 E------------------------RGVDLSG----------------------------------------VRNAFSGA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 250 SSMPLVLEDFFELLRTPVIV-GYGMTETSPVIT-NRVAEKNLAGSVGRTARDTEVKIVDPESGAR-LPEGQPGLVLMRGP 326
Cdd:PRK05605 346 MALPVSTVELWEKLTGGLLVeGYGLTETSPIIVgNPMSDDRRPGYVGVPFPDTEVRIVDPEDPDEtMPDGEEGELLVRGP 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585104306 327 QMMAGYKSNAEASKAVLdQEGFLDTGDLG--------RIHPLTKHLIITGrakdtivlsnGENVEPQPIEDVVC 392
Cdd:PRK05605 426 QVFKGYWNRPEETAKSF-LDGWFRTGDVVvmeedgfiRIVDRIKELIITG----------GFNVYPAEVEEVLR 488
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
54-483 |
1.32e-29 |
|
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: 121.24 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 54 ATLVYTSGTTNKPKGVVLRHSNLLHQVN----YNSFTDSpskepaynpvlgDVLVSVLPCWHIfertaeywmfsKGIHVV 129
Cdd:cd05941 92 ALILYTSGTTGRPKGVVLTHANLAANVRalvdAWRWTED------------DVLLHVLPLHHV-----------HGLVNA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 130 ysnvknfkadlakhqpqfivavprLLETIYRG----VLQKFAAEKGAK---KKIIEFFTRVGSAWVKawrvarglVLRSR 202
Cdd:cd05941 149 ------------------------LLCPLFAGasveFLPKFDPKEVAIsrlMPSITVFMGVPTIYTR--------LLQYY 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 203 APNPIERLlalvlalvlsplaavgdklvwsKVRAGLGGRIKVLVAGGSSMPL-VLEDFFELLRTPVIVGYGMTETSPVIT 281
Cdd:cd05941 197 EAHFTDPQ----------------------FARAAAAERLRLMVSGSAALPVpTLEEWEAITGHTLLERYGMTEIGMALS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 282 NRVAEKNLAGSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlT 361
Cdd:cd05941 255 NPLDGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDE-D 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 362 KHLIITGRAKDTIVLSNGENVEPQPIEDVvcansalvdqvmcvgqdekvlgMLVVPNVRALARAGLVDRGLAERVAELLg 441
Cdd:cd05941 334 GYYWILGRSSVDIIKSGGYKVSALEIERV----------------------LLAHPGVSECAVIGVPDPDWGERVVAVV- 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 585104306 442 gqVLTNGIAGsrAELEEVEASLREK----KEVKKALLAD-IAR-AMGK 483
Cdd:cd05941 391 --VLRAGAAA--LSLEELKEWAKQRlapyKRPRRLILVDeLPRnAMGK 434
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
15-429 |
4.18e-29 |
|
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: 120.49 E-value: 4.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 15 AELANLPPPTQVLTFDEALSASLARPLTFRPVPKDVRS-VATLVYTSGTTNKPKGVVLRHSNLLHQVNY--NSFTDSPSk 91
Cdd:cd05926 112 LELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDdLALILHTSGTTGRPKGVPLTHRNLAASATNitNTYKLTPD- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 92 epaynpvlgDVLVSVLPCWHIFERTAEYW--MFSKGIHVV---YSNVKnFKADLAKHQPQFIVAVPrlleTIYRgVLQKF 166
Cdd:cd05926 191 ---------DRTLVVMPLFHVHGLVASLLstLAAGGSVVLpprFSAST-FWPDVRDYNATWYTAVP----TIHQ-ILLNR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 167 AAEKGAKKKIIEFFTRVGSawvkawrvarglvlrsrapnpierllalvlalvlSPLAavgdklvwskvraglggrikvlv 246
Cdd:cd05926 256 PEPNPESPPPKLRFIRSCS----------------------------------ASLP----------------------- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 247 aggssmPLVLEDFFELLRTPVIVGYGMTETSPVIT-NRV-AEKNLAGSVGRtARDTEVKIVDpESGARLPEGQPGLVLMR 324
Cdd:cd05926 279 ------PAVLEALEATFGAPVLEAYGMTEAAHQMTsNPLpPGPRKPGSVGK-PVGVEVRILD-EDGEILPPGVVGEICLR 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 325 GPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIvlsN--GENVEPQPIEDVVCANSAlVDQVM 402
Cdd:cd05926 351 GPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDA-DGYLFLTGRIKELI---NrgGEKISPLEVDGVLLSHPA-VLEAV 425
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 585104306 403 CVG-QDEK---VLGMLVVPN---------VRALARAGLVD 429
Cdd:cd05926 426 AFGvPDEKygeEVAAAVVLRegasvteeeLRAFCRKHLAA 465
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
240-409 |
9.02e-29 |
|
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: 116.99 E-value: 9.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 240 GRIKVLVAGGSSMPL-VLEDFFELLR-TPVIVGYGMTETSPVITNRVAEKNL---AGSVGRTARDTEVKIVDPESGARLP 314
Cdd:cd05917 118 SSLRTGIMAGAPCPPeLMKRVIEVMNmKDVTIAYGMTETSPVSTQTRTDDSIekrVNTVGRIMPHTEAKIVDPEGGIVPP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 315 EGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVVCAN 394
Cdd:cd05917 198 VGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDE-DGYCRIVGRIKDMII-RGGENIYPREIEEFLHTH 275
|
170
....*....|....*.
gi 585104306 395 SALVD-QVMCVgQDEK 409
Cdd:cd05917 276 PKVSDvQVVGV-PDER 290
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
25-417 |
3.59e-27 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 115.30 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 25 QVLTFDEALSasLARPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNL---LHQVNYNSFTDSPSKEPAYNPVlGD 101
Cdd:PRK12492 183 QAVPFKQALR--QGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLvanMLQVRACLSQLGPDGQPLMKEG-QE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 102 VLVSVLPCWHIFERTAE-YWMFSKGIHVVysnvknfkadlakhqpqfIVAVPRlletiyrgvlqkfaaekgakkKIIEFF 180
Cdd:PRK12492 260 VMIAPLPLYHIYAFTANcMCMMVSGNHNV------------------LITNPR---------------------DIPGFI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 181 TRVGSawvkaWRVARGLVLRSRapnpierllalvlalvlspLAAVGDKLVWSKVRAGlggRIKVLVAGGSSM-PLVLEDF 259
Cdd:PRK12492 301 KELGK-----WRFSALLGLNTL-------------------FVALMDHPGFKDLDFS---ALKLTNSGGTALvKATAERW 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 260 FELLRTPVIVGYGMTETSPVI-TNRVAEKNLAGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAEA 338
Cdd:PRK12492 354 EQLTGCTIVEGYGLTETSPVAsTNPYGELARLGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 339 SKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVLSnGENVEPQPIEDVVCANSAlVDQVMCVG-QDEK---VLGML 414
Cdd:PRK12492 433 TAEALDAEGWFKTGDIAVIDP-DGFVRIVDRKKDLIIVS-GFNVYPNEIEDVVMAHPK-VANCAAIGvPDERsgeAVKLF 509
|
...
gi 585104306 415 VVP 417
Cdd:PRK12492 510 VVA 512
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
46-371 |
4.05e-27 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 114.35 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 46 VPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVnYNSFTdspskepAYNPVLGDVLVSVLPCWHIFERTAEYWM-FSK 124
Cdd:cd05909 142 APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANV-EQITA-------IFDPNPEDVVFGALPFFHSFGLTGCLWLpLLS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 125 GIHVV-YSNVKNFK--ADLA-KHQPQFIVAVPrlleTIYRGVLQKFAAEkgakkkiiEFFTrvgsawvkawrvarglvlr 200
Cdd:cd05909 214 GIKVVfHPNPLDYKkiPELIyDKKATILLGTP----TFLRGYARAAHPE--------DFSS------------------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 201 srapnpierllalvlalvlsplaavgdklvwskvraglggrIKVLVAGGSSMPLVLEDFF-ELLRTPVIVGYGMTETSPV 279
Cdd:cd05909 263 -----------------------------------------LRLVVAGAEKLKDTLRQEFqEKFGIRILEGYGTTECSPV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 280 IT-NRVAEKNLAGSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYkSNAEASKAVLDQEGFLDTGDLGRIH 358
Cdd:cd05909 302 ISvNTPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGY-LNEPELTSFAFGDGWYDTGDIGKID 380
|
330
....*....|...
gi 585104306 359 PlTKHLIITGRAK 371
Cdd:cd05909 381 G-EGFLTITGRLS 392
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
19-409 |
9.29e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 114.09 E-value: 9.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 19 NLPpptQVLTFDEALSASLARPltFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVnynsftdsPSKEPAYNPV 98
Cdd:PRK05677 180 HLP---QAVKFNDALAKGAGQP--VTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANM--------LQCRALMGSN 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 99 LGD---VLVSVLPCWHIFERTAE-YWMFSKGIH-VVYSNVKNFKA---DLAKHQPQFIVAvprlLETIYRGVLQKfaaek 170
Cdd:PRK05677 247 LNEgceILIAPLPLYHIYAFTFHcMAMMLIGNHnILISNPRDLPAmvkELGKWKFSGFVG----LNTLFVALCNN----- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 171 gakkkiiEFFTrvgsawvkawrvarglvlrsrapnpierllalvlalvlsplaavgdKLVWSkvraglggRIKVLVAGGS 250
Cdd:PRK05677 318 -------EAFR----------------------------------------------KLDFS--------ALKLTLSGGM 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 251 SMPL-VLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMM 329
Cdd:PRK05677 337 ALQLaTAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVM 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 330 AGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVLSnGENVEPQPIEDVVCANSALVdQVMCVG-QDE 408
Cdd:PRK05677 416 KGYWQRPEATDEILDSDGWLKTGDIALIQE-DGYMRIVDRKKDMILVS-GFNVYPNELEDVLAALPGVL-QCAAIGvPDE 492
|
.
gi 585104306 409 K 409
Cdd:PRK05677 493 K 493
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
53-415 |
2.39e-26 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 112.84 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 53 VATLVYTSGTTNKPKGVVLRHSNL---LHQVNYnsftdspskepAYNPVLGD---VLVSVLPCWHIFERTAEYWMF-SKG 125
Cdd:PRK08974 208 LAFLQYTGGTTGVAKGAMLTHRNMlanLEQAKA-----------AYGPLLHPgkeLVVTALPLYHIFALTVNCLLFiELG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 126 IH-VVYSN---VKNFKADLAKHQPQFIVAVprllETIYRGVLQKfaaekgakkkiiEFFTrvgsawvkawrvarglvlrs 201
Cdd:PRK08974 277 GQnLLITNprdIPGFVKELKKYPFTAITGV----NTLFNALLNN------------EEFQ-------------------- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 202 rapnpierllalvlalvlsplaavgdKLVWSKVRAGLGGRIKVLVAggssmplVLEDFFELLRTPVIVGYGMTETSPVIT 281
Cdd:PRK08974 321 --------------------------ELDFSSLKLSVGGGMAVQQA-------VAERWVKLTGQYLLEGYGLTECSPLVS 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 282 -NRVAEKNLAGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPl 360
Cdd:PRK08974 368 vNPYDLDYYSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDE- 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 585104306 361 TKHLIITGRAKDTIVLSnGENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLGMLV 415
Cdd:PRK08974 445 EGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMLHPK-VLEVAAVGVPSEVSGEAV 497
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
267-388 |
8.38e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 111.06 E-value: 8.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 267 VIVGYGMTETSPVIT---------NRVAeknlagSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAE 337
Cdd:PRK08315 344 VTIAYGMTETSPVSTqtrtddpleKRVT------TVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPE 417
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 585104306 338 ASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIE 388
Cdd:PRK08315 418 KTAEAIDADGWMHTGDLAVMDE-EGYVNIVGRIKDMII-RGGENIYPREIE 466
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-399 |
1.19e-25 |
|
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: 109.30 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 50 VRSVATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSftdspskepAYNPVL-GDVLVSVLPCWHI-FERTAEYWMFSKGIH 127
Cdd:cd05934 80 VVDPASILYTSGTTGPPKGVVITHANLTFAGYYSA---------RRFGLGeDDVYLTVLPLFHInAQAVSVLAALSVGAT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 128 VV----YSnVKNFKADLAKHQPQFIVAVPRLLETIYrgvlqkfaaekgakkkiiefftrvgsawvkawrvarglvlrSRA 203
Cdd:cd05934 151 LVllprFS-ASRFWSDVRRYGATVTNYLGAMLSYLL-----------------------------------------AQP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 204 PNPIERLlalvlalvlsplaavgdklvwSKVRAglggrikvlVAGGSSMPLVLEDFFELLRTPVIVGYGMTETSPVITNR 283
Cdd:cd05934 189 PSPDDRA---------------------HRLRA---------AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 284 VAEKNLAGSVGRTARDTEVKIVDPEsGARLPEGQPG-LVL--MRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPl 360
Cdd:cd05934 239 RDEPRRPGSIGRPAPGYEVRIVDDD-GQELPAGEPGeLVIrgLRGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDA- 315
|
330 340 350
....*....|....*....|....*....|....*....
gi 585104306 361 TKHLIITGRAKDTIVLSnGENVEPQPIEDVVCANSALVD 399
Cdd:cd05934 316 DGFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVRE 353
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
15-391 |
7.28e-25 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 107.65 E-value: 7.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 15 AELANLPPPTQVLTFDEALSASLA-----RPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQ----VNYNSF 85
Cdd:PRK07514 115 SKIAAAAGAPHVETLDADGTGSLLeaaaaAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNaltlVDYWRF 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 86 TDspskepaynpvlGDVLVSVLPcwhIFertaeywmfskgiHV----VYSNVKNFKAD----LAKHQP-QFIVAVPRllE 156
Cdd:PRK07514 195 TP------------DDVLIHALP---IF-------------HThglfVATNVALLAGAsmifLPKFDPdAVLALMPR--A 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 157 TIYRGVLQkfaaekgakkkiieFFTRVgsawvkawrvarglvLRSRAPNPierllalvlalvlsplAAVGdklvwskvra 236
Cdd:PRK07514 245 TVMMGVPT--------------FYTRL---------------LQEPRLTR----------------EAAA---------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 237 glggRIKVLVAGgsSMPLVLEDFFELL-RT--PVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDPESGARL 313
Cdd:PRK07514 270 ----HMRLFISG--SAPLLAETHREFQeRTghAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDPETGAEL 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585104306 314 PEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVV 391
Cdd:PRK07514 344 PPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDE-RGYVHIVGRGKDLII-SGGYNVYPKEVEGEI 419
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
22-416 |
7.42e-25 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 108.14 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 22 PPTQVLTFDEALSASLARPLTFRPVPKDVrsvATLVYTSGTTNKPKGVVLRHSNLL----HQVNynsftdspskepAYNP 97
Cdd:PLN02246 153 PPEGCLHFSELTQADENELPEVEISPDDV---VALPYSSGTTGLPKGVMLTHKGLVtsvaQQVD------------GENP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 98 VL----GDVLVSVLPCWHIfertaeywmfskgihvvYSNVKNFKADLakhqpqfivavpRLLETIYrgVLQKFaaEKGAk 173
Cdd:PLN02246 218 NLyfhsDDVILCVLPMFHI-----------------YSLNSVLLCGL------------RVGAAIL--IMPKF--EIGA- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 174 kkIIEFFTRVGsawVKAWRVARGLVLrSRAPNPIErllalvlalvlsplaavgDKLVWSKVRaglggrikVLVAGGSSMP 253
Cdd:PLN02246 264 --LLELIQRHK---VTIAPFVPPIVL-AIAKSPVV------------------EKYDLSSIR--------MVLSGAAPLG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 254 LVLEDFFELlRTPVIV---GYGMTETSPVITnrvaeKNLA----------GSVGRTARDTEVKIVDPESGARLPEGQPGL 320
Cdd:PLN02246 312 KELEDAFRA-KLPNAVlgqGYGMTEAGPVLA-----MCLAfakepfpvksGSCGTVVRNAELKIVDPETGASLPRNQPGE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 321 VLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVLsNGENVEPQPIEDVVCANSALVDq 400
Cdd:PLN02246 386 ICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDD-DDELFIVDRLKELIKY-KGFQVAPAELEALLISHPSIAD- 462
|
410
....*....|....*.
gi 585104306 401 VMCVGQDEKVLGMLVV 416
Cdd:PLN02246 463 AAVVPMKDEVAGEVPV 478
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
33-357 |
1.24e-24 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 108.47 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 33 LSASLARPLTFRPVPKDvrSVATLVYTSGTTNKPKGVVLRHSNLLhqVNYNSFTDspskepAYNPVLGDVLVSVLPCWHI 112
Cdd:PRK08633 766 LPARLLKRLYGPTFKPD--DTATIIFSSGSEGEPKGVMLSHHNIL--SNIEQISD------VFNLRNDDVILSSLPFFHS 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 113 FERTAEYWM-FSKGIHVVY----SNVKNFKADLAKHQPQFIVAVPrlletiyrgvlqkfaaekgakkkiiEFFtrvgSAW 187
Cdd:PRK08633 836 FGLTVTLWLpLLEGIKVVYhpdpTDALGIAKLVAKHRATILLGTP-------------------------TFL----RLY 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 188 VKAWRVarglvlrsrapnpierllalvlalvlsplaavgDKLVWSKVRaglggrikVLVAGGSSMPLVLEDFFEL-LRTP 266
Cdd:PRK08633 887 LRNKKL---------------------------------HPLMFASLR--------LVVAGAEKLKPEVADAFEEkFGIR 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 267 VIVGYGMTETSPVIT----NRVAEKNL------AGSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNA 336
Cdd:PRK08633 926 ILEGYGATETSPVASvnlpDVLAADFKrqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDP 1005
|
330 340
....*....|....*....|....
gi 585104306 337 EASKAVL---DQEGFLDTGDLGRI 357
Cdd:PRK08633 1006 EKTAEVIkdiDGIGWYVTGDKGHL 1029
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
53-405 |
3.35e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 106.27 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 53 VATLVYTSGTTNKPKGVVLRHSNLLHqvnyNSFTdspSKEPAYNPVLGD-VLVSVLPCWHIFERTAeywmfskgihvvys 131
Cdd:PRK06710 208 LALLQYTGGTTGFPKGVMLTHKNLVS----NTLM---GVQWLYNCKEGEeVVLGVLPFFHVYGMTA-------------- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 132 nVKNfkadLAKHQPQFIVAVPRL-LETIYRGVlqkfaaekgaKKKIIEFFTRVGSAWVkawrvarglvlrsrapnpierl 210
Cdd:PRK06710 267 -VMN----LSIMQGYKMVLIPKFdMKMVFEAI----------KKHKVTLFPGAPTIYI---------------------- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 211 lalvlALVLSPLAAVGDklvWSKVRAglggrikvLVAGGSSMPLVLEDFFELLRTPVIV-GYGMTETSPVI-TNRVAEKN 288
Cdd:PRK06710 310 -----ALLNSPLLKEYD---ISSIRA--------CISGSAPLPVEVQEKFETVTGGKLVeGYGLTESSPVThSNFLWEKR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 289 LAGSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITG 368
Cdd:PRK06710 374 VPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDE-DGFFYVKD 451
|
330 340 350
....*....|....*....|....*....|....*..
gi 585104306 369 RAKDTIVLSnGENVEPQPIEDVVCANSAlVDQVMCVG 405
Cdd:PRK06710 452 RKKDMIVAS-GFNVYPREVEEVLYEHEK-VQEVVTIG 486
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
29-427 |
1.16e-23 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 104.57 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 29 FDEALSasLARPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVNYNS--FTDSPSKEPAYnpvlgDVLVSV 106
Cdd:PRK08751 188 FREALA--LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHqwLAGTGKLEEGC-----EVVITA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 107 LPCWHIFERTAEYWMFSK--GIHVVYSNVKNFkadlakhqPQFIVAVPRLLETIYRGVLQKFaaekgakkkiiefftrvg 184
Cdd:PRK08751 261 LPLYHIFALTANGLVFMKigGCNHLISNPRDM--------PGFVKELKKTRFTAFTGVNTLF------------------ 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 185 sawvkawrvaRGLvlrsrapnpierllalvlalvlspLAAVG-DKLVWSKVRAGLGGRIKVLVAggssmplVLEDFFELL 263
Cdd:PRK08751 315 ----------NGL------------------------LNTPGfDQIDFSSLKMTLGGGMAVQRS-------VAERWKQVT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 264 RTPVIVGYGMTETSP-VITNRVAEKNLAGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAV 342
Cdd:PRK08751 354 GLTLVEAYGLTETSPaACINPLTLKEYNGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKV 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 343 LDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVLSnGENVEPQPIEDVVCANSAlVDQVMCVG-QDEK---VLGMLVV-- 416
Cdd:PRK08751 433 MDADGWLHTGDIARMDE-QGFVYIVDRKKDMILVS-GFNVYPNEIEDVIAMMPG-VLEVAAVGvPDEKsgeIVKVVIVkk 509
|
410
....*....|....*..
gi 585104306 417 -PN-----VRALARAGL 427
Cdd:PRK08751 510 dPAltaedVKAHARANL 526
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
261-409 |
1.52e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 104.08 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 261 ELLRTPVIVGYGMTETSPVITNRVAEKNL---AGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAE 337
Cdd:PRK12583 340 EMHMAEVQIAYGMTETSPVSLQTTAADDLerrVETVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNNPE 418
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585104306 338 ASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVVCANSALVD-QVMCVgQDEK 409
Cdd:PRK12583 419 ATAESIDEDGWMHTGDLATMDE-QGYVRIVGRSKDMII-RGGENIYPREIEEFLFTHPAVADvQVFGV-PDEK 488
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
15-389 |
3.51e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 103.50 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 15 AELANLPPPTQVLTFDEALSASLARPLTFRPVPKDVRsVATLVYTSGTTNKPKGVVLRHSNLLHQ---VNYNSFTDSpsk 91
Cdd:PRK07529 178 VPLIRRKAHARILDFDAELARQPGDRLFSGRPIGPDD-VAAYFHTGGTTGMPKLAQHTHGNEVANawlGALLLGLGP--- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 92 epaynpvlGDVLVSVLPCWHIFertAEY----WMFSKGIHVV------YSN---VKNFKADLAKHQPQFIVAVPrlleTI 158
Cdd:PRK07529 254 --------GDTVFCGLPLFHVN---ALLvtglAPLARGAHVVlatpqgYRGpgvIANFWKIVERYRINFLSGVP----TV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 159 YRGVLQKfaaekgakkkiiefftrvgsawvkawrvarglvlrsrapnPIERLLAlvlalvlsplaavgdklvwSKVRAGL 238
Cdd:PRK07529 319 YAALLQV----------------------------------------PVDGHDI-------------------SSLRYAL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 239 GGrikvlvagGSSMPL-VLEDFFELLRTPVIVGYGMTE-TSPVITNRVAEKNLAGSVGRTARDTEVKIV--DPEsGARL- 313
Cdd:PRK07529 340 CG--------AAPLPVeVFRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDA-GRYLr 410
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585104306 314 --PEGQPGLVLMRGPQMMAGYkSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIED 389
Cdd:PRK07529 411 dcAVDEVGVLCIAGPNVFSGY-LEAAHNKGLWLEDGWLNTGDLGRIDA-DGYFWLTGRAKDLII-RGGHNIDPAAIEE 485
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
26-440 |
1.29e-22 |
|
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: 101.16 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 26 VLTFDEALSASLARPLTFRPVPKDvrSVATLVYTSGTTNKPKGVVLRHSNLLHQVNyNSFTdspskepAYNPVLGDVLVS 105
Cdd:cd05931 126 RLLVVDLLPDTSAADWPPPSPDPD--DIAYLQYTSGSTGTPKGVVVTHRNLLANVR-QIRR-------AYGLDPGDVVVS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 106 VLPCWH-------IFerTAeywMFSkGIHVVYSnvknfkadlakhQPQFIVAVPRL-LETI--YRGVLQ---KFAAEKGA 172
Cdd:cd05931 196 WLPLYHdmgliggLL--TP---LYS-GGPSVLM------------SPAAFLRRPLRwLRLIsrYRATISaapNFAYDLCV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 173 KKkiiefFTRVGSAwvkawrvarGLVLrsrapnpierllalvlalvlsplaavgdklvwSKVR-AGLGG-RIKvlvaggs 250
Cdd:cd05931 258 RR-----VRDEDLE---------GLDL--------------------------------SSWRvALNGAePVR------- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 251 smPLVLEDFFEL-----LRTPVIV-GYGMTET----------SPVITNRVAEKNLAG----------------SVGRTAR 298
Cdd:cd05931 285 --PATLRRFAEAfapfgFRPEAFRpSYGLAEAtlfvsggppgTGPVVLRVDRDALAGravavaaddpaarelvSCGRPLP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 299 DTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAV------LDQEGFLDTGDLGRIHplTKHLIITGRAKD 372
Cdd:cd05931 363 DQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLH--DGELYITGRLKD 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 373 TIVLSnGENVEPQPIEDVVCANSALV--DQVMCVGQDEKVLGMLVVPNVRALARAGLVDRGLAERVAELL 440
Cdd:cd05931 441 LIIVR-GRNHYPQDIEATAEEAHPALrpGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAV 509
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
25-383 |
3.28e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 100.56 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 25 QVLTFDEALSAslaRPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQV----NYNSFTDspskepaYNPvlg 100
Cdd:PTZ00342 281 SIILFDDMTKN---KTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVvplcKHSIFKK-------YNP--- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 101 DVLVSVLPCWHIFERTAEYWMFSKG--IHVVYSNVKNFKADLAKHQPQFIVAVPRLLETIYRGVLQKFAAekgakkkiIE 178
Cdd:PTZ00342 348 KTHLSYLPISHIYERVIAYLSFMLGgtINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINN--------LP 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 179 FFTRvgsawvkaWRVARGLVLRSRAPNpierllalvlalvlSPLAAVGDKL--VWSKVRAGLGGRIKVLVAGGSSM-PLV 255
Cdd:PTZ00342 420 PLKR--------FLVKKILSLRKSNNN--------------GGFSKFLEGIthISSKIKDKVNPNLEVILNGGGKLsPKI 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 256 LEDFFELLRTPVIVGYGMTETS-PVITNRVAEKNLAGSVGRTARDTEVKIVDPE---SGARLPEGQpglVLMRGPQMMAG 331
Cdd:PTZ00342 478 AEELSVLLNVNYYQGYGLTETTgPIFVQHADDNNTESIGGPISPNTKYKVRTWEtykATDTLPKGE---LLIKSDSIFSG 554
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 585104306 332 YKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVLSNGENVE 383
Cdd:PTZ00342 555 YFLEKEQTKNAFTEDGYFKTGDIVQINK-NGSLTFLDRSKGLVKLSQGEYIE 605
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
20-409 |
5.51e-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: 99.24 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 20 LPPPTQVLTFDEALSAslARPLTFRPVpKDVRSVATLVYTSGTTNKPKGVVLRH-SNLLHQVNYNSfTDSPSKEPaynpv 98
Cdd:cd12119 135 EPAGVGVLAYEELLAA--ESPEYDWPD-FDENTAAAICYTSGTTGNPKGVVYSHrSLVLHAMAALL-TDGLGLSE----- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 99 lGDVLVSVLPCWHIFERTAEYWMFSKGIHVVYSNVKNFKADLAK----HQPQFIVAVPrlleTIYRGVLQKFAAEKGakk 174
Cdd:cd12119 206 -SDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYLDPASLAElierEGVTFAAGVP----TVWQGLLDHLEANGR--- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 175 kiiefftrvgsawvkawrvarglvlrsrapnpierllalvlalVLSPLaavgdklvwskvraglggriKVLVAGGSSMPL 254
Cdd:cd12119 278 -------------------------------------------DLSSL--------------------RRVVIGGSAVPR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 255 VLEDFFELLRTPVIVGYGMTETSPVIT-NRVAEKNLAGSV----------GRTARDTEVKIVDPEsGARLP-EGQP-GLV 321
Cdd:cd12119 295 SLIEAFEERGVRVIHAWGMTETSPLGTvARPPSEHSNLSEdeqlalrakqGRPVPGVELRIVDDD-GRELPwDGKAvGEL 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 322 LMRGPQMMAGYKSNAEASKAvLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGE---NVEpqpIEDVVCANSAlV 398
Cdd:cd12119 374 QVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDE-DGYLTITDRSKDVIK-SGGEwisSVE---LENAIMAHPA-V 446
|
410
....*....|..
gi 585104306 399 DQVMCVGQ-DEK 409
Cdd:cd12119 447 AEAAVIGVpHPK 458
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
49-417 |
8.36e-22 |
|
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: 97.80 E-value: 8.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 49 DVRSVATLVYTSGTTNKPKGVVLRHSNllhqvNYNSFTDSpskepAYNpvLG----DVLVSVLPCWHIfertaeywmfsK 124
Cdd:cd05912 75 KLDDIATIMYTSGTTGKPKGVQQTFGN-----HWWSAIGS-----ALN--LGltedDNWLCALPLFHI-----------S 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 125 GIHVVYSNVknfkadlakhqpqfIVAVPrlletIYrgVLQKFAAEKgAKKKIIEfftrvgsawvkawrvaRGLVLRSRAP 204
Cdd:cd05912 132 GLSILMRSV--------------IYGMT-----VY--LVDKFDAEQ-VLHLINS----------------GKVTIISVVP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 205 NPIERllalvlalvlspLAAVGDKLVWSKVRaglggriKVLVAGGSSMPLVLEDFfELLRTPVIVGYGMTETSPVITNRV 284
Cdd:cd05912 174 TMLQR------------LLEILGEGYPNNLR-------CILLGGGPAPKPLLEQC-KEKGIPVYQSYGMTETCSQIVTLS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 285 AEKNLA--GSVGRTARDTEVKIVDPESgarlPEGQPGLVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTK 362
Cdd:cd05912 234 PEDALNkiGSAGKPLFPVELKIEDDGQ----PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDE-EG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 585104306 363 HLIITGRAKDTIVlSNGENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLGMlvVP 417
Cdd:cd05912 308 FLYVLDRRSDLII-SGGENIYPAEIEEVLLSHPA-IKEAGVVGIPDDKWGQ--VP 358
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
241-442 |
3.41e-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: 94.71 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 241 RIKVLVAGGSSMPLVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDpesgarlpegqPGL 320
Cdd:cd17630 112 SLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DGE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 321 VLMRGPQMMAGYKSNAEASkaVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVVCANSAlVDQ 400
Cdd:cd17630 181 IWVGGASLAMGYLRGQLVP--EFNEDGWFTTKDLGELHA-DGRLTVLGRADNMII-SGGENIQPEEIEAALAAHPA-VRD 255
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 585104306 401 VMCVGQDEKVLGMLVVPNVRalARAGLVDRGLAERVAELLGG 442
Cdd:cd17630 256 AFVVGVPDEELGQRPVAVIV--GRGPADPAELRAWLKDKLAR 295
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
22-391 |
3.93e-21 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 96.58 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 22 PPTQVLTFDEALSASLARPLtfrpVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSFT-DSPSKEPAYNPVLG 100
Cdd:cd05906 142 PGIRVLSIEELLDTAADHDL----PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHnGLTPQDVFLNWVPL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 101 DVLVSVLPCwHIFErtaeywmfskgihvvysnvknfkADLAKHQpqfiVAVPrlLETIYRGVLQkfaaekgakkkiiefF 180
Cdd:cd05906 218 DHVGGLVEL-HLRA-----------------------VYLGCQQ----VHVP--TEEILADPLR---------------W 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 181 TRvgsaWVKAWRVARglvlrSRAPNpierllalvlalvlSPLAAVGDKLVWSKVRAGLGGRIKVLVAGGSSMPL-VLEDF 259
Cdd:cd05906 253 LD----LIDRYRVTI-----TWAPN--------------FAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAkTIRRL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 260 FELL-----RTPVIV-GYGMTETSPVIT-------NRVAEKNLAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGP 326
Cdd:cd05906 310 LRLLepyglPPDAIRpAFGMTETCSGVIysrsfptYDHSQALEFVSLGRPIPGVSMRIVDDE-GQLLPEGEVGRLQVRGP 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585104306 327 QMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHplTKHLIITGRAKDTIVLsNGENVEPQPIEDVV 391
Cdd:cd05906 389 VVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD--NGNLTITGRTKDTIIV-NGVNYYSHEIEAAV 450
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
19-532 |
4.30e-21 |
|
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: 96.73 E-value: 4.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 19 NLPPPTQVLTFDE--ALSASLARPLTFRPVPKDvrSVATLVYTSGTTNKPKGVVLRHSNL------LHQVnYNSFTDSPS 90
Cdd:cd05921 133 NAVAGRGAISFAElaATPPTAAVDAAFAAVGPD--TVAKFLFTSGSTGLPKAVINTQRMLcanqamLEQT-YPFFGEEPP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 91 kepaynpvlgdVLVSVLPCWHIFERtaeywmfSKGIHVVYSNVKNFKADLAKHQPQFIVAVPRLLETIYRGVLqkFAAEK 170
Cdd:cd05921 210 -----------VLVDWLPWNHTFGG-------NHNFNLVLYNGGTLYIDDGKPMPGGFEETLRNLREISPTVY--FNVPA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 171 GAkkkiiefftrvgSAWVKAWRVARGLvlrsrapnpierllalvlalvlsplaavgdklvwskvRAGLGGRIKVLVAGGS 250
Cdd:cd05921 270 GW------------EMLVAALEKDEAL-------------------------------------RRRFFKRLKLMFYAGA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 251 SMPLVLEDFFELL-------RTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVdpesgarlPEGQPGLVLM 323
Cdd:cd05921 301 GLSQDVWDRLQALavatvgeRIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV--------PSGGKYEVRV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 324 RGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRI---HPLTKHLIITGRAKDTIVLSNGENVEPQPIE-DVVCANSALVD 399
Cdd:cd05921 373 KGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpDDPAKGLVFDGRVAEDFKLASGTWVSVGPLRaRAVAACAPLVH 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 400 QVMCVGQDEKVLGMLVVPNVRALAR-AGLVDRGLAERVAellggqvltngiagsraeLEEVEASLREKkevkkalLADIA 478
Cdd:cd05921 453 DAVVAGEDRAEVGALVFPDLLACRRlVGLQEASDAEVLR------------------HAKVRAAFRDR-------LAALN 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 585104306 479 RAMGKSFRETERVGaveVVLEPFNMANGFLTQTLKVKRNVVSGHYAQEIEQMYR 532
Cdd:cd05921 508 GEATGSSSRIARAL---LLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYA 558
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
241-444 |
2.41e-20 |
|
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: 93.60 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 241 RIKVLVAGGSSMP-LVLEDFFELLRTPVIVGYGMTETSPVITNRVA--EKNLAGSVGRTARDTEVKIVDpESGARLPEGQ 317
Cdd:cd05903 209 RLRTFVCGGATVPrSLARRAAELLGAKVCSAYGSTECPGAVTSITPapEDRRLYTDGRPLPGVEIKVVD-DTGATLAPGV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 318 PGLVLMRGPQMMAGYKSNAEASKAVLDqEGFLDTGDLGRIHPlTKHLIITGRAKDtIVLSNGENVEPQPIEDVVCANSAl 397
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDE-DGYLRITGRSKD-IIIRGGENIPVLEVEDLLLGHPG- 363
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 585104306 398 VDQVMCVGQDEKVLGMLVVPNVRALARAGLvdrGLAERVAELLGGQV 444
Cdd:cd05903 364 VIEAAVVALPDERLGERACAVVVTKSGALL---TFDELVAYLDRQGV 407
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
23-417 |
5.13e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 93.10 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 23 PTQVLTFDEaLSASLARPLTFRPvPKDVRSVATLVYTSGTTNKPKGVVLRHSNllHqvnYNSFTDSpskepAYNpvLG-- 100
Cdd:PRK03640 115 PGISVKFAE-LMNGPKEEAEIQE-EFDLDEVATIMYTSGTTGKPKGVIQTYGN--H---WWSAVGS-----ALN--LGlt 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 101 --DVLVSVLPCWHIfertaeywmfsKGIHVVYSNVknfkadlakhqpqfIVAVPRLLEtiyrgvlQKFAAEKgAKKKIIE 178
Cdd:PRK03640 181 edDCWLAAVPIFHI-----------SGLSILMRSV--------------IYGMRVVLV-------EKFDAEK-INKLLQT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 179 fftrvgsawvkawrvaRGLVLRSRAPNPIERLlalvlalvlspLAAVGDKLVWSKVRAglggrikVLVAGGSSMPLVLED 258
Cdd:PRK03640 228 ----------------GGVTIISVVSTMLQRL-----------LERLGEGTYPSSFRC-------MLLGGGPAPKPLLEQ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 259 FfELLRTPVIVGYGMTETSPVITNRVAEKNLA--GSVGRTARDTEVKIVDpeSGARLPEGQPGLVLMRGPQMMAGYKSNA 336
Cdd:PRK03640 274 C-KEKGIPVYQSYGMTETASQIVTLSPEDALTklGSAGKPLFPCELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNRE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 337 EASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLGMlvV 416
Cdd:PRK03640 351 DATRETF-QDGWFKTGDIGYLDE-EGFLYVLDRRSDLII-SGGENIYPAEIEEVLLSHPG-VAEAGVVGVPDDKWGQ--V 424
|
.
gi 585104306 417 P 417
Cdd:PRK03640 425 P 425
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
53-438 |
9.36e-20 |
|
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: 91.00 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 53 VATLVYTSGTTNKPKGVVLRHSNLLHQ---VNYNSFTDSpskepaynpvlGDVLVSVLPCWHIFER-TAEYWMFSKGIHV 128
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNawmLALNSLFDP-----------DDVLLCGLPLFHVNGSvVTLLTPLASGAHV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 129 V------YSN---VKNFKADLAKHQPQFIVAVPrlleTIYRGVLQkfaaekgakkkiiefftRVGSAWVKAWRVArglvl 199
Cdd:cd05944 73 VlagpagYRNpglFDNFWKLVERYRITSLSTVP----TVYAALLQ-----------------VPVNADISSLRFA----- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 200 rsrapnpierllalvlalvlsplaavgdklvwskvraglggrikvlVAGGSSMPLVLEDFFE-LLRTPVIVGYGMTETSP 278
Cdd:cd05944 127 ----------------------------------------------MSGAAPLPVELRARFEdATGLPVVEGYGLTEATC 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 279 VIT-NRVAEKNLAGSVGRTARDTEVKIV--DPESGARLPEGQP--GLVLMRGPQMMAGYkSNAEASKAVLDQEGFLDTGD 353
Cdd:cd05944 161 LVAvNPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDCAPDevGEICVAGPGVFGGY-LYTEGNKNAFVADGWLNTGD 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 354 LGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLGMLVVPNVRaLARAGLVDRG-- 431
Cdd:cd05944 240 LGRLDA-DGYLFITGRAKDLII-RGGHNIDPALIEEALLRHPA-VAFAGAVGQPDAHAGELPVAYVQ-LKPGAVVEEEel 315
|
410
....*....|
gi 585104306 432 ---LAERVAE 438
Cdd:cd05944 316 lawARDHVPE 325
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
299-434 |
2.36e-19 |
|
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: 90.98 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 299 DTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIvlsN 378
Cdd:COG1021 362 DDEVRIVDED-GNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTP-DGYLVVEGRAKDQI---N 436
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585104306 379 --GENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLG----MLVVPNVRALARAGLV----DRGLAE 434
Cdd:COG1021 437 rgGEKIAAEEVENLLLAHPA-VHDAAVVAMPDEYLGerscAFVVPRGEPLTLAELRrflrERGLAA 501
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
241-526 |
1.15e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 89.33 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 241 RIKVLVAGGSSMPlvlEDFFELL----------RTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVdpesg 310
Cdd:PRK12582 347 NLRLMAYGGATLS---DDLYERMqalavrttghRIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLA----- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 311 arlPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGR-IHP--LTKHLIITGRAKDTIVLSNGENVEPQPI 387
Cdd:PRK12582 419 ---PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfVDPddPEKGLIFDGRVAEDFKLSTGTWVSVGTL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 388 E-DVVCANSALVDQVMCVGQDEKVLGMLVVPNVRALaraglvdRGLAERvAELLGGQVLTngiagsraeLEEVEASLREK 466
Cdd:PRK12582 496 RpDAVAACSPVIHDAVVAGQDRAFIGLLAWPNPAAC-------RQLAGD-PDAAPEDVVK---------HPAVLAILREG 558
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585104306 467 kevkkaLLADIARAMGKSfretERVGAVEVVLEPFNMANGFLTQ--------TLKVKRNVVSGHYAQE 526
Cdd:PRK12582 559 ------LSAHNAEAGGSS----SRIARALLMTEPPSIDAGEITDkgyinqraVLERRAALVERLYAEP 616
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
294-388 |
3.17e-18 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 87.75 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 294 GRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKaVLDQEGFLDTGDLGRIhpLTKHLIITGRAKDT 373
Cdd:PRK09192 388 GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDLGYL--LDGYLYITGRAKDL 463
|
90
....*....|....*
gi 585104306 374 IVLsNGENVEPQPIE 388
Cdd:PRK09192 464 III-NGRNIWPQDIE 477
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
53-399 |
5.94e-18 |
|
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: 86.81 E-value: 5.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 53 VATLVYTSGTTNKPKGVVLRHSNLLHQVnynsftdSPSKEPAY-NPVLGDV-LVSVLPCWHIFERTAEYWMFSKGIHVVY 130
Cdd:cd17642 186 VALIMNSSGSTGLPKGVQLTHKNIVARF-------SHARDPIFgNQIIPDTaILTVIPFHHGFGMFTTLGYLICGFRVVL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 131 S---NVKNFKADLAKHQPQFIVAVPRLLEtiyrgvlqkfaaekgakkkiieFFTRvgSAWVKAWRVARGLVLRSRApnpi 207
Cdd:cd17642 259 MykfEEELFLRSLQDYKVQSALLVPTLFA----------------------FFAK--STLVDKYDLSNLHEIASGG---- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 208 erllalvlalvlSPLA-AVGDKLvwsKVRAGLGGrikvlvaggssmplvledffellrtpVIVGYGMTETSPVITNRVAE 286
Cdd:cd17642 311 ------------APLSkEVGEAV---AKRFKLPG--------------------------IRQGYGLTETTSAILITPEG 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 287 KNLAGSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGrIHPLTKHLII 366
Cdd:cd17642 350 DDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIA-YYDEDGHFFI 428
|
330 340 350
....*....|....*....|....*....|...
gi 585104306 367 TGRAKDTIVLsNGENVEPQPIEDVVCANSALVD 399
Cdd:cd17642 429 VDRLKSLIKY-KGYQVPPAELESILLQHPKIFD 460
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
17-509 |
1.30e-17 |
|
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: 85.97 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 17 LANLPPPTQVLTFDEALSASLARPLTFRPVPKDVRsVATLVYTSGTTNKPKGVVLRHSNLLHqvnynSFTDSPSKEPAYN 96
Cdd:cd17632 190 LAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDP-LALLIYTSGSTGTPKGAMYTERLVAT-----FWLKVSSIQDIRP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 97 PVlgDVLVSVLPCWHIFERTAEYWMFSKG---IHVVYSNVKNFKADLAKHQPQFIVAVPRLLETIYrgvlQKFAAEKgak 173
Cdd:cd17632 264 PA--SITLNFMPMSHIAGRISLYGTLARGgtaYFAAASDMSTLFDDLALVRPTELFLVPRVCDMLF----QRYQAEL--- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 174 kkiiefftrvgsawvkAWRVARGLVLRSRApnpiERLLalvlalvlsplAAVGDKLvwskvragLGGRIKVLVAGGSSMP 253
Cdd:cd17632 335 ----------------DRRSVAGADAETLA----ERVK-----------AELRERV--------LGGRLLAAVCGSAPLS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 254 LVLEDFFE-LLRTPVIVGYGMTETSPVITNrvaeknlagsvGRTARD--TEVKIVD-PESGARL-----PEGQpglVLMR 324
Cdd:cd17632 376 AEMKAFMEsLLDLDLHDGYGSTEAGAVILD-----------GVIVRPpvLDYKLVDvPELGYFRtdrphPRGE---LLVK 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 325 GPQMMAGYKSNAEASKAVLDQEGFLDTGD-LGRIHPltKHLIITGRAKDTIVLSNGENVEPQPIEdVVCANSALVDQVMC 403
Cdd:cd17632 442 TDTLFPGYYKRPEVTAEVFDEDGFYRTGDvMAELGP--DRLVYVDRRNNVLKLSQGEFVTVARLE-AVFAASPLVRQIFV 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 404 VGQDEKV-LGMLVVPNVRALAraglvdrglAERVAELlggqvltngiagsRAELEEveaSLREkkevkkalladIARAMG 482
Cdd:cd17632 519 YGNSERAyLLAVVVPTQDALA---------GEDTARL-------------RAALAE---SLQR-----------IAREAG 562
|
490 500
....*....|....*....|....*..
gi 585104306 483 KSFRETERVGAVEVvlEPFNMANGFLT 509
Cdd:cd17632 563 LQSYEIPRDFLIET--EPFTIANGLLS 587
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
43-409 |
1.34e-17 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 85.66 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 43 FRPVPKDV---RSVATLVYTSGTTNKPKGVVLRHSNLLHQVN-YNSFTDSPSKEPAYNpvlgDVLVSVLPCWHIFertae 118
Cdd:PLN02574 187 FDFVPKPVikqDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElFVRFEASQYEYPGSD----NVYLAALPMFHIY----- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 119 ywmfskGIHVvysnvknfkadlakhqpqFIVAVPRLLETIYrgVLQKFAAekgakkkiiefftrvgsawvkawrvarglv 198
Cdd:PLN02574 258 ------GLSL------------------FVVGLLSLGSTIV--VMRRFDA------------------------------ 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 199 lrSRAPNPIERLLALVLALVLSPLAAVGdklvwSKVRAGLGGRIK--VLVAGGSSmPL---VLEDFFELL-RTPVIVGYG 272
Cdd:PLN02574 282 --SDMVKVIDRFKVTHFPVVPPILMALT-----KKAKGVCGEVLKslKQVSCGAA-PLsgkFIQDFVQTLpHVDFIQGYG 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 273 MTETSPVITNRVAEKNLA--GSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLD 350
Cdd:PLN02574 354 MTESTAVGTRGFNTEKLSkySSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLR 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 585104306 351 TGDLGRIHpLTKHLIITGRAKDtIVLSNGENVEPQPIEDVVCANSALVDQVMCVGQDEK 409
Cdd:PLN02574 434 TGDIAYFD-EDGYLYIVDRLKE-IIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKE 490
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
58-409 |
2.56e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 84.53 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 58 YTSGTTNKPKGVVLRHSNLLHQVNYNSFTDSPSKEpaynpvlgDVLVSVLPCWHI-----FERTAeywMFSKGIHVVysn 132
Cdd:PRK06839 156 YTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMH--------DRSIVLLPLFHIggiglFAFPT---LFAGGVIIV--- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 133 VKNFKADLA-----KHQPQFIVAVPrlleTIYRGVLQKFAAEKGAKKKIIEFFTrvgsawvkawrvarglvlrsrapnpi 207
Cdd:PRK06839 222 PRKFEPTKAlsmieKHKVTVVMGVP----TIHQALINCSKFETTNLQSVRWFYN-------------------------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 208 erllalvlalvlsplaavgdklvwskvraglggrikvlvaGGSSMPLVLEDFFELLRTPVIVGYGMTETSPVITNRVAE- 286
Cdd:PRK06839 272 ----------------------------------------GGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEd 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 287 -KNLAGSVGRTARDTEVKIVDPESGaRLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLI 365
Cdd:PRK06839 312 aRRKVGSIGKPVLFCDYELIDENKN-KVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDE-DGFVY 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 585104306 366 ITGRAKDTIVlSNGENVEPQPIEDVVCANSALVDQVMCVGQDEK 409
Cdd:PRK06839 389 IVGRKKEMII-SGGENIYPLEVEQVINKLSDVYEVAVVGRQHVK 431
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
245-417 |
6.35e-17 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 83.56 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 245 LVAGGSSMPLVLEDFFELLRTPVIVGYGMTETSPVITNRV--AEKNLAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVL 322
Cdd:PRK13295 318 LCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLddPDERASTTDGCPLPGVEVRVVDAD-GAPLPAGQIGRLQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 323 MRGPQMMAGYKSNAEASKAvlDQEGFLDTGDLGRIHPlTKHLIITGRAKDtIVLSNGENVEPQPIEDVVCANSAlVDQVM 402
Cdd:PRK13295 397 VRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDA-DGYIRISGRSKD-VIIRGGENIPVVEIEALLYRHPA-IAQVA 471
|
170
....*....|....*....
gi 585104306 403 CVGQDEKVLG----MLVVP 417
Cdd:PRK13295 472 IVAYPDERLGeracAFVVP 490
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
20-407 |
3.38e-16 |
|
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: 80.95 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 20 LPPPTQVLTFDEALSASLARPlTFRPVPKDVrsvATLVYTSGTTNKPKGVVLRHSNLLHQVNynsftdspskepAYNPVL 99
Cdd:cd05922 90 SPDPGTVLDADGIRAARASAP-AHEVSHEDL---ALLLYTSGSTGSPKLVRLSHQNLLANAR------------SIAEYL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 100 G----DVLVSVLPcwhifertaeyWMFSKGIHVVYSNVknfkadlakhqpqfivavprlletiyrgvlqkfaaEKGAKKk 175
Cdd:cd05922 154 GitadDRALTVLP-----------LSYDYGLSVLNTHL-----------------------------------LRGATL- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 176 IIEFFTRVGSAWVKAWRVARGLVLrSRAPnpierllalvlalvlsPLAAVGDKLVWSKvrAGLGGRIKVLVAGGSSMPLV 255
Cdd:cd05922 187 VLTNDGVLDDAFWEDLREHGATGL-AGVP----------------STYAMLTRLGFDP--AKLPSLRYLTQAGGRLPQET 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 256 LEDFFELLR-TPVIVGYGMTETSPVIT----NRVAEKnlAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMA 330
Cdd:cd05922 248 IARLRELLPgAQVYVMYGQTEATRRMTylppERILEK--PGSIGLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMK 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585104306 331 GYkSNAEASKAVLDQ-EGFLDTGDLGRIHPlTKHLIITGRAKDTIVLSnGENVEPQPIEDVVCAnSALVDQVMCVGQD 407
Cdd:cd05922 325 GY-WNDPPYRRKEGRgGGVLHTGDLARRDE-DGFLFIVGRRDRMIKLF-GNRISPTEIEAAARS-IGLIIEAAAVGLP 398
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
242-412 |
3.61e-16 |
|
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: 79.85 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 242 IKVLVAGGSSMPLVLEDFF--ELLRTPVIVGYGMTETSPVITNRVAE--KNLAGSVGRTARDTEVKIVDPesgarlpegq 317
Cdd:cd17638 117 LRAAVTGAATVPVELVRRMrsELGFETVLTAYGLTEAGVATMCRPGDdaETVATTCGRACPGFEVRIADD---------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 318 pGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDtIVLSNGENVEPQPIEDVVcANSAL 397
Cdd:cd17638 187 -GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDE-RGYLRITDRLKD-MYIVGGFNVYPAEVEGAL-AEHPG 262
|
170
....*....|....*
gi 585104306 398 VDQVMCVGQDEKVLG 412
Cdd:cd17638 263 VAQVAVIGVPDERMG 277
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
19-489 |
5.16e-16 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 80.95 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 19 NLPPPTQVLTFDEALSASlaRPLTfRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLhqvnynsftdspSKEPAYNPV 98
Cdd:PRK06087 158 KLAPATSSLSLSQIIADY--EPLT-TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNIL------------ASERAYCAR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 99 LGdvlvsvlpcwhifeRTAEYWMFskgihvvysnvknFKADLAkHQPQFI--VAVPRLLETiyRGVLQkfaaEKGAKKKI 176
Cdd:PRK06087 223 LN--------------LTWQDVFM-------------MPAPLG-HATGFLhgVTAPFLIGA--RSVLL----DIFTPDAC 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 177 IEFFTRVGSAWvkawrvarglvlrSRAPNPIERLLALVLALVLSPLAAvgdklvwskvraglggrIKVLVAGGSSMPL-V 255
Cdd:PRK06087 269 LALLEQQRCTC-------------MLGATPFIYDLLNLLEKQPADLSA-----------------LRFFLCGGTTIPKkV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 256 LEDFFE----LLRTpvivgYGMTETSP---VITNRVAEKNLAGSvGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQM 328
Cdd:PRK06087 319 ARECQQrgikLLSV-----YGSTESSPhavVNLDDPLSRFMHTD-GYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 329 MAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVVcansalvdqvmcvgqde 408
Cdd:PRK06087 392 FMGYLDEPELTARALDEEGWYYSGDLCRMDE-AGYIKITGRKKDIIV-RGGENISSREVEDIL----------------- 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 409 kvlgmLVVPNVRALARAGLVDRGLAERVAELLggqVLTNGIAgsRAELEEVEASLREKK--------------------- 467
Cdd:PRK06087 453 -----LQHPKIHDACVVAMPDERLGERSCAYV---VLKAPHH--SLTLEEVVAFFSRKRvakykypehivvidklprtas 522
|
490 500
....*....|....*....|....
gi 585104306 468 -EVKKALLA-DIARAMGKSFRETE 489
Cdd:PRK06087 523 gKIQKFLLRkDIMRRLTQDVCEEI 546
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
242-437 |
1.13e-15 |
|
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: 79.04 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 242 IKVLVAGGSSMPLVL-EDFFELLRTPVIVGYGMTETSPV-ITNRVAEKNLaGSVGRTARDTEVKIVDPEsGARLPEGQPG 319
Cdd:cd05919 210 LRLCVSAGEALPRGLgERWMEHFGGPILDGIGATEVGHIfLSNRPGAWRL-GSTGRPVPGYEIRLVDEE-GHTIPPGEEG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 320 LVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVLSnGENVEPQPIEDVVCANSALVD 399
Cdd:cd05919 288 DLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDA-DGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAE 364
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 585104306 400 QVM---CVGQDEKVLGMLVVP-----NVRALARAglVDRGLAERVA 437
Cdd:cd05919 365 AAVvavPESTGLSRLTAFVVLkspaaPQESLARD--IHRHLLERLS 408
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
243-420 |
1.34e-15 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 79.46 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 243 KVLVAGGSSMPLVLEDFFELL-RTPVIVGYGMTET---------------SPVITNRVAEKNLAGS--------VGRTAR 298
Cdd:PLN02860 292 KILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTEAcssltfmtlhdptleSPKQTLQTVNQTKSSSvhqpqgvcVGKPAP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 299 DTEVKIVDPESGarlPEGQpglVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSN 378
Cdd:PLN02860 372 HVELKIGLDESS---RVGR---ILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDK-AGNLWLIGRSNDRIK-TG 443
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 585104306 379 GENVEPQPIEDVVCANSALVdQVMCVGQDEKVLGMLVVPNVR 420
Cdd:PLN02860 444 GENVYPEEVEAVLSQHPGVA-SVVVVGVPDSRLTEMVVACVR 484
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
232-409 |
1.40e-15 |
|
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: 79.27 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 232 SKVRAGLGGRIKVLVAGGSSMPLVLEDFfELLRTPVIVGYGMTETSPVIT--------NRVAEKNLAGSVGRTARD---- 299
Cdd:cd12118 240 PSDARPLPHRVHVMTAGAPPPAAVLAKM-EELGFDVTHVYGLTETYGPATvcawkpewDELPTEERARLKARQGVRyvgl 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 300 TEVKIVDPESGARLP-EGQP-GLVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDtIVLS 377
Cdd:cd12118 319 EEVDVLDPETMKPVPrDGKTiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHP-DGYIEIKDRSKD-IIIS 395
|
170 180 190
....*....|....*....|....*....|..
gi 585104306 378 NGENVEPQPIEDVVCANSALVDQVMCVGQDEK 409
Cdd:cd12118 396 GGENISSVEVEGVLYKHPAVLEAAVVARPDEK 427
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
49-380 |
2.54e-15 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 78.64 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 49 DVRSVATLVYTSGTTNKPKGVVLRH-SNLLHQVNYNsftdspskepayNP-VLG----DVLVSVLPCWHifertAEYW-- 120
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSHrSNVLHALMAN------------NGdALGtsaaDTMLPVVPLFH-----ANSWgi 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 121 MFS---KGIHVVYSNVKNFKAD----LAKHQPQFIVAVPrlleTIYRGVLQKFAAEkgakkkiiefftrvgsawvkawrv 193
Cdd:PRK06018 238 AFSapsMGTKLVMPGAKLDGASvyelLDTEKVTFTAGVP----TVWLMLLQYMEKE------------------------ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 194 arGLVLrsraPNpierllalvlalvlsplaavgdklvwskvraglggrIKVLVAGGSSMPLVLEDFFELLRTPVIVGYGM 273
Cdd:PRK06018 290 --GLKL----PH------------------------------------LKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGM 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 274 TETSPVITNRVAEKNLAGSVGRTARD-----------TEVKIVDPEsGARLP-EGQ-PGLVLMRGPQMMAGYksnAEASK 340
Cdd:PRK06018 328 TEMSPLGTLAALKPPFSKLPGDARLDvlqkqgyppfgVEMKITDDA-GKELPwDGKtFGRLKVRGPAVAAAY---YRVDG 403
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 585104306 341 AVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGE 380
Cdd:PRK06018 404 EILDDDGFFDTGDVATIDA-YGYMRITDRSKDVIK-SGGE 441
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
242-357 |
3.74e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 78.08 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 242 IKVLVAGGSSMP-LVLEDFFELLRTPVIVGYGMTET-SPVITNRVAEKNLaGSVGRTARDTEVKIVDPESGARLPEGQPG 319
Cdd:PRK08314 307 LRYIGGGGAAMPeAVAERLKELTGLDYVEGYGLTETmAQTHSNPPDRPKL-QCLGIPTFGVDARVIDPETLEELPPGEVG 385
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 585104306 320 LVLMRGPQMMAGYKSNAEASKAV---LDQEGFLDTGDLGRI 357
Cdd:PRK08314 386 EIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRM 426
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
289-434 |
5.24e-15 |
|
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: 77.37 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 289 LAGSVGRTA-RDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIIT 367
Cdd:cd05920 306 IIHTQGRPMsPDDEIRVVD-EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTP-DGYLVVE 383
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585104306 368 GRAKDTIVlSNGENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLG----MLVVPN---VRALA-RAGLVDRGLAE 434
Cdd:cd05920 384 GRIKDQIN-RGGEKIAAEEVENLLLRHPA-VHDAAVVAMPDELLGerscAFVVLRdppPSAAQlRRFLRERGLAA 456
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
53-410 |
6.52e-15 |
|
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: 76.75 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 53 VATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSFtdspskepAYNPVLGDVLVSVLPCWHI--FERTAEYWMFSKGIHVVY 130
Cdd:cd05935 86 LALIPYTSGTTGLPKGCMHTHFSAAANALQSAV--------WTGLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLM 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 131 SNvknFKADLAkhqpqfivavPRLLETiYRGvlqkfaaekgakkkiiefftrvgSAWvkaWRVARGLVLRSRAPNPIERL 210
Cdd:cd05935 158 AR---WDRETA----------LELIEK-YKV-----------------------TFW---TNIPTMLVDLLATPEFKTRD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 211 lalvlalvlsplaavgdklvWSKvraglggrIKVLVAGGSSMP-LVLEDFFELLRTPVIVGYGMTET-SPVITNRVAEKN 288
Cdd:cd05935 198 --------------------LSS--------LKVLTGGGAPMPpAVAEKLLKLTGLRFVEGYGLTETmSQTHTNPPLRPK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 289 LAgSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGY-KSNAEASKAVLDQEG--FLDTGDLGRIHPlTKHLI 365
Cdd:cd05935 250 LQ-CLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYwNRPEETEESFIEIKGrrFFRTGDLGYMDE-EGYFF 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 585104306 366 ITGRAKDTIVLSnGENVEPQPIEDVVCANSALVDQVMCVGQDEKV 410
Cdd:cd05935 328 FVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVISVPDERV 371
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
240-427 |
7.55e-15 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 77.23 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 240 GRIKVLVAGGSSMPlvlEDFFELL----------RTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDpeS 309
Cdd:PRK08180 334 SRLKLLFYAGAALS---QDVWDRLdrvaeatcgeRIRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVP--V 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 310 GARLpEgqpglVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRI----HPlTKHLIITGRAKDTIVLSNGENVEPQ 385
Cdd:PRK08180 409 GGKL-E-----VRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvdpaDP-ERGLMFDGRIAEDFKLSSGTWVSVG 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 585104306 386 PIE-DVVCANSALVDQVMCVGQDEKVLGMLVVPNVRALAR-AGL 427
Cdd:PRK08180 482 PLRaRAVSAGAPLVQDVVITGHDRDEIGLLVFPNLDACRRlAGL 525
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
18-355 |
1.21e-14 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 76.26 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 18 ANLPPPTQVLTFDEALSASLARPLTFRPVPKDvrSVATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSFTDSPSKEpaynp 97
Cdd:PRK08008 142 VALPADDGVSSFTQLKAQQPATLCYAPPLSTD--DTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDD----- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 98 vlgDVLVSVLPCWHI-FERTAEYWMFSKGIHVV----YSnVKNFKADLAKHQPQFIVAVPRLLETIyrgVLQKFAA-EKG 171
Cdd:PRK08008 215 ---DVYLTVMPAFHIdCQCTAAMAAFSAGATFVllekYS-ARAFWGQVCKYRATITECIPMMIRTL---MVQPPSAnDRQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 172 AKKKIIEFFTRVGSAwvkawrvarglvlrsrapnpiERllalvlalvlsplaavgdklvwskvraglggrikvlvaggss 251
Cdd:PRK08008 288 HCLREVMFYLNLSDQ---------------------EK------------------------------------------ 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 252 mplvlEDFFELLRTPVIVGYGMTET-SPVITNRVAEKNLAGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMR---GPQ 327
Cdd:PRK08008 305 -----DAFEERFGVRLLTSYGMTETiVGIIGDRPGDKRRWPSIGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKgvpGKT 378
|
330 340
....*....|....*....|....*...
gi 585104306 328 MMAGYKSNAEASKAVLDQEGFLDTGDLG 355
Cdd:PRK08008 379 IFKEYYLDPKATAKVLEADGWLHTGDTG 406
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
292-391 |
1.62e-14 |
|
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: 75.99 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 292 SVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHplTKHLIITGRAK 371
Cdd:cd05908 315 EVGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIR--NGRLVITGREK 391
|
90 100
....*....|....*....|
gi 585104306 372 DtIVLSNGENVEPQPIEDVV 391
Cdd:cd05908 392 D-IIFVNGQNVYPHDIERIA 410
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
56-409 |
1.89e-14 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 75.79 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 56 LVYTSGTTNKPKGVVLRHSNLLHQVNYNSFTDSPSkepaynpVLGDVL-VSVLPCWHIFERTAEYW--MFSKGIHVVYS- 131
Cdd:PLN02330 189 LPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPE-------MIGQVVtLGLIPFFHIYGITGICCatLRNKGKVVVMSr 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 132 -NVKNFKADLAKHQPQFIVAVPRLLETIyrgvlqkfaaekgAKKKIIEFFTrvgsawvkawrvarglvlrsrapnpIERL 210
Cdd:PLN02330 262 fELRTFLNALITQEVSFAPIVPPIILNL-------------VKNPIVEEFD-------------------------LSKL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 211 LALVLALVLSPLAAvgdklvwskvraglggriKVLVAGGSSMPLVledffellrtPVIVGYGMTETS--------PVITN 282
Cdd:PLN02330 304 KLQAIMTAAAPLAP------------------ELLTAFEAKFPGV----------QVQEAYGLTEHScitlthgdPEKGH 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 283 RVAEKNlagSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTK 362
Cdd:PLN02330 356 GIAKKN---SVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDD-DG 431
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 585104306 363 HLIITGRAKDTIVLsNGENVEPQPIEDVVCANSALVDQVMCVGQDEK 409
Cdd:PLN02330 432 DIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAVVPLPDEE 477
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
15-429 |
4.16e-14 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 74.79 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 15 AELANLPPP----TQVLTFDEALSASLARPLTFRPVPK--------DVR--SVATLVYTSGTTNKPKGVVLRHSNLlHQV 80
Cdd:PRK06155 130 AALEAADPGdlplPAVWLLDAPASVSVPAGWSTAPLPPldapapaaAVQpgDTAAILYTSGTTGPSKGVCCPHAQF-YWW 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 81 NYNSFTDSPSKEpaynpvlGDVLVSVLPCWHIFERTAEYWMFSKGIHVVYS---NVKNFKADLAKHQpqfiVAVPRLLet 157
Cdd:PRK06155 209 GRNSAEDLEIGA-------DDVLYTTLPLFHTNALNAFFQALLAGATYVLEprfSASGFWPAVRRHG----ATVTYLL-- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 158 iyrgvlqkfaaekGAKKKIiefftrvgsawvkawrvarglvLRSRAPNPIERLlalvlalvlsplaavgdklvwSKVRAG 237
Cdd:PRK06155 276 -------------GAMVSI----------------------LLSQPARESDRA---------------------HRVRVA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 238 LGGrikvlvaGGSsmPLVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNlAGSVGRTARDTEVKIVDpESGARLPEGQ 317
Cdd:PRK06155 300 LGP-------GVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQR-PGSMGRLAPGFEARVVD-EHDQELPDGE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 318 PGLVLMRGPQ---MMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDTIvLSNGENVEPQPIEDVVCAN 394
Cdd:PRK06155 369 PGELLLRADEpfaFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDA-DGWFRFVDRIKDAI-RRRGENISSFEVEQVLLSH 445
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 585104306 395 SAL----VDQVMC-VGQDEkVLGMLVVPNVRALARAGLVD 429
Cdd:PRK06155 446 PAVaaaaVFPVPSeLGEDE-VMAAVVLRDGTALEPVALVR 484
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
17-441 |
6.87e-14 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 73.99 E-value: 6.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 17 LANLPPPTQVLTFD--------------EALSASLARPLTFRPVPKDvrSVATLVYTSGTTNKPKGVVLRHSNLLHQVNY 82
Cdd:COG0365 138 LEELPSLEHVIVVGrtgadvpmegdldwDELLAAASAEFEPEPTDAD--DPLFILYTSGTTGKPKGVVHTHGGYLVHAAT 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 83 NSftdspskEPAYNPVLGDVLVSVLPC----WHIfertaeYWMFSKGIH----VVYSNVKNFK-AD-----LAKHQPQFI 148
Cdd:COG0365 216 TA-------KYVLDLKPGDVFWCTADIgwatGHS------YIVYGPLLNgatvVLYEGRPDFPdPGrlwelIEKYGVTVF 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 149 VAVPrlleTIYRgvlqkfaaekgakkkiieFFTRVGSAWVKAWRVARglvLRSrapnpierllalvlalvlspLAAVGDK 228
Cdd:COG0365 283 FTAP----TAIR------------------ALMKAGDEPLKKYDLSS---LRL--------------------LGSAGEP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 229 L---VWSKVRAGLGgrikvlvaggssmplvledffellrTPVIVGYGMTET-SPVITNRVAEKNLAGSVGRTARDTEVKI 304
Cdd:COG0365 318 LnpeVWEWWYEAVG-------------------------VPIVDGWGQTETgGIFISNLPGLPVKPGSMGKPVPGYDVAV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 305 VDPEsGARLPEGQPGLVLMRGPQ--MMAGYKSNAEASKAVL--DQEGFLDTGDLGRIhplTKH--LIITGRAKDTIVlSN 378
Cdd:COG0365 373 VDED-GNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARR---DEDgyFWILGRSDDVIN-VS 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585104306 379 GENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLGML----VVPNVRALARAGLVDRgLAERVAELLG 441
Cdd:COG0365 448 GHRIGTAEIESALVSHPA-VAEAAVVGVPDEIRGQVvkafVVLKPGVEPSDELAKE-LQAHVREELG 512
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
240-399 |
1.32e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 72.92 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 240 GRIKVLVAGGSsmPLVLEDFFELLR--TPVIVGYGMTETS-----PVITNRVAEKnlAGSVGRTARDTEVKIVDpESGAR 312
Cdd:PRK09088 252 RHLTALFTGGA--PHAAEDILGWLDdgIPMVDGFGMSEAGtvfgmSVDCDVIRAK--AGAAGIPTPTVQTRVVD-DQGND 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 313 LPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPLTKHLIITgRAKDtIVLSNGENVEPQPIEDVVC 392
Cdd:PRK09088 327 CPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVD-RKKD-MFISGGENVYPAEIEAVLA 404
|
....*..
gi 585104306 393 ANSALVD 399
Cdd:PRK09088 405 DHPGIRE 411
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
48-392 |
1.55e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 72.93 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 48 KDVRSVATLVYTSGTTNKPKGVVLRHSNLLhqVNYNSFTDspskepAYNPVLGDVLVSVLPCWHI--FERTAEYWMFSkG 125
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTHANLL--ANQRACLK------FFSPKEDDVMMSFLPPFHAygFNSCTLFPLLS-G 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 126 IHVVYSnvknfkadlakHQPqfivavprlletiyrgvLQKfaaekgakKKIIEFFTRVGSAWVKAWRVARGLVLRSrapn 205
Cdd:PRK06334 251 VPVVFA-----------YNP-----------------LYP--------KKIVEMIDEAKVTFLGSTPVFFDYILKT---- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 206 pierllalvLALVLSPLAAvgdklvwskvraglggrIKVLVAGGSSMPLVLEDffELLRT-PVIV---GYGMTETSPVIT 281
Cdd:PRK06334 291 ---------AKKQESCLPS-----------------LRFVVIGGDAFKDSLYQ--EALKTfPHIQlrqGYGTTECSPVIT 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 282 -NRVAEKNLAGSVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAV-LDQEGFLDTGDLGRIHP 359
Cdd:PRK06334 343 iNTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVeLGGETWYVTGDLGYVDR 422
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 585104306 360 lTKHLIITGR---------------AKDTIVLSN-GENVEPQPIEDVVC 392
Cdd:PRK06334 423 -HGELFLKGRlsrfvkigaemvsleALESILMEGfGQNAADHAGPLVVC 470
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
230-440 |
1.84e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 72.72 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 230 VWSKV-------RAGLGGRIkvLVAGGSSMPL-VLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTE 301
Cdd:PRK07787 226 VWSRIaadpeaaRALRGARL--LVSGSAALPVpVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 302 VKIVDpESGARLP-EGQP-GLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPLTKHLIItGRAKDTIVLSNG 379
Cdd:PRK07787 304 TRLVD-EDGGPVPhDGETvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIV-GRESTDLIKSGG 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 585104306 380 ENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLGMLVVPNVraLARAGLVDRGLAERVAELL 440
Cdd:PRK07787 382 YRIGAGEIETALLGHPG-VREAAVVGVPDDDLGQRIVAYV--VGADDVAADELIDFVAQQL 439
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
51-402 |
2.47e-13 |
|
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: 71.14 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 51 RSVATLVYTSGTTNKPKGVVLRHSNLLhqvnynSFTDSPSKEpAYNPVLGDVLVSVLPCWHIFertAEYWM----FSKGI 126
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFF------AVPDILQKE-GLNWVVGDVTYLPLPATHIG---GLWWIltclIHGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 127 HVVYSNVKNFKADLakhqpqfivavprlletiyrgvlqkfaaekgakkKIIEFFTRVGSAWVKAwrvarglvlrsrapnp 206
Cdd:cd17635 71 CVTGGENTTYKSLF----------------------------------KILTTNAVTTTCLVPT---------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 207 ierllalvlalvlsplaavgdklVWSKVRAGLGGRIKV-----LVAGGSSMPLVLED-FFELLR-TPVIVGYGMTETSPV 279
Cdd:cd17635 101 -----------------------LLSKLVSELKSANATvpslrLIGYGGSRAIAADVrFIEATGlTNTAQVYGLSETGTA 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 280 ITNRVAEKNL-AGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIH 358
Cdd:cd17635 158 LCLPTDDDSIeINAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERR 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 585104306 359 PlTKHLIITGRAKDTIVLSnGENVEPQPIEDVV--------CANSALVDQVM 402
Cdd:cd17635 236 E-DGFLFITGRSSESINCG-GVKIAPDEVERIAegvsgvqeCACYEISDEEF 285
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
249-404 |
2.59e-13 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 71.15 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 249 GSSMPLVLEDFFELLRTPVIVGYGMTETSPVIT-NRVAEKnlAGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQ 327
Cdd:cd17637 121 GLDAPETIQRFEETTGATFWSLYGQTETSGLVTlSPYRER--PGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPL 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585104306 328 MMAGYKSNAEASKAVLDqEGFLDTGDLGRIHPlTKHLIITGR--AKDTIVlSNGENVEPQPIEDVVCANSAlVDQVmCV 404
Cdd:cd17637 198 VFQGYWNLPELTAYTFR-NGWHHTGDLGRFDE-DGYLWYAGRkpEKELIK-PGGENVYPAEVEKVILEHPA-IAEV-CV 271
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
240-391 |
5.22e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 71.59 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 240 GRIKVLvAGGSSMPLVLEDFFELLRTPVIVGYGMTE-TSPVIT-------NRVAEKN---LAGSVG-RTARDTEVKIVDP 307
Cdd:PLN03102 301 GPVHVL-TGGSPPPAALVKKVQRLGFQVMHAYGLTEaTGPVLFcewqdewNRLPENQqmeLKARQGvSILGLADVDVKNK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 308 ESGARLP-EGQP-GLVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDtIVLSNGENVEPQ 385
Cdd:PLN03102 380 ETQESVPrDGKTmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHP-DGHVEIKDRSKD-IIISGGENISSV 456
|
....*.
gi 585104306 386 PIEDVV 391
Cdd:PLN03102 457 EVENVL 462
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
21-391 |
7.06e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 70.73 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 21 PPPTQVLTFDEALSASLARPLtfrPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQvnYNSFTDSPSKEPaynpvlG 100
Cdd:PRK08316 144 EAPGGWLDFADWAEAGSVAEP---DVELADDDLAQILYTSGTESLPKGAMLTHRALIAE--YVSCIVAGDMSA------D 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 101 DVLVSVLPCWHifertaeywmfSKGIHVVYSnvknfkadlakhqPQF-------IVAVP---RLLETIYR-GVLQKFAAE 169
Cdd:PRK08316 213 DIPLHALPLYH-----------CAQLDVFLG-------------PYLyvgatnvILDAPdpeLILRTIEAeRITSFFAPP 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 170 kgakkkiiefftrvgSAWVkawrvarGLvLRSrapnpierllalvlalvlsPLAAvgdklvwskvRAGLGGRIKVLVaGG 249
Cdd:PRK08316 269 ---------------TVWI-------SL-LRH-------------------PDFD----------TRDLSSLRKGYY-GA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 250 SSMPL-VLEdffELLRTPVIVG----YGMTETSPVITNRVAEKNL--AGSVGRTARDTEVKIVDpESGARLPEGQPGLVL 322
Cdd:PRK08316 296 SIMPVeVLK---ELRERLPGLRfyncYGQTEIAPLATVLGPEEHLrrPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIV 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585104306 323 MRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVV 391
Cdd:PRK08316 372 HRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDE-EGYITVVDRKKDMIK-TGGENVASREVEEAL 437
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
233-391 |
7.16e-13 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 70.94 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 233 KVRAGLGGR-IKVLVAGGSSM-PLVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLA-GSVGRTARDTEVKIVDPEs 309
Cdd:PRK13382 304 EVRNRYSGRsLRFAAASGSRMrPDVVIAFMDQFGDVIYNNYNATEAGMIATATPADLRAApDTAGRPAEGTEIRILDQD- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 310 GARLPEGQPGLVLMRGPQMMAGYKSNAeaSKAVldQEGFLDTGDLGRIHPLTKhLIITGRAKDTIVlSNGENVEPQPIED 389
Cdd:PRK13382 383 FREVPTGEVGTIFVRNDTQFDGYTSGS--TKDF--HDGFMASGDVGYLDENGR-LFVVGRDDEMIV-SGGENVYPIEVEK 456
|
..
gi 585104306 390 VV 391
Cdd:PRK13382 457 TL 458
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
18-391 |
1.05e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.35 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 18 ANLPPPTQVLTFDEALSASLARPltfrPVPKDvrSVATLVYTSGTTNKPKGVVLRHSNLLHqvnyNSFTDSPSKEPAYNP 97
Cdd:PRK05691 139 ANAPELLCVDTLDPALAEAWQEP----ALQPD--DIAFLQYTSGSTALPKGVQVSHGNLVA----NEQLIRHGFGIDLNP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 98 vlGDVLVSVLPCWHifertaEYWMFSKGIHVVYSNVKnfkadLAKHQPQFIVAVP-RLLETI--YRGVLQ---KFAAEKG 171
Cdd:PRK05691 209 --DDVIVSWLPLYH------DMGLIGGLLQPIFSGVP-----CVLMSPAYFLERPlRWLEAIseYGGTISggpDFAYRLC 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 172 AKkkiiefftRVGSAWVKA-----WRVARGlvlrsrAPNPIERLLALVLALVLSPLAAVGDKLVWSkvrAGLGgRIKVLV 246
Cdd:PRK05691 276 SE--------RVSESALERldlsrWRVAYS------GSEPIRQDSLERFAEKFAACGFDPDSFFAS---YGLA-EATLFV 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 247 AG---GSSMPLVLEDFFELLRTPVIVGYGmtetSPVItnrvaeknlagSVGRTARDTEVKIVDPESGARLPEGQPGLVLM 323
Cdd:PRK05691 338 SGgrrGQGIPALELDAEALARNRAEPGTG----SVLM-----------SCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWA 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 585104306 324 RGPQMMAGYKSNAEAS-KAVLDQEG--FLDTGDLGRIHplTKHLIITGRAKDTIVLsNGENVEPQPIEDVV 391
Cdd:PRK05691 403 SGPSIAHGYWRNPEASaKTFVEHDGrtWLRTGDLGFLR--DGELFVTGRLKDMLIV-RGHNLYPQDIEKTV 470
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
253-392 |
3.97e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 68.48 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 253 PLVLEDF------FELLRTPVIVGYGMTETS---------------PVITNRVAEKNLA--GSVGRTAR---------DT 300
Cdd:PRK07768 290 PADVEDLldagarFGLRPEAILPAYGMAEATlavsfspcgaglvvdEVDADLLAALRRAvpATKGNTRRlatlgpplpGL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 301 EVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSnAEASKAVLDQEGFLDTGDLGRihpLTK--HLIITGRAKDTIVLSn 378
Cdd:PRK07768 370 EVRVVD-EDGQVLPPRGVGVIELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGY---LTEegEVVVCGRVKDVIIMA- 443
|
170
....*....|....
gi 585104306 379 GENVEPQPIEDVVC 392
Cdd:PRK07768 444 GRNIYPTDIERAAA 457
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
299-434 |
4.07e-12 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 68.48 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 299 DTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIvlsN 378
Cdd:PRK10946 362 DDEVWVAD-ADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDP-DGYITVVGREKDQI---N 436
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585104306 379 --GENVEPQPIEDVVCA-----NSALV---DQVMcvgqDEKVLGMLVVPN-VRALA-RAGLVDRGLAE 434
Cdd:PRK10946 437 rgGEKIAAEEIENLLLRhpaviHAALVsmeDELM----GEKSCAFLVVKEpLKAVQlRRFLREQGIAE 500
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
235-390 |
4.99e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 68.44 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 235 RAGLGGRIKVLVAGGSSMPLVLEDF----FELLRTpvivgYGMTET-SPVITNrvAEKN------LAGSVGRTARD---- 299
Cdd:PRK08162 292 RAGIDHPVHAMVAGAAPPAAVIAKMeeigFDLTHV-----YGLTETyGPATVC--AWQPewdalpLDERAQLKARQgvry 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 300 ---TEVKIVDPESGARLP-EGQP-GLVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDtI 374
Cdd:PRK08162 365 plqEGVTVLDPDTMQPVPaDGETiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHP-DGYIKIKDRSKD-I 441
|
170
....*....|....*.
gi 585104306 375 VLSNGENVEPQPIEDV 390
Cdd:PRK08162 442 IISGGENISSIEVEDV 457
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
242-391 |
6.62e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 68.03 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 242 IKVLVAGGSSMP-----LVLEDFfellrTPVIVG-YGMTETSPVITNRVAEKNLA-GSVGRTARDTEVKIVDpESGARLP 314
Cdd:PRK07788 325 LKIIFVSGSALSpelatRALEAF-----GPVLYNlYGSTEVAFATIATPEDLAEApGTVGRPPKGVTVKILD-ENGNEVP 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585104306 315 EGQPGLVLMRGPQMMAGYksNAEASKAVLDqeGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVV 391
Cdd:PRK07788 399 RGVVGRIFVGNGFPFEGY--TDGRDKQIID--GLLSSGDVGYFDE-DGLLFVDGRDDDMIV-SGGENVFPAEVEDLL 469
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
284-409 |
9.42e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 67.46 E-value: 9.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 284 VAEKNLAGsvGRTAR-DTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTK 362
Cdd:PRK06164 344 VSVRIEGG--GRPASpEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRG-DG 420
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 585104306 363 HLIITGRAKDTIVLSnGENVEPQPIEDVVCANSALVD-QVMCVGQDEK 409
Cdd:PRK06164 421 QFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVAAaQVVGATRDGK 467
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
271-428 |
1.18e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 66.99 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 271 YGMTE--TSPVITN--RVAEKNLAGS---VGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVL 343
Cdd:PRK06178 360 WGMTEthTCDTFTAgfQDDDFDLLSQpvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 344 dQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVLsNGENVEPQPIEdvvcansalvdqvMCVGQDEKVLGMLVVPnvRALA 423
Cdd:PRK06178 440 -RDGWLHTGDIGKIDE-QGFLHYLGRRKEMLKV-NGMSVFPSEVE-------------ALLGQHPAVLGSAVVG--RPDP 501
|
....*
gi 585104306 424 RAGLV 428
Cdd:PRK06178 502 DKGQV 506
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
271-409 |
1.26e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 66.93 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 271 YGMTETSPVIT------NRVAEKNLAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLd 344
Cdd:PRK06188 313 YGQTEAPMVITylrkrdHDPDDPKRLTSCGRPTPGLRVALLDED-GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF- 390
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585104306 345 QEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVVCANSAlVDQVMCVG-QDEK 409
Cdd:PRK06188 391 RDGWLHTGDVAREDE-DGFYYIVDRKKDMIV-TGGFNVFPREVEDVLAEHPA-VAQVAVIGvPDEK 453
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
266-465 |
1.30e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 67.03 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 266 PVIVG-YGMTETSpVITNRVAEKNLA--GSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAV 342
Cdd:PRK12406 297 PVIYEyYGSTESG-AVTFATSEDALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNPDFTYHNKPEKRAE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 343 LDQEGFLDTGDLGRIHPlTKHLIITGRAKDtIVLSNGENVEPQPIEDVVCAnsalvdqvmcvgqdekvlgmlvVPNVRAL 422
Cdd:PRK12406 375 IDRGGFITSGDVGYLDA-DGYLFLCDRKRD-MVISGGVNIYPAEIEAVLHA----------------------VPGVHDC 430
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 585104306 423 ARAGLVDRGLAERVAELLGGQvltngiAGSRAELEEVEASLRE 465
Cdd:PRK12406 431 AVFGIPDAEFGEALMAVVEPQ------PGATLDEADIRAQLKA 467
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
240-398 |
3.32e-11 |
|
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: 65.44 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 240 GRIKVLVAGGSSM-PLVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDpESGARLPEGQP 318
Cdd:cd05972 197 SHLRLVVSAGEPLnPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 319 GLVLMR--GPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDtIVLSNGENVEPQPIEdvvcanSA 396
Cdd:cd05972 276 GDIAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDE-DGYFWFVGRADD-IIKSSGYRIGPFEVE------SA 346
|
..
gi 585104306 397 LV 398
Cdd:cd05972 347 LL 348
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
49-440 |
3.38e-11 |
|
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: 65.24 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 49 DVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVNynsftdspSKEPAYNPVLGDVLVSVLPCWHIFERTAEYWMFSKG--I 126
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL--------WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGatL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 127 HVV-YSNVKNFKA---DLAKHQPQFIVAVPRLLETiyrgvlqkfaaekgakkkiiefftrvgsawvkawrvarglvlrsr 202
Cdd:cd05930 163 VVLpEEVRKDPEAladLLAEEGITVLHLTPSLLRL--------------------------------------------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 203 apnpierllalvlalvlspLAAVGDKLVWSKVRaglggrikVLVAGGSSMPL-VLEDFFELLRTPVIV-GYGMTETSPVI 280
Cdd:cd05930 198 -------------------LLQELELAALPSLR--------LVLVGGEALPPdLVRRWRELLPGARLVnLYGPTEATVDA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 281 T-NRVAEKNLAGS---VGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQEGFLD------ 350
Cdd:cd05930 251 TyYRVPPDDEEDGrvpIGRPIPNTRVYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPgermyr 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 351 TGDLGRIHPlTKHLIITGRAkDTIVLSNGENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLGMLVVPNVRALARAGLVDR 430
Cdd:cd05930 330 TGDLVRWLP-DGNLEFLGRI-DDQVKIRGYRIELGEIEAALLAHPG-VREAAVVAREDGDGEKRLVAYVVPDEGGELDEE 406
|
410
....*....|
gi 585104306 431 GLAERVAELL 440
Cdd:cd05930 407 ELRAHLAERL 416
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
26-444 |
6.96e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 64.80 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 26 VLTFDEALSASLArPLTFRPVPKDvrSVATLVYTSGTTNKPKGVVLRHSNLLHQVNYNSFT---DSPSkepaynpvlgDV 102
Cdd:PRK07786 152 VLGYEDLLAEAGP-AHAPVDIPND--SPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTngaDINS----------DV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 103 LVSVLPCWHIFERTAEYWMFSKGIHVVYSNVKNFKADlakhqpqfivavprlletiyrGVLQKFAAEKgakkkIIEFFTr 182
Cdd:PRK07786 219 GFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPG---------------------QLLDVLEAEK-----VTGIFL- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 183 VGSAW--VKAWRVARGLVLRSRApnpierllalvlalvlsplaavgdkLVWSKVRAGlggrikvlvaggssmPLVLEDFF 260
Cdd:PRK07786 272 VPAQWqaVCAEQQARPRDLALRV-------------------------LSWGAAPAS---------------DTLLRQMA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 261 ELL-RTPVIVGYGMTETSPVITNRVAEKNLA--GSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAE 337
Cdd:PRK07786 312 ATFpEAQILAAFGQTEMSPVTCMLLGEDAIRklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 338 ASKAVLDQeGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVVCANSALVDqVMCVGQDEKVLGMlvVP 417
Cdd:PRK07786 391 ATAEAFAG-GWFHSGDLVRQDE-EGYVWVVDRKKDMII-SGGENIYCAEVENVLASHPDIVE-VAVIGRADEKWGE--VP 464
|
410 420
....*....|....*....|....*..
gi 585104306 418 NVRALARAGLVDRGLAErVAELLGGQV 444
Cdd:PRK07786 465 VAVAAVRNDDAALTLED-LAEFLTDRL 490
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
292-388 |
8.50e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 64.37 E-value: 8.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 292 SVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAV--------LDQ---EG------FLDTGDL 354
Cdd:PRK07769 392 SAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATfqnilksrLSEshaEGapddalWVRTGDY 471
|
90 100 110
....*....|....*....|....*....|....
gi 585104306 355 GRIHplTKHLIITGRAKDtIVLSNGENVEPQPIE 388
Cdd:PRK07769 472 GVYF--DGELYITGRVKD-LVIIDGRNHYPQDLE 502
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
266-390 |
2.79e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 62.61 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 266 PVIVGY-------GMTetspVITnrvAEKNLA--GSVGRtARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNA 336
Cdd:PRK08276 288 PIIHEYyasseggGVT----VIT---SEDWLAhpGSVGK-AVLGEVRILD-EDGNELPPGEIGTVYFEMDGYPFEYHNDP 358
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 585104306 337 EASKAVLDQEGFLDTGDLGRihpLTK--HLIITGRAKDTIVlSNGENVEPQPIEDV 390
Cdd:PRK08276 359 EKTAAARNPHGWVTVGDVGY---LDEdgYLYLTDRKSDMII-SGGVNIYPQEIENL 410
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
291-412 |
3.27e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 62.37 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 291 GSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAEA-SKAVLDqeGFLDTGDLGRIHPlTKHLIITGR 369
Cdd:PRK07470 340 GTCGFERTGMEVQIQDDE-GRELPPGETGEICVIGPAVFAGYYNNPEAnAKAFRD--GWFRTGDLGHLDA-RGFLYITGR 415
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 585104306 370 AKDtIVLSNGENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLG 412
Cdd:PRK07470 416 ASD-MYISGGSNVYPREIEEKLLTHPA-VSEVAVLGVPDPVWG 456
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
33-440 |
5.46e-10 |
|
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: 61.56 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 33 LSASLARPLTFRPVPKDVrsvATLVYTSGTTNKPKGVVLRHSNLLHQVNYNS--FTDSPSKE------PAYNPVLGDVLV 104
Cdd:cd17653 90 LRTSGATLLLTTDSPDDL---AYIIFTSGSTGIPKGVMVPHRGVLNYVSQPParLDVGPGSRvaqvlsIAFDACIGEIFS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 105 SVlpcwhifertaeywmfSKGIHVVYSNVKNFKADLAKHQPQFIvAVPRLLETIyrgvlqkfaaekgakkkiiefftrvg 184
Cdd:cd17653 167 TL----------------CNGGTLVLADPSDPFAHVARTVDALM-STPSILSTL-------------------------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 185 sawvkawrvarglvlrSRAPNPierllalvlalvlsplaavgdklvwskvraglggRIKVLVAGGSSMPLVLEDFFELLR 264
Cdd:cd17653 204 ----------------SPQDFP----------------------------------NLKTIFLGGEAVPPSLLDRWSPGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 265 TpVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAE--ASKAV 342
Cdd:cd17653 234 R-LYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDAD-LQPVPEGVVGEICISGVQVARGYLGNPAltASKFV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 343 LDQ----EGFLDTGDLGRIhpLTKH-LIITGRaKDTIVLSNGENVEPQPIEDVVCANSALVDQVMCVgQDEKVLGMLVVP 417
Cdd:cd17653 312 PDPfwpgSRMYRTGDYGRW--TEDGgLEFLGR-EDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI-VVNGRLVAFVTP 387
|
410 420
....*....|....*....|...
gi 585104306 418 nvralarAGLVDRGLAERVAELL 440
Cdd:cd17653 388 -------ETVDVDGLRSELAKHL 403
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
249-409 |
9.80e-10 |
|
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: 60.99 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 249 GSSMP-LVLEDFFELLRTPVIVGYGMTETSPVITNRVAEknlAGSVGRTARDTEVKIVdpESGAR----LPEGQPG--LV 321
Cdd:cd05923 276 GATMPdAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDAR---TGTEMRPGFFSEVRIV--RIGGSpdeaLANGEEGelIV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 322 LMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVVCANSAlVDQV 401
Cdd:cd05923 351 AAAADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDP-SGDVRILGRVDDMII-SGGENIHPSEIERVLSRHPG-VTEV 426
|
....*....
gi 585104306 402 MCVG-QDEK 409
Cdd:cd05923 427 VVIGvADER 435
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
266-391 |
1.13e-09 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 60.67 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 266 PVIVGYGMTETSPVITNRVAE-----KNLAGSVGRTARDT--EVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSNAEA 338
Cdd:PRK05852 322 PVVCAFGMTEATHQVTTTQIEgigqtENPVVSTGLVGRSTgaQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTI 400
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 585104306 339 SKAVLdQEGFLDTGDLGRIHpLTKHLIITGRAKDTIVLSnGENVEPQPIEDVV 391
Cdd:PRK05852 401 TAANF-TDGWLRTGDLGSLS-AAGDLSIRGRIKELINRG-GEKISPERVEGVL 450
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
238-426 |
1.47e-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: 60.18 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 238 LGGRIKVLVAGGSSMPLVLED-FFELLRTPVIVGYGMTETSPV-ITNRVAEKNlAGSVGRTARDTEVKIVDpESGARLPE 315
Cdd:cd05958 211 DLSSLRKCVSAGEALPAALHRaWKEATGIPIIDGIGSTEMFHIfISARPGDAR-PGATGKPVPGYEAKVVD-DEGNPVPD 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 316 GQPGLVLMRGPqmmAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVVCANS 395
Cdd:cd05958 289 GTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRDP-DGYFRHQGRSDDMIV-SGGYNIAPPEVEDVLLQHP 363
|
170 180 190
....*....|....*....|....*....|.
gi 585104306 396 AlVDQVMCVGQDEKVLGMlvVPNVRALARAG 426
Cdd:cd05958 364 A-VAECAVVGHPDESRGV--VVKAFVVLRPG 391
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
246-417 |
1.73e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 60.11 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 246 VAGGSSMP-LVLEDFFELLRTPVIVGYGMTETSPVIT----------------NRVAEKNlagsvGRTARDTEVKIVDPE 308
Cdd:PRK07008 299 VIGGSACPpAMIRTFEDEYGVEVIHAWGMTEMSPLGTlcklkwkhsqlpldeqRKLLEKQ-----GRVIYGVDMKIVGDD 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 309 sGARLP-EGQP-GLVLMRGPQMMAGYKSNaEASKAVldqEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQP 386
Cdd:PRK07008 374 -GRELPwDGKAfGDLQVRGPWVIDRYFRG-DASPLV---DGWFPTGDVATIDA-DGFMQITDRSKDVIK-SGGEWISSID 446
|
170 180 190
....*....|....*....|....*....|....*.
gi 585104306 387 IEDVVCANSAlVDQVMCVGQ-----DEKVLgMLVVP 417
Cdd:PRK07008 447 IENVAVAHPA-VAEAACIACahpkwDERPL-LVVVK 480
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
47-409 |
2.41e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 59.86 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 47 PKDVRSVATLVYTSGTTNKPKGVVLRHSNllhqvnynsftdspskepAYNPVLGDVLVsvlpcWHIFERTAEYW---MFs 123
Cdd:PLN02479 191 PADEWQSIALGYTSGTTASPKGVVLHHRG------------------AYLMALSNALI-----WGMNEGAVYLWtlpMF- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 124 kgihvvYSNVKNFKADLAKHQPQFIVAVPRLLETIYRGVlqkfaaekgAKKKIIEFftrvgsawvkawrVARGLVLRSRA 203
Cdd:PLN02479 247 ------HCNGWCFTWTLAALCGTNICLRQVTAKAIYSAI---------ANYGVTHF-------------CAAPVVLNTIV 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 204 PNPIERLLAlvlalvlsPLAAVgdklvwskvraglggrIKVLVAGGSSMPLVL----EDFFELLRTpvivgYGMTETS-- 277
Cdd:PLN02479 299 NAPKSETIL--------PLPRV----------------VHVMTAGAAPPPSVLfamsEKGFRVTHT-----YGLSETYgp 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 278 -------------PVITN-RVAEKNLAGSVGRTARDtevkIVDPESGARLP-EGQP-GLVLMRGPQMMAGYKSNAEASKA 341
Cdd:PLN02479 350 stvcawkpewdslPPEEQaRLNARQGVRYIGLEGLD----VVDTKTMKPVPaDGKTmGEIVMRGNMVMKGYLKNPKANEE 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585104306 342 VLdQEGFLDTGDLGRIHPlTKHLIITGRAKDtIVLSNGENVEPQPIEDVVCANSALVDQVMCVGQDEK 409
Cdd:PLN02479 426 AF-ANGWFHSGDLGVKHP-DGYIEIKDRSKD-IIISGGENISSLEVENVVYTHPAVLEASVVARPDER 490
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
49-391 |
3.66e-09 |
|
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: 58.80 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 49 DVRSVATLVYTSGTTNKPKGVVLRHSNLLhqvnynSFTDspskepaynpvlgdvlvsvlpcwhifertaeyWM---FSKG 125
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLV------SFTN--------------------------------WMlsdFPLG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 126 IHVVYSNVKNFKADLAKHQ--PQFI-----VAVPRLLETIYRgVLQKFAAEKGakkkiIEFFTRVGSAWvkawrvarGLV 198
Cdd:cd05945 137 PGDVFLNQAPFSFDLSVMDlyPALAsgatlVPVPRDATADPK-QLFRFLAEHG-----ITVWVSTPSFA--------AMC 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 199 LRSRAPNPierllalvlalvlsplaavgdklvwskvrAGLGGRIKVLVAGgssMPLVLEDFFELLR----TPVIVGYGMT 274
Cdd:cd05945 203 LLSPTFTP-----------------------------ESLPSLRHFLFCG---EVLPHKTARALQQrfpdARIYNTYGPT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 275 E-----TSPVITNRVAEKNLAGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLDQ-EGF 348
Cdd:cd05945 251 EatvavTYIEVTPEVLDGYDRLPIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPdEGQ 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 585104306 349 L--DTGDLGRIHPlTKHLIITGRAKDTIVLsNGENVEPQPIEDVV 391
Cdd:cd05945 330 RayRTGDLVRLEA-DGLLFYRGRLDFQVKL-NGYRIELEEIEAAL 372
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
23-476 |
4.29e-09 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 59.28 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 23 PTQVLTFDEALS-ASLARPLTFRPVPKDVRSVATlvYTSGTTNKPKGVVLRHSNLLhqvnynSFTDSPSKEpAYNPVLGD 101
Cdd:PRK06060 118 PSRVAEAAELMSeAARVAPGGYEPMGGDALAYAT--YTSGTTGPPKAAIHRHADPL------TFVDAMCRK-ALRLTPED 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 102 VLVSVLPCWHIFERTAEYWM-FSKGIHVVYSNV---KNFKADL-AKHQPQFIVAVPrlletiyrgvlqkfaaekgakkki 176
Cdd:PRK06060 189 TGLCSARMYFAYGLGNSVWFpLATGGSAVINSApvtPEAAAILsARFGPSVLYGVP------------------------ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 177 iEFFTRV-GSAWVKAWRVARGLVLRSRAPNPierllalvlalvlsplaavgdklvwskvraGLGGRikvlvaggssmplv 255
Cdd:PRK06060 245 -NFFARViDSCSPDSFRSLRCVVSAGEALEL------------------------------GLAER-------------- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 256 LEDFFELLrtPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYKSN 335
Cdd:PRK06060 280 LMEFFGGI--PILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 336 AEaskAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVLSnGENVEPQPIEDVVCANSAlVDQVMCVGQDE----KVL 411
Cdd:PRK06060 357 PD---SPVANEGWLDTRDRVCIDS-DGWVTYRCRADDTEVIG-GVNVDPREVERLIIEDEA-VAEAAVVAVREstgaSTL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 412 GMLVVPNV--------------RALAR--AGLVDRGLA--ERVAELLGGQVLTNGIAGSRAELEEVEASLREKKEVKKAL 473
Cdd:PRK06060 431 QAFLVATSgatidgsvmrdlhrGLLNRlsAFKVPHRFAvvDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSGVRAQ 510
|
...
gi 585104306 474 LAD 476
Cdd:PRK06060 511 RDD 513
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
270-409 |
5.01e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 58.34 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 270 GYGMTET-SPVITNRVAEKNLAGSV--GRtardtEVKIVDPEsgarlpegqpglVLMRGPQMMAGYKSNAEAsKAVLDQE 346
Cdd:PRK09029 270 GYGLTEMaSTVCAKRADGLAGVGSPlpGR-----EVKLVDGE------------IWLRGASLALGYWRQGQL-VPLVNDE 331
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585104306 347 GFLDTGDLGRIHplTKHLIITGRAkDTIVLSNGENVEPQPIEDVVCANSaLVDQVMCVGQDEK 409
Cdd:PRK09029 332 GWFATRDRGEWQ--NGELTILGRL-DNLFFSGGEGIQPEEIERVINQHP-LVQQVFVVPVADA 390
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
15-427 |
8.87e-09 |
|
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: 57.87 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 15 AELANLPPPTQVLTFDEALSASLARPltfrPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNL-LHQVNYNSFTDSPSKep 93
Cdd:TIGR03098 131 AHASEGHPGEEPASWPKLLALGDADP----PHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLvAGAQSVATYLENRPD-- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 94 aynpvlgDVLVSVLPCWHIFERTAEYWMFSKGIHVV---YSNVKNFKADLAKHQPQFIVAVPRLLETIYRGVLQKFAAEK 170
Cdd:TIGR03098 205 -------DRLLAVLPLSFDYGFNQLTTAFYVGATVVlhdYLLPRDVLKALEKHGITGLAAVPPLWAQLAQLDWPESAAPS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 171 gakkkiIEFFTRVGSAWVKAwRVARglvLRSRAPNpierllalvlalvlsplaavgdklvwskvraglggrikvlvaggs 250
Cdd:TIGR03098 278 ------LRYLTNSGGAMPRA-TLSR---LRSFLPN--------------------------------------------- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 251 smplvledffellrTPVIVGYGMTE---TSPVITNRVAEKnlAGSVGRTARDTEVKIVDPESGARLPeGQPGLVLMRGPQ 327
Cdd:TIGR03098 303 --------------ARLFLMYGLTEafrSTYLPPEEVDRR--PDSIGKAIPNAEVLVLREDGSECAP-GEEGELVHRGAL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 328 MMAGYKSNAEASKAVLDQ-EGFLD----------TGDLGRIHPlTKHLIITGRaKDTIVLSNGENVEPQPIEDVVCAnSA 396
Cdd:TIGR03098 366 VAMGYWNDPEKTAERFRPlPPFPGelhlpelavwSGDTVRRDE-EGFLYFVGR-RDEMIKTSGYRVSPTEVEEVAYA-TG 442
|
410 420 430
....*....|....*....|....*....|....*.
gi 585104306 397 LVDQVMCVGQDEKVLG----MLVVPNVRA-LARAGL 427
Cdd:TIGR03098 443 LVAEAVAFGVPDPTLGqaivLVVTPPGGEeLDRAAL 478
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
271-416 |
1.87e-08 |
|
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: 56.26 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 271 YGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDPESGARlpegqpGLVLMRGPQMMAGYKSNAEASKavldqEGFLD 350
Cdd:cd17633 143 YGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYVRGGFSNP-----DGWMS 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585104306 351 TGDLGRIHPlTKHLIITGRAKDTIVLSnGENVEPQPIEDVVCANSAlVDQVMCVGQDEKVLGMLVV 416
Cdd:cd17633 212 VGDIGYVDE-EGYLYLVGRESDMIIIG-GINIFPTEIESVLKAIPG-IEEAIVVGIPDARFGEIAV 274
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
244-416 |
2.62e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 56.16 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 244 VLVAGGSSMPLVLEDFFELlRTPVIVGYGMTETSPVITNRVAEKNLAG--SVGRtardtevkiVDPESGARLPEGQPGLV 321
Cdd:PRK07445 235 ILLGGAPAWPSLLEQARQL-QLRLAPTYGMTETASQIATLKPDDFLAGnnSSGQ---------VLPHAQITIPANQTGNI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 322 LMRGPQMMAGYKSNAeaskavLDQEGFLDTGDLGRIHPlTKHLIITGRAKDTIvLSNGENVEPQPIEDVVCAnSALVDQV 401
Cdd:PRK07445 305 TIQAQSLALGYYPQI------LDSQGIFETDDLGYLDA-QGYLHILGRNSQKI-ITGGENVYPAEVEAAILA-TGLVQDV 375
|
170
....*....|....*
gi 585104306 402 MCVGQDEKVLGMLVV 416
Cdd:PRK07445 376 CVLGLPDPHWGEVVT 390
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
15-401 |
2.66e-08 |
|
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: 56.12 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 15 AELANLPPPTQVLTFDEALSASLARPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVNYNS---FTDSPSK 91
Cdd:TIGR01733 84 SRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLArryGLDPDDR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 92 EPAYNPVLGDVLVsvlpcWHIFerTAeyWMFSKGIHVVYSNVKNFKADL-----AKHQPQFIVAVPrlletiyrGVLQKF 166
Cdd:TIGR01733 164 VLQFASLSFDASV-----EEIF--GA--LLAGATLVVPPEDEERDDAALlaaliAEHPVTVLNLTP--------SLLALL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 167 AAEKGAKKKIIEFFTRVGSAwVKAWRVARglvLRSRAPNpierllalvlalvlsplaavgdklvwskvraglggrikvlv 246
Cdd:TIGR01733 227 AAALPPALASLRLVILGGEA-LTPALVDR---WRARGPG----------------------------------------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 247 aggssmplvledffellrTPVIVGYGMTETSPVITNR-----VAEKNLAGSVGRTARDTEVKIVDPEsGARLPEGQPGLV 321
Cdd:TIGR01733 262 ------------------ARLINLYGPTETTVWSTATlvdpdDAPRESPVPIGRPLANTRLYVLDDD-LRPVPVGVVGEL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 322 LMRGPQMMAGYKSNAEASKAVL--------DQEGFLDTGDLGRIHPlTKHLIITGRAkDTIVLSNGENVEPQPIEDVVCA 393
Cdd:TIGR01733 323 YIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLP-DGNLEFLGRI-DDQVKIRGYRIELGEIEAALLR 400
|
....*...
gi 585104306 394 NSAlVDQV 401
Cdd:TIGR01733 401 HPG-VREA 407
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
270-388 |
3.31e-08 |
|
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: 55.39 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 270 GYGMTETS-PVITNRVAEKNlAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRGPQMMAGYkSNAEASKAVLDQEGF 348
Cdd:cd17636 142 GYGQTEVMgLATFAALGGGA-IGGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGY-WNRPEVNARRTRGGW 218
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 585104306 349 LDTGDLGRIHPlTKHLIITGrAKDTIVLSNGENVEPQPIE 388
Cdd:cd17636 219 HHTNDLGRREP-DGSLSFVG-PKTRMIKSGAENIYPAEVE 256
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
292-398 |
4.45e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 55.90 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 292 SVGRTARDTEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVL------------------DQEGFLDTGD 353
Cdd:PRK12476 403 SCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaaDDGTWLRTGD 482
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 585104306 354 LGRIhpLTKHLIITGRAKDTIVLsNGENVEPQPIEDVVCANSALV 398
Cdd:PRK12476 483 LGVY--LDGELYITGRIADLIVI-DGRNHYPQDIEATVAEASPMV 524
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
244-440 |
4.61e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 55.05 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 244 VLVaGGSSMPLVLEDFFELLRTPVIVGYGMTETSpvitnrvaeknlAGSV--GRTARDTEVKIVDpesgarlpegqpGLV 321
Cdd:PRK07824 156 VLV-GGGPAPAPVLDAAAAAGINVVRTYGMSETS------------GGCVydGVPLDGVRVRVED------------GRI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 322 LMRGPQMMAGYKsNAEASKAvLDQEGFLDTGDLGRIHplTKHLIITGRAkDTIVLSNGENVEPQPIEDVVCANSAlVDQV 401
Cdd:PRK07824 211 ALGGPTLAKGYR-NPVDPDP-FAEPGWFRTDDLGALD--DGVLTVLGRA-DDAISTGGLTVLPQVVEAALATHPA-VADC 284
|
170 180 190
....*....|....*....|....*....|....*....
gi 585104306 402 MCVGQDEKVLGMLVVPNVRALARAGLVDRGLAERVAELL 440
Cdd:PRK07824 285 AVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTL 323
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
52-440 |
8.55e-08 |
|
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: 54.62 E-value: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 52 SVATLVYTSGTTNKPKGVVLRHSNLLHqvnynsftdspskepaynpvlgdvLVSVLPCWHIFERTAEYWMFskgihvvys 131
Cdd:cd17643 94 DLAYVIYTSGSTGRPKGVVVSHANVLA------------------------LFAATQRWFGFNEDDVWTLF--------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 132 nvknfkadlakHQPQFIVAVPRLLetiyrGVLQKfaaekGAKKKIIEFFTRVGSAWVKAWRVARGLVLRSRAPNPIERLL 211
Cdd:cd17643 141 -----------HSYAFDFSVWEIW-----GALLH-----GGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 212 ALVLALVLSPLAavgdklvwskvraglggrIKVLVAGGSSMPL-VLEDFFE---LLRTPVIVGYGMTETSPVITNRV--- 284
Cdd:cd17643 200 EAADRDGRDPLA------------------LRYVIFGGEALEAaMLRPWAGrfgLDRPQLVNMYGITETTVHVTFRPlda 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 285 --AEKNLAGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGY--KSNAEASKAVLDQEG-----FLDTGDLG 355
Cdd:cd17643 262 adLPAAAASPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYlgRPELTAERFVANPFGgpgsrMYRTGDLA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 356 RIHPlTKHLIITGRAkDTIVLSNGENVEPQPIEDVVCANSALVDQVMCVGQDE---KVLGMLVVPNvralARAGLVDRGL 432
Cdd:cd17643 341 RRLP-DGELEYLGRA-DEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEpgdTRLVAYVVAD----DGAAADIAEL 414
|
....*...
gi 585104306 433 AERVAELL 440
Cdd:cd17643 415 RALLKELL 422
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
261-440 |
9.36e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 54.38 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 261 ELLRTPVIVGYGMTETSPVITNRVAEKNlaGSVGRtardtE----VKIVDPESGARLPEGQPG-LVLmrgpqmmagyksn 335
Cdd:COG1541 225 ERWGIKAYDIYGLTEVGPGVAYECEAQD--GLHIW-----EdhflVEIIDPETGEPVPEGEEGeLVV------------- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 336 aeaskAVLDQEGF----LDTGDLGRIHP--------LTKHLIITGRAKDTIVLsNGENVEPQPIEDVVCANSALVDQVMC 403
Cdd:COG1541 285 -----TTLTKEAMplirYRTGDLTRLLPepcpcgrtHPRIGRILGRADDMLII-RGVNVFPSQIEEVLLRIPEVGPEYQI 358
|
170 180 190
....*....|....*....|....*....|....*..
gi 585104306 404 VGQDEKVLGMLVvpnVRALARAGLVDRGLAERVAELL 440
Cdd:COG1541 359 VVDREGGLDELT---VRVELAPGASLEALAEAIAAAL 392
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
245-399 |
1.00e-07 |
|
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: 54.39 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 245 LVAGGSSMPLVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMR 324
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 325 -GPQ----MMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDtIVLSNGENVEPQPIEDVVCANSALVD 399
Cdd:cd05928 376 vKPIrpfgLFSGYVDNPEKTAATI-RGDFYLTGDRGIMDE-DGYFWFMGRADD-VINSSGYRIGPFEVESALIEHPAVVE 452
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
267-418 |
2.69e-07 |
|
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: 52.93 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 267 VIVGYGMTETSP-VITNRVAEKNLAGSVGRTArDTEVKIVDPESGARL-PEGQPGLVLMRGPQMMAGYKSNAEASKAV-- 342
Cdd:cd05918 241 LINAYGPAECTIaATVSPVVPSTDPRNIGRPL-GATCWVVDPDNHDRLvPIGAVGELLIEGPILARGYLNDPEKTAAAfi 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 343 -----LDQEGFLD------TGDLGRIHPlTKHLIITGRaKDTIVLSNGENVEPQPIEDVV--CANSALVDQVMCV----G 405
Cdd:cd05918 320 edpawLKQEGSGRgrrlyrTGDLVRYNP-DGSLEYVGR-KDTQVKIRGQRVELGEIEHHLrqSLPGAKEVVVEVVkpkdG 397
|
170
....*....|...
gi 585104306 406 QDEKVLGMLVVPN 418
Cdd:cd05918 398 SSSPQLVAFVVLD 410
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
270-371 |
4.04e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.05 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 270 GYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKiVDP----ESGARLpegqpglvLMRGPQMMAGYksnAEASK-AVLD 344
Cdd:PRK06814 938 GYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYR-LEPvpgiDEGGRL--------FVRGPNVMLGY---LRAENpGVLE 1005
|
90 100
....*....|....*....|....*....
gi 585104306 345 --QEGFLDTGDLGRIHPLtKHLIITGRAK 371
Cdd:PRK06814 1006 ppADGWYDTGDIVTIDEE-GFITIKGRAK 1033
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
37-391 |
6.84e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.87 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 37 LARPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNL---LHQVNYNSFTDSPSKEPaynpvLGDVLVSVLPCWHif 113
Cdd:PRK05850 146 LDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVianFEQLMSDYFGDTGGVPP-----PDTTVVSWLPFYH-- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 114 ertaeywmfskgihvvysnvknfkaDLAkhqpqFIVAV--PRLLEtiYRGVLQKFAAekgakkkiiefFTRVGSAWVKAw 191
Cdd:PRK05850 219 -------------------------DMG-----LVLGVcaPILGG--CPAVLTSPVA-----------FLQRPARWMQL- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 192 rVARGLVLRSRAPN-PIErllalvlalvlspLAAvgdklvwSKVR----AGLG-GRIKVLVAGGSSM-PLVLEDF----- 259
Cdd:PRK05850 255 -LASNPHAFSAAPNfAFE-------------LAV-------RKTSdddmAGLDlGGVLGIISGSERVhPATLKRFadrfa 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 260 -FELLRTPVIVGYGMTE-----------TSPVITNRVAEKNLAGSVGRTA-------------RDTEVKIVDPESGARLP 314
Cdd:PRK05850 314 pFNLRETAIRPSYGLAEatvyvatrepgQPPESVRFDYEKLSAGHAKRCEtgggtplvsygspRSPTVRIVDPDTCIECP 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 315 EGQPGLVLMRGPQMMAGYKSNAEASK----AVLDQ------EG-FLDTGDLGRIHplTKHLIITGRAKDTIVLsNGENVE 383
Cdd:PRK05850 394 AGTVGEIWVHGDNVAAGYWQKPEETErtfgATLVDpspgtpEGpWLRTGDLGFIS--EGELFIVGRIKDLLIV-DGRNHY 470
|
....*...
gi 585104306 384 PQPIEDVV 391
Cdd:PRK05850 471 PDDIEATI 478
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
17-80 |
7.15e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 52.47 E-value: 7.15e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585104306 17 LANLPPPTQV--LTFDEALSASLARPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQV 80
Cdd:PRK12467 620 LAQLPVPAGLrsLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYV 685
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
300-430 |
8.82e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 51.69 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 300 TEVKIVDPESGARLPEGQPGLVLMRGPQMMAGYKSNAEaskavLDQEGFLDTGDLGRIhpLTKHLIITGRAKDTIVLSnG 379
Cdd:PRK05851 354 MEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL--VDGGLVVCGRAKELITVA-G 425
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585104306 380 ENVEPQPIEDVvcanSALVD-----QVMCVGQDEKVL--GMLVVPNVR----ALARAGLVDR 430
Cdd:PRK05851 426 RNIFPTEIERV----AAQVRgvregAVVAVGTGEGSArpGLVIAAEFRgpdeAGARSEVVQR 483
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
256-402 |
9.64e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 51.61 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 256 LEDFFELLRTPVIVGYGMTETSPVITNrvAEKNLAGSVGRTARDteVKIVDPESGARLPEGQPG-------------LVL 322
Cdd:PRK07867 282 IARFARRFGCVVVDGFGSTEGGVAITR--TPDTPPGALGPLPPG--VAIVDPDTGTECPPAEDAdgrllnadeaigeLVN 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 323 MRGPQMMAGYKSNAEASKAVLdQEGFLDTGDL------GRIHpltkhliITGRAKDTIVLsNGENVEPQPIEDVVC---- 392
Cdd:PRK07867 358 TAGPGGFEGYYNDPEADAERM-RGGVYWSGDLayrdadGYAY-------FAGRLGDWMRV-DGENLGTAPIERILLrypd 428
|
170
....*....|....*....
gi 585104306 393 ANSALV---------DQVM 402
Cdd:PRK07867 429 ATEVAVyavpdpvvgDQVM 447
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
58-441 |
1.03e-06 |
|
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: 51.22 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 58 YTSGTTNKPKGVVLRHSNLLHqvnynsftdspSKEPAYNPVLG----DVLVSVLPCWHIFER-TAEYWMFSKGIHVV--- 129
Cdd:cd05959 170 YSSGSTGRPKGVVHLHADIYW-----------TAELYARNVLGiredDVCFSAAKLFFAYGLgNSLTFPLSVGATTVlmp 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 130 -YSNVKNFKADLAKHQPQFIVAVPrlleTIYRGVLqkfaaekgakkkiiefftrvgsawvkawrvarglvlrsRAPNPIE 208
Cdd:cd05959 239 eRPTPAAVFKRIRRYRPTVFFGVP----TLYAAML--------------------------------------AAPNLPS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 209 RLLAlvlalvlsplaavgdklvwskvraglggRIKVLVAGGSSMPL-VLEDFFELLRTPVIVGYGMTETSPV-ITNRVAE 286
Cdd:cd05959 277 RDLS----------------------------SLRLCVSAGEALPAeVGERWKARFGLDILDGIGSTEMLHIfLSNRPGR 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 287 KNLaGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPLTKHLII 366
Cdd:cd05959 329 VRY-GTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYA 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 367 tGRAKDTIVLSnGENVEPQPIEDVVCANSAlVDQVMCVGQDEKVlGML-----VVPNVRALARAGLvDRGLAERVAELLG 441
Cdd:cd05959 406 -GRADDMLKVS-GIWVSPFEVESALVQHPA-VLEAAVVGVEDED-GLTkpkafVVLRPGYEDSEAL-EEELKEFVKDRLA 480
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
246-399 |
1.22e-06 |
|
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: 50.96 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 246 VAGGSSMPLVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVLMRG 325
Cdd:cd05970 308 TAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRT 386
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585104306 326 PQ-----MMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDtIVLSNGENVEPQPIEDVVCANSALVD 399
Cdd:cd05970 387 SKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDE-DGYLWFVGRTDD-LIKSSGYRIGPFEVESALIQHPAVLE 462
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
242-415 |
1.26e-06 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 51.16 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 242 IKVLVAGGSSMPLVLEDFFEL--LRTPVIvgYGMTETS------PVITNRVAeKNLAGSVGRTARDTEVKIVDPESGA-R 312
Cdd:PRK05857 288 LRLVGYGGSRAIAADVRFIEAtgVRTAQV--YGLSETGctalclPTDDGSIV-KIEAGAVGRPYPGVDVYLAATDGIGpT 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 313 LPEGQP----GLVLMRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIe 388
Cdd:PRK05857 365 APGAGPsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERRE-DGFFYIKGRSSEMII-CGGVNIAPDEV- 440
|
170 180
....*....|....*....|....*..
gi 585104306 389 DVVCANSALVDQVMCVGQDEKVLGMLV 415
Cdd:PRK05857 441 DRIAEGVSGVREAACYEIPDEEFGALV 467
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
44-438 |
1.39e-06 |
|
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: 50.81 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 44 RPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQVNYnsftdspsKEPAYNPVLGDvlvsvlpcwhifeRTAEYWMFS 123
Cdd:cd17651 129 PDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAW--------QARASSLGPGA-------------RTLQFAGLG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 124 kgihvvysnvknfkadlakhqpqFIVAVPRLLETI-YRGVLQKFAAEkgakkkiieffTRVGSAWVKAWRVARGLVlRSR 202
Cdd:cd17651 188 -----------------------FDVSVQEIFSTLcAGATLVLPPEE-----------VRTDPPALAAWLDEQRIS-RVF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 203 APNPIERLlalvlalvlspLAAVGDKLvwskvrAGLGGRIKVLVAGGSSMPLV--LEDFFELLRTP-VIVGYGMTETSPV 279
Cdd:cd17651 233 LPTVALRA-----------LAEHGRPL------GVRLAALRYLLTGGEQLVLTedLREFCAGLPGLrLHNHYGPTETHVV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 280 ----ITNRVAEKNLAGSVGRTARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAGYKSNAE--ASKAVLDQEG----FL 349
Cdd:cd17651 296 talsLPGDPAAWPAPPPIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPEltAERFVPDPFVpgarMY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 350 DTGDLGRIHPlTKHLIITGRAKDTIVLsNGENVEPQPIEDVVCANSALVDQVMCV---GQDEKVLGMLVVPNVRALARAG 426
Cdd:cd17651 375 RTGDLARWLP-DGELEFLGRADDQVKI-RGFRIELGEIEAALARHPGVREAVVLAredRPGEKRLVAYVVGDPEAPVDAA 452
|
410
....*....|..
gi 585104306 427 LVDRGLAERVAE 438
Cdd:cd17651 453 ELRAALATHLPE 464
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
28-379 |
4.44e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 49.51 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 28 TFDEALSASLARPLTFRPVPKDvrSVATLVYTSGTTNKPKGVVLRHSNLLHQVNY--NSF------TDSPSKePA---YN 96
Cdd:PRK09274 153 TLATLLRDGAAAPFPMADLAPD--DMAAILFTSGSTGTPKGVVYTHGMFEAQIEAlrEDYgiepgeIDLPTF-PLfalFG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 97 PVLGdvLVSVLPCwhifertaeywM-FSKGIhvvysnvknfKADlakhqPQFIVAVprlletIYR-GVLQKFAAekgakK 174
Cdd:PRK09274 230 PALG--MTSVIPD-----------MdPTRPA----------TVD-----PAKLFAA------IERyGVTNLFGS-----P 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 175 KIIEFFTRVGsawvkawrVARGLVLRSrapnpierllalvlalvlsplaavgdklvwskVRaglggriKVLVAGGSSMPL 254
Cdd:PRK09274 271 ALLERLGRYG--------EANGIKLPS--------------------------------LR-------RVISAGAPVPIA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 255 VLEDFFELLR--TPVIVGYGMTETSPVIT---------NRVAEKNLAGS-VGRTARDTEVKIVDPESGA--------RLP 314
Cdd:PRK09274 304 VIERFRAMLPpdAEILTPYGATEALPISSiesreilfaTRAATDNGAGIcVGRPVDGVEVRIIAISDAPipewddalRLA 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585104306 315 EGQPGLVLMRGPQMMAGYKSNAEASKA--VLDQEG--FLDTGDLGRIHPlTKHLIITGRAKDTIVLSNG 379
Cdd:PRK09274 384 TGEIGEIVVAGPMVTRSYYNRPEATRLakIPDGQGdvWHRMGDLGYLDA-QGRLWFCGRKAHRVETAGG 451
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
242-409 |
7.76e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 48.45 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 242 IKVLVAGGSSM-PLVLEDFFELLRTPVIVGYGMTETSPVITNRVAE-KNLAGSVGRTARDTEVKIVDPES---GARLPeg 316
Cdd:PRK13383 294 LRVVMSSGDRLdPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADlRDAPETVGKPVAGCPVRILDRNNrpvGPRVT-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 317 qpGLVLMRGPQMMAGYKSNAeaSKAVLDqeGFLDTGDLGRIHPlTKHLIITGRAKDTIVlSNGENVEPQPIEDVVCANSA 396
Cdd:PRK13383 372 --GRIFVGGELAGTRYTDGG--GKAVVD--GMTSTGDMGYLDN-AGRLFIVGREDDMII-SGGENVYPRAVENALAAHPA 443
|
170
....*....|...
gi 585104306 397 LVDQVMCVGQDEK 409
Cdd:PRK13383 444 VADNAVIGVPDER 456
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
243-426 |
1.72e-05 |
|
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: 47.18 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 243 KVLVAGGSSMPLVLEDFFELLRTPVIVGYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDPEsGARLPEGQPGLVL 322
Cdd:cd05974 204 EVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPD-GAPATEGEVALDL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 323 --MRGPQMMAGYKSNAEASKAVLdQEGFLDTGDLGRiHPLTKHLIITGRAKDtIVLSNGENVEPQPIEDVVCANSALVDQ 400
Cdd:cd05974 283 gdTRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAM-RDEDGYLTYVGRADD-VFKSSDYRISPFELESVLIEHPAVAEA 359
|
170 180
....*....|....*....|....*.
gi 585104306 401 VMCVGQDEKvlgMLVVPNVRALARAG 426
Cdd:cd05974 360 AVVPSPDPV---RLSVPKAFIVLRAG 382
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
245-412 |
4.40e-05 |
|
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: 46.27 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 245 LVAGGSSMPLVLEDFFELLRTPVIVGYGMTETSPVIT--------NRVAEKNlagSVGRTARD------TEVKIVDPESG 310
Cdd:cd05915 275 LVVGGSAAPRSLIARFERMGVEVRQGYGLTETSPVVVqnfvkshlESLSEEE---KLTLKAKTglpiplVRLRVADEEGR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 311 ARLPEGQP-GLVLMRGPQMMAGYKSNAEASKAVLDQEGFLDTGDLGRIHPlTKHLIITGRAKDtIVLSNGENVEPQPIED 389
Cdd:cd05915 352 PVPKDGKAlGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDE-EGYVEIKDRLKD-LIKSGGEWISSVDLEN 429
|
170 180
....*....|....*....|...
gi 585104306 390 VVCANSALVDQVMcVGQDEKVLG 412
Cdd:cd05915 430 ALMGHPKVKEAAV-VAIPHPKWQ 451
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
235-440 |
8.56e-05 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 44.96 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 235 RAGLGGRIKVLVAGGSSMPL-VLEDFFELLRTPVIVGYGMTETSPVITN-RVAEKNLAGSV--GRTARDTEVKIVDpESG 310
Cdd:cd17646 248 AAGSCASLRRVFCSGEALPPeLAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVPNTRLYVLD-DAL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 311 ARLPEGQPGLVLMRGPQMMAGYKSNAE--ASKAVLDQEG----FLDTGDLGRIHPlTKHLIITGRAKDTIVLsNGENVEP 384
Cdd:cd17646 327 RPVPVGVPGELYLGGVQLARGYLGRPAltAERFVPDPFGpgsrMYRTGDLARWRP-DGALEFLGRSDDQVKI-RGFRVEP 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 585104306 385 QPIEDVVCANSALVDQVMCVGQDEKVLGMLVVPNVRALARAGLVDRGLAERVAELL 440
Cdd:cd17646 405 GEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAALRAHLAERL 460
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
17-78 |
1.27e-04 |
|
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: 44.85 E-value: 1.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585104306 17 LANLPPPT-QVLTFDEALSAslARPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLH 78
Cdd:COG1020 584 AARLPELGvPVLALDALALA--AEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVN 644
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
31-79 |
1.38e-04 |
|
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: 44.59 E-value: 1.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 585104306 31 EALSASLARPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQ 79
Cdd:cd12116 106 LLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
271-390 |
2.46e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 43.53 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 271 YGMTETSPViTNRVAEKNLA--GSVGRtARDTEVKIVDpESGARLPEGQPGLVLMRGPQMMAgYKSNAEASKAVLDQEGF 348
Cdd:PRK13391 307 YAATEGLGF-TACDSEEWLAhpGTVGR-AMFGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGT 382
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 585104306 349 LDT-GDLGRIHPlTKHLIITGRAKDTIvLSNGENVEPQPIEDV 390
Cdd:PRK13391 383 WSTvGDIGYVDE-DGYLYLTDRAAFMI-ISGGVNIYPQEAENL 423
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
52-76 |
3.42e-04 |
|
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: 43.30 E-value: 3.42e-04
10 20
....*....|....*....|....*
gi 585104306 52 SVATLVYTSGTTNKPKGVVLRHSNL 76
Cdd:cd05918 107 DAAYVIFTSGSTGKPKGVVIEHRAL 131
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
18-87 |
4.62e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 42.96 E-value: 4.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585104306 18 ANLPP---PTQVLTFDEaLSASLARPLTF---RPVPKDvrSVATLVYTSGTTNKPKGVVLRHSNLLhqvnynSFTD 87
Cdd:PRK04813 107 EELPLeilGIPVITLDE-LKDIFATGNPYdfdHAVKGD--DNYYIIFTSGTTGKPKGVQISHDNLV------SFTN 173
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
45-80 |
5.07e-04 |
|
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: 42.70 E-value: 5.07e-04
10 20 30
....*....|....*....|....*....|....*.
gi 585104306 45 PVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLHQV 80
Cdd:cd17655 131 EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLV 166
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
18-73 |
5.57e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 42.86 E-value: 5.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 585104306 18 ANLPPPTQVLTFDEALSASLARPLTFRPVPKDvrsvATL--VYTSGTTNKPKGVVLRH 73
Cdd:PRK03584 232 AAAAALPGALLWEDFLAPAEAAELEFEPVPFD----HPLwiLYSSGTTGLPKCIVHGH 285
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-76 |
5.62e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 43.02 E-value: 5.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585104306 15 AELANLPPPTQVLTFDEA---LSASLARPLTFRPVPKDVrsvATLVYTSGTTNKPKGVVLRHSNL 76
Cdd:PRK12316 619 GRKLPLAAGVQVLDLDRPaawLEGYSEENPGTELNPENL---AYVIYTSGSTGKPKGAGNRHRAL 680
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
243-393 |
7.62e-04 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 42.03 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 243 KVLVAGGSSM-PLVLEDFFELLRTPVIVG-YGMTETSPVITNRVAEKNLAGSVGRTA-----------------RDTEVK 303
Cdd:cd05937 203 KVRVAWGNGLrPDIWERFRERFNVPEIGEfYAATEGVFALTNHNVGDFGAGAIGHHGlirrwkfenqvvlvkmdPETDDP 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 304 IVDPESG--ARLPEGQPGLVLMRGP----QMMAGYKSNAEA--SKAVLD--QEG--FLDTGDL------GRIHPLTKhLI 365
Cdd:cd05937 283 IRDPKTGfcVRAPVGEPGEMLGRVPfknrEAFQGYLHNEDAteSKLVRDvfRKGdiYFRTGDLlrqdadGRWYFLDR-LG 361
|
170 180
....*....|....*....|....*...
gi 585104306 366 ITGRAKdtivlsnGENVEPQPIEDVVCA 393
Cdd:cd05937 362 DTFRWK-------SENVSTTEVADVLGA 382
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
245-399 |
1.40e-03 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 41.31 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 245 LVAGGSSMPLVLEDFFE-LLRTPVIVGYGMTETSPVITNRVAEKNLAG--------SVGRTARDTEVKIVDPESGARLPE 315
Cdd:PRK05620 303 IYVGGSAVPPILIKAWEeRYGVDVVHVWGMTETSPVGTVARPPSGVSGearwayrvSQGRFPASLEYRIVNDGQVMESTD 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 316 GQPGLVLMRGPQMMAGY------KSNAEAS----KAVLD------QEGFLDTGDLGRIhplTK--HLIITGRAKDTIvLS 377
Cdd:PRK05620 383 RNEGEIQVRGNWVTASYyhspteEGGGAAStfrgEDVEDandrftADGWLRTGDVGSV---TRdgFLTIHDRARDVI-RS 458
|
170 180
....*....|....*....|..
gi 585104306 378 NGENVEPQPIEDVVCANSALVD 399
Cdd:PRK05620 459 GGEWIYSAQLENYIMAAPEVVE 480
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
15-73 |
1.54e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 1.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 585104306 15 AELANLP--PPTQVLTFDEALSASLARPLTfRPVPKDVrsvATLVYTSGTTNKPKGVVLRH 73
Cdd:PRK10252 564 DQLPRFAdvPDLTSLCYNAPLAPQGAAPLQ-LSQPHHT---AYIIFTSGSTGRPKGVMVGQ 620
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
53-80 |
1.60e-03 |
|
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: 40.91 E-value: 1.60e-03
10 20
....*....|....*....|....*...
gi 585104306 53 VATLVYTSGTTNKPKGVVLRHSNLLHQV 80
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHRNVAHAA 122
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
56-82 |
1.99e-03 |
|
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: 40.92 E-value: 1.99e-03
10 20
....*....|....*....|....*..
gi 585104306 56 LVYTSGTTNKPKGVVLRHSNLLHQVNY 82
Cdd:cd17656 133 IIYTSGTTGKPKGVQLEHKNMVNLLHF 159
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
17-77 |
3.18e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 40.53 E-value: 3.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585104306 17 LANLPPPT--QVLTFDEALSASLARPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLL 77
Cdd:PRK12467 1682 QARLPLPDglRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALV 1744
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
32-73 |
3.29e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.54 E-value: 3.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 585104306 32 ALSASLARPLTFRPVPkdvRSVATLVYTSGTTNKPKGVVLRH 73
Cdd:PRK05691 2317 ALAAYSDAPLPFLSLP---QHQAYLIYTSGSTGKPKGVVVSH 2355
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
270-371 |
3.33e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 40.08 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585104306 270 GYGMTETSPVITNRVAEKNLAGSVGRTARDTEVKIVDP---ESGARLPegqpglvlMRGPQMMAGY----------KSNA 336
Cdd:PRK08043 510 GYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVpgiEQGGRLQ--------LKGPNIMNGYlrvekpgvleVPTA 581
|
90 100 110
....*....|....*....|....*....|....*
gi 585104306 337 EASKAVLDQeGFLDTGDLGRIHPlTKHLIITGRAK 371
Cdd:PRK08043 582 ENARGEMER-GWYDTGDIVRFDE-QGFVQIQGRAK 614
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
21-74 |
4.04e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 39.87 E-value: 4.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 585104306 21 PPPTQVLTFDEALSASLARPLTFRPVPKDVrsvaTLVYTSGTTNKPKGVVLRHS 74
Cdd:PRK07798 137 DLLPGAVDYEDALAAGSPERDFGERSPDDL----YLLYTGGTTGMPKGVMWRQE 186
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
18-86 |
5.27e-03 |
|
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: 39.49 E-value: 5.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585104306 18 ANLPPPTQVLTFDEALSASLARPLtfrPVPKDVRSVATLVYTSGTTNKPKGVVLRHSN---LLHQVNYNSFT 86
Cdd:cd12117 106 GRAGGLEVAVVIDEALDAGPAGNP---AVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGvvrLVKNTNYVTLG 174
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
44-78 |
5.60e-03 |
|
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: 39.31 E-value: 5.60e-03
10 20 30
....*....|....*....|....*....|....*
gi 585104306 44 RPVPKDVRSVATLVYTSGTTNKPKGVVLRHSNLLH 78
Cdd:cd17648 87 RVVITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVN 121
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
26-82 |
8.45e-03 |
|
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: 38.80 E-value: 8.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 585104306 26 VLTFDEALSASLARPLTFRPVPKDVrsvATLVYTSGTTNKPKGVVLRHSNLlhqVNY 82
Cdd:cd17646 116 ALLGDEALAAPPATPPLVPPRPDNL---AYVIYTSGSTGRPKGVMVTHAGI---VNR 166
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
15-73 |
9.89e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 38.72 E-value: 9.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 585104306 15 AELANLPPPTqvLTFDEALSASlarPLTFRPVPKDVRSVATLVYTSGTTNKPKGVVLRH 73
Cdd:PRK04319 174 GEDVEEGPGT--LDFNALMEQA---SDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVH 227
|
|
| |
