|
Name |
Accession |
Description |
Interval |
E-value |
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
12-600 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 791.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 12 IDGADTVVKLWAAKCAERGDATAHREKDFGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAIS 91
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 92 AAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVENDEQLDKYLEVQDRVPTIVKVIVFDPKGLRDfsHPKVMFLSDLYEIG 171
Cdd:COG1022 87 AAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGLRD--DPRLLSLDELLALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 172 EKAPDAAErFRIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSV 251
Cdd:COG1022 165 REVADPAE-LEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 252 eFPIAVGSTVNFAESPDTVFDNLREVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASG----AAKLEGKG- 326
Cdd:COG1022 244 -YALAAGATVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGrryaRARLAGKSp 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 327 ----GAMHAVWDFLVLRNIRQMIGfDRNRRSNTGAAPISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIG 402
Cdd:COG1022 323 slllRLKHALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 403 CALPATELRIAENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAE 481
Cdd:COG1022 402 PPLPGVEVKIAEDGEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 482 IESRLKFSPFISDAVVIGDRRKYLTVLIMIDQENVEKYAQDHQIPFSDFASLTRAPQVVDLIDGVVREVNTHFAQVEQIK 561
Cdd:COG1022 482 IENALKASPLIEQAVVVGDGRPFLAALIVPDFEALGEWAEENGLPYTSYAELAQDPEVRALIQEEVDRANAGLSRAEQIK 561
|
570 580 590
....*....|....*....|....*....|....*....
gi 1821015446 562 YFRLIDILLTAEDDELTPTMKLKRGFVEKKHAALIDQMY 600
Cdd:COG1022 562 RFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALY 600
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
41-588 |
0e+00 |
|
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: 520.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 41 GIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAF 120
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 121 LFVENdeqldkylevqdrvptivkvivfdpkglrdfshpkvmflsdlyeigekapdaaerfrieinasqPEDTRMLIYTS 200
Cdd:cd05907 81 LFVED----------------------------------------------------------------PDDLATIIYTS 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 201 GTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPDTVFDNLREVSPH 280
Cdd:cd05907 97 GTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLSEVRPT 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 281 VFTAVPRLWEKIYSRvlIMRSEATPFGRWAFDRAmasgaaklegkggamhavwdflVLRNIRQMIgfdrnrrsnTGAAPI 360
Cdd:cd05907 177 VFLAVPRVWEKVYAA--IKVKAVPGLKRKLFDLA----------------------VGGRLRFAA---------SGGAPL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 361 SPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIAENGEICLKGPNVFKGYWRKPEKTAEDI 440
Cdd:cd05907 224 PAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADDGEILVRGPNVMLGYYKNPEATAEAL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 441 -RDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFSPFISDAVVIGDRRKYLTVLIMIDQENVEKY 519
Cdd:cd05907 304 dADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPEALEAW 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821015446 520 AQDHQIPFSDFASLTRAPQVVDLIDGVVREVNTHFAQVEQIKYFRLIDILLTAEDDELTPTMKLKRGFV 588
Cdd:cd05907 384 AEEHGIAYTDVAELAANPAVRAEIEAAVEAANARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
36-592 |
1.66e-178 |
|
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: 516.98 E-value: 1.66e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 36 REKDFGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLIND 115
Cdd:cd17641 2 REKDFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 116 SGSAFLFVENDEQLDKYLEVQDRVPTIVKVIVFDPKGLRDFSHPKVMFLSDLYEIGEKA----PDAAERfriEINASQPE 191
Cdd:cd17641 82 TGARVVIAEDEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALdrrdPGLYER---EVAAGKGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 192 DTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGqqvLRVDPK---DEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPD 268
Cdd:cd17641 159 DVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAY---LAADPLgpgDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 269 TVFDNLREVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASGAAKLE-GKGGAMHAVW--------DFLVLR 339
Cdd:cd17641 236 TMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDrGKRGRPVSLWlrlaswlaDALLFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 340 NIRQMIGFDRNRRSNTGAAPISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIAENGEIC 419
Cdd:cd17641 316 PLRDRLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEVGEIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 420 LKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:cd17641 396 VRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 499 GDRRKYLTVLIMIDQENVEKYAQDHQIPFSDFASLTRAPQVVDLIDGVVREVNTHFAQVEQIKYFRLIDILLTAEDDELT 578
Cdd:cd17641 476 GAGRPYLTAFICIDYAIVGKWAEQRGIAFTTYTDLASRPEVYELIRKEVEKVNASLPEAQRIRRFLLLYKELDADDGELT 555
|
570
....*....|....
gi 1821015446 579 PTMKLKRGFVEKKH 592
Cdd:cd17641 556 RTRKVRRGVIAEKY 569
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
43-600 |
2.16e-135 |
|
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: 407.51 E-value: 2.16e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 43 WQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLF 122
Cdd:cd05933 6 WHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 123 VENDEQLDKYLEVQDRVPTIVKVIVF--DPKGLRdfshPKVMFLSDLYEIGEKAPDAAERFRIEinASQPEDTRMLIYTS 200
Cdd:cd05933 86 VENQKQLQKILQIQDKLPHLKAIIQYkePLKEKE----PNLYSWDEFMELGRSIPDEQLDAIIS--SQKPNQCCTLIYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 201 GTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQ----LCFLPLCHVLERIVSVEFPIAVGSTVNFAEsPD----TVFD 272
Cdd:cd05933 160 GTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGqesvVSYLPLSHIAAQILDIWLPIKVGGQVYFAQ-PDalkgTLVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 273 NLREVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASGA-AKLEGKGGAMHAVWDF-----LVLRNIRQMIG 346
Cdd:cd05933 239 TLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLeTNLKLMGGESPSPLFYrlakkLVFKKVRKALG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 347 FDRNRRSNTGAAPISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIAE-----NGEICLK 421
Cdd:cd05933 319 LDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNpdadgIGEICFW 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 422 GPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFS-PFISDAVVIG 499
Cdd:cd05933 399 GRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKElPIISNAMLIG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 500 DRRKYLTVLIM----IDQENVE----------KYAQD---HQIPFSDFASlTRAPQVVDLIDGVVREVN---THFAQveQ 559
Cdd:cd05933 479 DKRKFLSMLLTlkceVNPETGEpldelteeaiEFCRKlgsQATRVSEIAG-GKDPKVYEAIEEGIKRVNkkaISNAQ--K 555
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1821015446 560 IKYFRLIDILLTAEDDELTPTMKLKRGFVEKKHAALIDQMY 600
Cdd:cd05933 556 IQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
41-600 |
2.06e-112 |
|
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: 346.51 E-value: 2.06e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 41 GIWQAYSWSDWYDRSQAIGMGLIELGLTR--GTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGS 118
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 119 AFLFVENDeqldkylevqdrvptiVKVIVFDpkglrdfshpkvmflsDLYEIGEKAPdaaerfrIEINASQPEDTRMLIY 198
Cdd:cd05927 81 SIVFCDAG----------------VKVYSLE----------------EFEKLGKKNK-------VPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 199 TSGTTGPPKGAMISHSNM------LYQMWAGQQvlRVDPKDEQLCFLPLCHVLERIVsVEFPIAVGSTVNFAESPDTV-F 271
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIvsnvagVFKILEILN--KINPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFYSGDIRLlL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 272 DNLREVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASGAAKLEGKGGAMHAVWDFLVLRNIRQMIGfDRNR 351
Cdd:cd05927 199 DDIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALG-GNVR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 352 RSNTGAAPISPDLIRWY-GALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIAE-------------NGE 417
Cdd:cd05927 278 LMLTGSAPLSPEVLEFLrVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpemnydakdpnpRGE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 418 ICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFSPFISDAV 496
Cdd:cd05927 358 VCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIF 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 497 VIGDRRK-YLTVLIMIDQENVEKYAQDHQIPFSDFASLTRAPqvvDLIDGVVREVNTHFAQ-----VEQIKYFRLIDILL 570
Cdd:cd05927 438 VYGDSLKsFLVAIVVPDPDVLKEWAASKGGGTGSFEELCKNP---EVKKAILEDLVRLGKEnglkgFEQVKAIHLEPEPF 514
|
570 580 590
....*....|....*....|....*....|
gi 1821015446 571 TAEDDELTPTMKLKRGFVEKKHAALIDQMY 600
Cdd:cd05927 515 SVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
44-588 |
8.26e-106 |
|
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: 327.01 E-value: 8.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 44 QAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGG--IPSGvyTTDSAGQLEYLINDSGSAFL 121
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAvdVVRG--SDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 122 FVENDeqldkylevqdrvptivkvivfdpkglrdfshpkvmflsdlyeigekapdaaerfrieinasqPEDTRMLIYTSG 201
Cdd:cd17640 82 VVEND---------------------------------------------------------------SDDLATIIYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 202 TTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERivSVE-FPIAVGSTVNFAeSPDTVFDNLREVSPH 280
Cdd:cd17640 99 TTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYER--SAEyFIFACGCSQAYT-SIRTLKDDLKRVKPH 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 281 VFTAVPRLWEKIYSRVLIMRSEATPFgrwafdRAMASGAAKLEGkggamhavwdflvlrNIRQMIgfdrnrrSNTGAAPI 360
Cdd:cd17640 176 YIVSVPRLWESLYSGIQKQVSKSSPI------KQFLFLFFLSGG---------------IFKFGI-------SGGGALPP 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 361 SPDliRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRI-----------AENGEICLKGPNVFKGY 429
Cdd:cd17640 228 HVD--TFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIvdpegnvvlppGEKGIVWVRGPQVMKGY 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 430 WRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFSPFISDAVVIGDRRKYLTVL 508
Cdd:cd17640 306 YKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGAL 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 509 IMIDQENVEKYAQDHQIPF-SDFASLTRAPQVVDLI-DGVVREVNTH--FAQVEQIKYFRLIDILLTaEDDELTPTMKLK 584
Cdd:cd17640 386 IVPNFEELEKWAKESGVKLaNDRSQLLASKKVLKLYkNEIKDEISNRpgFKSFEQIAPFALLEEPFI-ENGEMTQTMKIK 464
|
....
gi 1821015446 585 RGFV 588
Cdd:cd17640 465 RNVV 468
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
41-592 |
2.64e-101 |
|
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: 316.72 E-value: 2.64e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 41 GIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAF 120
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 121 LFVEndeQLDKYLEVQDRVP-TIVKVIVFDPKGLRDFSHpkvmfLSDLYEIGEKAPDAAERFrieinasqPEDTRMLIYT 199
Cdd:cd05932 82 LFVG---KLDDWKAMAPGVPeGLISISLPPPSAANCQYQ-----WDDLIAQHPPLEERPTRF--------PEQLATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 200 SGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPDTVFDNLREVSP 279
Cdd:cd05932 146 SGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDVQRARP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 280 HVFTAVPRLWEKIYSRVLimrsEATPFGRwaFDRAMasgaaKLegkggamhAVWDFLVLRNIRQMIGFDRNRRSNTGAAP 359
Cdd:cd05932 226 TLFFSVPRLWTKFQQGVQ----DKIPQQK--LNLLL-----KI--------PVVNSLVKRKVLKGLGLDQCRLAGCGSAP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 360 ISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIAENGEICLKGPNVFKGYWRKPEKTAED 439
Cdd:cd05932 287 VPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISEDGEILVRSPALMMGYYKDPEATAEA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 440 I-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFSPFISDAVVIGDRRKYLTVLIMIDQENVEK 518
Cdd:cd05932 367 FtADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLSEEARLR 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821015446 519 YAQdhqipfSDFASLTRAPQvvDLIDGVVREVNTHfaqvEQIKYFRLIDILLTAEDDELTPTMKLKRGFVEKKH 592
Cdd:cd05932 447 ADA------FARAELEASLR--AHLARVNSTLDSH----EQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
22-472 |
2.64e-98 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 305.78 E-value: 2.64e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 22 WAAKCAERGDATAHrekDFGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVY 101
Cdd:pfam00501 1 LERQAARTPDKTAL---EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 102 TTDSAGQLEYLINDSGSAFLFVENDEQLDKYLEVQDRVPTIVKVIVFDpkglrdfsHPKVMFLSDLYEIGEKAPDAAErf 181
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLD--------RDPVLKEEPLPEEAKPADVPPP-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 182 riEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWA----GQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAV 257
Cdd:pfam00501 148 --PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSikrvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 258 GSTVNFAE-----SPDTVFDNLREVSPHVFTAVPRLWEKIysrvlimrseatpfgrwafdraMASGAAKLEGKGGamhav 332
Cdd:pfam00501 226 GATVVLPPgfpalDPAALLELIERYKVTVLYGVPTLLNML----------------------LEAGAPKRALLSS----- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 333 wdflvlrnIRQMIgfdrnrrsnTGAAPISPDLIRWY-GALGVTLLEGYGMTETSGVASVNVIGD---NRIGTIGCALPAT 408
Cdd:pfam00501 279 --------LRLVL---------SGGAPLPPELARRFrELFGGALVNGYGLTETTGVVTTPLPLDedlRSLGSVGRPLPGT 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821015446 409 ELRIA-----------ENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITA 472
Cdd:pfam00501 342 EVKIVddetgepvppgEPGELCVRGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
45-600 |
1.47e-90 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 292.77 E-value: 1.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 45 AYSWSDW---YDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFL 121
Cdd:PLN02736 75 EYKWMTYgeaGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 122 FVENDeQLDKYLEVQDRVPTIVKVIVF--DPKGLRdfSHP-----KVMFLSDLYEIGEKAPDAaerFRieinASQPEDTR 194
Cdd:PLN02736 155 FCVPQ-TLNTLLSCLSEIPSVRLIVVVggADEPLP--SLPsgtgvEIVTYSKLLAQGRSSPQP---FR----PPKPEDVA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 195 MLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLER---IVSVEFPIAVGstvnFAESPD-TV 270
Cdd:PLN02736 225 TICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERvnqIVMLHYGVAVG----FYQGDNlKL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 271 FDNLREVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASGAAKLEgKGGAMHAVWDFLVLRNIRQMIGfDRN 350
Cdd:PLN02736 301 MDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALE-NGKNPSPMWDRLVFNKIKAKLG-GRV 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 351 RRSNTGAAPISPDLIRWYG-ALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIAE--------------N 415
Cdd:PLN02736 379 RFMSSGASPLSPDVMEFLRiCFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemnytsedqpypR 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 GEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFSPFISD 494
Cdd:PLN02736 459 GEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQ 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 495 AVVIGDR-RKYLTVLIMIDQENVEKYAQDHQIPFSDFASLTRAPQVVDLI----DGVVREvnthfAQV---EQIKYFRLI 566
Cdd:PLN02736 539 CFVYGDSlNSSLVAVVVVDPEVLKAWAASEGIKYEDLKQLCNDPRVRAAVladmDAVGRE-----AQLrgfEFAKAVTLV 613
|
570 580 590
....*....|....*....|....*....|....
gi 1821015446 567 DILLTAEDDELTPTMKLKRGFVEKKHAALIDQMY 600
Cdd:PLN02736 614 PEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMY 647
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
47-588 |
2.05e-90 |
|
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: 288.34 E-value: 2.05e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 47 SWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSaflfvend 126
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETEC-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 127 eqldkylevqdrvptivKVIVFDPKglrdfshpkvmflsdlyeigekapdaaerfrieinasqPEDTRMLIYTSGTTGPP 206
Cdd:cd17639 79 -----------------SAIFTDGK--------------------------------------PDDLACIMYTSGSTGNP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 207 KGAMISHSNMLYQMwAGQQ---VLRVDPKDEQLCFLPLCHVLERIVSVEFpIAVGSTVNFAeSPDTVFDN--------LR 275
Cdd:cd17639 104 KGVMLTHGNLVAGI-AGLGdrvPELLGPDDRYLAYLPLAHIFELAAENVC-LYRGGTIGYG-SPRTLTDKskrgckgdLT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 276 EVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASGAAKL-EGKGGAmhaVWDFLVLRNIRQMIGfDRNRRSN 354
Cdd:cd17639 181 EFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALkEGPGTP---LLDELVFKKVRAALG-GRLRYML 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 355 TGAAPISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELR---IAE----------NGEICLK 421
Cdd:cd17639 257 SGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKlvdWEEggystdkpppRGEILIR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 422 GPNVFKGYWRKPEKTAEDIR-DGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFSPFISDAVVIGD 500
Cdd:cd17639 337 GPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYAD 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 501 RRK-YLTVLIMIDQENVEKYAQDHQIPFSDFASLTRAPQVVDLIDGVVREV--NTHFAQVEQIKYFRLIDILLTAEDDEL 577
Cdd:cd17639 417 PDKsYPVAIVVPNEKHLTKLAEKHGVINSEWEELCEDKKLQKAVLKSLAETarAAGLEKFEIPQGVVLLDEEWTPENGLV 496
|
570
....*....|.
gi 1821015446 578 TPTMKLKRGFV 588
Cdd:cd17639 497 TAAQKLKRKEI 507
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
21-499 |
2.23e-89 |
|
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: 284.01 E-value: 2.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 21 LWAAKCAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGV 100
Cdd:COG0318 4 LLRRAAARHPDRPALVFGG----RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 101 YTTDSAGQLEYLINDSGSAFLFvendeqldkylevqdrvptivkvivfdpkglrdfshpkvmflsdlyeigekapdaaer 180
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALV---------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 181 frieinasqpedTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGST 260
Cdd:COG0318 102 ------------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGAT 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 261 VNFAE--SPDTVFDNLREVSPHVFTAVPRLWEKIysrvlimrseatpfgrwafdramasgaaklegkggAMHAVWDFLVL 338
Cdd:COG0318 170 LVLLPrfDPERVLELIERERVTVLFGVPTMLARL-----------------------------------LRHPEFARYDL 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 339 RNIRQMIgfdrnrrsnTGAAPISPDLI-RWYGALGVTLLEGYGMTETSGVASVNV--IGDNRIGTIGCALPATELRIA-- 413
Cdd:COG0318 215 SSLRLVV---------SGGAPLPPELLeRFEERFGVRIVEGYGLTETSPVVTVNPedPGERRPGSVGRPLPGVEVRIVde 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 414 --------ENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESR 485
Cdd:COG0318 286 dgrelppgEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEV 364
|
490
....*....|....
gi 1821015446 486 LKFSPFISDAVVIG 499
Cdd:COG0318 365 LAAHPGVAEAAVVG 378
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
26-504 |
9.12e-76 |
|
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: 248.63 E-value: 9.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 26 CAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDS 105
Cdd:cd05936 9 ARRFPDKTALIFMG----RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 106 AGQLEYLINDSGSAFLFVendeqldkylevqdrvptivkvivfdpkglrdfshpkVMFLSDLYEIGEKAPDAAERfriei 185
Cdd:cd05936 85 PRELEHILNDSGAKALIV-------------------------------------AVSFTDLLAAGAPLGERVAL----- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 186 nasQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVL--RVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNF 263
Cdd:cd05936 123 ---TPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 264 AESPD--TVFDNLREVSPHVFTAVPRLWEKIYSrvlimrseatpfgrwafdramasgaaklegkggamHAVWDFLVLRNI 341
Cdd:cd05936 200 IPRFRpiGVLKEIRKHRVTIFPGVPTMYIALLN-----------------------------------APEFKKRDFSSL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 342 RQMIGfdrnrrsntGAAPISPDLI-RWYGALGVTLLEGYGMTETSGVASVNVI-GDNRIGTIGCALPATELRIA------ 413
Cdd:cd05936 245 RLCIS---------GGAPLPVEVAeRFEELTGVPIVEGYGLTETSPVVAVNPLdGPRKPGSIGIPLPGTEVKIVdddgee 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 414 ----ENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIItAGGKNITPAEIESRLKFS 489
Cdd:cd05936 316 lppgEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGFNVYPREVEEVLYEH 394
|
490
....*....|....*
gi 1821015446 490 PFISDAVVIGDRRKY 504
Cdd:cd05936 395 PAVAEAAVVGVPDPY 409
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
13-499 |
3.80e-73 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 243.27 E-value: 3.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 13 DGADTVVKLWAAKCAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISA 92
Cdd:PRK07656 2 NEWMTLPELLARAARRFGDKEAYVFGD----QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 93 AGG--IP-SGVYTTDSAGqleYLINDSGSAFLFVEnDEQLDKYLEVQDRVPTIVKVIVFDPKGLRDFShPKVMFLSDLYE 169
Cdd:PRK07656 78 AGAvvVPlNTRYTADEAA---YILARGDAKALFVL-GLFLGVDYSATTRLPALEHVVICETEEDDPHT-EKMKTFTDFLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 170 IGEKAPDAAERfrieinasQPEDTRMLIYTSGTTGPPKGAMISHSNML--YQMWAGqqVLRVDPKDEQLCFLPLCHVLER 247
Cdd:PRK07656 153 AGDPAERAPEV--------DPDDVADILFTSGTTGRPKGAMLTHRQLLsnAADWAE--YLGLTEGDRYLAANPFFHVFGY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 248 IVSVEFPIAVGSTV----NFaeSPDTVFDNLREVSPHVFTAVPRLWEKIYSRVlimrseatpfGRWAFDramasgaakle 323
Cdd:PRK07656 223 KAGVNAPLMRGATIlplpVF--DPDEVFRLIETERITVLPGPPTMYNSLLQHP----------DRSAED----------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 324 gkggamhavwdflvLRNIRQMIgfdrnrrsnTGAAPISPDLI-RWYGALGV-TLLEGYGMTETSGVASVNVIGDNRI--- 398
Cdd:PRK07656 280 --------------LSSLRLAV---------TGAASMPVALLeRFESELGVdIVLTGYGLSEASGVTTFNRLDDDRKtva 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 399 GTIGCALPATELRIA----------ENGEICLKGPNVFKGYWRKPEKTAEDIR-DGWLYTGDVGRIGDDGAITITGRVKD 467
Cdd:PRK07656 337 GTIGTAIAGVENKIVnelgeevpvgEVGELLVRGPNVMKGYYDDPEATAAAIDaDGWLHTGDLGRLDEEGYLYIVDRKKD 416
|
490 500 510
....*....|....*....|....*....|..
gi 1821015446 468 IIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK07656 417 MFIV-GGFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
17-499 |
2.75e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 238.55 E-value: 2.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 17 TVVKLWAAKCAERGDATA-HREKdfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGG 95
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAvYFDG-----RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 96 IPSGVYTTDSAGQLEYLINDSGSAFLFVeNDEQLDKYLEVQDRVPTIVKVIVFDPKGLrdfsHPKVMFLSDLYEIGEKAP 175
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLV-DSEFVPLLAAILPQLPTVRTVIVEGDGPA----APLAPEVGEYEELLAAAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 176 DAAERFRIEINasqpeDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVeFPI 255
Cdd:PRK06187 157 DTFDFPDIDEN-----DAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPY-LAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 256 AVGSTVNFAES--PDTVFDNLREVSPHVFTAVPRLWEkiysrvlIMRSEATPFGRWafdramasgaaklegkggamhavw 333
Cdd:PRK06187 231 MAGAKQVIPRRfdPENLLDLIETERVTFFFAVPTIWQ-------MLLKAPRAYFVD------------------------ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 334 dflvLRNIRQMIgfdrnrrsnTGAAPISPDLIRWYGA-LGVTLLEGYGMTETSGVASVN-----VIGDNRI-GTIGCALP 406
Cdd:PRK06187 280 ----FSSLRLVI---------YGGAALPPALLREFKEkFGIDLVQGYGMTETSPVVSVLppedqLPGQWTKrRSAGRPLP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 407 ATELRIA------------ENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGG 474
Cdd:PRK06187 347 GVEARIVdddgdelppdggEVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIIS-GG 425
|
490 500
....*....|....*....|....*
gi 1821015446 475 KNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK06187 426 ENIYPRELEDALYGHPAVAEVAVIG 450
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
66-585 |
7.01e-70 |
|
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: 233.10 E-value: 7.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 66 GLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVendeqldkylevqdrvptivkv 145
Cdd:cd05914 28 GVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV---------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 146 ivfdpkglrdfshpkvmflsdlyeigekapdaaerfrieinaSQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQ 225
Cdd:cd05914 86 ------------------------------------------SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 226 VLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAE---SPDTVFDNLREVSPHVftAVPRLW--EKIYSRVLIMR 300
Cdd:cd05914 124 VVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDkipSAKIIALAFAQVTPTL--GVPVPLviEKIFKMDIIPK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 301 SEATPFgRWA-----FDRAMASGAAK--LEGKGGamhavwdflvlrNIRQMIgfdrnrrsnTGAAPISPDLIRWYGALGV 373
Cdd:cd05914 202 LTLKKF-KFKlakkiNNRKIRKLAFKkvHEAFGG------------NIKEFV---------IGGAKINPDVEEFLRTIGF 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 374 TLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIA------ENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLY 446
Cdd:cd05914 260 PYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDspdpatGEGEIIVRGPNVMKGYYKNPEATAEAFdKDGWFH 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 447 TGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFSPFISDA-VVIGDRRKYLTVLIMIDQENVEKYAQDHQI 525
Cdd:cd05914 340 TGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESlVVVQEKKLVALAYIDPDFLDVKALKQRNII 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 526 pfsdfasltrapqvVDLIDGVVREVNTHFAQveqikYFRLIDILLTAEDDELTPTMKLKR 585
Cdd:cd05914 420 --------------DAIKWEVRDKVNQKVPN-----YKKISKVKIVKEEFEKTPKGKIKR 460
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
26-499 |
4.17e-66 |
|
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: 222.10 E-value: 4.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 26 CAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDS 105
Cdd:cd17631 5 ARRHPDRTALVFGG----RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 106 AGQLEYLINDSGSAFLFvendeqldkylevqdrvptivkvivfdpkglrdfshpkvmflsdlyeigekapdaaerfriei 185
Cdd:cd17631 81 PPEVAYILADSGAKVLF--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 186 nasqpEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAE 265
Cdd:cd17631 98 -----DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILR 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 266 S--PDTVFDNLREVSPHVFTAVPRLWEkiysrvlimrseatpfgrwafdrAMASgaaklegkggamHAVWDFLVLRNIRQ 343
Cdd:cd17631 173 KfdPETVLDLIERHRVTSFFLVPTMIQ-----------------------ALLQ------------HPRFATTDLSSLRA 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 344 MIGfdrnrrsntGAAPISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNR--IGTIGCALPATELRI--------- 412
Cdd:cd17631 218 VIY---------GGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIvdpdgrevp 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 -AENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPF 491
Cdd:cd17631 289 pGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVEDVLYEHPA 367
|
....*...
gi 1821015446 492 ISDAVVIG 499
Cdd:cd17631 368 VAEVAVIG 375
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
192-499 |
4.34e-66 |
|
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: 219.08 E-value: 4.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 192 DTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLErIVSVEFPIAVGSTVNFAE--SPDT 269
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPkfDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 270 VFDNLREVSPHVFTAVPRLWEkiysrvLIMRSEATPfgrwAFDramasgaaklegkggamhavwdflvlrnirqmigFDR 349
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLA------RLLKAPESA----GYD----------------------------------LSS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 350 NRRSNTGAAPISPDLI-RWYGALGVTLLEGYGMTETSGVASVN--VIGDNRIGTIGCALPATELRIA----------ENG 416
Cdd:cd04433 116 LRALVSGGAPLPPELLeRFEEAPGIKLVNGYGLTETGGTVATGppDDDARKPGSVGRPVPGVEVRIVdpdggelppgEIG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 417 EICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAV 496
Cdd:cd04433 196 ELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAVLLGHPGVAEAA 274
|
...
gi 1821015446 497 VIG 499
Cdd:cd04433 275 VVG 277
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
46-499 |
1.21e-64 |
|
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: 218.70 E-value: 1.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELG-LTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAflfve 124
Cdd:cd05941 12 ITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPS----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 125 ndeqldkylevqdrvptivkvIVFDPKglrdfshpkvmflsdlyeigekapdaaerfrieinasqpedtrMLIYTSGTTG 204
Cdd:cd05941 87 ---------------------LVLDPA-------------------------------------------LILYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 205 PPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPDTVFDNLREVSPH--VF 282
Cdd:cd05941 103 RPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSitVF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 283 TAVPrlweKIYSRvLIMRSEATPFgrwafDRAMASGAAklegkggamhavwdflvLRNIRQMIgfdrnrrsnTGAAPIS- 361
Cdd:cd05941 183 MGVP----TIYTR-LLQYYEAHFT-----DPQFARAAA-----------------AERLRLMV---------SGSAALPv 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 362 PDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIA-----------ENGEICLKGPNVFKGYW 430
Cdd:cd05941 227 PTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVdeetgeplprgEVGEIQVRGPSVFKEYW 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 431 RKPEKTAEDIR-DGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05941 307 NKPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIG 376
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
42-600 |
3.96e-63 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 220.07 E-value: 3.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 42 IWQAYSwsDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFL 121
Cdd:PLN02430 75 MWKTYK--EVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 122 FVEnDEQLDKYLEVQDRVPTIVKVIVFDPKGLRDFSHP------KVMFLSDLYEIGEKAPDaaerfriEINASQPEDTRM 195
Cdd:PLN02430 153 FVQ-DKKIKELLEPDCKSAKRLKAIVSFTSVTEEESDKasqigvKTYSWIDFLHMGKENPS-------ETNPPKPLDICT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 196 LIYTSGTTGPPKGAMISHSNML-----YQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSvEFPIAVGSTVNFAESP-DT 269
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVAtfvrgVDLFMEQFEDKMTHDDVYLSFLPLAHILDRMIE-EYFFRKGASVGYYHGDlNA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 270 VFDNLREVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASGAAKLegKGGAMHA----VWDFLVLRNIRQMI 345
Cdd:PLN02430 304 LRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWM--NRGYSHKkaspMADFLAFRKVKAKL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 346 GfDRNRRSNTGAAPISPDLIRWygaLGVT----LLEGYGMTETSGVASVNVIGD-NRIGTIGCALPATELRIAE------ 414
Cdd:PLN02430 382 G-GRLRLLISGGAPLSTEIEEF---LRVTscafVVQGYGLTETLGPTTLGFPDEmCMLGTVGAPAVYNELRLEEvpemgy 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 415 -------NGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLK 487
Cdd:PLN02430 458 dplgeppRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYG 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 488 FSPFISDAVVIGDRRKYLTV-LIMIDQENVEKYAQD--HQIPFSDFASLtraPQVVDLIDGVVREV--NTHFAQVEQIKY 562
Cdd:PLN02430 538 QNPIVEDIWVYGDSFKSMLVaVVVPNEENTNKWAKDngFTGSFEELCSL---PELKEHILSELKSTaeKNKLRGFEYIKG 614
|
570 580 590
....*....|....*....|....*....|....*...
gi 1821015446 563 FRLIDILLTAEDDELTPTMKLKRGFVEKKHAALIDQMY 600
Cdd:PLN02430 615 VILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
15-600 |
1.96e-61 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 216.00 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 15 ADTVVKLWAAKCAERGDATA------------------HREKDFGIW----QAY-SWSDWYDRSQAIGMGLIELGLTRGT 71
Cdd:PTZ00216 68 GPNFLQRLERICKERGDRRAlayrpvervekevvkdadGKERTMEVThfneTRYiTYAELWERIVNFGRGLAELGLTKGS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 72 PVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLfVENDEQLDKYLE-VQDRVPTIVKVIVFD- 149
Cdd:PTZ00216 148 NVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI-VCNGKNVPNLLRlMKSGGMPNTTIIYLDs 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 150 -PKGLRDFSHpKVMFLSDLYEIGEKAPdAAERFRIEINAsqpEDTRMLIYTSGTTGPPKGAMISHSNmLYQ--MWAGQQV 226
Cdd:PTZ00216 227 lPASVDTEGC-RLVAWTDVVAKGHSAG-SHHPLNIPENN---DDLALIMYTSGTTGDPKGVMHTHGS-LTAgiLALEDRL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 227 LRV-DPKDEQ---LCFLPLCHVLERIVSVEFpIAVGSTVNFAeSPDTVFD-------NLREVSPHVFTAVPRLWEKIYSR 295
Cdd:PTZ00216 301 NDLiGPPEEDetyCSYLPLAHIMEFGVTNIF-LARGALIGFG-SPRTLTDtfarphgDLTEFRPVFLIGVPRIFDTIKKA 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 296 VLIMRSEATPFGRWAFDRAMASGAAKLegKGGAMHAVWDFLVLRNIRQMIGfDRNRRSNTGAAPISPDLIRWYGALGVTL 375
Cdd:PTZ00216 379 VEAKLPPVGSLKRRVFDHAYQSRLRAL--KEGKDTPYWNEKVFSAPRAVLG-GRVRAMLSGGGPLSAATQEFVNVVFGMV 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 376 LEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIAE------------NGEICLKGPNVFKGYWRKPEKTAEDI-RD 442
Cdd:PTZ00216 456 IQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDteeykhtdtpepRGEILLRGPFLFKGYYKQEELTREVLdED 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 443 GWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFSPFISD---AVVIGDRRKYLTVLIMIDQENVEKY 519
Cdd:PTZ00216 536 GWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPngvCVLVHPARSYICALVLTDEAKAMAF 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 520 AQDHQIPfSDFASLTRAPQVVDLIDGVVREV--NTHFAQVEQIKYFRLIDILLTAEDDELTPTMKLKRGFVEKKHAALID 597
Cdd:PTZ00216 616 AKEHGIE-GEYPAILKDPEFQKKATESLQETarAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIK 694
|
...
gi 1821015446 598 QMY 600
Cdd:PTZ00216 695 ELF 697
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
43-600 |
2.71e-61 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 215.75 E-value: 2.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 43 WQAYSwsDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLycdlaISAAGGIPSGV-----YTTDSAGQLEYLINDSG 117
Cdd:PLN02387 106 WITYG--QVFERVCNFASGLVALGHNKEERVAIFADTRAEWL-----IALQGCFRQNItvvtiYASLGEEALCHSLNETE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 118 SAFLfVENDEQLDKYLEVQDRVPTIVKVIVFD------PKGLRDFSHPKVMFLSDLYEIGEKAPdaaerfrIEINASQPE 191
Cdd:PLN02387 179 VTTV-ICDSKQLKKLIDISSQLETVKRVIYMDdegvdsDSSLSGSSNWTVSSFSEVEKLGKENP-------VDPDLPSPN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 192 DTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVL-RVDPKDEQLCFLPLCHVLErIVSVEFPIAVGSTVNFAeSPDTV 270
Cdd:PLN02387 251 DIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHILE-LAAESVMAAVGAAIGYG-SPLTL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 271 FD-----------NLREVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASGAAKLEGK----GGAMHAVWDF 335
Cdd:PLN02387 329 TDtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIEGSwfgaWGLEKLLWDA 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 336 LVLRNIRQMIGfDRNRRSNTGAAPISPDLIRWYG-ALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIAE 414
Cdd:PLN02387 409 LVFKKIRAVLG-GRIRFMLSGGAPLSGDTQRFINiCLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVS 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 415 --------------NGEICLKGPNVFKGYWRKPEKTAEDIRDG-----WLYTGDVGRIGDDGAITITGRVKDIIITAGGK 475
Cdd:PLN02387 488 weeggylisdkpmpRGEIVIGGPSVTLGYFKNQEKTDEVYKVDergmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGE 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 476 NITPAEIESRLKFSPFISDAVVIGDR-RKYLTVLIMIDQENVEKYAQDHQIPFSDFASLTRAPQvvdlidgVVREVNTHF 554
Cdd:PLN02387 568 YVSLGKVEAALSVSPYVDNIMVHADPfHSYCVALVVPSQQALEKWAKKAGIDYSNFAELCEKEE-------AVKEVQQSL 640
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821015446 555 AQVEqiKYFRL--------IDIL---LTAEDDELTPTMKLKRGFVEKKHAALIDQMY 600
Cdd:PLN02387 641 SKAA--KAARLekfeipakIKLLpepWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
44-499 |
5.33e-61 |
|
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: 210.15 E-value: 5.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 44 QAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFV 123
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 124 ENDEqLDKYLEVQDRVPTIVKVIVFDPKGlrdfshPKVMFLSDLYEIGEKAPDAaERFRIEINAsqPEDTRMLIYTSGTT 203
Cdd:cd05911 89 DPDG-LEKVKEAAKELGPKDKIIVLDDKP------DGVLSIEDLLSPTLGEEDE-DLPPPLKDG--KDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 204 GPPKGAMISHSN---MLYQMWAGQQVLrVDPKDEQLCFLPLCHVLERIVSVEFPIAvGSTV----NFaeSPDTVFDNLRE 276
Cdd:cd05911 159 GLPKGVCLSHRNliaNLSQVQTFLYGN-DGSNDVILGFLPLYHIYGLFTTLASLLN-GATViimpKF--DSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 277 VSPHVFTAVPRLwekiysrVLIMrseatpfgrwafdramasgaaklegkggAMHAVWDFLVLRNIRQMigfdrnrrsNTG 356
Cdd:cd05911 235 YKITFLYLVPPI-------AAAL----------------------------AKSPLLDKYDLSSLRVI---------LSG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 357 AAPISPDLIRWYGAL--GVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIA-----------ENGEICLKGP 423
Cdd:cd05911 271 GAPLSKELQELLAKRfpNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVdddgkdslgpnEPGEICVRGP 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821015446 424 NVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05911 351 QVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKE-LIKYKGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
45-499 |
1.36e-55 |
|
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: 195.61 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 45 AYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVE 124
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 125 NDEQLDKYLEVQDRVPTIVKVIVFDPKGLRDFSHPKVMFLSDLYEIGEKAPdaaerfrieinASQPEDTRMLIYTSGTTG 204
Cdd:cd05926 94 KGELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEG-----------VPLPDDLALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 205 PPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAE--SPDTVFDNLREVSPHVF 282
Cdd:cd05926 163 RPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPrfSASTFWPDVRDYNATWY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 283 TAVPRLwekiySRVLIMRSEATPfgrwafdramasgaaklegkGGAMHAvwdflvLRNIRqmigfdrnrrsnTGAAPISP 362
Cdd:cd05926 243 TAVPTI-----HQILLNRPEPNP--------------------ESPPPK------LRFIR------------SCSASLPP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 363 D-LIRWYGALGVTLLEGYGMTETSGVASVNVI--GDNRIGTIGCALpATELRI----------AENGEICLKGPNVFKGY 429
Cdd:cd05926 280 AvLEALEATFGAPVLEAYGMTEAAHQMTSNPLppGPRKPGSVGKPV-GVEVRIldedgeilppGVVGEICLRGPNVTRGY 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821015446 430 WRKPEKTAED-IRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05926 359 LNNPEANAEAaFKDGWFRTGDLGYLDADGYLFLTGRIKELINR-GGEKISPLEVDGVLLSHPAVLEAVAFG 428
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
44-499 |
6.59e-55 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 193.94 E-value: 6.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 44 QAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGipsgVY----TTDSAGQLEYLINDSGSA 119
Cdd:PRK07514 27 LRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplnTAYTLAELDYFIGDAEPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 120 fLFVENDEQLDKYLEVQDRVPTIvKVIVFDPKGLRDFShpkvmflsdlyeigEKAPDAAERFriEINASQPEDTRMLIYT 199
Cdd:PRK07514 103 -LVVCDPANFAWLSKIAAAAGAP-HVETLDADGTGSLL--------------EAAAAAPDDF--ETVPRGADDLAAILYT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 200 SGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAES--PDTVFDNLREV 277
Cdd:PRK07514 165 SGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKfdPDAVLALMPRA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 278 SphVFTAVPRLwekiYSRVLimrseATPfgrwAFDRAMAsgaaklegkggamhavwdflvlRNIRQMIgfdrnrrsnTGA 357
Cdd:PRK07514 245 T--VMMGVPTF----YTRLL-----QEP----RLTREAA----------------------AHMRLFI---------SGS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 358 APISPDLIR-WYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIA-----------ENGEICLKGPNV 425
Cdd:PRK07514 279 APLLAETHReFQERTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTdpetgaelppgEIGMIEVKGPNV 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821015446 426 FKGYWRKPEKTAEDIR-DGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK07514 359 FKGYWRMPEKTAEEFRaDGFFITGDLGKIDERGYVHIVGRGKDLIIS-GGYNVYPKEVEGEIDELPGVVESAVIG 432
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
190-499 |
1.65e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 194.45 E-value: 1.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 190 PEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQ-VLRVDPKDEQ-LCFLPLCHVLERIVSVEFPIAVGSTVNFAESP 267
Cdd:PRK05605 218 PDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwVPGLGDGPERvLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 268 --DTVFDNLREVSPHVFTAVPRLWEKIysrvlimrseatpfgrwafdramasgAAKLEGKGGAMHAVwdflvlrnirqmi 345
Cdd:PRK05605 298 diDLILDAMKKHPPTWLPGVPPLYEKI--------------------------AEAAEERGVDLSGV------------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 346 gfdrnRRSNTGAAPISPDLI-RWYGALGVTLLEGYGMTETSGVASVNVIGDNR-IGTIGCALPATELRIA---------- 413
Cdd:PRK05605 339 -----RNAFSGAMALPVSTVeLWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRrPGYVGVPFPDTEVRIVdpedpdetmp 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 414 --ENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPF 491
Cdd:PRK05605 414 dgEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEEVLREHPG 492
|
....*...
gi 1821015446 492 ISDAVVIG 499
Cdd:PRK05605 493 VEDAAVVG 500
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
27-499 |
1.51e-52 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 189.17 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 27 AERGDATA-HREKDFGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDS 105
Cdd:COG0365 20 EGRGDKVAlIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 106 AGQLEYLINDSGSAFLFVEND--------EQLDKYLEVQDRVPTIVKVIVFDPKGLrDFSHPKVMFLSDLYEIGEKAPDA 177
Cdd:COG0365 100 AEALADRIEDAEAKVLITADGglrggkviDLKEKVDEALEELPSLEHVIVVGRTGA-DVPMEGDLDWDELLAAASAEFEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 178 AERfrieinasQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQM-WAGQQVLRVDPKDEQLCFLPL----CH---VLeriv 249
Cdd:COG0365 179 EPT--------DADDPLFILYTSGTTGKPKGVVHTHGGYLVHAaTTAKYVLDLKPGDVFWCTADIgwatGHsyiVY---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 250 sveFPIAVGSTV------NFAESPDTVFDNLREVSPHVFTAVPRLWekiysRVLimrseatpfgrwafdraMASGAAKLE 323
Cdd:COG0365 247 ---GPLLNGATVvlyegrPDFPDPGRLWELIEKYGVTVFFTAPTAI-----RAL-----------------MKAGDEPLK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 324 GkggamhavWDFLVLRNIrqmigfdrnrrSNTGAaPISPDLIRW-YGALGVTLLEGYGMTETSG-VASVNVIGDNRIGTI 401
Cdd:COG0365 302 K--------YDLSSLRLL-----------GSAGE-PLNPEVWEWwYEAVGVPIVDGWGQTETGGiFISNLPGLPVKPGSM 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 402 GCALPATELRI----------AENGEICLKG--PNVFKGYWRKPEKTAE---DIRDGWLYTGDVGRIGDDGAITITGRVK 466
Cdd:COG0365 362 GKPVPGYDVAVvdedgnpvppGEEGELVIKGpwPGMFRGYWNDPERYREtyfGRFPGWYRTGDGARRDEDGYFWILGRSD 441
|
490 500 510
....*....|....*....|....*....|...
gi 1821015446 467 DIIITAgGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:COG0365 442 DVINVS-GHRIGTAEIESALVSHPAVAEAAVVG 473
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
42-600 |
1.06e-50 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 185.61 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 42 IWQAYSwsDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFL 121
Cdd:PLN02614 78 VWQTYQ--EVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 122 FVENDEQLDKYLEVQDRVPTIVKVIVFDpkGLRDFSHPKVMFLSDLYEIGEKAPDAAERFRIEINASQPEDTRMLIYTSG 201
Cdd:PLN02614 156 FVEEKKISELFKTCPNSTEYMKTVVSFG--GVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 202 TTGPPKGAMISHSNMLYQMWAGQQVLR-----VDPKDEQLCFLPLCHVLERIVSvEFPIAVGSTVNFAESP-DTVFDNLR 275
Cdd:PLN02614 234 TTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAHIFDRVIE-ECFIQHGAAIGFWRGDvKLLIEDLG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 276 EVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASGAAKLegKGGAMHA----VWDFLVLRNIRQMIGFDRnR 351
Cdd:PLN02614 313 ELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNM--KKGQSHVeaspLCDKLVFNKVKQGLGGNV-R 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 352 RSNTGAAPISPDLIRWYGALGV-TLLEGYGMTETSGVASVNVIGD-NRIGTIGCALPATELRIAE-------------NG 416
Cdd:PLN02614 390 IILSGAAPLASHVESFLRVVACcHVLQGYGLTESCAGTFVSLPDElDMLGTVGPPVPNVDIRLESvpemeydalastpRG 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 417 EICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKFSPFISDAV 496
Cdd:PLN02614 470 EICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVW 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 497 VIGDR-RKYLTVLIMIDQENVEKYAQDHQIPfSDFASLTRAPQVVDLIDG--VVREVNTHFAQVEQIKYFRLIDILLTAE 573
Cdd:PLN02614 550 VYGNSfESFLVAIANPNQQILERWAAENGVS-GDYNALCQNEKAKEFILGelVKMAKEKKMKGFEIIKAIHLDPVPFDME 628
|
570 580
....*....|....*....|....*..
gi 1821015446 574 DDELTPTMKLKRGFVEKKHAALIDQMY 600
Cdd:PLN02614 629 RDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
130-499 |
2.45e-50 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 184.00 E-value: 2.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 130 DKYLEVQDRVPTIVKVIVFDPKG------------LRDFSHPKVM-FLSDLYEIGEKAPDAAERFRieinasqPEDTRML 196
Cdd:PRK07529 146 QKVAEVLAALPELRTVVEVDLARylpgpkrlavplIRRKAHARILdFDAELARQPGDRLFSGRPIG-------PDDVAAY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 197 IYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAeSP-----DTVF 271
Cdd:PRK07529 219 FHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLA-TPqgyrgPGVI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 272 DNLREVSPH----VFTAVPrlweKIYSRVLimrseatpfgrwafdrAMASGAAKLEGKGGAMhavwdflvlrnirqmigf 347
Cdd:PRK07529 298 ANFWKIVERyrinFLSGVP----TVYAALL----------------QVPVDGHDISSLRYAL------------------ 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 348 drnrrsnTGAAPISPDLIRWY-GALGVTLLEGYGMTETSGVASVN-VIGDNRIGTIGCALPATELRIA------------ 413
Cdd:PRK07529 340 -------CGAAPLPVEVFRRFeAATGVRIVEGYGLTEATCVSSVNpPDGERRIGSVGLRLPYQRVRVVilddagrylrdc 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 414 ---ENGEICLKGPNVFKGYWRkpEKTAEDIR--DGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKF 488
Cdd:PRK07529 413 avdEVGVLCIAGPNVFSGYLE--AAHNKGLWleDGWLNTGDLGRIDADGYFWLTGRAKDLIIR-GGHNIDPAAIEEALLR 489
|
410
....*....|.
gi 1821015446 489 SPFISDAVVIG 499
Cdd:PRK07529 490 HPAVALAAAVG 500
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
42-600 |
4.00e-49 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 181.19 E-value: 4.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 42 IWQAYSwsDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFL 121
Cdd:PLN02861 76 VWLTYK--EVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 122 FVEnDEQLDKYLEVQDRVPTIVKVIVfdpkglrDFSHPKVMFLSDLYEIGEKAPDAAE-----RFRIEINASQPEDTRML 196
Cdd:PLN02861 154 FVQ-ESKISSILSCLPKCSSNLKTIV-------SFGDVSSEQKEEAEELGVSCFSWEEfslmgSLDCELPPKQKTDICTI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 197 IYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPK-----DEQLCFLPLCHVLERIVSVEFpIAVGSTVNFAESpDTVF 271
Cdd:PLN02861 226 MYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRvateeDSYFSYLPLAHVYDQVIETYC-ISKGASIGFWQG-DIRY 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 272 --DNLREVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASGAAKLEgKGGAMHAV---WDFLVLRNIRQMIG 346
Cdd:PLN02861 304 lmEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLR-KGLKQEEAsprLDRLVFDKIKEGLG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 347 fDRNRRSNTGAAPIS---PDLIRWYGAlgVTLLEGYGMTETSGvASVNVIGD--NRIGTIGCALPATELRIAE------- 414
Cdd:PLN02861 383 -GRVRLLLSGAAPLPrhvEEFLRVTSC--SVLSQGYGLTESCG-GCFTSIANvfSMVGTVGVPMTTIEARLESvpemgyd 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 415 ------NGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIESRLKF 488
Cdd:PLN02861 459 alsdvpRGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSR 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 489 SPFISDAVVIGDR-RKYLTVLIMIDQENVEKYAQDHQIPfSDFASLTRAPQVVDLIdgvVREVNTHFAQ-----VEQIKY 562
Cdd:PLN02861 539 CPLIASIWVYGNSfESFLVAVVVPDRQALEDWAANNNKT-GDFKSLCKNLKARKYI---LDELNSTGKKlqlrgFEMLKA 614
|
570 580 590
....*....|....*....|....*....|....*...
gi 1821015446 563 FRLIDILLTAEDDELTPTMKLKRGFVEKKHAALIDQMY 600
Cdd:PLN02861 615 IHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
23-499 |
1.31e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 178.04 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 23 AAKCAERgDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYT 102
Cdd:PRK12583 28 VARFPDR-EALVVRHQA----LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 103 TDSAGQLEYLINDSGSAFLFVENDEQLDKYLEVQD-----------------RVPTIVKVIVFDPKglrdfshPKVMFLS 165
Cdd:PRK12583 103 AYRASELEYALGQSGVRWVICADAFKTSDYHAMLQellpglaegqpgalaceRLPELRGVVSLAPA-------PPPGFLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 166 dlYEIGEKAPDAAERFRI-EINAS-QPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDeQLCF-LPLC 242
Cdd:PRK12583 176 --WHELQARGETVSREALaERQASlDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHD-RLCVpVPLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 243 HVLERIVSVEFPIAVGSTVNFaesPDTVFD---NLREVSPHVFTA---VPRLWekiysrvlIMRSEATPFGRwaFDrama 316
Cdd:PRK12583 253 HCFGMVLANLGCMTVGACLVY---PNEAFDplaTLQAVEEERCTAlygVPTMF--------IAELDHPQRGN--FD---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 317 sgaaklegkggamhavwdflvLRNIRQMIgfdrnrrsnTGAAPISPDLI-RWYGALGVT-LLEGYGMTETSGVASVNVIG 394
Cdd:PRK12583 316 ---------------------LSSLRTGI---------MAGAPCPIEVMrRVMDEMHMAeVQIAYGMTETSPVSLQTTAA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 395 DN---RIGTIGCALPATELRI----------AENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAIT 460
Cdd:PRK12583 366 DDlerRVETVGRTQPHLEVKVvdpdgatvprGEIGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVR 445
|
490 500 510
....*....|....*....|....*....|....*....
gi 1821015446 461 ITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK12583 446 IVGRSKDMIIR-GGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
44-499 |
1.52e-47 |
|
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: 173.96 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 44 QAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFV 123
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 124 ENdeqldkylEVQDRVPTI-VKVIVFDpkglrdfSHPkvmFLSDLYEIGEKAPDAAERFRIEINASqpeDTRMLIYTSGT 202
Cdd:cd05904 111 TA--------ELAEKLASLaLPVVLLD-------SAE---FDSLSFSDLLFEADEAEPPVVVIKQD---DVAALLYSSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 203 TGPPKGAMISHSNmLYQMWAGQ---QVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVnfaespdtvfdnlrevsp 279
Cdd:cd05904 170 TGRSKGVMLTHRN-LIAMVAQFvagEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATV------------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 280 hvftavprlwekiysrvLIMRSeatpfgrwaFDramASGAAKLEGKGGAMHA-VWDFLVLRNIRQMIGFDRNRRS----N 354
Cdd:cd05904 231 -----------------VVMPR---------FD---LEELLAAIERYKVTHLpVVPPIVLALVKSPIVDKYDLSSlrqiM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 355 TGAAPISPDLIRWYGAL--GVTLLEGYGMTETSGVASVNVIGDN---RIGTIGCALPATELRIA-----------ENGEI 418
Cdd:cd05904 282 SGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVVAMCFAPEKdraKYGSVGRLVPNVEAKIVdpetgeslppnQTGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 419 CLKGPNVFKGYWRKPEKTAEDIR-DGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRLKFSPFISDAVV 497
Cdd:cd05904 362 WIRGPSIMKGYLNNPEATAATIDkEGWLHTGDLCYIDEDGYLFIVDRLKE-LIKYKGFQVAPAELEALLLSHPEILDAAV 440
|
..
gi 1821015446 498 IG 499
Cdd:cd05904 441 IP 442
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
44-499 |
1.44e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 168.50 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 44 QAYSWSDWYDRSQAIGMGLI-ELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLF 122
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 123 VENdeqldkylEVQDRVPTIVKVIVFDPkglrdfshpkVMFLSDLYEIGEKAPDAAErfrieinaSQPEDTRMLI-YTSG 201
Cdd:PRK06839 106 VEK--------TFQNMALSMQKVSYVQR----------VISITSLKEIEDRKIDNFV--------EKNESASFIIcYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 202 TTGPPKGAMISHSNMLYQmwAGQQVLRVDPKDEQLC--FLPLCHVlERIVSVEFPiavgstvnfaespdTVFDNLREVSP 279
Cdd:PRK06839 160 TTGKPKGAVLTQENMFWN--ALNNTFAIDLTMHDRSivLLPLFHI-GGIGLFAFP--------------TLFAGGVIIVP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 280 HVF--TAVPRLWEKiySRVLIMrseatpFGrwafdramasgaaklegkggaMHAVWDFLVLRNIRQMIGFDRNRRSNTGA 357
Cdd:PRK06839 223 RKFepTKALSMIEK--HKVTVV------MG---------------------VPTIHQALINCSKFETTNLQSVRWFYNGG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 358 APISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNR--IGTIGCALPATELRI----------AENGEICLKGPNV 425
Cdd:PRK06839 274 APCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELidenknkvevGEVGELLIRGPNV 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821015446 426 FKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK06839 354 MKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
22-502 |
2.83e-45 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 168.84 E-value: 2.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 22 WAAKCAERgDATAHREKDFgiwqAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVY 101
Cdd:PRK08315 25 TAARYPDR-EALVYRDQGL----RWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 102 TTDSAGQLEYLINDSGSAFLFVENDEQLDKYLE-VQD----------------RVPTIVKVIVFDPKglrdfSHPKVMFL 164
Cdd:PRK08315 100 PAYRLSELEYALNQSGCKALIAADGFKDSDYVAmLYElapelatcepgqlqsaRLPELRRVIFLGDE-----KHPGMLNF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 165 SDLYEIGEKAPDAAERfriEINAS-QPEDTRMLIYTSGTTGPPKGAMISHSNML---YqmWAGQQvLRVDPKDeQLCF-L 239
Cdd:PRK08315 175 DELLALGRAVDDAELA---ARQATlDPDDPINIQYTSGTTGFPKGATLTHRNILnngY--FIGEA-MKLTEED-RLCIpV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 240 PLCH----VLERIVSVefpiAVGST-VNFAES--PDTVfdnLREVSPHVFTA---VPrlwekiysrvlimrseaTPFgrw 309
Cdd:PRK08315 248 PLYHcfgmVLGNLACV----THGATmVYPGEGfdPLAT---LAAVEEERCTAlygVP-----------------TMF--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 310 afdramasgAAKLEGKggaMHAVWDFLVLRnirqmigfdrnrrsnTGAAPISP-------DLIRWYGALGVTLleGYGMT 382
Cdd:PRK08315 301 ---------IAELDHP---DFARFDLSSLR---------------TGIMAGSPcpievmkRVIDKMHMSEVTI--AYGMT 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 383 ETSGVASVNVIGD---NRIGTIGCALPATELRIA-----------ENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYT 447
Cdd:PRK08315 352 ETSPVSTQTRTDDpleKRVTTVGRALPHLEVKIVdpetgetvprgEQGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHT 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821015446 448 GDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG--DRR 502
Cdd:PRK08315 432 GDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIEEFLYTHPKIQDVQVVGvpDEK 487
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
46-499 |
3.36e-45 |
|
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: 167.81 E-value: 3.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIpsgVYTTD---SAGQLEYLINDSGSAFLF 122
Cdd:cd12119 26 YTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAV---LHTINprlFPEQIAYIINHAEDRVVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 123 VeNDEQLDKYLEVQDRVPTIVKVIVFDPKGLRDFSHPK-VMFLSDLyeIGEKAPDaaerfriEINASQPEDTR-MLIYTS 200
Cdd:cd12119 103 V-DRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVgVLAYEEL--LAAESPE-------YDWPDFDENTAaAICYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 201 GTTGPPKGAMISH-SNMLYQMWAGQ-QVLRVDPKDEQLCFLPLCHVLerivSVEFPIA---VGSTVNF---AESPDTVFD 272
Cdd:cd12119 173 GTTGNPKGVVYSHrSLVLHAMAALLtDGLGLSESDVVLPVVPMFHVN----AWGLPYAaamVGAKLVLpgpYLDPASLAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 273 NLREVSPHVFTAVPRLWekiysrvLIMRSEatpfgrwafdramasgaakLEGKGGAMHAVWdflvlrniRQMIGfdrnrr 352
Cdd:cd12119 249 LIEREGVTFAAGVPTVW-------QGLLDH-------------------LEANGRDLSSLR--------RVVIG------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 353 sntGAAPiSPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIG-----------TIGCALPATELRIA-------- 413
Cdd:cd12119 289 ---GSAV-PRSLIEAFEERGVRVIHAWGMTETSPLGTVARPPSEHSNlsedeqlalraKQGRPVPGVELRIVdddgrelp 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 414 ----ENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRLKFS 489
Cdd:cd12119 365 wdgkAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKD-VIKSGGEWISSVELENAIMAH 443
|
490
....*....|
gi 1821015446 490 PFISDAVVIG 499
Cdd:cd12119 444 PAVAEAAVIG 453
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-499 |
9.53e-45 |
|
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: 162.65 E-value: 9.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 190 PEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAeSP-- 267
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLA-GPag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 268 ---DTVFDNLrevsphvftavprlWEkiysrvLIMRSEATpfgrwAFDRAMASGAAKLEGKGGAmhavwDFLVLRNirqm 344
Cdd:cd05944 80 yrnPGLFDNF--------------WK------LVERYRIT-----SLSTVPTVYAALLQVPVNA-----DISSLRF---- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 345 igfdrnrrSNTGAAPISPDLIRWY-GALGVTLLEGYGMTETSGVASVNVI-GDNRIGTIGCALPATELRIA--------- 413
Cdd:cd05944 126 --------AMSGAAPLPVELRARFeDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvldgvgrll 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 414 ------ENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLK 487
Cdd:cd05944 198 rdcapdEVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIR-GGHNIDPALIEEALL 276
|
330
....*....|..
gi 1821015446 488 FSPFISDAVVIG 499
Cdd:cd05944 277 RHPAVAFAGAVG 288
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
179-502 |
3.57e-44 |
|
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: 162.94 E-value: 3.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 179 ERFRIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVG 258
Cdd:cd05903 81 ERFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 259 STVNFAE--SPDTVFDNLREvsphvftavprlwekiySRVLIMRSeATPFGRWAFDRAMASGAAklegkggamhavwdfl 336
Cdd:cd05903 161 APVVLQDiwDPDKALALMRE-----------------HGVTFMMG-ATPFLTDLLNAVEEAGEP---------------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 337 vLRNIRQMIgfdrnrrsnTGAAPISPDLIRWYGALGVTLLEG-YGMTETSGVASVNVIG--DNRIGTIGCALPATELRI- 412
Cdd:cd05903 207 -LSRLRTFV---------CGGATVPRSLARRAAELLGAKVCSaYGSTECPGAVTSITPApeDRRLYTDGRPLPGVEIKVv 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 ---------AENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIE 483
Cdd:cd05903 277 ddtgatlapGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVE 355
|
330 340
....*....|....*....|.
gi 1821015446 484 SRLKFSPFISDAVVIG--DRR 502
Cdd:cd05903 356 DLLLGHPGVIEAAVVAlpDER 376
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
44-499 |
1.10e-43 |
|
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: 161.31 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 44 QAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFV 123
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 124 endeqldkylevqdrvptivkvivfdpkglrdfshpkvmflsdlyeigekapdaaerfrieinasqpeDTRMLIYTSGTT 203
Cdd:cd05934 82 --------------------------------------------------------------------DPASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 204 GPPKGAMISHSNMLyqmWAGQ---QVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAE--SPDTVFDNLREVS 278
Cdd:cd05934 94 GPPKGVVITHANLT---FAGYysaRRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPrfSASRFWSDVRRYG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 279 PHVFTAVPRLWEkiysrvLIMRSEATPFgrwafDRAmasgaaklegkggamhavwdflvlrnirqmigfdrNRRSNTGAA 358
Cdd:cd05934 171 ATVTNYLGAMLS------YLLAQPPSPD-----DRA-----------------------------------HRLRAAYGA 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 359 PISPDLIR-WYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIA----------ENGEICLK---GPN 424
Cdd:cd05934 205 PNPPELHEeFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVdddgqelpagEPGELVIRglrGWG 284
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821015446 425 VFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05934 285 FFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKD-MIRRRGENISSAEVERAILRHPAVREAAVVA 358
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
47-499 |
1.10e-43 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 161.85 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 47 SWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFveND 126
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLL--TD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 127 EQLDKylevqdrvptivKVIVFDpkglrdfshpkvmflsDLYEIGekAPDAAErfrIEINASQP-EDTRMLIYTSGTTGP 205
Cdd:TIGR01923 79 SLLEE------------KDFQAD----------------SLDRIE--AAGRYE---TSLSASFNmDQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 206 PKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLEriVSVEFP-IAVGSTVNFAESPDTVFDNL-REVSPHVfT 283
Cdd:TIGR01923 126 PKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISG--LSILFRwLIEGATLRIVDKFNQLLEMIaNERVTHI-S 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 284 AVPRLWEKIysrvliMRSEATPfgrwafdramasgaaklegkggamhavwdfLVLRNIRqmigfdrnrrsnTGAAPISPD 363
Cdd:TIGR01923 203 LVPTQLNRL------LDEGGHN------------------------------ENLRKIL------------LGGSAIPAP 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 364 LIRWYGALGVTLLEGYGMTET-SGVASVNVIGDNRIGTIGCALPATELRI-----AENGEICLKGPNVFKGYWRKPEKTA 437
Cdd:TIGR01923 235 LIEEAQQYGLPIYLSYGMTETcSQVTTATPEMLHARPDVGRPLAGREIKIkvdnkEGHGEIMVKGANLMKGYLYQGELTP 314
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821015446 438 EDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:TIGR01923 315 AFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIIS-GGENIYPEEIETVLYQHPGIQEAVVVP 375
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-499 |
3.33e-43 |
|
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: 158.21 E-value: 3.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 190 PEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPDT 269
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 270 VFDNLREVSphvftavprlwekiysrvlimrseatpfgrwafdramasgaaklEGKGGAMHAVWD-FLVLRNIRQMIGFD 348
Cdd:cd05917 81 PLAVLEAIE--------------------------------------------KEKCTALHGVPTmFIAELEHPDFDKFD 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 349 --RNRRSNTGAAPISPDLI-RWYGALGVT-LLEGYGMTETSGVASVNVIGDN---RIGTIGCALPATELRI--------- 412
Cdd:cd05917 117 lsSLRTGIMAGAPCPPELMkRVIEVMNMKdVTIAYGMTETSPVSTQTRTDDSiekRVNTVGRIMPHTEAKIvdpeggivp 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 --AENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFS 489
Cdd:cd05917 197 pvGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENIYPREIEEFLHTH 275
|
330
....*....|
gi 1821015446 490 PFISDAVVIG 499
Cdd:cd05917 276 PKVSDVQVVG 285
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
46-499 |
8.31e-43 |
|
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: 161.00 E-value: 8.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVEN 125
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 126 D--EQLDKYLEvqDRVPTIVKVIVFDPKGlrdfSHPKVMFLSDLyeIGEKAPDAAErfrieiNASQPEDTRMLIYTSGTT 203
Cdd:cd05959 110 ElaPVLAAALT--KSEHTLVVLIVSGGAG----PEAGALLLAEL--VAAEAEQLKP------AATHADDPAFWLYSSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 204 GPPKGAMISHSNMLYQM-WAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVG-STVNFAE--SPDTVFDNLREVSP 279
Cdd:cd05959 176 GRPKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGaTTVLMPErpTPAAVFKRIRRYRP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 280 HVFTAVPRLwekiYSRVLimRSEATPfgrwafDRamasgaaklegkggamhavwdflvlrnirqmiGFDRNRRSNTGAAP 359
Cdd:cd05959 256 TVFFGVPTL----YAAML--AAPNLP------SR--------------------------------DLSSLRLCVSAGEA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 360 ISPDLI-RWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRI----------AENGEICLKGPNVFKG 428
Cdd:cd05959 292 LPAEVGeRWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELrdedggdvadGEPGELYVRGPSSATM 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821015446 429 YWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05959 372 YWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADD-MLKVSGIWVSPFEVESALVQHPAVLEAAVVG 441
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
31-499 |
2.63e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 159.94 E-value: 2.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 31 DATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLE 110
Cdd:PRK07786 32 DAPALRFLG----NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 111 YLINDSGSAFLFVEnDEQLDKYLEVQDRVPTIVKVIVfdpkgLRDFSHPKVMFLSDLyeIGEKAPDAAErfrieinASQP 190
Cdd:PRK07786 108 FLVSDCGAHVVVTE-AALAPVATAVRDIVPLLSTVVV-----AGGSSDDSVLGYEDL--LAEAGPAHAP-------VDIP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 191 EDTRMLI-YTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVD-PKDEQLCFLPLCHVlerivsvefpIAVGSTVNF----- 263
Cdd:PRK07786 173 NDSPALImYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADiNSDVGFVGVPLFHI----------AGIGSMLPGlllga 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 264 --------AESPDTVFDNL-REVSPHVFTaVPRLWEKIYSrvlimrsEATPFGRwafdramasgaaklegkggamhavwd 334
Cdd:PRK07786 243 ptviyplgAFDPGQLLDVLeAEKVTGIFL-VPAQWQAVCA-------EQQARPR-------------------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 335 FLVLRNIrqmigfdrnrrsNTGAAPISPDLIRWYGAL--GVTLLEGYGMTETSGVASVnVIGDN---RIGTIGCALPATE 409
Cdd:PRK07786 289 DLALRVL------------SWGAAPASDTLLRQMAATfpEAQILAAFGQTEMSPVTCM-LLGEDairKLGSVGKVIPTVA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 410 LRI----------AENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITP 479
Cdd:PRK07786 356 ARVvdenmndvpvGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYC 434
|
490 500
....*....|....*....|
gi 1821015446 480 AEIESRLKFSPFISDAVVIG 499
Cdd:PRK07786 435 AEVENVLASHPDIVEVAVIG 454
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
181-499 |
2.21e-41 |
|
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: 154.81 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 181 FRIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHV-----LERIVSVEFPI 255
Cdd:cd05912 67 FQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHIsglsiLMRSVIYGMTV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 256 avgsTVNFAESPDTVFDNLREVSPHVFTAVPRLWEKIYSRVLIMRSEatpfgrwafdramasgaaklegkggamhavwdf 335
Cdd:cd05912 147 ----YLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPN--------------------------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 336 lvlrNIRQMIgfdrnrrsnTGAAPISPDLIRWYGALGVTLLEGYGMTET-SGVASVNvIGD--NRIGTIGCALPATELRI 412
Cdd:cd05912 190 ----NLRCIL---------LGGGPAPKPLLEQCKEKGIPVYQSYGMTETcSQIVTLS-PEDalNKIGSAGKPLFPVELKI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 A-------ENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIItAGGKNITPAEIESR 485
Cdd:cd05912 256 EddgqppyEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEV 334
|
330
....*....|....
gi 1821015446 486 LKFSPFISDAVVIG 499
Cdd:cd05912 335 LLSHPAIKEAGVVG 348
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
150-526 |
1.01e-40 |
|
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: 154.41 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 150 PKGLRDFSHPKVMFLSDLYE-----------IGEKAPDAAERFRIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLY 218
Cdd:cd05909 95 HHLFDVEYDARIVYLEDLRAkiskadkckafLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 219 QMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESP-DTvfdnlrevsphvfTAVPRLWEKIYSRVL 297
Cdd:cd05909 175 NVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPlDY-------------KKIPELIYDKKATIL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 298 ImrseATPfgrwAFDRAMASGAAKlegkggamhavWDFLVLRNIRqmigfdrnrrsnTGAAPISPDLIR-WYGALGVTLL 376
Cdd:cd05909 242 L----GTP----TFLRGYARAAHP-----------EDFSSLRLVV------------AGAEKLKDTLRQeFQEKFGIRIL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 377 EGYGMTETSGVASVNVIG-DNRIGTIGCALPATELRI-----------AENGEICLKGPNVFKGYWRKPEKTAEDIRDGW 444
Cdd:cd05909 291 EGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIvsvetheevpiGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGW 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 445 LYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRL-KFSP--FISDAVVIGDRRK-----YLTVLIMIDQENV 516
Cdd:cd05909 371 YDTGDIGKIDGEGFLTITGRLSR-FAKIAGEMVSLEAIEDILsEILPedNEVAVVSVPDGRKgekivLLTTTTDTDPSSL 449
|
410
....*....|
gi 1821015446 517 EKYAQDHQIP 526
Cdd:cd05909 450 NDILKNAGIS 459
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
192-499 |
3.12e-39 |
|
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: 146.65 E-value: 3.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 192 DTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAEspdtvF 271
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEK-----F 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 272 DNLREVSphvftavprlwekiysrvLIMRSEATPFGrwAFDRAMASGAAKLEGKGgamhavwdfLVLRNIRQMIGFDrnr 351
Cdd:cd17637 76 DPAEALE------------------LIEEEKVTLMG--SFPPILSNLLDAAEKSG---------VDLSSLRHVLGLD--- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 352 rsntgaapiSPDLI-RWYGALGVTLLEGYGMTETSGVASVNVIgDNRIGTIGCALPATELRIA----------ENGEICL 420
Cdd:cd17637 124 ---------APETIqRFEETTGATFWSLYGQTETSGLVTLSPY-RERPGSAGRPGPLVRVRIVddndrpvpagETGEIVV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 421 KGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRV--KDIIITaGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:cd17637 194 RGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPAEVEKVILEHPAIAEVCVI 272
|
.
gi 1821015446 499 G 499
Cdd:cd17637 273 G 273
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
196-499 |
3.98e-39 |
|
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: 146.32 E-value: 3.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 196 LIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHV--LERIVSVefpIAVGSTVNFAESPDTVFDN 273
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVggLAILVRS---LLAGAELVLLERNQALAED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 274 LREVSPHVFTAVPR-LWekiysrvlimrseatpfgrwafdRAMASGAAklegkggamhAVWdflvLRNIRQMIgfdrnrr 352
Cdd:cd17630 82 LAPPGVTHVSLVPTqLQ-----------------------RLLDSGQG----------PAA----LKSLRAVL------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 353 snTGAAPISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIAENGEICLKGPNVFKGYWRK 432
Cdd:cd17630 118 --LGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVEDGEIWVGGASLAMGYLRG 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821015446 433 PEKTAEDiRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd17630 196 QLVPEFN-EDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAALAAHPAVRDAFVVG 260
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
157-499 |
4.16e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 149.96 E-value: 4.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 157 SHPKVMFLSDLYEIGEKAPDAAERFRIEINASQPEDTR--------MLIYTSGTTGPPKGAMISHSNmLYQMWAGQQVL- 227
Cdd:PRK09088 93 AEPRLLLGDDAVAAGRTDVEDLAAFIASADALEPADTPsippervsLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLg 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 228 RVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVnfaespdtvfdnlrEVSPHVftavprlwekiysrvlimrsEATPFG 307
Cdd:PRK09088 172 RVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSI--------------LVSNGF--------------------EPKRTL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 308 RWAFDRAMasgaaklegkgGAMHAVWDFLVLRNIRQMIGFDRNRRSN-----TGAAPISPDLIRWYGALGVTLLEGYGMT 382
Cdd:PRK09088 218 GRLGDPAL-----------GITHYFCVPQMAQAFRAQPGFDAAALRHltalfTGGAPHAAEDILGWLDDGIPMVDGFGMS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 383 ETSGVASVNV---IGDNRIGTIGCALPATELRIAEN----------GEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTG 448
Cdd:PRK09088 287 EAGTVFGMSVdcdVIRAKAGAAGIPTPTVQTRVVDDqgndcpagvpGELLLRGPNLSPGYWRRPQATARAFtGDGWFRTG 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1821015446 449 DVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK09088 367 DIARRDADGFFWVVDRKKDMFIS-GGENVYPAEIEAVLADHPGIRECAVVG 416
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
190-499 |
7.72e-39 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 150.59 E-value: 7.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 190 PEDTRMLIYTSGTTGPPKGAMISHSNMLYQM----WAGQQVLRvDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAE 265
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqakAAYGPLLH-PGKELVVTALPLYHIFALTVNCLLFIELGGQNLLIT 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 266 SPDTVFDNLREVSPHVFTAVprlwekiysrvlimrseatpfgrwafdramaSGAAKLegkggamhavwdFLVLRNIRQM- 344
Cdd:PRK08974 284 NPRDIPGFVKELKKYPFTAI-------------------------------TGVNTL------------FNALLNNEEFq 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 345 -IGFDRNRRSNTGAAPISPDLI-RWYGALGVTLLEGYGMTETSGVASVNVIG-DNRIGTIGCALPATELRI--------- 412
Cdd:PRK08974 321 eLDFSSLKLSVGGGMAVQQAVAeRWVKLTGQYLLEGYGLTECSPLVSVNPYDlDYYSGSIGLPVPSTEIKLvdddgnevp 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 -AENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAgGKNITPAEIESRLKFSPF 491
Cdd:PRK08974 401 pGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMLHPK 479
|
....*...
gi 1821015446 492 ISDAVVIG 499
Cdd:PRK08974 480 VLEVAAVG 487
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
55-499 |
1.70e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 148.98 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 55 SQAIGMgLIELGLTRGTPVSILSEDNKEwlycDLAISAAGGIPSGVYTTDSA-GQLE---YLINDSGSAFLFVENDEQLD 130
Cdd:PRK06188 48 SRYIQA-FEALGLGTGDAVALLSLNRPE----VLMAIGAAQLAGLRRTALHPlGSLDdhaYVLEDAGISTLIVDPAPFVE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 131 KYLEVQDRVPTIVKVIVFDPkglrdfshpkVMFLSDLYEIGEKAPDAAERfrieiNASQPEDTRMLIYTSGTTGPPKGAM 210
Cdd:PRK06188 123 RALALLARVPSLKHVLTLGP----------VPDGVDLLAAAAKFGPAPLV-----AAALPPDIAGLAYTGGTTGKPKGVM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 211 ISHSnmlyQMWAGQQVLRVD---PKDEQ-LCFLPLCHVlerivSVEFPIAV---GSTVNFAES--PDTVfdnLREVSPHV 281
Cdd:PRK06188 188 GTHR----SIATMAQIQLAEwewPADPRfLMCTPLSHA-----GGAFFLPTllrGGTVIVLAKfdPAEV---LRAIEEQR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 282 FTA---VPRLwekIYSrvlIMRSEATPfgrwafDRAMASgaakLEgkggamhavwdfLVLrnirqmigfdrnrrsnTGAA 358
Cdd:PRK06188 256 ITAtflVPTM---IYA---LLDHPDLR------TRDLSS----LE------------TVY----------------YGAS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 359 PISPDLIRWYGA-LGVTLLEGYGMTETSGVASVNVIGDN------RIGTIGCALPATELRI----------AENGEICLK 421
Cdd:PRK06188 292 PMSPVRLAEAIErFGPIFAQYYGQTEAPMVITYLRKRDHdpddpkRLTSCGRPTPGLRVALldedgrevaqGEVGEICVR 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821015446 422 GPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK06188 372 GPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVT-GGFNVFPREVEDVLAEHPAVAQVAVIG 448
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
23-502 |
2.18e-38 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 149.05 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 23 AAKCAERGDATAHReKDFGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYT 102
Cdd:PRK13295 34 VASCPDKTAVTAVR-LGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 103 TDSAGQLEYLINDSGSAFLFVE------NDEQLDKylEVQDRVPTIVKVIVFDPKGLRDFSHpkvmFLSDlyEIGEKAPD 176
Cdd:PRK13295 113 IFRERELSFMLKHAESKVLVVPktfrgfDHAAMAR--RLRPELPALRHVVVVGGDGADSFEA----LLIT--PAWEQEPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 177 AAERFRIeiNASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIA 256
Cdd:PRK13295 185 APAILAR--LRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 257 VGSTVNFAEspdtVFDNLREVsphvftavprlwEKIYSRVLIMRSEATPFgrwAFDRAmasGAAKLEGkggamhavwdfl 336
Cdd:PRK13295 263 LGATAVLQD----IWDPARAA------------ELIRTEGVTFTMASTPF---LTDLT---RAVKESG------------ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 337 vlRNIRQMigfdrnRRSNTGAAPISPDLI-RWYGALGVTLLEGYGMTETsGVASVNVIGDN---RIGTIGCALPATELRI 412
Cdd:PRK13295 309 --RPVSSL------RTFLCAGAPIPGALVeRARAALGAKIVSAWGMTEN-GAVTLTKLDDPderASTTDGCPLPGVEVRV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 ----------AENGEICLKGPNVFKGYWRKPEKTAEDIrDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEI 482
Cdd:PRK13295 380 vdadgaplpaGQIGRLQVRGCSNFGGYLKRPQLNGTDA-DGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEI 457
|
490 500
....*....|....*....|..
gi 1821015446 483 ESRLKFSPFISDAVVIG--DRR 502
Cdd:PRK13295 458 EALLYRHPAIAQVAIVAypDER 479
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
192-548 |
2.19e-38 |
|
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: 144.18 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 192 DTRMLIYTSGTTGPPKGAMISH--SNMLYQMWAGQQVLRVDpkDEQLCFLPLCHVLERIVSVEFPIAVGSTVnfaeSPDT 269
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrqTLRAAAAWADCADLTED--DRYLIINPFFHTFGYKAGIVACLLTGATV----VPVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 270 VFDnlrevSPHVFTAVPRlwekiySRVLIMRSEATPFgrwafdramasgaaklegkggamHAVWDFLVLRNirqmigFDR 349
Cdd:cd17638 75 VFD-----VDAILEAIER------ERITVLPGPPTLF-----------------------QSLLDHPGRKK------FDL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 350 N--RRSNTGAAPISPDLI-RWYGALGV-TLLEGYGMTEtSGVASVNVIGDNRI---GTIGCALPATELRIAENGEICLKG 422
Cdd:cd17638 115 SslRAAVTGAATVPVELVrRMRSELGFeTVLTAYGLTE-AGVATMCRPGDDAEtvaTTCGRACPGFEVRIADDGEVLVRG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 423 PNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIItAGGKNITPAEIESRLKFSPFISDAVVIG-- 499
Cdd:cd17638 194 YNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGALAEHPGVAQVAVIGvp 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821015446 500 DRR-----KYLTVL---IMIDQENVEKYAQDHQIPFsdfasltRAPQVVDLIDGVVR 548
Cdd:cd17638 273 DERmgevgKAFVVArpgVTLTEEDVIAWCRERLANY-------KVPRFVRFLDELPR 322
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
191-499 |
2.40e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 146.12 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 191 EDTRMLIYTSGTTGPPKGAMISHSNMLYQMwagQQV---LRVDPKDEQLCF----------LPLCHVLERIVSVEFPIAV 257
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANM---LQVracLSQLGPDGQPLMkegqevmiapLPLYHIYAFTANCMCMMVS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 258 GSTvnfaespDTVFDNLREVSPHVftavprlwekiysrvlimrseaTPFGRWAFdramasgaAKLEGKGGAMHAVWDFLV 337
Cdd:PRK12492 284 GNH-------NVLITNPRDIPGFI----------------------KELGKWRF--------SALLGLNTLFVALMDHPG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 338 LRNIrqmiGFDRNRRSNTGA-APISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGD-NRIGTIGCALPAT------- 408
Cdd:PRK12492 327 FKDL----DFSALKLTNSGGtALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGElARLGTVGIPVPGTalkvidd 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 409 ---ELRIAENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAgGKNITPAEIES 484
Cdd:PRK12492 403 dgnELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS-GFNVYPNEIED 481
|
330
....*....|....*
gi 1821015446 485 RLKFSPFISDAVVIG 499
Cdd:PRK12492 482 VVMAHPKVANCAAIG 496
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
44-501 |
3.36e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 144.64 E-value: 3.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 44 QAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFV 123
Cdd:PRK06145 26 QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 124 enDEQLDKylevqdRVPTIVKVIVFDPKGLRDFSHpkvmflsdLYEIGEKAPDAAerfrieinASQPEDTRMLIYTSGTT 203
Cdd:PRK06145 106 --DEEFDA------IVALETPKIVIDAAAQADSRR--------LAQGGLEIPPQA--------AVAPTDLVRLMYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 204 GPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVleriVSVEFP----IAVGSTV----NFaeSPDTVfdnLR 275
Cdd:PRK06145 162 DRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHV----GAFDLPgiavLWVGGTLrihrEF--DPEAV---LA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 276 EVSPHVFTAVprlWekiYSRVLIMRSEATPfGRWAFDramasgaaklegkggamhavwdflvLRNIRQMIGfdrnrrsnt 355
Cdd:PRK06145 233 AIERHRLTCA---W---MAPVMLSRVLTVP-DRDRFD-------------------------LDSLAWCIG--------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 356 GAAPISPDLIRWYGAL--GVTLLEGYGMTETSGVASVNVIGD--NRIGTIGCALPATELRIAE----------NGEICLK 421
Cdd:PRK06145 272 GGEKTPESRIRDFTRVftRARYIDAYGLTETCSGDTLMEAGReiEKIGSTGRALAHVEIRIADgagrwlppnmKGEICMR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 422 GPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIGDR 501
Cdd:PRK06145 352 GPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEVERVIYELPEVAEAAVIGVH 430
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
61-500 |
6.86e-37 |
|
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: 142.96 E-value: 6.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 61 GLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYT----TDSAGQLEYLINDSGSAFLFVEN--DEQLDKYLe 134
Cdd:cd05922 9 ALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVplnpTLKESVLRYLVADAGGRIVLADAgaADRLRDAL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 135 VQDRVPTIVkvivFDPKGLRDFSHPkvmflsdlyeigekapdaAERFRIEinasqPEDTRMLIYTSGTTGPPKGAMISHS 214
Cdd:cd05922 88 PASPDPGTV----LDADGIRAARAS------------------APAHEVS-----HEDLALLLYTSGSTGSPKLVRLSHQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 215 NMLYQMWAGQQVLRVDPKDEQLCFLPL--CHVLERIVSvefPIAVGSTVNFAES---PDTVFDNLREVSPHVFTAVPRLW 289
Cdd:cd05922 141 NLLANARSIAEYLGITADDRALTVLPLsyDYGLSVLNT---HLLRGATLVLTNDgvlDDAFWEDLREHGATGLAGVPSTY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 290 EKIysRVLIMRSEATPFGRWafdramasgaakLEGKGGAMHAVwdflVLRNIRQmigfdrnrrsntgAAPispdlirwyg 369
Cdd:cd05922 218 AML--TRLGFDPAKLPSLRY------------LTQAGGRLPQE----TIARLRE-------------LLP---------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 370 alGVTLLEGYGMTETSGVASV---NVIgDNRIGTIGCALPATELRI----------AENGEICLKGPNVFKGYWRKP-EK 435
Cdd:cd05922 257 --GAQVYVMYGQTEATRRMTYlppERI-LEKPGSIGLAIPGGEFEIldddgtptppGEPGEIVHRGPNVMKGYWNDPpYR 333
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821015446 436 TAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKnITPAEIESRLKFSPFISDAVVIGD 500
Cdd:cd05922 334 RKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNR-ISPTEIEAAARSIGLIIEAAAVGL 397
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
100-499 |
7.57e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 144.91 E-value: 7.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 100 VYTtdsAGQLEYLINDSGS-AFLFVEN-DEQLDKYL-----------EVQDRVPTIVKVIV-----FDPKGLRDFSHPKV 161
Cdd:PRK05677 108 LYT---AREMEHQFNDSGAkALVCLANmAHLAEKVLpktgvkhvivtEVADMLPPLKRLLInavvkHVKKMVPAYHLPQA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 162 MFLSDLYEIGEKAPdaaerfrIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVL--RVDPKDEQLCF- 238
Cdd:PRK05677 185 VKFNDALAKGAGQP-------VTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMgsNLNEGCEILIAp 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 239 LPLCHVLERIVSVEFPIAVGSTVNFAESPDTVFDNLREVSPHVFTAVPRLwEKIYsrVLIMRSEATpfgrwafdRAMASG 318
Cdd:PRK05677 258 LPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGL-NTLF--VALCNNEAF--------RKLDFS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 319 AAKLEGKGGAmhavwdflvlrnirqmigfdrnrrsntgaAPISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRI 398
Cdd:PRK05677 327 ALKLTLSGGM-----------------------------ALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQV 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 399 GTIGCALPAT----------ELRIAENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKD 467
Cdd:PRK05677 378 GTIGIPVPSTlckvidddgnELPLGEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKD 457
|
410 420 430
....*....|....*....|....*....|..
gi 1821015446 468 IIITAgGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK05677 458 MILVS-GFNVYPNELEDVLAALPGVLQCAAIG 488
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
23-600 |
9.49e-37 |
|
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: 144.50 E-value: 9.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 23 AAKCAERGDAT--AHREKDfGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAgGIP--- 97
Cdd:cd05921 2 AHWARQAPDRTwlAEREGN-GGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYA-GVPaap 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 98 -SGVYTTDSA--GQLEYLINDSGSAFLFVENDEQLDKYLEVQDRVPTIVKVIVFDPKGLRDFSHPKVMflsdLYEIGEKA 174
Cdd:cd05921 80 vSPAYSLMSQdlAKLKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISFAELA----ATPPTAAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 175 PDAaerfrieINASQPEDTRMLIYTSGTTGPPKgAMISHSNMLYQMWAGQQVLRVDPKDEQ---LCFLPLCHVLERIVSV 251
Cdd:cd05921 156 DAA-------FAAVGPDTVAKFLFTSGSTGLPK-AVINTQRMLCANQAMLEQTYPFFGEEPpvlVDWLPWNHTFGGNHNF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 252 EFPIAVGSTV----------NFAESpdtvFDNLREVSPHVFTAVPRLWEKIysrVLIMRSEATPFGRWaFDR--AMASGA 319
Cdd:cd05921 228 NLVLYNGGTLyiddgkpmpgGFEET----LRNLREISPTVYFNVPAGWEML---VAALEKDEALRRRF-FKRlkLMFYAG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 320 AKLEgkggamHAVWDFLvlrnirqmigfDRNRRSNTGAApispdlirwygalgVTLLEGYGMTETSGVASVNVIGDNRIG 399
Cdd:cd05921 300 AGLS------QDVWDRL-----------QALAVATVGER--------------IPMMAGLGATETAPTATFTHWPTERSG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 400 TIGCALPATELRIAENG---EICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDG----AITITGRV-KDIII 470
Cdd:cd05921 349 LIGLPAPGTELKLVPSGgkyEVRVKGPNVTPGYWRQPELTAQAFdEEGFYCLGDAAKLADPDdpakGLVFDGRVaEDFKL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 471 TAGG-KNITPAEIESRLKFSPFISDAVVIGDRRKYLTVLIMIDQENVEKYAqdhQIPFSDFASLTRAPQVVDLIdgvVRE 549
Cdd:cd05921 429 ASGTwVSVGPLRARAVAACAPLVHDAVVAGEDRAEVGALVFPDLLACRRLV---GLQEASDAEVLRHAKVRAAF---RDR 502
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1821015446 550 VNTHFAQVE----QIKYFRLIDILLTAEDDELTPTMKLKRGFVEKKHAALIDQMY 600
Cdd:cd05921 503 LAALNGEATgsssRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLY 557
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
26-483 |
3.15e-36 |
|
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: 142.76 E-value: 3.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 26 CAERGDATAHR--EKDFGIWQAYSWSDWYDRSQAIGMGLIELGLtRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTT 103
Cdd:cd05931 3 AAARPDRPAYTflDDEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 104 DSAGQLEYLIN---DSGSAFLfvendeqldkyLEVQDRVPTIVKVIVFDPKGLRDfshpkVMFLSDLYEIGekAPDAAER 180
Cdd:cd05931 82 TPGRHAERLAAilaDAGPRVV-----------LTTAAALAAVRAFAASRPAAGTP-----RLLVVDLLPDT--SAADWPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 181 FRIEinasqPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGST 260
Cdd:cd05931 144 PSPD-----PDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 261 VNFaespdtvfdnlreVSPHVFTAVPRLWEKiysrvLIMRSEAT-----PFG-RWAFDRAMASGAAKLegkggamhavwD 334
Cdd:cd05931 219 SVL-------------MSPAAFLRRPLRWLR-----LISRYRATisaapNFAyDLCVRRVRDEDLEGL-----------D 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 335 FLVLRNIrqMIGfdrnrrsntgAAPISPDLIRW-------YGALGVTLLEGYGMTETSGVASVNVIGDNRIGTI------ 401
Cdd:cd05931 270 LSSWRVA--LNG----------AEPVRPATLRRfaeafapFGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLRvdrdal 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 402 --------------------GCALPATELRI-----------AENGEICLKGPNVFKGYWRKPEKTAE-------DIRDG 443
Cdd:cd05931 338 agravavaaddpaarelvscGRPLPDQEVRIvdpetgrelpdGEVGEIWVRGPSVASGYWGRPEATAEtfgalaaTDEGG 417
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1821015446 444 WLYTGDVGRIGdDGAITITGRVKDIIITAgGKNITPAEIE 483
Cdd:cd05931 418 WLRTGDLGFLH-DGELYITGRLKDLIIVR-GRNHYPQDIE 455
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
61-499 |
6.68e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 141.22 E-value: 6.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 61 GLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVEND--EQLDKYLEVQDR 138
Cdd:PRK08316 52 ALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPAlaPTAEAALALLPV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 139 VPTIVKVIV---FDPKGLRDFShpkvmflsDLYEIGEKAPDAAErfrIEInasqpEDTRMLIYTSGTTGPPKGAMISHSN 215
Cdd:PRK08316 132 DTLILSLVLggrEAPGGWLDFA--------DWAEAGSVAEPDVE---LAD-----DDLAQILYTSGTESLPKGAMLTHRA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 216 MLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPD--TVFDNLREVSPHVFTAVPRLWekiy 293
Cdd:PRK08316 196 LIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDpeLILRTIEAERITSFFAPPTVW---- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 294 srVLIMRSeatPfgrwAFDRAMASGAAKleGKGGAmhAVWDFLVLRNIRQMIgfdrnrrsntgaapisPDLiRWYGAlgv 373
Cdd:PRK08316 272 --ISLLRH---P----DFDTRDLSSLRK--GYYGA--SIMPVEVLKELRERL----------------PGL-RFYNC--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 374 tllegYGMTETSGVASVnvIG----DNRIGTIGCALPATELRI----------AENGEICLKGPNVFKGYWRKPEKTAED 439
Cdd:PRK08316 319 -----YGQTEIAPLATV--LGpeehLRRPGSAGRPVLNVETRVvdddgndvapGEVGEIVHRSPQLMLGYWDDPEKTAEA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 440 IRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK08316 392 FRGGWFHSGDLGVMDEEGYITVVDRKKDMIKT-GGENVASREVEEALYTHPAVAEVAVIG 450
|
|
| pimA |
TIGR03205 |
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found ... |
104-504 |
7.71e-36 |
|
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found in a characteristic operon pimFABCDE for the metabolism of pimelate and related compounds. It is found, so far, in Bradyrhizobium japonicum and several strains of Rhodopseudomonas palustris. PimA from R. palustris was shown to be active as a CoA ligase for C(7) to C(14) dicarboxylates and fatty acids.
Pssm-ID: 132249 [Multi-domain] Cd Length: 541 Bit Score: 141.64 E-value: 7.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 104 DSAGQLEYLINDSGSAFLFVENDEQLdkylevqdrVPTIVKvivFDPKGLRDF--------------------SHPKVMF 163
Cdd:TIGR03205 105 DGERALSHKLSDSGARLLITSDLAAL---------LPMALK---FLEKGLLDRlivceddnwgkvgtpqapipADPRIVT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 164 LSDLYEiGEKAPdaaerfrIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNM-----LYQMWAGQQVLRVDPKDEQLCF 238
Cdd:TIGR03205 173 YADFVK-GAAAP-------AEWPAVTPDDVALLQYTGGTTGLPKGAMLTHGNLtsavsIYDVWGKPSRATRGDVERVICV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 239 LPLCHVLERIVSVEFPIAVGSTVNFAESPD--TVFDNLREVSPHVFTAVPRLWEKIysrvlimrseatpfgrwafdrama 316
Cdd:TIGR03205 245 LPLFHIYALTVILLRSLRRGDLISLHQRFDvaAVFRDIEEKRATVFPGVPTMWIAL------------------------ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 317 SGAAKLEGKggamhavwDFLVLrnirQMIGfdrnrrsnTGAAPISPDLIRWYG-ALGVTLLEGYGMTET-SGVASVNVIG 394
Cdd:TIGR03205 301 ANDPSLEKR--------DLSSL----ATIG--------SGGAPLPVEVANFFErKTGLKLKSGWGMTETcSPGTGHPPEG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 395 DNRIGTIGCALPATELRI------------AENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITIT 462
Cdd:TIGR03205 361 PDKPGSIGLMLPGIELDVvslddptkvlppGEVGELRIRGPNVTRGYWNRPEESAEAFVGDRFLTGDIGYMDTDGYFFLV 440
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1821015446 463 GRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIGDRRKY 504
Cdd:TIGR03205 441 DRKKDMIIS-GGFNVYPQMIEQAIYEHPGVQEVIVIGIPDQY 481
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
47-499 |
9.19e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 141.71 E-value: 9.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 47 SWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVEnD 126
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCL-D 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 127 EQLDKYLEVQDR-------VPTIVKVIVFDPKGLRDFSHPK----VMFLSD-----LYEIGEKAPDAAerfrIEINASQP 190
Cdd:PRK06710 130 LVFPRVTNVQSAtkiehviVTRIADFLPFPKNLLYPFVQKKqsnlVVKVSEsetihLWNSVEKEVNTG----VEVPCDPE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 191 EDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLR--VDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPD 268
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYncKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 269 T--VFDNLREVSPHVFTAVPRLWEKIYSRVLIMRSEATPFgrwafdRAMASGAAKLEgkggamhavwdflvlrnIRQMIG 346
Cdd:PRK06710 286 MkmVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSI------RACISGSAPLP-----------------VEVQEK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 347 FDRnrrsntgaapispdlirwygALGVTLLEGYGMTETSGVASVNVIGDNRI-GTIGCALPATELRI-----------AE 414
Cdd:PRK06710 343 FET--------------------VTGGKLVEGYGLTESSPVTHSNFLWEKRVpGSIGVPWPDTEAMImsletgealppGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 415 NGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIItAGGKNITPAEIESRLKFSPFISD 494
Cdd:PRK06710 403 IGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIV-ASGFNVYPREVEEVLYEHEKVQE 481
|
....*
gi 1821015446 495 AVVIG 499
Cdd:PRK06710 482 VVTIG 486
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
6-499 |
2.47e-35 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 140.40 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 6 LPKPILIDGADTVVKLWAAKCAERGDATAHreKDFGIWQAYSWSDWYDRSQAIGMgLIELGLTRGTPVSILSEDNKEWLY 85
Cdd:PRK08751 15 VAAEIDLEQFRTVAEVFATSVAKFADRPAY--HSFGKTITYREADQLVEQFAAYL-LGELQLKKGDRVALMMPNCLQYPI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 86 CDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVEND-----EQLDKYLEVQDRVPTIVKVIVFDPKG-LRDFSHP 159
Cdd:PRK08751 92 ATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNfgttvQQVIADTPVKQVITTGLGDMLGFPKAaLVNFVVK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 160 KVMFLSDLYEIgekapDAAERFR-------------IEInasQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQV 226
Cdd:PRK08751 172 YVKKLVPEYRI-----NGAIRFRealalgrkhsmptLQI---EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 227 LRVDPKDEQ-----LCFLPLCHVLERIVSVEFPIAVGSTVNFAESP---DTVFDNLREVSPHVFTAVPRLWEKIYSrvli 298
Cdd:PRK08751 244 LAGTGKLEEgcevvITALPLYHIFALTANGLVFMKIGGCNHLISNPrdmPGFVKELKKTRFTAFTGVNTLFNGLLN---- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 299 mrseaTPfgrwAFDRAMASGAAKLEGKGGAmhavwdflVLRNIRQmigfdrnrrsntgaapispdliRWYGALGVTLLEG 378
Cdd:PRK08751 320 -----TP----GFDQIDFSSLKMTLGGGMA--------VQRSVAE----------------------RWKQVTGLTLVEA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 379 YGMTETSGVASVNVIG-DNRIGTIGCALPATE----------LRIAENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLY 446
Cdd:PRK08751 361 YGLTETSPAACINPLTlKEYNGSIGLPIPSTDacikddagtvLAIGEIGELCIKGPQVMKGYWKRPEETAKVMdADGWLH 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1821015446 447 TGDVGRIGDDGAITITGRVKDIIITAgGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK08751 441 TGDIARMDEQGFVYIVDRKKDMILVS-GFNVYPNEIEDVIAMMPGVLEVAAVG 492
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
17-499 |
3.47e-35 |
|
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: 139.15 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 17 TVVKLWAAKCAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGI 96
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHD----RTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 97 PSGVYTTDSAGQLEYLINDSGSAFLfVENDEQLDKYLEVQDRVPTIVKVIVFDPKGLRDFSHPKVMFLSdlYEIGEKAPD 176
Cdd:TIGR03098 77 FVPINPLLKAEQVAHILADCNVRLL-VTSSERLDLLHPALPGCHDLRTLIIVGDPAHASEGHPGEEPAS--WPKLLALGD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 177 AAERFRIeinasQPEDTRMLIYTSGTTGPPKGAMISHSNmlyqMWAGQQV----LRVDPKDEQLCFLPLC--HVLERIVS 250
Cdd:TIGR03098 154 ADPPHPV-----IDSDMAAILYTSGSTGRPKGVVLSHRN----LVAGAQSvatyLENRPDDRLLAVLPLSfdYGFNQLTT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 251 VefpIAVGSTV---NFAespdTVFDNLREVSPH---VFTAVPRLWEKIYSrvLIMRSEATPFGRWafdramasgaakLEG 324
Cdd:TIGR03098 225 A---FYVGATVvlhDYL----LPRDVLKALEKHgitGLAAVPPLWAQLAQ--LDWPESAAPSLRY------------LTN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 325 KGGAMHAVwdflVLRNIRQMIgfdrnrrSNTGAAPIspdlirwygalgvtllegYGMTE---TSGVASVNVigDNRIGTI 401
Cdd:TIGR03098 284 SGGAMPRA----TLSRLRSFL-------PNARLFLM------------------YGLTEafrSTYLPPEEV--DRRPDSI 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 402 GCALPATELRIA----------ENGEICLKGPNVFKGYWRKPEKTAEDIR------------DGWLYTGDVGRIGDDGAI 459
Cdd:TIGR03098 333 GKAIPNAEVLVLredgsecapgEEGELVHRGALVAMGYWNDPEKTAERFRplppfpgelhlpELAVWSGDTVRRDEEGFL 412
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1821015446 460 TITGRVKDIIITAGGKnITPAEIESRLKFSPFISDAVVIG 499
Cdd:TIGR03098 413 YFVGRRDEMIKTSGYR-VSPTEVEEVAYATGLVAEAVAFG 451
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
47-548 |
1.52e-34 |
|
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: 135.68 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 47 SWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVend 126
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 127 eqldkylevqdrvptivkvivfdpkglrdfshpkvmflsdlyeigekapdaaerfrieinASQPEDTRMLIYTSGTTGPP 206
Cdd:cd05935 80 ------------------------------------------------------------GSELDDLALIPYTSGTTGLP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 207 KGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAE--SPDTVFDNLREVSPHVFTA 284
Cdd:cd05935 100 KGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMArwDRETALELIEKYKVTFWTN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 285 VPRLWEKIYSRVLIMRSeatpfgrwafdramasgaaklegkggamhavwDFLVLRnirqMIGfdrnrrsnTGAAPISPDL 364
Cdd:cd05935 180 IPTMLVDLLATPEFKTR--------------------------------DLSSLK----VLT--------GGGAPMPPAV 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 365 I-RWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRI-----------AENGEICLKGPNVFKGYWRK 432
Cdd:cd05935 216 AeKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVidietgrelppNEVGEIVVRGPQIFKGYWNR 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 433 PEKTAED-IRDG---WLYTGDVGRIGDDGAITITGRVKDIIITAGGKnITPAEIESRLKFSPFISDAVVI-------GDR 501
Cdd:cd05935 296 PEETEESfIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK-VWPAEVEAKLYKHPAI*EVCVIsvpdervGEE 374
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1821015446 502 RKYLTVL-----IMIDQENVEKYAQDHQipfsdfaSLTRAPQVVDLIDGVVR 548
Cdd:cd05935 375 VKAFIVLrpeyrGKVTEEDIIEWAREQM-------AAYKYPREVEFVDELPR 419
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
11-541 |
2.83e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 137.87 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 11 LIDGADTVVKLWAAKCAERGDAT--AHREKDFGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDL 88
Cdd:PRK12582 44 LGPYPRSIPHLLAKWAAEAPDRPwlAQREPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 89 AISAAGgIP----SGVYTTDSAG--QLEYLINDSGSAFLFVENDEQLDKYLEVQDRvpTIVKVIVFDPKGLRDFSHPkvm 162
Cdd:PRK12582 124 AAMQAG-VPaapvSPAYSLMSHDhaKLKHLFDLVKPRVVFAQSGAPFARALAALDL--LDVTVVHVTGPGEGIASIA--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 163 flsdLYEIGEKAPDAAerFRIEINASQPEDTRMLIYTSGTTGPPKGAMISHSnMLYQMWAGQQVLRVDPKDE----QLCF 238
Cdd:PRK12582 198 ----FADLAATPPTAA--VAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQR-MMCANIAMQEQLRPREPDPpppvSLDW 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 239 LPLCHVLerivsvefpiavGSTVNF------------------AESPDTVFDNLREVSPHVFTAVPRlwekiysrvlimr 300
Cdd:PRK12582 271 MPWNHTM------------GGNANFngllwgggtlyiddgkplPGMFEETIRNLREISPTVYGNVPA------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 301 seatpfgrwafdrAMASGAAKLEGkggamhavwDFLVLRNIrqmigFDRNRRSNTGAAPISPDLIRWYGALGVT------ 374
Cdd:PRK12582 326 -------------GYAMLAEAMEK---------DDALRRSF-----FKNLRLMAYGGATLSDDLYERMQALAVRttghri 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 375 -LLEGYGMTETSGVaSVNVIGD-NRIGTIGCALPATELRIAENG---EICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTG 448
Cdd:PRK12582 379 pFYTGYGATETAPT-TTGTHWDtERVGLIGLPLPGVELKLAPVGdkyEVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 449 DVGRIGDDG----AITITGRV-KDIIITAGG-KNITPAEIESRLKFSPFISDAVVIGDRRKYLTVLIMIDQENVEKYAQD 522
Cdd:PRK12582 458 DAARFVDPDdpekGLIFDGRVaEDFKLSTGTwVSVGTLRPDAVAACSPVIHDAVVAGQDRAFIGLLAWPNPAACRQLAGD 537
|
570
....*....|....*....
gi 1821015446 523 HQIPFSDfasLTRAPQVVD 541
Cdd:PRK12582 538 PDAAPED---VVKHPAVLA 553
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
22-600 |
3.67e-34 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 137.32 E-value: 3.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 22 WAAkcaERGDAT--AHREKDfGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGgIP-- 97
Cdd:PRK08180 48 WAQ---EAPDRVflAERGAD-GGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAG-VPya 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 98 --SGVYTTDSA--GQLEYLINDSGSAFLFVENDEQLDKYLE--VQDRVPTIVkviVFDPKGLRdfshpKVMFLSDLYEIG 171
Cdd:PRK08180 123 pvSPAYSLVSQdfGKLRHVLELLTPGLVFADDGAAFARALAavVPADVEVVA---VRGAVPGR-----AATPFAALLATP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 172 EkAPDAAERFRieinASQPEDTRMLIYTSGTTGPPKGAMISHSNMLyqmwAGQQVLR---VDPKDEQ---LCFLPLCHVL 245
Cdd:PRK08180 195 P-TAAVDAAHA----AVGPDTIAKFLFTSGSTGLPKAVINTHRMLC----ANQQMLAqtfPFLAEEPpvlVDWLPWNHTF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 246 ERIVSVEFPIAVGSTV----------NFAEspdTVfDNLREVSPHVFTAVPRLWEKIysrVLIMRSEA----TPFGRWaf 311
Cdd:PRK08180 266 GGNHNLGIVLYNGGTLyiddgkptpgGFDE---TL-RNLREISPTVYFNVPKGWEML---VPALERDAalrrRFFSRL-- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 312 dRAMASGAAKLEgkggamHAVWDFLvlrnirqmigfDRNRRSNTGAApispdlirwygalgVTLLEGYGMTETSGVASvN 391
Cdd:PRK08180 337 -KLLFYAGAALS------QDVWDRL-----------DRVAEATCGER--------------IRMMTGLGMTETAPSAT-F 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 392 VIGDN-RIGTIGCALPATELRIAENG---EICLKGPNVFKGYWRKPEKTAE--DiRDGWLYTGDVGRIGD---------- 455
Cdd:PRK08180 384 TTGPLsRAGNIGLPAPGCEVKLVPVGgklEVRVKGPNVTPGYWRAPELTAEafD-EEGYYRSGDAVRFVDpadperglmf 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 456 DGAIT-----ITG--------RVKdiIITAGGknitpaeiesrlkfsPFISDAVVIGDRRKYLTVLIMIDQENVEKYAQD 522
Cdd:PRK08180 463 DGRIAedfklSSGtwvsvgplRAR--AVSAGA---------------PLVQDVVITGHDRDEIGLLVFPNLDACRRLAGL 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 523 hqIPFSDFASLTRAPQVVDLIDGVVREVNTHF----AQVEQIkyfRLIDILLTAEDDELTPTMKLKRGFVEKKHAALIDQ 598
Cdd:PRK08180 526 --LADASLAEVLAHPAVRAAFRERLARLNAQAtgssTRVARA---LLLDEPPSLDAGEITDKGYINQRAVLARRAALVEA 600
|
..
gi 1821015446 599 MY 600
Cdd:PRK08180 601 LY 602
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
64-544 |
3.77e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 136.63 E-value: 3.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 64 ELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVeNDEQLDKYLEVQDRVPtIV 143
Cdd:PRK08314 55 ECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV-GSELAPKVAPAVGNLR-LR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 144 KVIV------FDPKG-------------LRDFSHPKVMFLSDLYEIGEKAPDAAerfrieinaSQPEDTRMLIYTSGTTG 204
Cdd:PRK08314 133 HVIVaqysdyLPAEPeiavpawlraeppLQALAPGGVVAWKEALAAGLAPPPHT---------AGPDDLAVLPYTSGTTG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 205 PPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVnfaespdtvfdnlrevsphvfTA 284
Cdd:PRK08314 204 VPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATV---------------------VL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 285 VPRlWEKIYSRVLIMRSEATpfgRWAFDRAMasgaaklegkggamhaVWDFLVLRNIRQmigFDRNRRSNT--GAAPIsP 362
Cdd:PRK08314 263 MPR-WDREAAARLIERYRVT---HWTNIPTM----------------VVDFLASPGLAE---RDLSSLRYIggGGAAM-P 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 363 DLI--RWYGALGVTLLEGYGMTETS----------------GVASVNVigDNRIgtigcALPAT--ELRIAENGEICLKG 422
Cdd:PRK08314 319 EAVaeRLKELTGLDYVEGYGLTETMaqthsnppdrpklqclGIPTFGV--DARV-----IDPETleELPPGEVGEIVVHG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 423 PNVFKGYWRKPEKTAEDI--RDG--WLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK08314 392 PQVFKGYWNRPEATAEAFieIDGkrFFRTGDLGRMDEEGYFFITDRLKR-MINASGFKVWPAEVENLLYKHPAIQEACVI 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821015446 499 G---DRR----KYLTVL-----IMIDQENVEKYAQDHQIPFsdfasltRAPQVVDLID 544
Cdd:PRK08314 471 AtpdPRRgetvKAVVVLrpearGKTTEEEIIAWAREHMAAY-------KYPRIVEFVD 521
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
191-502 |
4.42e-34 |
|
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: 134.51 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 191 EDTRMLIYTSGTTGPPKGAMISHSNMLY--QMWAgQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAE--- 265
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLfaDAMA-REALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPgwp 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 266 SPDTVFDNLREVSPHVFTAVPrlweKIYSRVLimRSEATPFGRWAFDRAMASGAAKLEgkggamhavwdflvlRNIRQmi 345
Cdd:cd05919 170 TAERVLATLARFRPTVLYGVP----TFYANLL--DSCAGSPDALRSLRLCVSAGEALP---------------RGLGE-- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 346 gfdrnrrsntgaapispdliRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRI----------AEN 415
Cdd:cd05919 227 --------------------RWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLvdeeghtippGEE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 GEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDA 495
Cdd:cd05919 287 GDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLIIQHPAVAEA 365
|
....*..
gi 1821015446 496 VVIGDRR 502
Cdd:cd05919 366 AVVAVPE 372
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
14-502 |
1.20e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 135.26 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 14 GADTVVKLWAAKCAERGDATAHREkDFGiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAA 93
Cdd:PRK06087 21 GDASLADYWQQTARAMPDKIAVVD-NHG--ASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 94 GGIPSGVYTTDSAGQLEYLINDSGSAFLF----VENDEQLDKYLEVQDRVPTIVKVIVFDPKGlrdfshPKVMFLSdLYE 169
Cdd:PRK06087 98 GAVSVPLLPSWREAELVWVLNKCQAKMFFaptlFKQTRPVDLILPLQNQLPQLQQIVGVDKLA------PATSSLS-LSQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 170 IGEKAPDAAErfriEINASQpEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIV 249
Cdd:PRK06087 171 IIADYEPLTT----AITTHG-DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 250 SVEFPIAVGSTVNFAE--SPDTVFDNLREvsphvftavprlwekiySRVLIMrSEATPFgrwafdramasgaaklegkgg 327
Cdd:PRK06087 246 GVTAPFLIGARSVLLDifTPDACLALLEQ-----------------QRCTCM-LGATPF--------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 328 amhaVWDflVLRNIRQmigfDRNRRSN-----TGAAPISPDLIRWYGALGVTLLEGYGMTETSGVASVNvIGDN---RIG 399
Cdd:PRK06087 287 ----IYD--LLNLLEK----QPADLSAlrfflCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVN-LDDPlsrFMH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 400 TIGCALPATELRI----------AENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDI 468
Cdd:PRK06087 356 TDGYAAAGVEIKVvdearktlppGCEGEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDI 435
|
490 500 510
....*....|....*....|....*....|....*.
gi 1821015446 469 IITaGGKNITPAEIESRLKFSPFISDAVVIG--DRR 502
Cdd:PRK06087 436 IVR-GGENISSREVEDILLQHPKIHDACVVAmpDER 470
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
45-499 |
6.93e-33 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 132.27 E-value: 6.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 45 AYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVe 124
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFV- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 125 NDEQLDKYLEVQDRVPTIVKVIVF--DPKGLRDFSHpkvmFLSDLYEIGEKApdaaerfrieinASQPEDTRMLIYTSGT 202
Cdd:TIGR02262 109 SGALLPVIKAALGKSPHLEHRVVVgrPEAGEVQLAE----LLATESEQFKPA------------ATQADDPAFWLYSSGS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 203 TGPPKGAMISHSNMLY--QMWAGQqvlRVDPKDEQLCF----LPLCHVLERivSVEFPIAVGST-VNFAE--SPDTVFDN 273
Cdd:TIGR02262 173 TGMPKGVVHTHSNPYWtaELYARN---TLGIREDDVCFsaakLFFAYGLGN--ALTFPMSVGATtVLMGErpTPDAVFDR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 274 LREVSPHVFTAVPRLWEKIysrvlimrseatpfgrwafdraMASGAAKLEGKggamhavwdflvlrnirqmigfDRNRRS 353
Cdd:TIGR02262 248 LRRHQPTIFYGVPTLYAAM----------------------LADPNLPSEDQ----------------------VRLRLC 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 354 NTGAAPISPDL-IRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRI----------AENGEICLKG 422
Cdd:TIGR02262 284 TSAGEALPAEVgQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLvgdggqdvadGEPGELLISG 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821015446 423 PNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:TIGR02262 364 PSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDD-MLKVSGIYVSPFEIESALIQHPAVLEAAVVG 439
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
189-499 |
6.95e-33 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 132.84 E-value: 6.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 189 QPEDTRMLIYTSGTTGPPKGAMISHSNMLYQM-----WAgQQVLRVDPKDEQL---CFLPLCHVLERIVSVEFPIAVGST 260
Cdd:PRK07059 202 GPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeaWL-QPAFEKKPRPDQLnfvCALPLYHIFALTVCGLLGMRTGGR 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 261 VNFAESPDTVFDNLREVSP---HVFTAVPRLWEKIysrvliMRSEAtpFGRWAFDRAMASgaaklegKGGAMhavwdfLV 337
Cdd:PRK07059 281 NILIPNPRDIPGFIKELKKyqvHIFPAVNTLYNAL------LNNPD--FDKLDFSKLIVA-------NGGGM------AV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 338 LRNIRQmigfdrnrrsntgaapispdliRWYGALGVTLLEGYGMTETSGVASVN-VIGDNRIGTIGCALPATELRI---- 412
Cdd:PRK07059 340 QRPVAE----------------------RWLEMTGCPITEGYGLSETSPVATCNpVDATEFSGTIGLPLPSTEVSIrddd 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 ------AENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAgGKNITPAEIESR 485
Cdd:PRK07059 398 gndlplGEPGEICIRGPQVMAGYWNRPDETAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVS-GFNVYPNEIEEV 476
|
330
....*....|....
gi 1821015446 486 LKFSPFISDAVVIG 499
Cdd:PRK07059 477 VASHPGVLEVAAVG 490
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
46-499 |
8.31e-33 |
|
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: 131.65 E-value: 8.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVen 125
Cdd:cd12118 30 YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFV-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 126 DEQLDKYlevqdrvptivkvivfdpkglrdfshpkvmflsDLYEIGEKAPDAAerfrieinasQPEDTRMLI---YTSGT 202
Cdd:cd12118 108 DREFEYE---------------------------------DLLAEGDPDFEWI----------PPADEWDPIalnYTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 203 TGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVleriVSVEFP---IAVGSTVNFaespdtvfdnLREVSP 279
Cdd:cd12118 145 TGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHC----NGWCFPwtvAAVGGTNVC----------LRKVDA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 280 hvftavprlwEKIYSrvLIMRSEATPFGrwafdramasGAAklegkggamhAVWDFLVLRNIRQMIGFDRNRRSNTGAAP 359
Cdd:cd12118 211 ----------KAIYD--LIEKHKVTHFC----------GAP----------TVLNMLANAPPSDARPLPHRVHVMTAGAP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 360 ISPDLIRWYGALGVTLLEGYGMTETSGVASVNVI--------GDNR--------IGTIGcalpATELRIAEN-------- 415
Cdd:cd12118 259 PPAAVLAKMEELGFDVTHVYGLTETYGPATVCAWkpewdelpTEERarlkarqgVRYVG----LEEVDVLDPetmkpvpr 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 -----GEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSP 490
Cdd:cd12118 335 dgktiGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEGVLYKHP 413
|
....*....
gi 1821015446 491 FISDAVVIG 499
Cdd:cd12118 414 AVLEAAVVA 422
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
190-499 |
1.06e-32 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 130.70 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 190 PEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPdt 269
Cdd:cd05969 88 PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGR-- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 270 vFDnlrevsphvftavPRLWEKIYSRVLIMRSEATPFgrwAFDRAMASGAAklegkggaMHAVWDFLVLRNIRqmigfdr 349
Cdd:cd05969 166 -FD-------------AESWYGIIERVKVTVWYTAPT---AIRMLMKEGDE--------LARKYDLSSLRFIH------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 350 nrrsnTGAAPISPDLIRW-YGALGVTLLEGYGMTETSGVASVNVIG-DNRIGTIGCALPA----------TELRIAENGE 417
Cdd:cd05969 214 -----SVGEPLNPEAIRWgMEVFGVPIHDTWWQTETGSIMIANYPCmPIKPGSMGKPLPGvkaavvdengNELPPGTKGI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 418 ICLKG--PNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKnITPAEIESRLKFSPFISDA 495
Cdd:cd05969 289 LALKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHR-VGPFEVESALMEHPAVAEA 367
|
....
gi 1821015446 496 VVIG 499
Cdd:cd05969 368 GVIG 371
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
47-497 |
1.08e-32 |
|
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: 130.08 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 47 SWSDWYDRSQAIGMGLIEL-GLTRGTPVSILSEdNKEWLYCD-LAISAAGGipsgVY----TTDSAGQLEYLINDSGSAF 120
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLE-RSAELVVAiLAVLKAGA----AYvpldPAYPAERLAFILEDAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 121 LFVenDEQLDkylevqDRVPTIVKVIVfdpkglrdfshpkvMFLSDLYEIGEKAPDAAERFRieinASQPEDTRMLIYTS 200
Cdd:TIGR01733 76 LLT--DSALA------SRLAGLVLPVI--------------LLDPLELAALDDAPAPPPPDA----PSGPDDLAYVIYTS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 201 GTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVleriVSVE---FPIAVGSTVNFAeSPDTVFDNLREV 277
Cdd:TIGR01733 130 GSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFD----ASVEeifGALLAGATLVVP-PEDEERDDAALL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 278 SPHVFTavprlwekiySRVLIMRSEATPFGRWAfdramasgaaklegkggaMHAVWDFLVLRNIrqmigfdrnrrsNTGA 357
Cdd:TIGR01733 205 AALIAE----------HPVTVLNLTPSLLALLA------------------AALPPALASLRLV------------ILGG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 358 APISPDLI-RWYGALG-VTLLEGYGMTETSGVASVNVI-----GDNRIGTIGCALPATELRI----------AENGEICL 420
Cdd:TIGR01733 245 EALTPALVdRWRARGPgARLINLYGPTETTVWSTATLVdpddaPRESPVPIGRPLANTRLYVldddlrpvpvGVVGELYI 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 421 KGPNVFKGYWRKPEKTAEDIRDGW--------LY-TGDVGRIGDDGAITITGR----VKdIiitaGGKNITPAEIESRLK 487
Cdd:TIGR01733 325 GGPGVARGYLNRPELTAERFVPDPfaggdgarLYrTGDLVRYLPDGNLEFLGRiddqVK-I----RGYRIELGEIEAALL 399
|
490
....*....|
gi 1821015446 488 FSPFISDAVV 497
Cdd:TIGR01733 400 RHPGVREAVV 409
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
52-499 |
1.96e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 130.85 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 52 YDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVEnDEQLDK 131
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD-DDFEAK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 132 YLEVQdrvptivkvivfdpkglrdfshpkVMFLSDLYEIGEKAPDAAERFRIEINASqpedtrmLIYTSGTTGPPKGAMI 211
Cdd:PRK03640 113 LIPGI------------------------SVKFAELMNGPKEEAEIQEEFDLDEVAT-------IMYTSGTTGKPKGVIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 212 SHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVlerivsVEFPIAVGSTvnfaespdtvfdnlrevsphvftavprlwek 291
Cdd:PRK03640 162 TYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHI------SGLSILMRSV------------------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 292 IYS-RVLIMRSeatpfgrwaFDrAMASGAAKLEGKGGAMHAVWDFLvlrniRQMIG-FDRNRRSNT------GAAPISPD 363
Cdd:PRK03640 205 IYGmRVVLVEK---------FD-AEKINKLLQTGGVTIISVVSTML-----QRLLErLGEGTYPSSfrcmllGGGPAPKP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 364 LIRWYGALGVTLLEGYGMTETsgvASVNVIGD-----NRIGTIGCALPATELRIA---------ENGEICLKGPNVFKGY 429
Cdd:PRK03640 270 LLEQCKEKGIPVYQSYGMTET---ASQIVTLSpedalTKLGSAGKPLFPCELKIEkdgvvvppfEEGEIVVKGPNVTKGY 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 430 WRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK03640 347 LNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
190-499 |
7.48e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 128.95 E-value: 7.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 190 PEDTRMLIYTSGTTGPPKGAMISHS------NMLYQMWAGQqvlrvdPKDEQLCFLPLCHVLERIVSVEFPIAVGS---- 259
Cdd:PRK07787 127 PDAPALIVYTSGTTGPPKGVVLSRRaiaadlDALAEAWQWT------ADDVLVHGLPLFHVHGLVLGVLGPLRIGNrfvh 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 260 TVNFaeSPDTVfdnLREVSPH--VFTAVPRLWekiySRVLIMRSEAtpfgrwafdRAMASgaAKLegkggamhavwdfLV 337
Cdd:PRK07787 201 TGRP--TPEAY---AQALSEGgtLYFGVPTVW----SRIAADPEAA---------RALRG--ARL-------------LV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 338 lrnirqmigfdrnrrsnTGAAPIS-PDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIAEN- 415
Cdd:PRK07787 248 -----------------SGSAALPvPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEd 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 -----------GEICLKGPNVFKGYWRKPEKTAEDIR-DGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPAEIE 483
Cdd:PRK07787 311 ggpvphdgetvGELQVRGPTLFDGYLNRPDATAAAFTaDGWFRTGDVAVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIE 390
|
330
....*....|....*.
gi 1821015446 484 SRLKFSPFISDAVVIG 499
Cdd:PRK07787 391 TALLGHPGVREAAVVG 406
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
47-514 |
9.12e-32 |
|
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: 129.88 E-value: 9.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 47 SWSDWYDRSQAIGMGL-IELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVEN 125
Cdd:cd17632 69 TYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 126 dEQLDKYLEVQDRVPTIVKVIVFD--PKG-----------LRDFSHPKVMFLSDLYEIGEKAPDAAERFRIEinaSQPED 192
Cdd:cd17632 149 -EHLDLAVEAVLEGGTPPRLVVFDhrPEVdahraalesarERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPE---PDDDP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 193 TRMLIYTSGTTGPPKGAMISHsNMLYQMWAGQQVLR-VDPKDE-QLCFLPLCHVLERIVSVEfPIAVGSTVNFAESPD-- 268
Cdd:cd17632 225 LALLIYTSGSTGTPKGAMYTE-RLVATFWLKVSSIQdIRPPASiTLNFMPMSHIAGRISLYG-TLARGGTAYFAAASDms 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 269 TVFDNLREVSPHVFTAVPRLWEKIYSRVLimrSEATPFGRWAFDRAMASGAAKLEgkggamhavwdflvLRNirQMIGfD 348
Cdd:cd17632 303 TLFDDLALVRPTELFLVPRVCDMLFQRYQ---AELDRRSVAGADAETLAERVKAE--------------LRE--RVLG-G 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 349 RNRRSNTGAAPISPDLIRWY-GALGVTLLEGYGMTETSGvasvnVIGDNRIgtigCALPATELRIAE------------- 414
Cdd:cd17632 363 RLLAAVCGSAPLSAEMKAFMeSLLDLDLHDGYGSTEAGA-----VILDGVI----VRPPVLDYKLVDvpelgyfrtdrph 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 415 -NGEICLKGPNVFKGYWRKPEKTAE--DiRDGWLYTGDV-GRIGDDGAITITGRvKDIIITAGGKNITPAEIESRLKFSP 490
Cdd:cd17632 434 pRGELLVKTDTLFPGYYKRPEVTAEvfD-EDGFYRTGDVmAELGPDRLVYVDRR-NNVLKLSQGEFVTVARLEAVFAASP 511
|
490 500
....*....|....*....|....*
gi 1821015446 491 FISDAVVIGD-RRKYLTVLIMIDQE 514
Cdd:cd17632 512 LVRQIFVYGNsERAYLLAVVVPTQD 536
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
47-499 |
2.12e-31 |
|
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: 128.01 E-value: 2.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 47 SWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVEND 126
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 127 EQLdkylevqdrVPTIVKVIVfdpkglrdfshpKVMFLSDLYEIGEKAPDAAErfrIEINASQPEDTRMLIYTSGTTGPP 206
Cdd:cd05923 110 AQV---------MDAIFQSGV------------RVLALSDLVGLGEPESAGPL---IEDPPREPEQPAFVFYTSGTTGLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 207 KGAMISH----SNMLYQmwAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPDTVfDNLREVSPHVF 282
Cdd:cd05923 166 KGAVIPQraaeSRVLFM--STQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPA-DALKLIEQERV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 283 T---AVPRLWEkiysrVLIMRSEATPFGRWAFDRAMASGAAKLEGkggamhavwdflVLRNIRQMIgfdRNRRSNT-GAA 358
Cdd:cd05923 243 TslfATPTHLD-----ALAAAAEFAGLKLSSLRHVTFAGATMPDA------------VLERVNQHL---PGEKVNIyGTT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 359 PISPDLIRWYGALGVTLLEGYgmtetsgVASVNVIgdnRIGtigcALPATELRIAENGEICLK--GPNVFKGYWRKPEKT 436
Cdd:cd05923 303 EAMNSLYMRDARTGTEMRPGF-------FSEVRIV---RIG----GSPDEALANGEEGELIVAaaADAAFTGYLNQPEAT 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821015446 437 AEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05923 369 AKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
195-499 |
2.60e-31 |
|
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: 124.34 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 195 MLIYTSGTTGPPKGAMISHSNMLYQMWagqQVLRVDPKDEQLCFL---PLCHvlerIVSVEFPIAVgstvnFAESPDTVF 271
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQAL---VLAVLQAIDEGTVFLnsgPLFH----IGTLMFTLAT-----FHAGGTNVF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 272 dnLREVSPhvfTAVPRLWEkiysrvlimrseatpfgrwafdramasgaaklegkggAMHAVWDFLVLRNIRQMIGFDRNR 351
Cdd:cd17636 72 --VRRVDA---EEVLELIE-------------------------------------AERCTHAFLLPPTIDQIVELNADG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 352 RSN-----------TGAAPISPDLIRWYGALGvtlleGYGMTETSGVASVNVIGDNRIGTIGCALPATELRI-------- 412
Cdd:cd17636 110 LYDlsslrsspaapEWNDMATVDTSPWGRKPG-----GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRIldedgrev 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 --AENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRvKDIIITAGGKNITPAEIESRLKFSP 490
Cdd:cd17636 185 pdGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYPAEVERCLRQHP 263
|
....*....
gi 1821015446 491 FISDAVVIG 499
Cdd:cd17636 264 AVADAAVIG 272
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
189-464 |
4.24e-31 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 129.66 E-value: 4.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 189 QPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPD 268
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPT 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 269 TVFdnlrevsphvftAVPRLWEKIYSRVLImrseATPfgrwAFDRAMAsgaaklegKGGAMHAvwdfLVLRNIRQMIgfd 348
Cdd:PRK08633 860 DAL------------GIAKLVAKHRATILL----GTP----TFLRLYL--------RNKKLHP----LMFASLRLVV--- 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 349 rnrrsnTGAAPISPDL-IRWYGALGVTLLEGYGMTETSGVASVNV----IGD------NRIGTIGCALPATELRI----- 412
Cdd:PRK08633 905 ------AGAEKLKPEVaDAFEEKFGIRILEGYGATETSPVASVNLpdvlAADfkrqtgSKEGSVGMPLPGVAVRIvdpet 978
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821015446 413 ------AENGEICLKGPNVFKGYWRKPEKTAEDIRD----GWLYTGDVGRIGDDGAITITGR 464
Cdd:PRK08633 979 feelppGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
106-503 |
5.35e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 124.38 E-value: 5.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 106 AGQLEYLINDSGSAFLFVENdeQLDKYLE-VQDRVPtIVKVIVfdpKGLRDF--SHPKVMfLSDLYEIGEKAPDAAERF- 181
Cdd:PRK06178 119 EHELSYELNDAGAEVLLALD--QLAPVVEqVRAETS-LRHVIV---TSLADVlpAEPTLP-LPDSLRAPRLAAAGAIDLl 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 182 ------RIEINASQPE--DTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQV-LRVDPKDEQLCFLPLCHVLERIVSVE 252
Cdd:PRK06178 192 palracTAPVPLPPPAldALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVaVVGGEDSVFLSFLPEFWIAGENFGLL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 253 FPIAVGSTVNFAESPDTVfdnlrevspHVFTAVPRlwekiYsRVLIMrseatpfgrwafdrAM-ASGAAKLEGKGGAmhA 331
Cdd:PRK06178 272 FPLFSGATLVLLARWDAV---------AFMAAVER-----Y-RVTRT--------------VMlVDNAVELMDHPRF--A 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 332 VWDFLVLRNIRqMIGFDRNrrsntgaapISPDL-IRWYGALGVTLLEG-YGMTETSGVASVNV---IGDNRIGT----IG 402
Cdd:PRK06178 321 EYDLSSLRQVR-VVSFVKK---------LNPDYrQRWRALTGSVLAEAaWGMTETHTCDTFTAgfqDDDFDLLSqpvfVG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 403 CALPATELRI-----------AENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIIT 471
Cdd:PRK06178 391 LPVPGTEFKIcdfetgellplGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV 470
|
410 420 430
....*....|....*....|....*....|....
gi 1821015446 472 AgGKNITPAEIESRLKFSPFISDAVVIG--DRRK 503
Cdd:PRK06178 471 N-GMSVFPSEVEALLGQHPAVLGSAVVGrpDPDK 503
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
46-499 |
2.43e-29 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 122.40 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGV---YTtdsAGQLEYLINDSGsAFLF 122
Cdd:PLN02246 51 YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAnpfYT---PAEIAKQAKASG-AKLI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 123 VENDEQLDKYLEVQDRVPtiVKVIVFDpkglrdfSHPKV-MFLSDLYEIGEKAPDAaerfrIEINasqPEDTRMLIYTSG 201
Cdd:PLN02246 127 ITQSCYVDKLKGLAEDDG--VTVVTID-------DPPEGcLHFSELTQADENELPE-----VEIS---PDDVVALPYSSG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 202 TTGPPKGAMISHSNMLYQMwaGQQV------LRVDPKDEQLCFLPLCHVLErIVSVEF-PIAVGSTVNFAESPDTVfDNL 274
Cdd:PLN02246 190 TTGLPKGVMLTHKGLVTSV--AQQVdgenpnLYFHSDDVILCVLPMFHIYS-LNSVLLcGLRVGAAILIMPKFEIG-ALL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 275 REVSPHVFTA---VPRLwekiysrVL-IMRSEATPfgrwAFDramasgaaklegkggamhavwdflvLRNIRQMIgfdrn 350
Cdd:PLN02246 266 ELIQRHKVTIapfVPPI-------VLaIAKSPVVE----KYD-------------------------LSSIRMVL----- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 351 rrsnTGAAPISPDLIRWYGAL--GVTLLEGYGMTETSGVASVNV--------IGDNRIGTI-------------GCALPA 407
Cdd:PLN02246 305 ----SGAAPLGKELEDAFRAKlpNAVLGQGYGMTEAGPVLAMCLafakepfpVKSGSCGTVvrnaelkivdpetGASLPR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 408 TelriaENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKnITPAEIESRL 486
Cdd:PLN02246 381 N-----QPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQ-VAPAELEALL 454
|
490
....*....|...
gi 1821015446 487 KFSPFISDAVVIG 499
Cdd:PLN02246 455 ISHPSIADAAVVP 467
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
54-505 |
5.66e-29 |
|
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: 119.94 E-value: 5.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 54 RSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGipsgVYT----TDSAGQLEYLINDSGSAFLFVendeql 129
Cdd:cd05930 21 RANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA----AYVpldpSYPAERLAYILEDSGAKLVLT------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 130 dkylevqdrvptivkvivfdpkglrdfshpkvmflsdlyeigekapdaaerfrieinasQPEDTRMLIYTSGTTGPPKGA 209
Cdd:cd05930 91 -----------------------------------------------------------DPDDLAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 210 MISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHvlerIVSVE---FPIAVGSTVNFAE-----SPDTVFDNLREVSPHV 281
Cdd:cd05930 112 MVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSF----DVSVWeifGALLAGATLVVLPeevrkDPEALADLLAEEGITV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 282 FTAVPrlwekiysrvlimrSEATPFGRWAFDRAMASgaaklegkggamhavWDFLVLrnirqmigfdrnrrsntGAAPIS 361
Cdd:cd05930 188 LHLTP--------------SLLRLLLQELELAALPS---------------LRLVLV-----------------GGEALP 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 362 PDLIR-WYGAL-GVTLLEGYGMTETSGVASVNVIGDNRIG----TIGCALPATELRI-AEN---------GEICLKGPNV 425
Cdd:cd05930 222 PDLVRrWRELLpGARLVNLYGPTEATVDATYYRVPPDDEEdgrvPIGRPIPNTRVYVlDENlrpvppgvpGELYIGGAGL 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 426 FKGYWRKPEKTAEDIRD------GWLY-TGDVGRIGDDGAITITGRVKDII-ItaGGKNITPAEIESRLKFSPFISDAVV 497
Cdd:cd05930 302 ARGYLNRPELTAERFVPnpfgpgERMYrTGDLVRWLPDGNLEFLGRIDDQVkI--RGYRIELGEIEAALLAHPGVREAAV 379
|
490
....*....|..
gi 1821015446 498 I----GDRRKYL 505
Cdd:cd05930 380 VaredGDGEKRL 391
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
17-498 |
8.35e-29 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 120.63 E-value: 8.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 17 TVVKLWAAKCAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGI 96
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVFGG----TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 97 PSGVYTTDSAGQLEYLINDSGSAFLFVENDeqldkYLEVQDRVPtivkvivfdpkgLRDFSHPKVMFLSdlyEIGEKAPD 176
Cdd:PRK06155 98 AVPINTALRGPQLEHILRNSGARLLVVEAA-----LLAALEAAD------------PGDLPLPAVWLLD---APASVSVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 177 AAERF--------RIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLyqmWAGQ---QVLRVDPKDEQLCFLPLCHV- 244
Cdd:PRK06155 158 AGWSTaplppldaPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFY---WWGRnsaEDLEIGADDVLYTTLPLFHTn 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 245 -LERIVSVefpIAVGSTVNFAESpdtvfdnlrevsphvFTAvPRLWEKIysrvliMRSEATPF---GrwafdrAMASgaa 320
Cdd:PRK06155 235 aLNAFFQA---LLAGATYVLEPR---------------FSA-SGFWPAV------RRHGATVTyllG------AMVS--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 321 klegkggamhavwdFLVLRNIRQMigfDRNRRSNTGAAP-ISPDLIRWYGA-LGVTLLEGYGMTETSGVASVnVIGDNRI 398
Cdd:PRK06155 281 --------------ILLSQPARES---DRAHRVRVALGPgVPAALHAAFRErFGVDLLDGYGSTETNFVIAV-THGSQRP 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 399 GTIGCALPATELRIA----------ENGEICLKG--PNVF-KGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRV 465
Cdd:PRK06155 343 GSMGRLAPGFEARVVdehdqelpdgEPGELLLRAdePFAFaTGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRI 422
|
490 500 510
....*....|....*....|....*....|...
gi 1821015446 466 KDiIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK06155 423 KD-AIRRRGENISSFEVEQVLLSHPAVAAAAVF 454
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
53-499 |
1.29e-28 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 120.29 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 53 DRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIpsgvyttdsAGQLEYL--INDSGSAFLFVE-----N 125
Cdd:PLN02860 40 DGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGI---------VAPLNYRwsFEEAKSAMLLVRpvmlvT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 126 DEQLDK-YLEVQ-DRVPTIvKVIVFdpkgLRDFSHPKVMFLSDL--------YEIGEKAPDAAerfrieinaSQPEDTRM 195
Cdd:PLN02860 111 DETCSSwYEELQnDRLPSL-MWQVF----LESPSSSVFIFLNSFlttemlkqRALGTTELDYA---------WAPDDAVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 196 LIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVlERIVSVEFPIAVGSTVNFAESPD--TVFDN 273
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHI-GGLSSALAMLMVGACHVLLPKFDakAALQA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 274 LREVSPHVFTAVPRLWEKIYSrvlIMRSEATpfgrWAFDRAMAsgaaKLEGKGGAMHAvwdfLVLRNIRQMigFDRNRrs 353
Cdd:PLN02860 256 IKQHNVTSMITVPAMMADLIS---LTRKSMT----WKVFPSVR----KILNGGGSLSS----RLLPDAKKL--FPNAK-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 354 ntgaapispdlirwygalgvtLLEGYGMTETSGVASVNVIGDNRIGT-----------------------IGCALPATEL 410
Cdd:PLN02860 317 ---------------------LFSAYGMTEACSSLTFMTLHDPTLESpkqtlqtvnqtksssvhqpqgvcVGKPAPHVEL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 411 RIAEN-----GEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIES 484
Cdd:PLN02860 376 KIGLDessrvGRILTRGPHVMLGYWGQNSETASVLsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKT-GGENVYPEEVEA 454
|
490
....*....|....*
gi 1821015446 485 RLKFSPFISDAVVIG 499
Cdd:PLN02860 455 VLSQHPGVASVVVVG 469
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
191-499 |
7.32e-28 |
|
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: 116.28 E-value: 7.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 191 EDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVnfaespdtV 270
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATV--------F 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 271 FDNLREVSPhvftavpRLWEKIYSRVLIMRSEATPFgrwAFDRAMASGAAKLegkggamhavwDFLVLRNIRqmigfdrn 350
Cdd:cd05972 153 VYEGPRFDA-------ERILELLERYGVTSFCGPPT---AYRMLIKQDLSSY-----------KFSHLRLVV-------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 351 rrsnTGAAPISPDLIRWY-GALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIA----------ENGEIC 419
Cdd:cd05972 204 ----SAGEPLNPEVIEWWrAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIdddgrelppgEEGDIA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 420 LKGPNV--FKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAgGKNITPAEIESRLKFSPFISDAVV 497
Cdd:cd05972 280 IKLPPPglFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS-GYRIGPFEVESALLEHPAVAEAAV 358
|
..
gi 1821015446 498 IG 499
Cdd:cd05972 359 VG 360
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
183-598 |
1.12e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 118.28 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 183 IEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMW--AGQQVLRVDPKDEQLCFLPLCHVLERIVsVEFPIAVGST 260
Cdd:PTZ00342 296 YKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVplCKHSIFKKYNPKTHLSYLPISHIYERVI-AYLSFMLGGT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 261 VNFAeSPDTVF--DNLREVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASGAAKLEGKGGamhavwDFL-V 337
Cdd:PTZ00342 375 INIW-SKDINYfsKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILSLRKSNNNGGFS------KFLeG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 338 LRNIRQMIGFDRNRRSN---TGAAPISPDLIRWYGA-LGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCAL-PATELRI 412
Cdd:PTZ00342 448 ITHISSKIKDKVNPNLEvilNGGGKLSPKIAEELSVlLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 AE-----------NGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKNITPA 480
Cdd:PTZ00342 528 RTwetykatdtlpKGELLIKSDSIFSGYFLEKEQTKNAFtEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 481 EIESRLKFSPFISDAVVIGDRR-----------KYLTVLIM----------IDQENVEKYAQDHQIPFSDFasltrapqv 539
Cdd:PTZ00342 608 MLNNLYSQISFINFCVVYGDDSmdgplaiisvdKYLLFKCLkddnmlestgINEKNYLEKLTDETINNNIY--------- 678
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821015446 540 VDLIDGVVREVnthFAQVEQIKYFRLIDILLTAE----DDELTPTMKLKRGFVEKKHAALIDQ 598
Cdd:PTZ00342 679 VDYVKGKMLEV---YKKTNLNRYNIINDIYLTSKvwdtNNYLTPTFKVKRFYVFKDYAFFIDQ 738
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
46-499 |
2.72e-27 |
|
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: 114.88 E-value: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLI-ELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVe 124
Cdd:cd05958 11 WTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 125 nDEQLdkylevqdrvptivkvivfdpkglrdfshpkvmflsdlyeigekapdaaerfrieinaSQPEDTRMLIYTSGTTG 204
Cdd:cd05958 90 -AHAL----------------------------------------------------------TASDDICILAFTSGTTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 205 PPKGAMISHSNML--YQMWAgQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVG-STVNFAES-PDTVFDNLREVSPH 280
Cdd:cd05958 111 APKATMHFHRDPLasADRYA-VNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGaSGVLLEEAtPDLLLSAIARYKPT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 281 VFTAVPRLWekiysrvlimrseatpfgrwafdRAMASGAAKLEGKGGAMhavwdflvlrnirqmigfdrnRRSNTGAAPI 360
Cdd:cd05958 190 VLFTAPTAY-----------------------RAMLAHPDAAGPDLSSL---------------------RKCVSAGEAL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 361 SPDLIR-WYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRI----------AENGEICLKGPNvfkGY 429
Cdd:cd05958 226 PAALHRaWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVvddegnpvpdGTIGRLAVRGPT---GC 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821015446 430 WRKPEKTAED-IRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05958 303 RYLADKRQRTyVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVEDVLLQHPAVAECAVVG 372
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
190-499 |
2.91e-27 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 114.84 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 190 PEDTRMLIYTSGTTGPPKGAMISHsnmlyqmwagqqvlRVdpkdeqlcflplchVLERIVSVEFPIavgstvNFAESPDT 269
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKGALHAH--------------RV--------------LLGHLPGVQFPF------NLFPRDGD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 270 VFdnlrevsphvFTavPRLWEKI-----------YSRVLIMRSEATPFGrwafdramASGAAKLEGKGGAMHAvwdFL-- 336
Cdd:cd05971 133 LY----------WT--PADWAWIgglldvllpslYFGVPVLAHRMTKFD--------PKAALDLMSRYGVTTA---FLpp 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 337 -VLRNIR----QMIGFDRNRRS-NTGAAPISPDLIRWYG-ALGVTLLEGYGMTETSGVASVN-VIGDNRIGTIGCALPA- 407
Cdd:cd05971 190 tALKMMRqqgeQLKHAQVKLRAiATGGESLGEELLGWAReQFGVEVNEFYGQTECNLVIGNCsALFPIKPGSMGKPIPGh 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 408 ---------TELRIAENGEICLKGPN--VFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKn 476
Cdd:cd05971 270 rvaivddngTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYR- 348
|
330 340
....*....|....*....|...
gi 1821015446 477 ITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05971 349 IGPAEIEECLLKHPAVLMAAVVG 371
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
21-498 |
2.96e-27 |
|
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: 115.45 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 21 LWAAKCAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGV 100
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEG----RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 101 YTTDSAGQLEYLINDSGSAFLFVENDEQldkylevqDRVPTIVKVIVFDPKGLRDFSHpkvmflsdlyeigeKAPDAAER 180
Cdd:cd17646 79 DPGYPADRLAYMLADAGPAVVLTTADLA--------ARLPAGGDVALLGDEALAAPPA--------------TPPLVPPR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 181 frieinasqPEDTRMLIYTSGTTGPPKGAMISH---SNMLYQMwagQQVLRVDPKDEQLCFLPLCHvlerIVSV-EF--P 254
Cdd:cd17646 137 ---------PDNLAYVIYTSGSTGRPKGVMVTHagiVNRLLWM---QDEYPLGPGDRVLQKTPLSF----DVSVwELfwP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 255 IAVGSTVNFAE-----SPDTVFDNLREvspHVFTA---VPRLWEkiysrvlimrseatpfgrwAFDRAMASGAAklegkg 326
Cdd:cd17646 201 LVAGARLVVARpgghrDPAYLAALIRE---HGVTTchfVPSMLR-------------------VFLAEPAAGSC------ 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 327 gamhavwdflvlRNIRQMIgfdrnrrsnTGAAPISPDLI-RWYGALGVTLLEGYGMTETS-GVASVNVIGDNRIGT--IG 402
Cdd:cd17646 253 ------------ASLRRVF---------CSGEALPPELAaRFLALPGAELHNLYGPTEAAiDVTHWPVRGPAETPSvpIG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 403 CALPATELRIAEN----------GEICLKGPNVFKGYWRKPEKTAEDIRDGW------LY-TGDVGRIGDDGAITITGRV 465
Cdd:cd17646 312 RPVPNTRLYVLDDalrpvpvgvpGELYLGGVQLARGYLGRPALTAERFVPDPfgpgsrMYrTGDLARWRPDGALEFLGRS 391
|
490 500 510
....*....|....*....|....*....|...
gi 1821015446 466 kDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:cd17646 392 -DDQVKIRGFRVEPGEIEAALAAHPAVTHAVVV 423
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
46-499 |
4.29e-27 |
|
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: 115.32 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVeN 125
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC-S 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 126 DEQLDKYLEVQDRVPTIVKVIVFDPK----GLRDFSHPKVMFLSDLYEIGEKAPDAAERfrieinasqPEDTRMLIYTSG 201
Cdd:cd17642 124 KKGLQKVLNVQKKLKIIKTIIILDSKedykGYQCLYTFITQNLPPGFNEYDFKPPSFDR---------DEQVALIMNSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 202 TTGPPKGAMISHSNMLYQMWAGQQVL---RVDPKDEQLCFLPLCHVLERIVSVEFPIaVGSTVNFaespdtvfdnlrevs 278
Cdd:cd17642 195 STGLPKGVQLTHKNIVARFSHARDPIfgnQIIPDTAILTVIPFHHGFGMFTTLGYLI-CGFRVVL--------------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 279 phvftaVPRLWEKIYSRVL----IMRSEATPfgrwafdrAMASGAAKlegkggamHAVWDFLVLRNIRQMIgfdrnrrsn 354
Cdd:cd17642 259 ------MYKFEEELFLRSLqdykVQSALLVP--------TLFAFFAK--------STLVDKYDLSNLHEIA--------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 355 TGAAPISPD----LIRWYGALGVTllEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIA-----------ENGEIC 419
Cdd:cd17642 308 SGGAPLSKEvgeaVAKRFKLPGIR--QGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVdldtgktlgpnERGELC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 420 LKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:cd17642 386 VKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKS-LIKYKGYQVPPAELESILLQHPKIFDAGVA 464
|
.
gi 1821015446 499 G 499
Cdd:cd17642 465 G 465
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
192-500 |
8.87e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 114.60 E-value: 8.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 192 DTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAE----SP 267
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPArgrfSA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 268 DTVFDNLREVSPHVFTAVPRLwekiySRVLIMRSEATPFGRwafdramasGAAKLegkggamhavwdflvlRNIRqmigf 347
Cdd:PRK05852 257 HTFWDDIKAVGATWYTAVPTI-----HQILLERAATEPSGR---------KPAAL----------------RFIR----- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 348 drnrrsnTGAAPISPD----LIRWYGAlgvTLLEGYGMTE-TSGVASVNVIG----DNRIGTIGCALPATELRI------ 412
Cdd:PRK05852 302 -------SCSAPLTAEtaqaLQTEFAA---PVVCAFGMTEaTHQVTTTQIEGigqtENPVVSTGLVGRSTGAQIrivgsd 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 ------AENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRL 486
Cdd:PRK05852 372 glplpaGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKE-LINRGGEKISPERVEGVL 450
|
330
....*....|....
gi 1821015446 487 KFSPFISDAVVIGD 500
Cdd:PRK05852 451 ASHPNVMEAAVFGV 464
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
12-499 |
1.83e-26 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 113.24 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 12 IDGADTVVKLWAAKCAERGDATAHREKDF-GIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAI 90
Cdd:PRK08008 3 IVGGQHLRQMWDDLADVYGHKTALIFESSgGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 91 SAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVEnDEQLDKYLEVQDRVPTIVKVIVfdpkgLRDFSHPKVMFLSDLYEI 170
Cdd:PRK08008 83 AKIGAIMVPINARLLREESAWILQNSQASLLVTS-AQFYPMYRQIQQEDATPLRHIC-----LTRVALPADDGVSSFTQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 171 GEKAPdAAERFRIEINAsqpEDTRMLIYTSGTTGPPKGAMISHSNML----YQMWagQQVLRVDpkDEQLCFLPLCHVLE 246
Cdd:PRK08008 157 KAQQP-ATLCYAPPLST---DDTAEILFTSGTTSRPKGVVITHYNLRfagyYSAW--QCALRDD--DVYLTVMPAFHIDC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 247 RIVSVEFPIAVGSTVNFAE--SPDTVFDNLREVSPHVFTAVPRLwekiySRVLiMRSEATPFGRwafdramasgaakleg 324
Cdd:PRK08008 229 QCTAAMAAFSAGATFVLLEkySARAFWGQVCKYRATITECIPMM-----IRTL-MVQPPSANDR---------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 325 kggaMHAVWDFLVLRNIRQMIGFDRNRRsntgaapispdlirwygaLGVTLLEGYGMTETSgvasVNVIGDN-------- 396
Cdd:PRK08008 287 ----QHCLREVMFYLNLSDQEKDAFEER------------------FGVRLLTSYGMTETI----VGIIGDRpgdkrrwp 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 397 RIGTIGCALPA-------TELRIAENGEICLKG---PNVFKGYWRKPEKTAEDIR-DGWLYTGDVGRIGDDGAITITGRv 465
Cdd:PRK08008 341 SIGRPGFCYEAeirddhnRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDR- 419
|
490 500 510
....*....|....*....|....*....|....
gi 1821015446 466 KDIIITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK08008 420 RCNMIKRGGENVSCVELENIIATHPKIQDIVVVG 453
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
17-502 |
2.52e-26 |
|
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: 114.95 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 17 TVVKLWAAKCAERGDATA--HREkdfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAG 94
Cdd:COG1020 477 TLHELFEAQAARTPDAVAvvFGD------QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 95 GipsgVY----TTDSAGQLEYLINDSGSAFLFVENDeqldkyleVQDRVPTI-VKVIVFDPKGLRDFShpkvmflsdlye 169
Cdd:COG1020 551 A----AYvpldPAYPAERLAYMLEDAGARLVLTQSA--------LAARLPELgVPVLALDALALAAEP------------ 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 170 igEKAPDAAerfrieinaSQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVleriV 249
Cdd:COG1020 607 --ATNPPVP---------VTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFD----A 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 250 SV-EF--PIAVGSTVnfaespdtVFdnlreVSPHVFTAVPRLWEKI-YSRVLIMrsEATPfgrwAFDRAMASGAAKlegk 325
Cdd:COG1020 672 SVwEIfgALLSGATL--------VL-----APPEARRDPAALAELLaRHRVTVL--NLTP----SLLRALLDAAPE---- 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 326 ggamhavwdflVLRNIRQMIgfdrnrrsnTGAAPISPDLI-RWYGAL-GVTLLEGYGMTETSGVASVNVIGDNRIG---- 399
Cdd:COG1020 729 -----------ALPSLRLVL---------VGGEALPPELVrRWRARLpGARLVNLYGPTETTVDSTYYEVTPPDADggsv 788
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 400 TIGCALPATELRIA-EN---------GEICLKGPNVFKGYWRKPEKTAE-------DIRDGWLY-TGDVGRIGDDGAITI 461
Cdd:COG1020 789 PIGRPIANTRVYVLdAHlqpvpvgvpGELYIGGAGLARGYLNRPELTAErfvadpfGFPGARLYrTGDLARWLPDGNLEF 868
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1821015446 462 TGR----VKdIiitaGGKNITPAEIESRLKFSPFISDAVVI------GDRR 502
Cdd:COG1020 869 LGRaddqVK-I----RGFRIELGEIEAALLQHPGVREAVVVaredapGDKR 914
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
42-499 |
4.38e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 112.44 E-value: 4.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 42 IW--QAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSA 119
Cdd:PRK07470 27 VWgdRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 120 FLFVENDeqLDKYLE-VQDRVPTIVKVIVFdpkGLRDFSHPKVMFLSDlyEIGEKAPDAA-ERfrieinasqpEDTRMLI 197
Cdd:PRK07470 107 AMICHAD--FPEHAAaVRAASPDLTHVVAI---GGARAGLDYEALVAR--HLGARVANAAvDH----------DDPCWFF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 198 YTSGTTGPPKGAMISHSNM-------LYQMWAGqqvlrVDPKDEQLCFLPLCHvlerivsvefPIAVGSTVNFAESPDTV 270
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMafvitnhLADLMPG-----TTEQDASLVVAPLSH----------GAGIHQLCQVARGAATV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 271 FDNLREVSPhvfTAVPRLWEKiysrvlimrseatpfgrwafdramasgaaklegkggamHAVWDFLVLRNIRQMI----- 345
Cdd:PRK07470 235 LLPSERFDP---AEVWALVER--------------------------------------HRVTNLFTVPTILKMLvehpa 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 346 --GFDRN--RRSNTGAAPI-SPDLIRWYGALGVTLLEGYGMTETSGvaSVNVI---------GDN-RIGTigCALPAT-- 408
Cdd:PRK07470 274 vdRYDHSslRYVIYAGAPMyRADQKRALAKLGKVLVQYFGLGEVTG--NITVLppalhdaedGPDaRIGT--CGFERTgm 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 409 ----------ELRIAENGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNIT 478
Cdd:PRK07470 350 evqiqddegrELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYIS-GGSNVY 428
|
490 500
....*....|....*....|.
gi 1821015446 479 PAEIESRLKFSPFISDAVVIG 499
Cdd:PRK07470 429 PREIEEKLLTHPAVSEVAVLG 449
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
30-500 |
4.80e-26 |
|
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: 111.61 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 30 GDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGI-----PSGvyttd 104
Cdd:cd12116 1 PDATAVRDDD----RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAyvpldPDY----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 105 SAGQLEYLINDSGSAFLFVENDEQldkylevqDRVPTIVKVIVFDPkglrdfshpkvmflsdlyEIGEKAPDAAERfrie 184
Cdd:cd12116 72 PADRLRYILEDAEPALVLTDDALP--------DRLPAGLPVLLLAL------------------AAAAAAPAAPRT---- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 185 inASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLC---HVLERIVsvefPIAVGSTV 261
Cdd:cd12116 122 --PVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAfdiSLLELLL----PLLAGARV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 262 NFAeSPDTVFDN------LREVSPHVFTAVPRLWekiysRVLimrseatpfgrwafdraMASGAAKLEGkggaMHAVwdf 335
Cdd:cd12116 196 VIA-PRETQRDPealarlIEAHSITVMQATPATW-----RML-----------------LDAGWQGRAG----LTAL--- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 336 lvlrnirqmigfdrnrrsnTGAAPISPDLIRWYGALGVTLLEGYGMTET---SGVASVNViGDNRIgTIGCALPATELRI 412
Cdd:cd12116 246 -------------------CGGEALPPDLAARLLSRVGSLWNLYGPTETtiwSTAARVTA-AAGPI-PIGRPLANTQVYV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 AEN----------GEICLKGPNVFKGYWRKPEKTAEDIRD-------GWLY-TGDVGRIGDDGAITITGRVkDIIITAGG 474
Cdd:cd12116 305 LDAalrpvppgvpGELYIGGDGVAQGYLGRPALTAERFVPdpfagpgSRLYrTGDLVRRRADGRLEYLGRA-DGQVKIRG 383
|
490 500
....*....|....*....|....*.
gi 1821015446 475 KNITPAEIESRLKFSPFISDAVVIGD 500
Cdd:cd12116 384 HRIELGEIEAALAAHPGVAQAAVVVR 409
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
182-466 |
5.72e-26 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 113.52 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 182 RIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQmwAGQQVLRVD--PKDEQLCFLPLCHVLERIVSVEFPIAVGS 259
Cdd:PRK06814 784 LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLAN--RAQVAARIDfsPEDKVFNALPVFHSFGLTGGLVLPLLSGV 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 260 TVNFAESPdtvfdnlrevsPHvFTAVPRLwekIYSrvlimrSEATP-FGRWAFdramasgaakLEGKGGAMHAvWDFLVL 338
Cdd:PRK06814 862 KVFLYPSP-----------LH-YRIIPEL---IYD------TNATIlFGTDTF----------LNGYARYAHP-YDFRSL 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 339 RNIrqmigFdrnrrsnTGAAPISPDLIR-WYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELR------ 411
Cdd:PRK06814 910 RYV-----F-------AGAEKVKEETRQtWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRlepvpg 977
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821015446 412 IAENGEICLKGPNVFKGYWRkPEK--TAEDIRDGWLYTGDVGRIGDDGAITITGRVK 466
Cdd:PRK06814 978 IDEGGRLFVRGPNVMLGYLR-AENpgVLEPPADGWYDTGDIVTIDEEGFITIKGRAK 1033
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
2-498 |
7.63e-26 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 111.61 E-value: 7.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 2 NQLSLPKPILIDgadtvVKLWAAKCAERGDATAhrekdfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNK 81
Cdd:PLN02330 26 DKLTLPDFVLQD-----AELYADKVAFVEAVTG---------KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 82 EWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGsAFLFVENDEQLDKYLEVQdrVPTIVkvivfdpkgLRDFSHPKV 161
Cdd:PLN02330 92 EYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAG-AKLIVTNDTNYGKVKGLG--LPVIV---------LGEEKIEGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 162 MFLSDLYEIGEKAPDAAERFRIeinasQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAgqQVLRVDP----KDEQLC 237
Cdd:PLN02330 160 VNWKELLEAADRAGDTSDNEEI-----LQTDLCALPFSSGTTGISKGVMLTHRNLVANLCS--SLFSVGPemigQVVTLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 238 FLPLCHVLErIVSVefpiavgstvnfaespdtVFDNLREVSPHVftAVPRLWEKIYSRVLImrSEATPFGrwafdramas 317
Cdd:PLN02330 233 LIPFFHIYG-ITGI------------------CCATLRNKGKVV--VMSRFELRTFLNALI--TQEVSFA---------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 318 gaaklegkggamhAVWDFLVLRNIRQMI--GFD----RNRRSNTGAAPISPDLIRWYGAL--GVTLLEGYGMTETSGVAS 389
Cdd:PLN02330 280 -------------PIVPPIILNLVKNPIveEFDlsklKLQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHSCITL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 390 VNviGDNRIG-------TIGCALPATELR---------IAEN--GEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDV 450
Cdd:PLN02330 347 TH--GDPEKGhgiakknSVGFILPNLEVKfidpdtgrsLPKNtpGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDI 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1821015446 451 GRIGDDGAITITGRVKDIIITAGGKnITPAEIESRLKFSPFISDAVVI 498
Cdd:PLN02330 425 GYIDDDGDIFIVDRIKELIKYKGFQ-VAPAELEAILLTHPSVEDAAVV 471
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
187-473 |
1.11e-25 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 112.11 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 187 ASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAES 266
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 267 PdtvfdnlrevsPHvFTAVPRLwekIYSR---VLIMRSeaTPFGRWA-----FD----RAMASGAAKLEgkggamhavwd 334
Cdd:PRK08043 441 P-----------LH-YRIVPEL---VYDRnctVLFGTS--TFLGNYArfanpYDfarlRYVVAGAEKLQ----------- 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 335 flvlRNIRQMigfdrnrrsntgaapispdlirWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELR--- 411
Cdd:PRK08043 493 ----ESTKQL----------------------WQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARlls 546
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821015446 412 ---IAENGEICLKGPNVFKGYWR--KPEK----TAEDIRD----GWLYTGDVGRIGDDGAITITGRVKDIIITAG 473
Cdd:PRK08043 547 vpgIEQGGRLQLKGPNIMNGYLRveKPGVlevpTAENARGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
182-498 |
5.67e-25 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 107.78 E-value: 5.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 182 RIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPL---CHVLErIVSVefpIAVG 258
Cdd:cd17653 96 TLLLTTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIafdACIGE-IFST---LCNG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 259 STVNFAESPDTVFDNLREVspHVFTAVPRlwekiysrVLIMRSEAtpfgrwafdramasgaaklegkggamhavwdflvl 338
Cdd:cd17653 172 GTLVLADPSDPFAHVARTV--DALMSTPS--------ILSTLSPQ----------------------------------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 339 rnirqmiGFDRNRRSNTGAAPISPDLI-RWygALGVTLLEGYGMTETS-GVASVNVIGDNRIgTIGCALPATELRI---- 412
Cdd:cd17653 207 -------DFPNLKTIFLGGEAVPPSLLdRW--SPGRRLYNAYGPTECTiSSTMTELLPGQPV-TIGKPIPNSTCYIldad 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 ------AENGEICLKGPNVFKGYWRKPEKTAE-----DIRDGW-LY-TGDVGRIGDDGAITITGRvKDIIITAGGKNITP 479
Cdd:cd17653 277 lqpvpeGVVGEICISGVQVARGYLGNPALTASkfvpdPFWPGSrMYrTGDYGRWTEDGGLEFLGR-EDNQVKVRGFRINL 355
|
330 340
....*....|....*....|
gi 1821015446 480 AEIESR-LKFSPFISDAVVI 498
Cdd:cd17653 356 EEIEEVvLQSQPEVTQAAAI 375
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
2-558 |
7.72e-25 |
|
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: 108.74 E-value: 7.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 2 NQLSLPKPILIDGADTVVKLWAAKCAERgDATAHREkDFGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNK 81
Cdd:cd05970 6 NNFSINVPENFNFAYDVVDAMAKEYPDK-LALVWCD-DAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 82 EWLYCDLAISAAGG--IPSGVYTTdsAGQLEYLINDSGSAFLFVEND----EQLDKYLEVQDRVPTIVKVIVFDPKGLRD 155
Cdd:cd05970 84 EFWYSLLALHKLGAiaIPATHQLT--AKDIVYRIESADIKMIVAIAEdnipEEIEKAAPECPSKPKLVWVGDPVPEGWID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 156 FSHpkvmflsdlyEIGEKAPDaaerFRIEINASQP--EDTRMLIYTSGTTGPPKgaMISHsNMLYqmwagqqvlrvdpkd 233
Cdd:cd05970 162 FRK----------LIKNASPD----FERPTANSYPcgEDILLVYFSSGTTGMPK--MVEH-DFTY--------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 234 eqlcflPLCHvlerIVSVEFpiavgstvnfaespdtvFDNLREVSPHVFTA----VPRLWEKIYsrvlimrseatpfGRW 309
Cdd:cd05970 210 ------PLGH----IVTAKY-----------------WQNVREGGLHLTVAdtgwGKAVWGKIY-------------GQW 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 310 -------AFDRAMASGAAKLE--GKGG-----AMHAVWDFLVLRNIRQMiGFDRNRRSNTGAAPISPDLI-RWYGALGVT 374
Cdd:cd05970 250 iagaavfVYDYDKFDPKALLEklSKYGvttfcAPPTIYRFLIREDLSRY-DLSSLRYCTTAGEALNPEVFnTFKEKTGIK 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 375 LLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRI----------AENGEICL---KGPNV--FKGYWRKPEKTAED 439
Cdd:cd05970 329 LMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLidregrsceaGEEGEIVIrtsKGKPVglFGGYYKDAEKTAEV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 440 IRDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKnITPAEIESRLKFSPFISDAVVIG----DRRKYLTVLIMIDQ-- 513
Cdd:cd05970 409 WHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYR-IGPFEVESALIQHPAVLECAVTGvpdpIRGQVVKATIVLAKgy 487
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1821015446 514 ---ENVEKYAQDHqipFSDFASLTRAPQVVDLIDGVVREVNTHFAQVE 558
Cdd:cd05970 488 epsEELKKELQDH---VKKVTAPYKYPRIVEFVDELPKTISGKIRRVE 532
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
187-484 |
7.81e-25 |
|
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: 108.52 E-value: 7.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 187 ASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVlerIVSVEFPI-AV---GSTVN 262
Cdd:cd05906 163 QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHV---GGLVELHLrAVylgCQQVH 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 263 FAesPDTVfdnLREvsphvftavPRLWEKIYSRVLIMRSeatpfgrWAFDRAMASGAAKLE-GKGGAmhavWDflvLRNI 341
Cdd:cd05906 240 VP--TEEI---LAD---------PLRWLDLIDRYRVTIT-------WAPNFAFALLNDLLEeIEDGT----WD---LSSL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 342 RQMIgfdrnrrsNTGAAPISP------DLIRWYGALGVTLLEGYGMTET-SGV------ASVNVIGDNRIGTIGCALPAT 408
Cdd:cd05906 292 RYLV--------NAGEAVVAKtirrllRLLEPYGLPPDAIRPAFGMTETcSGViysrsfPTYDHSQALEFVSLGRPIPGV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 409 ELRI----------AENGEICLKGPNVFKGYWRKPEKTAEDIR-DGWLYTGDVGRIgDDGAITITGRVKDIIITaGGKNI 477
Cdd:cd05906 364 SMRIvddegqllpeGEVGRLQVRGPVVTKGYYNNPEANAEAFTeDGWFRTGDLGFL-DNGNLTITGRTKDTIIV-NGVNY 441
|
....*..
gi 1821015446 478 TPAEIES 484
Cdd:cd05906 442 YSHEIEA 448
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
14-507 |
1.63e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 107.52 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 14 GADTVVKLWAAKCAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAA 93
Cdd:PRK06164 8 RADTLASLLDAHARARPDAVALIDED----RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 94 GGIPSGVYTTDSAGQLEYLINDSGSAFLFVENDEQLDKYLEV-----QDRVPTIVKVIVFDpKGLRDFSHPKVMFLSDLY 168
Cdd:PRK06164 84 GATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDFAAIlaavpPDALPPLRAIAVVD-DAADATPAPAPGARVQLF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 169 EIGEKAPDAAERFRieinASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLErI 248
Cdd:PRK06164 163 ALPDPAPPAAAGER----AADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFG-F 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 249 VSVEFPIAVGSTVNFAEspdtVFDNLREVS-------PHVFTAvprlwEKIYSRVLIMRSEATPF------GRWAFDRAM 315
Cdd:PRK06164 238 STLLGALAGGAPLVCEP----VFDAARTARalrrhrvTHTFGN-----DEMLRRILDTAGERADFpsarlfGFASFAPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 316 ASGAAKLEGKGGAMHAVW---DFLVLRNIrQMIGFDRNRRSNTGAAPISPDlirwygalgvtllegygmtetsgvASVNV 392
Cdd:PRK06164 309 GELAALARARGVPLTGLYgssEVQALVAL-QPATDPVSVRIEGGGRPASPE------------------------ARVRA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 393 igdnRIGTIGCALPAtelriAENGEICLKGPNVFKGYWRKPEKTAEDIR-DGWLYTGDVGRIGDDGAITITGRVKDiIIT 471
Cdd:PRK06164 364 ----RDPQDGALLPD-----GESGEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQFVYQTRMGD-SLR 433
|
490 500 510
....*....|....*....|....*....|....*.
gi 1821015446 472 AGGKNITPAEIESRLKFSPFISDAVVIGDRRKYLTV 507
Cdd:PRK06164 434 LGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTV 469
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
28-499 |
1.91e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 107.67 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 28 ERGDATAHREKDFGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAG 107
Cdd:PRK04319 56 GRKDKVALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 108 QLEYLINDSGSAFLfVENDEQLDKylEVQDRVPTIVKVIVFDPKGLRDfshPKVMFLSDLYEigekapDAAERFRIEinA 187
Cdd:PRK04319 136 AVRDRLEDSEAKVL-ITTPALLER--KPADDLPSLKHVLLVGEDVEEG---PGTLDFNALME------QASDEFDIE--W 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 188 SQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLC--------------FLPLCHvlerivsvef 253
Cdd:PRK04319 202 TDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDVYWCtadpgwvtgtsygiFAPWLN---------- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 254 piAVGSTVNFAEspdtvFDnlrevsphvftavPRLWEKIYS--RVLIMRSEATpfgrwAFDRAMASGAAKLEGkggamha 331
Cdd:PRK04319 272 --GATNVIDGGR-----FS-------------PERWYRILEdyKVTVWYTAPT-----AIRMLMGAGDDLVKK------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 332 vWDFLVLRNIrQMIGfdrnrrsntgaAPISPDLIRWyG--ALGVTLLEGYGMTETSGVASVNVIG-DNRIGTIGCALPAT 408
Cdd:PRK04319 320 -YDLSSLRHI-LSVG-----------EPLNPEVVRW-GmkVFGLPIHDNWWMTETGGIMIANYPAmDIKPGSMGKPLPGI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 409 ELRIAEN----------GEICLKG--PNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAgGKN 476
Cdd:PRK04319 386 EAAIVDDqgnelppnrmGNLAIKKgwPSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTS-GER 464
|
490 500
....*....|....*....|...
gi 1821015446 477 ITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK04319 465 VGPFEVESKLMEHPAVAEAGVIG 487
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
53-590 |
2.26e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 107.08 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 53 DRSQAIGMGLIELGLTRGTPVSILSEDNKEWLycdlaISAAGGIPSGVYTTD-----SAGQLEYLINDSGSAFLFVENDe 127
Cdd:PRK13391 32 ERSNRLAHLFRSLGLKRGDHVAIFMENNLRYL-----EVCWAAERSGLYYTCvnshlTPAEAAYIVDDSGARALITSAA- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 128 QLDKYLEVQDRVPTIVKVIVFDPKGLRDFshpkvmfLSDLYEIGEKAPDAaerfRIeinASQPEDTRMLiYTSGTTGPPK 207
Cdd:PRK13391 106 KLDVARALLKQCPGVRHRLVLDGDGELEG-------FVGYAEAVAGLPAT----PI---ADESLGTDML-YSSGTTGRPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 208 GamishsnmlyqmwagqqVLRVDPKDEQLCFLPLCHVLERIVSVEfpiavgstvnfaesPDTVFdnlreVSPH-VFTAVP 286
Cdd:PRK13391 171 G-----------------IKRPLPEQPPDTPLPLTAFLQRLWGFR--------------SDMVY-----LSPApLYHSAP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 287 RLWEKIYSR----VLIMRseatpfgrwAFDramASGAAKLEGKGGAMHAVW------DFLVL-RNIRQMIGFDRNRRSNT 355
Cdd:PRK13391 215 QRAVMLVIRlggtVIVME---------HFD---AEQYLALIEEYGVTHTQLvptmfsRMLKLpEEVRDKYDLSSLEVAIH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 356 GAAPISPD----LIRWYGALgvtLLEGYGMTETSGVASVN--------------VIGDNRIgtigCALPATELRIAENGE 417
Cdd:PRK13391 283 AAAPCPPQvkeqMIDWWGPI---IHEYYAATEGLGFTACDseewlahpgtvgraMFGDLHI----LDDDGAELPPGEPGT 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 418 ICLKGPNVFKgYWRKPEKTAE--DIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDA 495
Cdd:PRK13391 356 IWFEGGRPFE-YLNDPAKTAEarHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIIS-GGVNIYPQEAENLLITHPKVADA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 496 VVIGdrrkyltvlimidqenvekyaqdhqIPFSDFASLTRApqVVDLIDGVvrEVNTHFAQ---------VEQIKYFRLI 566
Cdd:PRK13391 434 AVFG-------------------------VPNEDLGEEVKA--VVQPVDGV--DPGPALAAeliafcrqrLSRQKCPRSI 484
|
570 580
....*....|....*....|....*..
gi 1821015446 567 DILltaedDEL--TPTMKL-KRGFVEK 590
Cdd:PRK13391 485 DFE-----DELprLPTGKLyKRLLRDR 506
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
21-499 |
4.98e-24 |
|
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: 106.00 E-value: 4.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 21 LWAAKCAERGDATA--HREkdfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPs 98
Cdd:COG1021 30 LLRRRAERHPDRIAvvDGE------RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 99 gVYTTDS--AGQLEYLINDSG-SAFLFVENDEQLDkYL----EVQDRVPTIVKVIVF-DPKGLRDfshpkvmfLSDLYEi 170
Cdd:COG1021 103 -VFALPAhrRAEISHFAEQSEaVAYIIPDRHRGFD-YRalarELQAEVPSLRHVLVVgDAGEFTS--------LDALLA- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 171 gekAPDAAERFRIeinasQPEDTRMLIYTSGTTGPPKgaMI--SHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHvleri 248
Cdd:COG1021 172 ---APADLSEPRP-----DPDDVAFFQLSGGTTGLPK--LIprTHDDYLYSVRASAEICGLDADTVYLAALPAAH----- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 249 vsvEFPIA---------VGSTVNFAE--SPDTVFDnL--REvspHV-FTA-VPrlweKIYSRVLimrsEATPFGRWAFD- 312
Cdd:COG1021 237 ---NFPLSspgvlgvlyAGGTVVLAPdpSPDTAFP-LieRE---RVtVTAlVP----PLALLWL----DAAERSRYDLSs 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 313 -RAMASGAAKLegkggamhavwdflvlrnirqmigfdrnrrSNTGAAPISPdlirwygALGVTLLEGYGMTEtsGVasVN 391
Cdd:COG1021 302 lRVLQVGGAKL------------------------------SPELARRVRP-------ALGCTLQQVFGMAE--GL--VN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 392 V--IGDN---RIGTIGCAL-PATELRIA----------ENGEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIG 454
Cdd:COG1021 341 YtrLDDPeevILTTQGRPIsPDDEVRIVdedgnpvppgEVGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRT 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1821015446 455 DDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:COG1021 421 PDGYLVVEGRAKDQINR-GGEKIAAEEVENLLLAHPAVHDAAVVA 464
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
191-483 |
8.24e-24 |
|
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: 102.72 E-value: 8.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 191 EDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQ-QVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAE--SP 267
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQkEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEntTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 268 DTVFDNLREVSPHVFTAVPRLWEKIYSrvlimrseatpfgrwafdraMASGAAKLEGKggamhavwdflvLRnirqMIGF 347
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVS--------------------ELKSANATVPS------------LR----LIGY 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 348 DrnrrsntGAAPISPD--LIRWYGAlgVTLLEGYGMTETSGVASVNVIGDNR-IGTIGCALPATELRI----------AE 414
Cdd:cd17635 125 G-------GSRAIAADvrFIEATGL--TNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLaatdgiagpsAS 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821015446 415 NGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIItAGGKNITPAEIE 483
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFLFITGRSSESIN-CGGVKIAPDEVE 263
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
176-499 |
2.34e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 102.98 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 176 DAAERFRIEinasqpEDTRMLIYTSGTTGPPKGAMISHSNML----YQMWAgqqvLRVDPKDEQLCFLPLCHVLERIVSV 251
Cdd:cd05973 79 DAANRHKLD------SDPFVMMFTSGTTGLPKGVPVPLRALAafgaYLRDA----VDLRPEDSFWNAADPGWAYGLYYAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 252 EFPIAVGSTVNFAE---SPDTVFDNLREVSPHVFTAVPRLWekiysRVLimrseatpfgrwafdraMASGAAKLEGKGGa 328
Cdd:cd05973 149 TGPLALGHPTILLEggfSVESTWRVIERLGVTNLAGSPTAY-----RLL-----------------MAAGAEVPARPKG- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 329 mhavwdflvlrnirqmigfdRNRRSNTGAAPISPDLIRWYGA-LGVTLLEGYGMTETsGVASVNVIGDN---RIGTIGCA 404
Cdd:cd05973 206 --------------------RLRRVSSAGEPLTPEVIRWFDAaLGVPIHDHYGQTEL-GMVLANHHALEhpvHAGSAGRA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 405 LPA----------TELRIAENGEICLKGPNV----FKGYWRKPEKTAEDirdGWLYTGDVGRIGDDGAITITGRVKDIII 470
Cdd:cd05973 265 MPGwrvavldddgDELGPGEPGRLAIDIANSplmwFRGYQLPDTPAIDG---GYYLTGDTVEFDPDGSFSFIGRADDVIT 341
|
330 340
....*....|....*....|....*....
gi 1821015446 471 TAGGKnITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05973 342 MSGYR-IGPFDVESALIEHPAVAEAAVIG 369
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
176-501 |
2.50e-23 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 104.73 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 176 DAAERFRiEINASQPEDTRML--------IYTSGTTGPPKGAMISHSNMLYQMWA-GQQVLRVDPKDEQLCFLPLCHVLE 246
Cdd:PRK06060 123 EAAELMS-EAARVAPGGYEPMggdalayaTYTSGTTGPPKAAIHRHADPLTFVDAmCRKALRLTPEDTGLCSARMYFAYG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 247 RIVSVEFPIAVGSTVNF------AESPDTVFDNLRevsPHVFTAVPRLwekiYSRVLimrsEATPFGRWAFDRAMASGAA 320
Cdd:PRK06060 202 LGNSVWFPLATGGSAVInsapvtPEAAAILSARFG---PSVLYGVPNF----FARVI----DSCSPDSFRSLRCVVSAGE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 321 KLEgkggamhavwdflvlrnirqmigfdrnrrsntgaAPISPDLIRWYGalGVTLLEGYGMTETSGVASVNVIGDNRIGT 400
Cdd:PRK06060 271 ALE----------------------------------LGLAERLMEFFG--GIPILDGIGSTEVGQTFVSNRVDEWRLGT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 401 IGCALPATELRIAE----------NGEICLKGPNVFKGYWRKPEKTAEDirDGWLYTGDVGRIGDDGAITITGRVKDIII 470
Cdd:PRK06060 315 LGRVLPPYEIRVVApdgttagpgvEGDLWVRGPAIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEV 392
|
330 340 350
....*....|....*....|....*....|.
gi 1821015446 471 TaGGKNITPAEIESRLKFSPFISDAVVIGDR 501
Cdd:PRK06060 393 I-GGVNVDPREVERLIIEDEAVAEAAVVAVR 422
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
45-499 |
2.99e-23 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 103.77 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 45 AYSWSDWYDRSQAIGMGLIE-LGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFV 123
Cdd:PLN02574 66 SISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 124 ENDeqldkylevqdrvptivKVIVFDPKGLrdfshpKVMFLSDLYEIGEKAPDAAERFRIEINASQP--------EDTRM 195
Cdd:PLN02574 146 SPE-----------------NVEKLSPLGV------PVIGVPENYDFDSKRIEFPKFYELIKEDFDFvpkpvikqDDVAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 196 LIYTSGTTGPPKGAMISHSNMLYQM-----WAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESpdtv 270
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIAMVelfvrFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRR---- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 271 FDnlreVSPHVftavprlweKIYSRVLIMRSEATPFGRWAFDRAMASGAAKlegkggamhavwdflVLRNIRQMigfdrn 350
Cdd:PLN02574 279 FD----ASDMV---------KVIDRFKVTHFPVVPPILMALTKKAKGVCGE---------------VLKSLKQV------ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 351 rrsNTGAAPISPDLIR-WYGALG-VTLLEGYGMTETSGVAS--VNVIGDNRIGTIGCALPATELRIAE-----------N 415
Cdd:PLN02574 325 ---SCGAAPLSGKFIQdFVQTLPhVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDwstgcllppgnC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 GEICLKGPNVFKGYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKnITPAEIESRLKFSPFISD 494
Cdd:PLN02574 402 GELWIQGPGVMKGYLNNPKATQSTIdKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQ-IAPADLEAVLISHPEIID 480
|
....*
gi 1821015446 495 AVVIG 499
Cdd:PLN02574 481 AAVTA 485
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
47-483 |
1.13e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 102.00 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 47 SWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKE--------WLycdlaisaAGG----IPSGVYTTDSAGQLEylin 114
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEiaptaqglWM--------RGAsltmLHQPTPRTDLAVWAE---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 115 DSGSAFLFVEndeqlDKYLEVQDrvPTIVKVIVFDPKGLRdfshpkVMFLSDLYeigekAPDAAERfrIEINasqPEDTR 194
Cdd:PRK07768 99 DTLRVIGMIG-----AKAVVVGE--PFLAAAPVLEEKGIR------VLTVADLL-----AADPIDP--VETG---EDDLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 195 MLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDP-KDEQLCFLPLCHVLERIVSVEFPIAVGStvnfaespDTVFdn 273
Cdd:PRK07768 156 LMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVeTDVMVSWLPLFHDMGMVGFLTVPMYFGA--------ELVK-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 274 lreVSPHVFTAVPRLWEKIYSRVLIMRSEATPFGRWAFDRAMASGAaklegKGGAmhavwdfLVLRNIRQMIgfdrnrrs 353
Cdd:PRK07768 226 ---VTPMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRRQA-----KPGA-------FDLSSLRFAL-------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 354 nTGAAPISPDLIRWYGALGV-------TLLEGYGMTETSGVAS------------------------VNVIGDN--RIGT 400
Cdd:PRK07768 283 -NGAEPIDPADVEDLLDAGArfglrpeAILPAYGMAEATLAVSfspcgaglvvdevdadllaalrraVPATKGNtrRLAT 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 401 IGCALPATELRIAEN----------GEICLKGPNVFKGYwRKPE--KTAEDiRDGWLYTGDVGRIGDDGAITITGRVKDI 468
Cdd:PRK07768 362 LGPPLPGLEVRVVDEdgqvlpprgvGVIELRGESVTPGY-LTMDgfIPAQD-ADGWLDTGDLGYLTEEGEVVVCGRVKDV 439
|
490
....*....|....*
gi 1821015446 469 IITaGGKNITPAEIE 483
Cdd:PRK07768 440 IIM-AGRNIYPTDIE 453
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
174-499 |
1.29e-22 |
|
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: 101.25 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 174 APDAAERFR-----IEINASQPeDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHvleri 248
Cdd:cd05920 118 VPDRHAGFDhralaRELAESIP-EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH----- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 249 vsvEFPIA---------VGSTVNFAE--SPDTVFDNLREVSPHVFTAVPRLWEkiysrvlimrseatpfgRWAfdramas 317
Cdd:cd05920 192 ---NFPLAcpgvlgtllAGGRVVLAPdpSPDAAFPLIEREGVTVTALVPALVS-----------------LWL------- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 318 GAAKLEGkggamhavWDFLVLRNIRqmigfdrnrrsnTGAAPISPDLIRWYGA-LGVTLLEGYGMTEtsGVASVNVIGDN 396
Cdd:cd05920 245 DAAASRR--------ADLSSLRLLQ------------VGGARLSPALARRVPPvLGCTLQQVFGMAE--GLLNYTRLDDP 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 397 R---IGTIGCAL-PATELRIA----------ENGEICLKGPNVFKGYWRKPEKTAEDIR-DGWLYTGDVGRIGDDGAITI 461
Cdd:cd05920 303 DeviIHTQGRPMsPDDEIRVVdeegnpvppgEEGELLTRGPYTIRGYYRAPEHNARAFTpDGFYRTGDLVRRTPDGYLVV 382
|
330 340 350
....*....|....*....|....*....|....*...
gi 1821015446 462 TGRVKDiIITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05920 383 EGRIKD-QINRGGEKIAAEEVENLLLRHPAVHDAAVVA 419
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
46-498 |
1.83e-22 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 101.63 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVEN 125
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 126 D-----EQLDKYLEVQDRVPTIVkvIVFdpkgLRDFSHPKVMFLSDL-YEI----GEKAPD-AAERFRIEinasQPEDTR 194
Cdd:PLN03102 120 SfeplaREVLHLLSSEDSNLNLP--VIF----IHEIDFPKRPSSEELdYECliqrGEPTPSlVARMFRIQ----DEHDPI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 195 MLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNfaespdtvfdnL 274
Cdd:PLN03102 190 SLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVC-----------M 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 275 REVSphvftaVPRLWEKI-YSRVLIMRSEATpfgrwAFDRAMASGAAKLEGKGGAMHAVwdflvlrnirqmigfdrnrrs 353
Cdd:PLN03102 259 RHVT------APEIYKNIeMHNVTHMCCVPT-----VFNILLKGNSLDLSPRSGPVHVL--------------------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 354 nTGAAPISPDLIRWYGALGVTLLEGYGMTETSGVA-------SVNVIGDN-------RIGTIGCALPATELRIAEN---- 415
Cdd:PLN03102 307 -TGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVlfcewqdEWNRLPENqqmelkaRQGVSILGLADVDVKNKETqesv 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 -------GEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKF 488
Cdd:PLN03102 386 prdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEVENVLYK 464
|
490
....*....|
gi 1821015446 489 SPFISDAVVI 498
Cdd:PLN03102 465 YPKVLETAVV 474
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
175-502 |
5.48e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 97.81 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 175 PDAAERFRIEINASQP--EDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQvlRVDPKDEQLCFLPLCH-----VLER 247
Cdd:PRK07824 17 ERRAALLRDALRVGEPidDDVALVVATSGTTGTPKGAMLTAAALTASADATHD--RLGGPGQWLLALPAHHiaglqVLVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 248 -IVSVEFPIAVGSTVNFaeSPDTVFDNLREVSPhvftavprlwEKIYSRVLIMRseatpfgrwaFDRAMASGAAKlegkg 326
Cdd:PRK07824 95 sVIAGSEPVELDVSAGF--DPTALPRAVAELGG----------GRRYTSLVPMQ----------LAKALDDPAAT----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 327 gAMHAVWDFLVLrnirqmigfdrnrrsntGAAPISPDLIRWYGALGVTLLEGYGMTETSGvasvnvigdnrigtiGC--- 403
Cdd:PRK07824 148 -AALAELDAVLV-----------------GGGPAPAPVLDAAAAAGINVVRTYGMSETSG---------------GCvyd 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 404 --ALPATELRIaENGEICLKGPNVFKGYwRKPEKTAEDIRDGWLYTGDVGRIgDDGAITITGRVKDIIITaGGKNITPAE 481
Cdd:PRK07824 195 gvPLDGVRVRV-EDGRIALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGAL-DDGVLTVLGRADDAIST-GGLTVLPQV 270
|
330 340
....*....|....*....|...
gi 1821015446 482 IESRLKFSPFISDAVVIG--DRR 502
Cdd:PRK07824 271 VEAALATHPAVADCAVFGlpDDR 293
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
190-483 |
1.04e-21 |
|
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: 98.71 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 190 PEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESpdt 269
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPT--- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 270 vfdnlrevspHVFTAVPRLWEKIYSRVLIMRSEATPFG-RWAFDRAMASGAAKlegkggamhavWDflvLRNIRQMIgfd 348
Cdd:cd05908 182 ----------RLFIRRPILWLKKASEHKATIVSSPNFGyKYFLKTLKPEKAND-----------WD---LSSIRMIL--- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 349 rnrrsnTGAAPISPDLIRW-------YGALGVTLLEGYGMTETSGVAS--------VNVIGDNRIGTIGCALPA------ 407
Cdd:cd05908 235 ------NGAEPIDYELCHEfldhmskYGLKRNAILPVYGLAEASVGASlpkaqspfKTITLGRRHVTHGEPEPEvdkkds 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 408 --------------TELRIAEN----------GEICLKGPNVFKGYWRKPEKTAEDIR-DGWLYTGDVGRIgDDGAITIT 462
Cdd:cd05908 309 ecltfvevgkpideTDIRICDEdnkilpdgyiGHIQIRGKNVTPGYYNNPEATAKVFTdDGWLKTGDLGFI-RNGRLVIT 387
|
330 340
....*....|....*....|.
gi 1821015446 463 GRVKDIIITaGGKNITPAEIE 483
Cdd:cd05908 388 GREKDIIFV-NGQNVYPHDIE 407
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
196-498 |
2.19e-21 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 97.44 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 196 LIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCH--VLERIVSvefPIAVGSTV-----NFAESPD 268
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFdgAHEQLLP---PLICGACVvlrpdELWASAD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 269 TVFDNLREVSPHVFTAVPRLWEKiysrvlimrseatpFGRWAfDRAMASGAAKLegkggamhavwdflvlrniRQMIgfd 348
Cdd:cd17649 176 ELAEMVRELGVTVLDLPPAYLQQ--------------LAEEA-DRTGDGRPPSL-------------------RLYI--- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 349 rnrrsnTGAAPISPDLIRWYGALGVTLLEGYGMTETSGVASVNVI--GDNRIGT---IGCALPATELRIAEN-------- 415
Cdd:cd17649 219 ------FGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKCeaGAARAGAsmpIGRPLGGRSAYILDAdlnpvpvg 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 --GEICLKGPNVFKGYWRKPEKTAED-IRD------GWLY-TGDVGRIGDDGAITITGRVkDIIITAGGKNITPAEIESR 485
Cdd:cd17649 293 vtGELYIGGEGLARGYLGRPELTAERfVPDpfgapgSRLYrTGDLARWRDDGVIEYLGRV-DHQVKIRGFRIELGEIEAA 371
|
330
....*....|...
gi 1821015446 486 LKFSPFISDAVVI 498
Cdd:cd17649 372 LLEHPGVREAAVV 384
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
18-498 |
2.62e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.26 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 18 VVKLWAAKCAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIP 97
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVVFGD----QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY 2080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 98 SGVYTTDSAGQLEYLINDSGSAFLFVENDeqldkyleVQDRVPTivkvivfdPKGLRDFSHPKVMFLSDlYEIGEKAPDA 177
Cdd:PRK12316 2081 VPLDPNYPAERLAYMLEDSGAALLLTQRH--------LLERLPL--------PAGVARLPLDRDAEWAD-YPDTAPAVQL 2143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 178 AerfrieinasqPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHvlerIVSVE---FP 254
Cdd:PRK12316 2144 A-----------GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSF----DGAHEqwfHP 2208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 255 IAVGSTVNFAE----SPDTVFDNLREVSPHVFTAVPRLWEKIysrvlimrseatpfgrwafdramasgAAKLEGKGGAMh 330
Cdd:PRK12316 2209 LLNGARVLIRDdelwDPEQLYDEMERHGVTILDFPPVYLQQL--------------------------AEHAERDGRPP- 2261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 331 avwdflvlrNIRQMIgfdrnrrsNTGAAPISPDLIRWYGAL-GVTLLEGYGMTET--------------SGVASVNV--- 392
Cdd:PRK12316 2262 ---------AVRVYC--------FGGEAVPAASLRLAWEALrPVYLFNGYGPTEAvvtpllwkcrpqdpCGAAYVPIgra 2324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 393 IGDNRIGTIGCALPATELRIAenGEICLKGPNVFKGYWRKPEKTAE-------DIRDGWLY-TGDVGRIGDDGAITITGR 464
Cdd:PRK12316 2325 LGNRRAYILDADLNLLAPGMA--GELYLGGEGLARGYLNRPGLTAErfvpdpfSASGERLYrTGDLARYRADGVVEYLGR 2402
|
490 500 510
....*....|....*....|....*....|....
gi 1821015446 465 VkDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK12316 2403 I-DHQVKIRGFRIELGEIEARLQAHPAVREAVVV 2435
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
54-537 |
6.43e-21 |
|
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: 96.24 E-value: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 54 RSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGG----IPSGvYTTDsagQLEYLINDSGSAFLFVEndEQL 129
Cdd:cd17655 31 RANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGaylpIDPD-YPEE---RIQYILEDSGADILLTQ--SHL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 130 DkylevqdrvptivkvivfdpkglrdfshPKVMFLSDLYEIGEKAPDAAERFRIEiNASQPEDTRMLIYTSGTTGPPKGA 209
Cdd:cd17655 105 Q----------------------------PPIAFIGLIDLLDEDTIYHEESENLE-PVSKSDDLAYVIYTSGSTGKPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 210 MISHSNMLYQMWAGQQVLrvdPKDEQLCFLPLchvleriVSVEFPIAVGSTVNFAESPDTVFdnlreVSPHVFTAVPRLW 289
Cdd:cd17655 156 MIEHRGVVNLVEWANKVI---YQGEHLRVALF-------ASISFDASVTEIFASLLSGNTLY-----IVRKETVLDGQAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 290 EKIYSRVLIMRSEATPfgrwafdramasgaAKLEgkggaMHAVWDFLVLRNIRQMIgfdrnrrsnTGAAPISPDLIR-WY 368
Cdd:cd17655 221 TQYIRQNRITIIDLTP--------------AHLK-----LLDAADDSEGLSLKHLI---------VGGEALSTELAKkII 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 369 GALG--VTLLEGYGMTETSGVASV-NVIGDNRIGT---IGCALPATELRIAEN----------GEICLKGPNVFKGYWRK 432
Cdd:cd17655 273 ELFGtnPTITNAYGPTETTVDASIyQYEPETDQQVsvpIGKPLGNTRIYILDQygrpqpvgvaGELYIGGEGVARGYLNR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 433 PEKTAEDIRD------GWLY-TGDVGRIGDDGAITITGRVkDIIITAGGKNITPAEIESRLKFSPFISDAVVIG----DR 501
Cdd:cd17655 353 PELTAEKFVDdpfvpgERMYrTGDLARWLPDGNIEFLGRI-DHQVKIRGYRIELGEIEARLLQHPDIKEAVVIArkdeQG 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1821015446 502 RKYLTVLIMID--------QENVEKYAQDHQIPfSDFASLTRAP 537
Cdd:cd17655 432 QNYLCAYIVSEkelpvaqlREFLARELPDYMIP-SYFIKLDEIP 474
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
46-498 |
1.18e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 95.78 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFV-- 123
Cdd:PRK08162 44 RTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVdt 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 124 ENDEQLDKYLEVQDRvPTIVKVIVFDPkglrdfSHPKVMFLSDL-YE--IGEKAPDAAerfrieinASQPEDTRMLI--- 197
Cdd:PRK08162 124 EFAEVAREALALLPG-PKPLVIDVDDP------EYPGGRFIGALdYEafLASGDPDFA--------WTLPADEWDAIaln 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 198 YTSGTTGPPKGaMISHSNMLYQMWAGQQVLRVDPKDE-QLCFLPL------ChvlerivsveFP--IAVGSTVNfaespd 268
Cdd:PRK08162 189 YTSGTTGNPKG-VVYHHRGAYLNALSNILAWGMPKHPvYLWTLPMfhcngwC----------FPwtVAARAGTN------ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 269 tVFdnLREVSPH-VFTAVPRlwEKI--YSRVLIMRSeatpfgrwafdrAMASGAAklEGKGGAMHAVwdflvlrnirqmi 345
Cdd:PRK08162 252 -VC--LRKVDPKlIFDLIRE--HGVthYCGAPIVLS------------ALINAPA--EWRAGIDHPV------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 346 gfdrnrRSNTGAAPISPDLIRWYGALGVTLLEGYGMTETSGVASVnvigdnrigtigCA-------LPATElRIAEN--- 415
Cdd:PRK08162 300 ------HAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTETYGPATV------------CAwqpewdaLPLDE-RAQLKarq 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 ----------------------------GEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKD 467
Cdd:PRK08162 361 gvryplqegvtvldpdtmqpvpadgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKD 440
|
490 500 510
....*....|....*....|....*....|.
gi 1821015446 468 IIITaGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK08162 441 IIIS-GGENISSIEVEDVLYRHPAVLVAAVV 470
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
39-501 |
1.25e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 95.52 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 39 DFGIW---QAYSWSDWYDRSQAIGMGLIELgLTRGTP--VSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLI 113
Cdd:PRK07867 19 DRGLYfedSFTSWREHIRGSAARAAALRAR-LDPTRPphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 114 NDSGSAFLFVEndeqlDKYLEVQDRVPTIVKVIVFDPKGLRDFSHPkvmflsdlyeigekAPDAAERFRieinASQPEDT 193
Cdd:PRK07867 98 AHADCQLVLTE-----SAHAELLDGLDPGVRVINVDSPAWADELAA--------------HRDAEPPFR----VADPDDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 194 RMLIYTSGTTGPPKGAMISHS------NMLYQMWAgqqvlrVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTV----NF 263
Cdd:PRK07867 155 FMLIFTSGTSGDPKAVRCTHRkvasagVMLAQRFG------LGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIalrrKF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 264 AESpdTVFDNLREVSPHVFTAVprlwEKIYSRVLimrseATPfgrwafdramasgaaklEGKGGAMHAvwdflvlrnIRQ 343
Cdd:PRK07867 229 SAS--GFLPDVRRYGATYANYV----GKPLSYVL-----ATP-----------------ERPDDADNP---------LRI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 344 MIGfdrnrrsNTGAAPispDLIRWYGALGVTLLEGYGMTEtsGVASVNVIGDNRIGTIGCALPATELRIAENGEIC---- 419
Cdd:PRK07867 272 VYG-------NEGAPG---DIARFARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPPGVAIVDPDTGTECppae 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 420 ------------------LKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAE 481
Cdd:PRK07867 340 dadgrllnadeaigelvnTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGD-WMRVDGENLGTAP 418
|
490 500
....*....|....*....|....*..
gi 1821015446 482 IESRLKFSPFISDAVV-------IGDR 501
Cdd:PRK07867 419 IERILLRYPDATEVAVyavpdpvVGDQ 445
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
53-499 |
1.48e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 95.15 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 53 DRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVENDeqldkY 132
Cdd:PRK12406 19 QRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHAD-----L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 133 LE-VQDRVPTIVKVIVFDPKglrdfshPKVMFLSDLYEIGEKAPDAAERFRIEINASQPEDT------RMLIYTSGTTGP 205
Cdd:PRK12406 94 LHgLASALPAGVTVLSVPTP-------PEIAAAYRISPALLTPPAGAIDWEGWLAQQEPYDGppvpqpQSMIYTSGTTGH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 206 PKGamishsnmlyqmwagqqVLRVDPKDEQLCflplchVLERIVSVEFPIAVGSTVnFAESPdtvfdnLREVSPHVFTAV 285
Cdd:PRK12406 167 PKG-----------------VRRAAPTPEQAA------AAEQMRALIYGLKPGIRA-LLTGP------LYHSAPNAYGLR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 286 P-RLWEKIysrVLIMRSEATPF----GRWAFDRA-----MASGAAKLEGkggAMHAVWDFLVLRNIRQmigfdrnrrsnt 355
Cdd:PRK12406 217 AgRLGGVL---VLQPRFDPEELlqliERHRITHMhmvptMFIRLLKLPE---EVRAKYDVSSLRHVIH------------ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 356 GAAPISPD----LIRWYGALgvtLLEGYGMTETSGVA---SVNVIgdNRIGTIGCALPATELRI----------AENGEI 418
Cdd:PRK12406 279 AAAPCPADvkraMIEWWGPV---IYEYYGSTESGAVTfatSEDAL--SHPGTVGKAAPGAELRFvdedgrplpqGEIGEI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 419 CLKGPNV--FKgYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAV 496
Cdd:PRK12406 354 YSRIAGNpdFT-YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEIEAVLHAVPGVHDCA 431
|
...
gi 1821015446 497 VIG 499
Cdd:PRK12406 432 VFG 434
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
46-499 |
1.53e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 95.34 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGV---YTTDsagQLEYLINDSGSAFLF 122
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyrYVED---ELRYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 123 VEnDEQLDKYLEVQDRVPTIVKVIVFDPKGLRDFSHPKVMFlSDLYEIGEKAPDAAERfrieinasQPEDtRMLIYTSGT 202
Cdd:PRK07798 106 YE-REFAPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDY-EDALAAGSPERDFGER--------SPDD-LYLLYTGGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 203 TGPPKGAMISHSNMLYQMWAGQQVLRVDP-KDEQLcflplchVLERIV----SVEFPIA----------------VGSTV 261
Cdd:PRK07798 175 TGMPKGVMWRQEDIFRVLLGGRDFATGEPiEDEEE-------LAKRAAagpgMRRFPAPplmhgagqwaafaalfSGQTV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 262 NFAesPDTVFDnlrevsPHvftavpRLWEKIY-SRVLIMrseaTPFGRwAFDRAMasgAAKLEGKGGamhavWDFLVLRN 340
Cdd:PRK07798 248 VLL--PDVRFD------AD------EVWRTIErEKVNVI----TIVGD-AMARPL---LDALEARGP-----YDLSSLFA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 341 IRqmigfdrnrrsnTGAAPISPDLIRWYGAL--GVTLLEGYGMTET-----SGVASVNVIGDNRIGTIG--CALPATELR 411
Cdd:PRK07798 301 IA------------SGGALFSPSVKEALLELlpNVVLTDSIGSSETgfggsGTVAKGAVHTGGPRFTIGprTVVLDEDGN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 412 IAENGE----ICLKGPNVFKGYWRKPEKTAEDIR--DG--WLYTGDVGRIGDDGAITITGRVKDIIITAGGKnITPAEIE 483
Cdd:PRK07798 369 PVEPGSgeigWIARRGHIPLGYYKDPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEK-VFPEEVE 447
|
490
....*....|....*.
gi 1821015446 484 SRLKFSPFISDAVVIG 499
Cdd:PRK07798 448 EALKAHPDVADALVVG 463
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
28-499 |
1.67e-20 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 95.34 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 28 ERGDATA--HREKDFGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDS 105
Cdd:cd17634 65 ENGDRTAiiYEGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 106 AGQLEYLINDSGSAFLfVENDEQL------------DKYLEVQdrVPTIVKVIVFDPKGL-------RDFshpkvmflsD 166
Cdd:cd17634 145 PEAVAGRIIDSSSRLL-ITADGGVragrsvplkknvDDALNPN--VTSVEHVIVLKRTGSdidwqegRDL---------W 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 167 LYEIGEKAPDAAERFRIEinasqPEDTRMLIYTSGTTGPPKGAMISHSN-MLYQMWAGQQVLRVDPKDEQLCFLPLCHVL 245
Cdd:cd17634 213 WRDLIAKASPEHQPEAMN-----AEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 246 ERIVSVEFPIAVGSTVNfaespdtvfdnLREVSPhVFTAVPRLWEKIYSR-VLIMRSEATpfgrwAFDRAMASGAAKLEG 324
Cdd:cd17634 288 GHSYLLYGPLACGATTL-----------LYEGVP-NWPTPARMWQVVDKHgVNILYTAPT-----AIRALMAAGDDAIEG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 325 kggamhavwdflvlrnirqmigFDRNRRSNTGAA--PISPDLIRWY----GALGVTLLEGYGMTETSGVASVNVIG--DN 396
Cdd:cd17634 351 ----------------------TDRSSLRILGSVgePINPEAYEWYwkkiGKEKCPVVDTWWQTETGGFMITPLPGaiEL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 397 RIGTIGCALPATELRIAEN----------GEICLKG--PNVFKGYWRKPEKTAEDIR---DGWLYTGDVGRIGDDGAITI 461
Cdd:cd17634 409 KAGSATRPVFGVQPAVVDNeghpqpggteGNLVITDpwPGQTRTLFGDHERFEQTYFstfKGMYFSGDGARRDEDGYYWI 488
|
490 500 510
....*....|....*....|....*....|....*...
gi 1821015446 462 TGRVKDIIITAgGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd17634 489 TGRSDDVINVA-GHRLGTAEIESVLVAHPKVAEAAVVG 525
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
198-502 |
4.93e-20 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 91.31 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 198 YTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLErIVSVEFPIAVGSTV----NFaeSPDTVFDN 273
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLF-LYGAISALYLGGTFigqrKF--NPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 274 LREVSPHVFTAVPRLWE---KIYSRVLIMRSeatpfgrwafdraMASGAAKlegkggamhavWDFLVLRNIRQmigfdrn 350
Cdd:cd17633 84 INQYNATVIYLVPTMLQalaRTLEPESKIKS-------------IFSSGQK-----------LFESTKKKLKN------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 351 rrsntgaapISPDLirwygalgvTLLEGYGMTETSGVaSVNVIGDNR-IGTIGCALPATELRI--AENGEI---CLKGPN 424
Cdd:cd17633 133 ---------IFPKA---------NLIEFYGTSELSFI-TYNFNQESRpPNSVGRPFPNVEIEIrnADGGEIgkiFVKSEM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 425 VFKGYWRKPEKTAedirDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG--DRR 502
Cdd:cd17633 194 VFSGYVRGGFSNP----DGWMSVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLKAIPGIEEAIVVGipDAR 268
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
32-499 |
1.06e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 92.92 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 32 ATAHREKDFGIW-----QAYSWSDWYDRSQAIGMGLI-ELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDS 105
Cdd:PRK05620 20 STVHGDTTVTTWggaeqEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 106 AGQLEYLINDSGSAFLFVE--NDEQLDKYLEvqdRVPTIVKVIVFdpkGLRDFSHPKVMFLSDLyEIGEKAPDAAERFRI 183
Cdd:PRK05620 100 NDQIVHIINHAEDEVIVADprLAEQLGEILK---ECPCVRAVVFI---GPSDADSAAAHMPEGI-KVYSYEALLDGRSTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 184 EINASQPEDTRMLI-YTSGTTGPPKGAMISHSNMLYQmwaGQQVLRVDPKDEQ-----LCFLPLCHVLERIVsvefPIAV 257
Cdd:PRK05620 173 YDWPELDETTAAAIcYSTGTTGAPKGVVYSHRSLYLQ---SLSLRTTDSLAVThgesfLCCVPIYHVLSWGV----PLAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 258 ----------GSTVnfaeSPDTVFDNLREVSPHVFTAVPRLWEKiysrvLIMRSEATPFGRwafdramasgaaklegkgg 327
Cdd:PRK05620 246 fmsgtplvfpGPDL----SAPTLAKIIATAMPRVAHGVPTLWIQ-----LMVHYLKNPPER------------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 328 amhavwdfLVLRNIRqmigfdrnrrsnTGAAPISPDLIR-WYGALGVTLLEGYGMTETSGVASV-----NVIGDNRI--- 398
Cdd:PRK05620 298 --------MSLQEIY------------VGGSAVPPILIKaWEERYGVDVVHVWGMTETSPVGTVarppsGVSGEARWayr 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 399 ---GTIGCALpatELRIAEN-----------GEICLKGPNVFKGYWRKP------------EKTAEDIR-----DGWLYT 447
Cdd:PRK05620 358 vsqGRFPASL---EYRIVNDgqvmestdrneGEIQVRGNWVTASYYHSPteegggaastfrGEDVEDANdrftaDGWLRT 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1821015446 448 GDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK05620 435 GDVGSVTRDGFLTIHDRARD-VIRSGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
62-502 |
1.22e-19 |
|
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: 92.41 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 62 LIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGipsgVYTTDSAGQ----LEYLINDSGSAFLFVENDEQLDkyLEVQD 137
Cdd:cd17651 37 LRARGVGPGDLVALCARRSAELVVALLAILKAGA----AYVPLDPAYpaerLAFMLADAGPVLVLTHPALAGE--LAVEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 138 RVPTIVkvivfDPKGLRdfshpkvmflsdlyeigekAPDAAERFRieinASQPEDTRMLIYTSGTTGPPKGAMISHSNML 217
Cdd:cd17651 111 VAVTLL-----DQPGAA-------------------AGADAEPDP----ALDADDLAYVIYTSGSTGRPKGVVMPHRSLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 218 YQMWAGQQVLRVDPKDEQLCFLPL---CHVLErIVSvefPIAVGSTVNFAespdtvfdnlrevSPHVFTAVPRLW----E 290
Cdd:cd17651 163 NLVAWQARASSLGPGARTLQFAGLgfdVSVQE-IFS---TLCAGATLVLP-------------PEEVRTDPPALAawldE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 291 KIYSRVLImrseATPFGRWAFDRAMASGAAklegkggamhavwdflvLRNIRQMIgfdrnrrsnTG--AAPISPDLIRWY 368
Cdd:cd17651 226 QRISRVFL----PTVALRALAEHGRPLGVR-----------------LAALRYLL---------TGgeQLVLTEDLREFC 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 369 GAL-GVTLLEGYGMTETSGVASVNVIGDN----RIGTIGCALPATELRIAEN----------GEICLKGPNVFKGYWRKP 433
Cdd:cd17651 276 AGLpGLRLHNHYGPTETHVVTALSLPGDPaawpAPPPIGRPIDNTRVYVLDAalrpvppgvpGELYIGGAGLARGYLNRP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 434 EKTAED------IRDGWLY-TGDVGRIGDDGAITITGRVKDIIITAGGKnITPAEIESRLKFSPFISDAVVI------GD 500
Cdd:cd17651 356 ELTAERfvpdpfVPGARMYrTGDLARWLPDGELEFLGRADDQVKIRGFR-IELGEIEAALARHPGVREAVVLaredrpGE 434
|
..
gi 1821015446 501 RR 502
Cdd:cd17651 435 KR 436
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
178-498 |
1.47e-19 |
|
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: 91.54 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 178 AERFRIEINASQPE-------DTRMLIYTSGTTGPPKGAMISHSNML-YQMWAGQQvLRVDPKDEQLCFLPL---CHVLE 246
Cdd:cd05945 77 AERIREILDAAKPAlliadgdDNAYIIFTSGSTGRPKGVQISHDNLVsFTNWMLSD-FPLGPGDVFLNQAPFsfdLSVMD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 247 RIVSVefpiAVGSTVN-----FAESPDTVFDNLREVSPHVFTAVPRLWEkiysrvLIMRSEAtpfgrwaFDRAMasgaak 321
Cdd:cd05945 156 LYPAL----ASGATLVpvprdATADPKQLFRFLAEHGITVWVSTPSFAA------MCLLSPT-------FTPES------ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 322 legkggamhavwdflvLRNIRQMIgFDrnrrsntGAAPISPDLIRWYGAL-GVTLLEGYGMTETSGVASVNVI------G 394
Cdd:cd05945 213 ----------------LPSLRHFL-FC-------GEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEVtpevldG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 395 DNRIgTIGCALPATELRI----------AENGEICLKGPNVFKGYWRKPEKTAE----DIRDGWLYTGDVGRIGDDGAIT 460
Cdd:cd05945 269 YDRL-PIGYAKPGAKLVIldedgrpvppGEKGELVISGPSVSKGYLNNPEKTAAaffpDEGQRAYRTGDLVRLEADGLLF 347
|
330 340 350
....*....|....*....|....*....|....*...
gi 1821015446 461 ITGRvKDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:cd05945 348 YRGR-LDFQVKLNGYRIELEEIEAALRQVPGVKEAVVV 384
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
62-498 |
3.53e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 92.53 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 62 LIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFveNDEQLDKYLEVQDRVPT 141
Cdd:PRK12467 554 LIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL--TQSHLLAQLPVPAGLRS 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 142 IVKVIVFDPKGLRDFSHPKVmflsdlyeigekapdaaerfrieinASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMW 221
Cdd:PRK12467 632 LCLDEPADLLCGYSGHNPEV-------------------------ALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVC 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 222 AGQQVLRVDPKDEQLCFLPLCHVLEriVSVEF-PIAVGSTVNFAeSPDTVFDN---LREVSPH---VFTAVPRLWEkiys 294
Cdd:PRK12467 687 VIAERLQLAADDSMLMVSTFAFDLG--VTELFgALASGATLHLL-PPDCARDAeafAALMADQgvtVLKIVPSHLQ---- 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 295 rvLIMRSEATpfgrwafdrAMASGAAKLEGKGGAMHavWDFLVLrnIRQMigfdrnrrsntgaapispdlirwygALGVT 374
Cdd:PRK12467 760 --ALLQASRV---------ALPRPQRALVCGGEALQ--VDLLAR--VRAL-------------------------GPGAR 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 375 LLEGYGMTETSGVASVNVIG----DNRIGTIGCALPATELRIAEN----------GEICLKGPNVFKGYWRKPEKTAEDI 440
Cdd:PRK12467 800 LINHYGPTETTVGVSTYELSdeerDFGNVPIGQPLANLGLYILDHylnpvpvgvvGELYIGGAGLARGYHRRPALTAERF 879
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821015446 441 -------RDGWLY-TGDVGRIGDDGAITITGRVkDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK12467 880 vpdpfgaDGGRLYrTGDLARYRADGVIEYLGRM-DHQVKIRGFRIELGEIEARLLAQPGVREAVVL 944
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
19-483 |
4.43e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 90.94 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 19 VKLWAAkcaERGDATAHREKDF-----GIWQAYSWSDWYDRSQAIGMGLIELGlTRGTPVSILSEDNKEWLYCDLAISAA 93
Cdd:PRK07769 27 VERWAK---VRGDKLAYRFLDFsterdGVARDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 94 GGIPSGVYTTDSAGQLEylindsgsaflfvendeQLDKYLEvqDRVPTIVKVIVFDPKGLRDFShpkvmflsdlyeigeK 173
Cdd:PRK07769 103 GRIAVPLFDPAEPGHVG-----------------RLHAVLD--DCTPSAILTTTDSAEGVRKFF---------------R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 174 APDAAERFRI--------EINAS--QPE----DTRMLIYTSGTTGPPKGAMISHSNM---LYQMWAGqqvLRVDPKDEQL 236
Cdd:PRK07769 149 ARPAKERPRViavdavpdEVGATwvPPEanedTIAYLQYTSGSTRIPAGVQITHLNLptnVLQVIDA---LEGQEGDRGV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 237 CFLPLCHVLERIvSVEFPIAVGSTVNFaespdtvfdnlreVSPHVFTAVPRLWEKIYSRVLIMRSE---ATPfgRWAFDR 313
Cdd:PRK07769 226 SWLPFFHDMGLI-TVLLPALLGHYITF-------------MSPAAFVRRPGRWIRELARKPGGTGGtfsAAP--NFAFEH 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 314 AMASGAAKlEGKggamhAVWDflvLRNIRQMIgfdrnrrsnTGAAPISPDLIRW-------YGALGVTLLEGYGMTE-TS 385
Cdd:PRK07769 290 AAARGLPK-DGE-----PPLD---LSNVKGLL---------NGSEPVSPASMRKfneafapYGLPPTAIKPSYGMAEaTL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 386 GVAS----------------------VNVIGD--NRIGTIGC-------------ALPATELRIAENGEICLKGPNVFKG 428
Cdd:PRK07769 352 FVSTtpmdeeptviyvdrdelnagrfVEVPADapNAVAQVSAgkvgvsewavivdPETASELPDGQIGEIWLHGNNIGTG 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821015446 429 YWRKPEKTAEDIR------------------DGWLYTGDVGrIGDDGAITITGRVKDIIITaGGKNITPAEIE 483
Cdd:PRK07769 432 YWGKPEETAATFQnilksrlseshaegapddALWVRTGDYG-VYFDGELYITGRVKDLVII-DGRNHYPQDLE 502
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
62-498 |
5.30e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 91.94 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 62 LIELGLTRGTPVSILSEDNKEWLYCDLAISAAGG--IPSGV-YTTDsagQLEYLINDSGSAFLFVENdeqldkylEVQDR 138
Cdd:PRK12316 4593 LIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGayVPLDPeYPRE---RLAYMMEDSGAALLLTQS--------HLLQR 4661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 139 VPTivkvivfdPKGLrdfshpKVMFLsDLYEIGEKAPDAAERFRIEinasqPEDTRMLIYTSGTTGPPKGAMISHSNMLY 218
Cdd:PRK12316 4662 LPI--------PDGL------ASLAL-DRDEDWEGFPAHDPAVRLH-----PDNLAYVIYTSGSTGRPKGVAVSHGSLVN 4721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 219 QMWAGQQVLRVDPKDEQLCFLPLCHvlerIVSVE---FPIAVGSTVNFAEspdtvfdnlrevsphvftavPRLWEKIYSR 295
Cdd:PRK12316 4722 HLHATGERYELTPDDRVLQFMSFSF----DGSHEglyHPLINGASVVIRD--------------------DSLWDPERLY 4777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 296 VLIMRSEAT----PFGRWafdRAMASGAAKlEGKGGAMhavwdflvlrnirqmigfdrnRRSNTGAAPISPDLIR-WYGA 370
Cdd:PRK12316 4778 AEIHEHRVTvlvfPPVYL---QQLAEHAER-DGEPPSL---------------------RVYCFGGEAVAQASYDlAWRA 4832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 371 LGVT-LLEGYGMTETSGVASVNVIGDNRIGT-----IGCALPATELRIAEN----------GEICLKGPNVFKGYWRKPE 434
Cdd:PRK12316 4833 LKPVyLFNGYGPTETTVTVLLWKARDGDACGaaympIGTPLGNRSGYVLDGqlnplpvgvaGELYLGGEGVARGYLERPA 4912
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821015446 435 KTAE-------DIRDGWLY-TGDVGRIGDDGAITITGRVkDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK12316 4913 LTAErfvpdpfGAPGGRLYrTGDLARYRADGVIDYLGRV-DHQVKIRGFRIELGEIEARLREHPAVREAVVI 4983
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
45-483 |
2.41e-18 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 88.52 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 45 AYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPS-----------GVYTTDSAGQLEyli 113
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVplplpmgfggrESYIAQLRGMLA--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 114 ndSGSAFLFVENDEQLDkylevqdrvptIVKVIVFDPKGLRDFSHpkVMFlsdlyeigeKAPDAAerfRIEINASQPEDT 193
Cdd:PRK09192 126 --SAQPAAIITPDELLP-----------WVNEATHGNPLLHVLSH--AWF---------KALPEA---DVALPRPTPDDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 194 RMLIYTSGTTGPPKGAMISHSNMLYQMWA-GQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPDtvfd 272
Cdd:PRK09192 179 AYLQYSSGSTRFPRGVIITHRALMANLRAiSHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRD---- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 273 nlrevsphvFTAVPRLWEKiysrvLIMRSEAT-----PFGrwaFD----RAMASGAAKLE-------GKGGAMhavwdfl 336
Cdd:PRK09192 255 ---------FARRPLQWLD-----LISRNRGTisyspPFG---YElcarRVNSKDLAELDlscwrvaGIGADM------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 337 vlrnIRQMI-----------GFDRNR-------RSNTGAAPISP-------DLIRwygalgVTLLEGYGMTETSGVASVN 391
Cdd:PRK09192 311 ----IRPDVlhqfaeafapaGFDDKAfmpsyglAEATLAVSFSPlgsgivvEEVD------RDRLEYQGKAVAPGAETRR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 392 VigdNRIGTIGCALPATELRI-AENGE---------ICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIgDDGAITI 461
Cdd:PRK09192 381 V---RTFVNCGKALPGHEIEIrNEAGMplpervvghICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYI 456
|
490 500
....*....|....*....|..
gi 1821015446 462 TGRVKDIIITaGGKNITPAEIE 483
Cdd:PRK09192 457 TGRAKDLIII-NGRNIWPQDIE 477
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
188-498 |
2.55e-18 |
|
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: 87.75 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 188 SQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLcflpLCH-------VLE---------RIVSV 251
Cdd:cd17643 90 TDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHsyafdfsVWEiwgallhggRLVVV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 252 EFPIAvgstvnfaESPDTVFDNLREVSPHVFTAVPRlwekiysrvlimrseatpfgrwAFDRAMASgaakLEGKGGAMHA 331
Cdd:cd17643 166 PYEVA--------RSPEDFARLLRDEGVTVLNQTPS----------------------AFYQLVEA----ADRDGRDPLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 332 vwdflvlrnIRQMIgFdrnrrsntGAAPISPDLIR-WYGALGV---TLLEGYGMTETSGVASVNVI-----GDNRIGTIG 402
Cdd:cd17643 212 ---------LRYVI-F--------GGEALEAAMLRpWAGRFGLdrpQLVNMYGITETTVHVTFRPLdaadlPAAAASPIG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 403 CALPATELRIAEN----------GEICLKGPNVFKGYWRKPEKTAEDIRDG-------WLY-TGDVGRIGDDGAITITGR 464
Cdd:cd17643 274 RPLPGLRVYVLDAdgrpvppgvvGELYVSGAGVARGYLGRPELTAERFVANpfggpgsRMYrTGDLARRLPDGELEYLGR 353
|
330 340 350
....*....|....*....|....*....|....
gi 1821015446 465 VkDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:cd17643 354 A-DEQVKIRGFRIELGEIEAALATHPSVRDAAVI 386
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
18-505 |
5.66e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 5.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 18 VVKLWAAKCAERGDATAHRekdFGIwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIP 97
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALA---FGE-ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 98 SGVYTTDSAGQLEYLINDSGSAFLFveNDEQLDKYLEVqdrvPTIVKVIVFDPKGLRDFSHPkvmflsdlyeigEKAPDa 177
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGVQLLL--SQSHLGRKLPL----AAGVQVLDLDRPAAWLEGYS------------EENPG- 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 178 aerfrIEINasqPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHvlerIVSV-EF--P 254
Cdd:PRK12316 650 -----TELN---PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSF----DVSVwEFfwP 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 255 IAVGSTVNFAespdtvfdnlrevSPHVFTAVPRLWEkiysrvLIMRSEATPFgrwAFDRAMASGAAKLEGkggamhaVWD 334
Cdd:PRK12316 718 LMSGARLVVA-------------APGDHRDPAKLVE------LINREGVDTL---HFVPSMLQAFLQDED-------VAS 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 335 FLVLRNIrqmigfdrnrrsNTGAAPISPDLI-RWYGALGVT-LLEGYGMTETS-----------GVASVNvIGdNRIGTI 401
Cdd:PRK12316 769 CTSLRRI------------VCSGEALPADAQeQVFAKLPQAgLYNLYGPTEAAidvthwtcveeGGDSVP-IG-RPIANL 834
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 402 GCALPATELR---IAENGEICLKGPNVFKGYWRKPEKTAE-----DIRDG-WLY-TGDVGRIGDDGAITITGRVkDIIIT 471
Cdd:PRK12316 835 ACYILDANLEpvpVGVLGELYLAGRGLARGYHGRPGLTAErfvpsPFVAGeRMYrTGDLARYRADGVIEYAGRI-DHQVK 913
|
490 500 510
....*....|....*....|....*....|....
gi 1821015446 472 AGGKNITPAEIESRLKFSPFISDAVVIGDRRKYL 505
Cdd:PRK12316 914 LRGLRIELGEIEARLLEHPWVREAAVLAVDGKQL 947
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
178-504 |
6.22e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 86.60 E-value: 6.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 178 AERFRIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQM-WAGQqvlrVDPKDE--------QLCF-LPlchVLER 247
Cdd:cd12115 92 LEDAQARLVLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLqWAAA----AFSAEElagvlastSICFdLS---VFEL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 248 IVsvefPIAVGSTVNFAESPDTVFDNLREVSPHVFTAVPrlwekiysrvlimrseatpfgrwafdramaSGAAKLEGKGG 327
Cdd:cd12115 165 FG----PLATGGKVVLADNVLALPDLPAAAEVTLINTVP------------------------------SAAAELLRHDA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 328 AMHAVwdflvlrnirqmigfdrnRRSNTGAAPISPDLI-RWYGALGVT-LLEGYGMTETSGVASVNVI--GDNRIGTIGC 403
Cdd:cd12115 211 LPASV------------------RVVNLAGEPLPRDLVqRLYARLQVErVVNLYGPSEDTTYSTVAPVppGASGEVSIGR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 404 ALPATELRIAEN----------GEICLKGPNVFKGYWRKPEKTAEDIR------DGWLY-TGDVGRIGDDGAITITGRvK 466
Cdd:cd12115 273 PLANTQAYVLDRalqpvplgvpGELYIGGAGVARGYLGRPGLTAERFLpdpfgpGARLYrTGDLVRWRPDGLLEFLGR-A 351
|
330 340 350
....*....|....*....|....*....|....*...
gi 1821015446 467 DIIITAGGKNITPAEIESRLKFSPFISDAVVIGDRRKY 504
Cdd:cd12115 352 DNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAA 389
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
44-514 |
7.33e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 44 QAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFV 123
Cdd:PRK12316 3081 QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 124 ENDEQLDKYLEVQdrvptivkVIVFDPkglrdfshpkvmflsDLYEIGEKAPDaaerfrieiNASQPEDTRMLIYTSGTT 203
Cdd:PRK12316 3161 QSHLRLPLAQGVQ--------VLDLDR---------------GDENYAEANPA---------IRTMPENLAYVIYTSGST 3208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 204 GPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLErIVSVEFPIAVGSTV-----NFAESPDTVFDNLREVS 278
Cdd:PRK12316 3209 GKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVF-VEELFWPLMSGARVvlagpEDWRDPALLVELINSEG 3287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 279 PHVFTAVPRLWEKIYSRVLIMRseatpfgrwafdramasgaaklegkggamhavwdflvLRNIRQMIGfdrnrrsnTGAA 358
Cdd:PRK12316 3288 VDVLHAYPSMLQAFLEEEDAHR-------------------------------------CTSLKRIVC--------GGEA 3322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 359 PISPDLIRWYgaLGVTLLEGYGMTETSGVASVNVIGDNRIGT--IGCALPATELRIAEN----------GEICLKGPNVF 426
Cdd:PRK12316 3323 LPADLQQQVF--AGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGslepvpvgalGELYLGGEGLA 3400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 427 KGYWRKPEKTAEDI------RDGWLY-TGDVGRIGDDGAITITGRVkDIIITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK12316 3401 RGYHNRPGLTAERFvpdpfvPGERLYrTGDLARYRADGVIEYIGRV-DHQVKIRGFRIELGEIEARLLEHPWVREAVVLA 3479
|
490
....*....|....*
gi 1821015446 500 DRRKYLTVLIMIDQE 514
Cdd:PRK12316 3480 VDGRQLVAYVVPEDE 3494
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
187-483 |
9.86e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.92 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 187 ASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVD--PKDEQLCFLPLCHVLERIVSVEFPIavgstvnFA 264
Cdd:PRK05691 162 ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDlnPDDVIVSWLPLYHDMGLIGGLLQPI-------FS 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 265 ESPDTVfdnlreVSPHVFTAVPRLWEKIYSRVLIMRSEATPFG-RWAFDRAMASGAAKLEgkggamhavwdflvlrnirq 343
Cdd:PRK05691 235 GVPCVL------MSPAYFLERPLRWLEAISEYGGTISGGPDFAyRLCSERVSESALERLD-------------------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 344 migFDRNRRSNTGAAPISPDLIRWYG----ALGVT---LLEGYGMTETS----------GVASVNVIGD----NRI--GT 400
Cdd:PRK05691 289 ---LSRWRVAYSGSEPIRQDSLERFAekfaACGFDpdsFFASYGLAEATlfvsggrrgqGIPALELDAEalarNRAepGT 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 401 ----IGCAL--PATELRIAEN-----------GEICLKGPNVFKGYWRKPEKTAEDI--RDG--WLYTGDVGRIgDDGAI 459
Cdd:PRK05691 366 gsvlMSCGRsqPGHAVLIVDPqslevlgdnrvGEIWASGPSIAHGYWRNPEASAKTFveHDGrtWLRTGDLGFL-RDGEL 444
|
330 340
....*....|....*....|....
gi 1821015446 460 TITGRVKDIIITAgGKNITPAEIE 483
Cdd:PRK05691 445 FVTGRLKDMLIVR-GHNLYPQDIE 467
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
195-523 |
1.22e-17 |
|
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: 86.37 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 195 MLIY-TSGTTGPPKGAMISHSNMLYQMWA-GQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVnFAES-----P 267
Cdd:cd05928 177 MAIYfTSGTTGSPKMAEHSHSSLGLGLKVnGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACV-FVHHlprfdP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 268 DTVFDNLREVSPHVFTAVPrlwekiysrvlimrseatpfgrwafdramasgaaklegkggamhAVWDFLVLRNIRQmIGF 347
Cdd:cd05928 256 LVILKTLSSYPITTFCGAP--------------------------------------------TVYRMLVQQDLSS-YKF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 348 DRNRRSNTGAAPISPDLI-RWYGALGVTLLEGYGMTETsGVASVNVIGDN-RIGTIGCALPATELRIA-ENGEICLKG-- 422
Cdd:cd05928 291 PSLQHCVTGGEPLNPEVLeKWKAQTGLDIYEGYGQTET-GLICANFKGMKiKPGSMGKASPPYDVQIIdDNGNVLPPGte 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 423 --------PN----VFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKnITPAEIESRLKFSP 490
Cdd:cd05928 370 gdigirvkPIrpfgLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYR-IGPFEVESALIEHP 448
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1821015446 491 FISDAVVI-------GDRRKYLTVL----IMIDQENVEKYAQDH 523
Cdd:cd05928 449 AVVESAVVsspdpirGEVVKAFVVLapqfLSHDPEQLTKELQQH 492
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
54-499 |
1.58e-17 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 86.00 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 54 RSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLF----------- 122
Cdd:cd05968 100 EVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALItadgftrrgre 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 123 VENDEQLDKYLEvqdRVPTIVKVIVFDPKGlRDFSHPKVMFLSdLYEIGEKAPDAAERfrieinaSQPEDTRMLIYTSGT 202
Cdd:cd05968 180 VNLKEEADKACA---QCPTVEKVVVVRHLG-NDFTPAKGRDLS-YDEEKETAGDGAER-------TESEDPLMIIYTSGT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 203 TGPPKGAMisHSNMLYQMWAGQQV---LRVDPKDEQLCFLPLCHVLErivsvefPIAV-GSTVNFAespdTVFdnLREVS 278
Cdd:cd05968 248 TGKPKGTV--HVHAGFPLKAAQDMyfqFDLKPGDLLTWFTDLGWMMG-------PWLIfGGLILGA----TMV--LYDGA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 279 PHvFTAVPRLWEkiysrvLIMRSEATPFGrwafdrAMASGAAKLEGKGGAMHAVWDFLVLRNIrqmigfdrnrrSNTGaA 358
Cdd:cd05968 313 PD-HPKADRLWR------MVEDHEITHLG------LSPTLIRALKPRGDAPVNAHDLSSLRVL-----------GSTG-E 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 359 PISPDLIRWY----GALGVTLLEGYGMTETSGvasvNVIGDNRIGTI-----GCALPATELRI---------AENGEICL 420
Cdd:cd05968 368 PWNPEPWNWLfetvGKGRNPIINYSGGTEISG----GILGNVLIKPIkpssfNGPVPGMKADVldesgkparPEVGELVL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 421 KGP--NVFKGYWRKPEKTAED----IRDGWLYtGDVGRIGDDGAITITGRVKDIIITAgGKNITPAEIESRLKFSPFISD 494
Cdd:cd05968 444 LAPwpGMTRGFWRDEDRYLETywsrFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVA-GKRVGPAEIESVLNAHPAVLE 521
|
....*
gi 1821015446 495 AVVIG 499
Cdd:cd05968 522 SAAIG 526
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
53-509 |
2.25e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 85.02 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 53 DRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLfvendeqldky 132
Cdd:cd12114 20 ERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV----------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 133 leVQDRVPTIVKVIVFDpkglrdfshpkVMFLSDLYEIGEKAPDAAErfrieinaSQPEDTRMLIYTSGTTGPPKGAMIS 212
Cdd:cd12114 89 --LTDGPDAQLDVAVFD-----------VLILDLDALAAPAPPPPVD--------VAPDDLAYVIFTSGSTGTPKGVMIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 213 HSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLerivSVE--F-PIAVGSTVNFAespdtvfDNLREVSPHvftavprLW 289
Cdd:cd12114 148 HRAALNTILDINRRFAVGPDDRVLALSSLSFDL----SVYdiFgALSAGATLVLP-------DEARRRDPA-------HW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 290 EKiysrvLIMRSEATpfgRW-----AFDRAMASGAAKLEGKGGamhavwdflvLRNIrqMIGFD--------RNRRSNTG 356
Cdd:cd12114 210 AE-----LIERHGVT---LWnsvpaLLEMLLDVLEAAQALLPS----------LRLV--LLSGDwipldlpaRLRALAPD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 357 AAPISpdlirwygaLGvtllegyGMTETSGVASVNVIG--DNRIGTI--GCALPATELRIAEN----------GEICLKG 422
Cdd:cd12114 270 ARLIS---------LG-------GATEASIWSIYHPIDevPPDWRSIpyGRPLANQRYRVLDPrgrdcpdwvpGELWIGG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 423 PNVFKGYWRKPEKTAE---DIRDG--WLYTGDVGRIGDDGAITITGRvKDIIITAGGKNITPAEIESRLKFSPFISDAVV 497
Cdd:cd12114 334 RGVALGYLGDPELTAArfvTHPDGerLYRTGDLGRYRPDGTLEFLGR-RDGQVKVRGYRIELGEIEAALQAHPGVARAVV 412
|
490
....*....|..
gi 1821015446 498 IGDRRKYLTVLI 509
Cdd:cd12114 413 VVLGDPGGKRLA 424
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
13-498 |
3.04e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 86.37 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 13 DGADTVVKLWAAKCAERGDATAHRekdFGiWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISA 92
Cdd:PRK12467 1571 PLARLVHQLIEDQAAATPEAVALV---FG-EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILK 1646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 93 AGG--IPSGV-YTTDsagQLEYLINDSGSAFLFVENdeqldkylEVQDRVPTivkvivfdPKGLRdfshpkVMFLSDLYE 169
Cdd:PRK12467 1647 AGGayVPLDPeYPRE---RLAYMIEDSGIELLLTQS--------HLQARLPL--------PDGLR------SLVLDQEDD 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 170 IGEKAPDAAErfrieINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHvlerIV 249
Cdd:PRK12467 1702 WLEGYSDSNP-----AVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAF----DV 1772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 250 SVE---FPIAVGSTVNFAE-----SPDTVFDNLRE--VSPHVFT---------AVPRLWEKIYSRVLIMRSEATPFGrwA 310
Cdd:PRK12467 1773 SVWelfWPLINGARLVIAPpgahrDPEQLIQLIERqqVTTLHFVpsmlqqllqMDEQVEHPLSLRRVVCGGEALEVE--A 1850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 311 FDRAMAS-GAAKLEGKGGAMHAVWDfLVLRNIRQmiGFDRNRRSNTGAAPIsPDLiRWYgalgvtLLEgygmtetsgvAS 389
Cdd:PRK12467 1851 LRPWLERlPDTGLFNLYGPTETAVD-VTHWTCRR--KDLEGRDSVPIGQPI-ANL-STY------ILD----------AS 1909
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 390 VNVIgdnrigTIGCAlpatelriaenGEICLKGPNVFKGYWRKPEKTAE-------DIRDGWLY-TGDVGRIGDDGAITI 461
Cdd:PRK12467 1910 LNPV------PIGVA-----------GELYLGGVGLARGYLNRPALTAErfvadpfGTVGSRLYrTGDLARYRADGVIEY 1972
|
490 500 510
....*....|....*....|....*....|....*..
gi 1821015446 462 TGRVkDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK12467 1973 LGRI-DHQVKIRGFRIELGEIEARLREQGGVREAVVI 2008
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
21-498 |
1.24e-16 |
|
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: 83.02 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 21 LWAAKCAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGV 100
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGD----RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 101 YTTDSAGQLEYLINDSGsaflfvendeqldkylevqdrvptiVKVIVFDPK--GLRDFSHPKVMFLSDLYEIGEKAPDAA 178
Cdd:cd12117 78 DPELPAERLAFMLADAG-------------------------AKVLLTDRSlaGRAGGLEVAVVIDEALDAGPAGNPAVP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 179 erfrieinaSQPEDTRMLIYTSGTTGPPKGAMISHSNmlyqmwagqqVLRVdpkdeqlcflplchVLERivsvefpiavg 258
Cdd:cd12117 133 ---------VSPDDLAYVMYTSGSTGRPKGVAVTHRG----------VVRL--------------VKNT----------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 259 stvNFAE-SPDTVFdnLReVSPHVFTAVP-RLWEKIYS--RVLIMRSEAtpfgrwaFDRAMASGAAKLEGKGGAMH---A 331
Cdd:cd12117 169 ---NYVTlGPDDRV--LQ-TSPLAFDASTfEIWGALLNgaRLVLAPKGT-------LLDPDALGALIAEEGVTVLWltaA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 332 VWDFLV------LRNIRQMIgfdrnrrsnTGAAPISPDLIR-WYGAL-GVTLLEGYGMTETSGVASVNVI--GDNRIGT- 400
Cdd:cd12117 236 LFNQLAdedpecFAGLRELL---------TGGEVVSPPHVRrVLAACpGLRLVNGYGPTENTTFTTSHVVteLDEVAGSi 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 401 -IGCALPATE-------LRIAENG---EICLKGPNVFKGYWRKPEKTAED-IRDGW-----LY-TGDVGRIGDDGAITIT 462
Cdd:cd12117 307 pIGRPIANTRvyvldedGRPVPPGvpgELYVGGDGLALGYLNRPALTAERfVADPFgpgerLYrTGDLARWLPDGRLEFL 386
|
490 500 510
....*....|....*....|....*....|....*..
gi 1821015446 463 GRVKD-IIITagGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:cd12117 387 GRIDDqVKIR--GFRIELGEIEAALRAHPGVREAVVV 421
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
187-536 |
1.58e-16 |
|
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: 82.59 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 187 ASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLC---HVLERIvsveFPIAVGSTVnF 263
Cdd:cd05918 102 TSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTfdvSILEIF----TTLAAGGCL-C 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 264 AESPDTVFDNLREVsphvftavprlwekiysrvlIMRSEATpfgrWAFdraMASGAAKLEGKGgamhavwdflVLRNIRQ 343
Cdd:cd05918 177 IPSEEDRLNDLAGF--------------------INRLRVT----WAF---LTPSVARLLDPE----------DVPSLRT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 344 MIgfdrnrrsnTGAAPISPDLI-RWygALGVTLLEGYGMTETSGVASVNVIGDN-RIGTIGCALPAT----------ELR 411
Cdd:cd05918 220 LV---------LGGEALTQSDVdTW--ADRVRLINAYGPAECTIAATVSPVVPStDPRNIGRPLGATcwvvdpdnhdRLV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 412 -IAENGEICLKGPNVFKGYWRKPEKTAE-DIRD-GW-----------LY-TGDVGRIGDDGAITITGRvKDIIITAGGKN 476
Cdd:cd05918 289 pIGAVGELLIEGPILARGYLNDPEKTAAaFIEDpAWlkqegsgrgrrLYrTGDLVRYNPDGSLEYVGR-KDTQVKIRGQR 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821015446 477 ITPAEIESRLK-FSPFISDAVVI------GDRRKYLTVLIMIDQENVEKYAQDHQI--PFSDFASLTRA 536
Cdd:cd05918 368 VELGEIEHHLRqSLPGAKEVVVEvvkpkdGSSSPQLVAFVVLDGSSSGSGDGDSLFlePSDEFRALVAE 436
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
189-498 |
2.23e-16 |
|
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: 81.74 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 189 QPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDeqlcflplcHVLERIVSVEFPIAVGstvNFAESpd 268
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP---------VRLLQMASFSFDVFAG---DFARS-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 269 TVFDNLREVSPHVFTAVPRLWEKIYSRVLIMRSEATPfgrwAFDRAMasgaaklegkggaMHAV-WDFLVLRNIRQMI-G 346
Cdd:cd17650 157 LLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTP----ALIRPV-------------MAYVyRNGLDLSAMRLLIvG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 347 fdrnrrSNTGAAPISPDLIRWYGAlGVTLLEGYGMTETSGVASVNVIGDNRIGT-----IGCALPATELRIAEN------ 415
Cdd:cd17650 220 ------SDGCKAQDFKTLAARFGQ-GMRIINSYGVTEATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLDErlqpqp 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 ----GEICLKGPNVFKGYWRKPEKTAEDIRD------GWLY-TGDVGRIGDDGAITITGRVkDIIITAGGKNITPAEIES 484
Cdd:cd17650 293 vgvaGELYIGGAGVARGYLNRPELTAERFVEnpfapgERMYrTGDLARWRADGNVELLGRV-DHQVKIRGFRIELGEIES 371
|
330
....*....|....
gi 1821015446 485 RLKFSPFISDAVVI 498
Cdd:cd17650 372 QLARHPAIDEAVVA 385
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
188-502 |
3.45e-16 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 81.15 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 188 SQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFlplchvleriVSVEFPIAV---------G 258
Cdd:cd17652 90 TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQF----------ASPSFDASVwellmallaG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 259 STVNFAESPDTVF-DNLREVsphvftavprLWEKIYSRVLImrseaTPfgrwafdramaSGAAKLEGKggamhavwDFLV 337
Cdd:cd17652 160 ATLVLAPAEELLPgEPLADL----------LREHRITHVTL-----PP-----------AALAALPPD--------DLPD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 338 LRNIrqMIGfdrnrrsntGAAPiSPDLI-RWygALGVTLLEGYGMTETSGVASV-NVIGDNRIGTIGCALPATELRIAEN 415
Cdd:cd17652 206 LRTL--VVA---------GEAC-PAELVdRW--APGRRMINAYGPTETTVCATMaGPLPGGGVPPIGRPVPGTRVYVLDA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 ----------GEICLKGPNVFKGYWRKPEKTAED-IRD------GWLY-TGDVGRIGDDGAITITGRVKDIIITAGGKnI 477
Cdd:cd17652 272 rlrpvppgvpGELYIAGAGLARGYLNRPGLTAERfVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKIRGFR-I 350
|
330 340 350
....*....|....*....|....*....|.
gi 1821015446 478 TPAEIESRLKFSPFISDAVVI------GDRR 502
Cdd:cd17652 351 ELGEVEAALTEHPGVAEAVVVvrddrpGDKR 381
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
357-499 |
5.42e-16 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 80.88 E-value: 5.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 357 AAPISPDL----IRWYGALgvtLLEGYGMTETSGVASVNviGDNRI---GTIGCALpATELRI----------AENGEIC 419
Cdd:cd05929 253 AAPCPPWVkeqwIDWGGPI---IWEYYGGTEGQGLTIIN--GEEWLthpGSVGRAV-LGKVHIldedgnevppGEIGEVY 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 420 LKGPNVFKgYWRKPEKTAEDI-RDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:cd05929 327 FANGPGFE-YTNDPEKTAAARnEGGWSTLGDVGYLDEDGYLYLTDRRSDMIIS-GGVNIYPQEIENALIAHPKVLDAAVV 404
|
.
gi 1821015446 499 G 499
Cdd:cd05929 405 G 405
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
187-474 |
6.70e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 80.71 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 187 ASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLcHVLerivsveFPIAVG-------- 258
Cdd:PRK09274 170 DLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL-FAL-------FGPALGmtsvipdm 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 259 -----STVNfaesPDTVFDNLR--EVSpHVFTAvPRLWEKIysrvlimrseatpfGRWAfdramasgaaklEGKGgamha 331
Cdd:PRK09274 242 dptrpATVD----PAKLFAAIEryGVT-NLFGS-PALLERL--------------GRYG------------EANG----- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 332 vwdfLVLRNIRQMIGfdrnrrsntGAAPISPDLIRWYGAL---GVTLLEGYGMTET---SGVASVNVIGDNRIGT----- 400
Cdd:PRK09274 285 ----IKLPSLRRVIS---------AGAPVPIAVIERFRAMlppDAEILTPYGATEAlpiSSIESREILFATRAATdngag 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 401 --IGCALPATELRI-------------------AENGEICLKGPNVFKGYWRKPEKTAED-IRDG----WLYTGDVGRIG 454
Cdd:PRK09274 352 icVGRPVDGVEVRIiaisdapipewddalrlatGEIGEIVVAGPMVTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLD 431
|
330 340
....*....|....*....|
gi 1821015446 455 DDGAITITGRVKDIIITAGG 474
Cdd:PRK09274 432 AQGRLWFCGRKAHRVETAGG 451
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
183-502 |
1.79e-15 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 79.02 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 183 IEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHvlerIVSVE--FP-IAVGS 259
Cdd:cd17644 98 ISVLLTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAF----DVAAEeiYVtLLSGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 260 TVNFaeSPDTVFDnlrevSPHVFTAVPRLWEkiysrvlIMRSEATPfgrwafdramasgaaklegkggamhAVWDFLVLR 339
Cdd:cd17644 174 TLVL--RPEEMRS-----SLEDFVQYIQQWQ-------LTVLSLPP-------------------------AYWHLLVLE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 340 NIRQMIGFDRNRRS-NTGAAPISPDLIR-WYGALG--VTLLEGYGMTETSGVASVNVIGDNRIG-----TIGCALPATEL 410
Cdd:cd17644 215 LLLSTIDLPSSLRLvIVGGEAVQPELVRqWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERnitsvPIGRPIANTQV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 411 RIAEN----------GEICLKGPNVFKGYWRKPEKTAED-IRDGW-------LY-TGDVGRIGDDGAITITGRVkDIIIT 471
Cdd:cd17644 295 YILDEnlqpvpvgvpGELHIGGVGLARGYLNRPELTAEKfISHPFnsseserLYkTGDLARYLPDGNIEYLGRI-DNQVK 373
|
330 340 350
....*....|....*....|....*....|....*..
gi 1821015446 472 AGGKNITPAEIESRLKFSPFISDAVVI------GDRR 502
Cdd:cd17644 374 IRGFRIELGEIEAVLSQHNDVKTAVVIvredqpGNKR 410
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
356-499 |
2.22e-15 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 78.88 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 356 GAAPISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGTIGC--ALPATELRIAEN--GEICLKGPNVFKGYWr 431
Cdd:PRK07445 238 GGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATLKPDDFLAGNNSSgqVLPHAQITIPANqtGNITIQAQSLALGYY- 316
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821015446 432 kPEKTAEDirdGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK07445 317 -PQILDSQ---GIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAILATGLVQDVCVLG 379
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
332-498 |
3.50e-15 |
|
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: 77.99 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 332 VWDFLVLRNirqMIGFDRNRRSNTGAA-PISPDLI-RWYGALGVTLLEGYGMTETSGVASvNVIGDN-RIGTIGCALPAT 408
Cdd:cd05974 186 VWRMLIQQD---LASFDVKLREVVGAGePLNPEVIeQVRRAWGLTIRDGYGQTETTALVG-NSPGQPvKAGSMGRPLPGY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 409 ELRI-------AENGEICL-----KGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAGGKn 476
Cdd:cd05974 262 RVALldpdgapATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR- 340
|
170 180
....*....|....*....|..
gi 1821015446 477 ITPAEIESRLKFSPFISDAVVI 498
Cdd:cd05974 341 ISPFELESVLIEHPAVAEAAVV 362
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
53-499 |
3.52e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 78.41 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 53 DRSQAIGMGLIELGLTRGTPVSILSEDNKEwlYCDLAISAaggIPSGVYTTD-----SAGQLEYLINDSGSAFLFVENDe 127
Cdd:PRK08276 19 ARSNRLAHGLRALGLREGDVVAILLENNPE--FFEVYWAA---RRSGLYYTPinwhlTAAEIAYIVDDSGAKVLIVSAA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 128 QLDKYLEVQDRVP---TIVKVIVFDPKGLRDFshpkvmflsdlyeigEKAPDAAERFRIeinASQPEDTRMLiYTSGTTG 204
Cdd:PRK08276 93 LADTAAELAAELPagvPLLLVVAGPVPGFRSY---------------EEALAAQPDTPI---ADETAGADML-YSSGTTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 205 PPKGamishsnmlyqmwagqqVLR----VDPKDEQLCFLplchvleRIVsVEFPIAVGSTVNFAESPdtvfdnLREVSPH 280
Cdd:PRK08276 154 RPKG-----------------IKRplpgLDPDEAPGMML-------ALL-GFGMYGGPDSVYLSPAP------LYHTAPL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 281 VFT-AVPRLWEkiysRVLIMrseatpfgrwafDRAMASGAAKLEGKGGAMHAVW------DFLVL-RNIRQmiGFDRN-- 350
Cdd:PRK08276 203 RFGmSALALGG----TVVVM------------EKFDAEEALALIERYRVTHSQLvptmfvRMLKLpEEVRA--RYDVSsl 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 351 RRSNTGAAPISPD----LIRWYGALgvtLLEGYGMTETSGVASVN--------------VIGDNRI-GTIGCALPATELr 411
Cdd:PRK08276 265 RVAIHAAAPCPVEvkraMIDWWGPI---IHEYYASSEGGGVTVITsedwlahpgsvgkaVLGEVRIlDEDGNELPPGEI- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 412 iaenGEICLKGPNVFKGYWRKPEKTAE-DIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSP 490
Cdd:PRK08276 341 ----GTVYFEMDGYPFEYHNDPEKTAAaRNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIIS-GGVNIYPQEIENLLVTHP 415
|
....*....
gi 1821015446 491 FISDAVVIG 499
Cdd:PRK08276 416 KVADVAVFG 424
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
46-498 |
3.54e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 78.73 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEdNKEWLY-CDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVE 124
Cdd:PLN02479 46 YTWAQTYQRCRRLASALAKRSIGPGSTVAVIAP-NIPAMYeAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 125 ND-----EQLDKYLEVQDR---VPTIVKVI---VFDPKGLRDFSHPKVMFLSDLYEIGEKapdaaerfriEINASQPEDT 193
Cdd:PLN02479 125 QEfftlaEEALKILAEKKKssfKPPLLIVIgdpTCDPKSLQYALGKGAIEYEKFLETGDP----------EFAWKPPADE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 194 RMLI---YTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNfaespdtv 270
Cdd:PLN02479 195 WQSIalgYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGTNIC-------- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 271 fdnLREVSPhvftavprlwEKIYSRVlimrseatpfgrwafdramasgaakleGKGGAMHAVWDFLVLRNI------RQM 344
Cdd:PLN02479 267 ---LRQVTA----------KAIYSAI---------------------------ANYGVTHFCAAPVVLNTIvnapksETI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 345 IGFDRNRRSNT-GAAPiSPDLIRWYGALGVTLLEGYGMTETSGVASV------------------------NVIGDNRIG 399
Cdd:PLN02479 307 LPLPRVVHVMTaGAAP-PPSVLFAMSEKGFRVTHTYGLSETYGPSTVcawkpewdslppeeqarlnarqgvRYIGLEGLD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 400 TI----GCALPATELRIaenGEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGK 475
Cdd:PLN02479 386 VVdtktMKPVPADGKTM---GEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIIS-GGE 461
|
490 500
....*....|....*....|...
gi 1821015446 476 NITPAEIESRLKFSPFISDAVVI 498
Cdd:PLN02479 462 NISSLEVENVVYTHPAVLEASVV 484
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
17-484 |
3.61e-15 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 78.63 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 17 TVVKLWAAKCAERGDATAHREKDF-----GIWQAYSWSDWYDRSQAIGMGLIELGlTRGTPVSILSEDNKEWLYCDLAIS 91
Cdd:PRK12476 35 TLISLIERNIANVGDTVAYRYLDHshsaaGCAVELTWTQLGVRLRAVGARLQQVA-GPGDRVAILAPQGIDYVAGFFAAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 92 AAGGIPSGVYTTDSAGqleylindsgsaflfveNDEQLDKYLEvqDRVPTIVKVIVFDPKGLRDF-------SHPKVMFL 164
Cdd:PRK12476 114 KAGTIAVPLFAPELPG-----------------HAERLDTALR--DAEPTVVLTTTAAAEAVEGFlrnlprlRRPRVIAI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 165 SDLyeigekaPD-AAERF-RIEInasQPEDTRMLIYTSGTTGPPKGAMISHSNM---LYQMwagqqVLRVDPKDEQ---L 236
Cdd:PRK12476 175 DAI-------PDsAGESFvPVEL---DTDDVSHLQYTSGSTRPPVGVEITHRAVgtnLVQM-----ILSIDLLDRNthgV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 237 CFLPLCHVLERIVsVEFPIAVG--STVnfaespdtvfdnlreVSPHVFTAVPRLWEKIYSrvlimrsEATPFGR------ 308
Cdd:PRK12476 240 SWLPLYHDMGLSM-IGFPAVYGghSTL---------------MSPTAFVRRPQRWIKALS-------EGSRTGRvvtaap 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 309 -WAFDRAMASGaakLEGKGgamhavwDFLVLRNIRQMIGfdrnrrsntgAAPISPDLIRW-------YGALGVTLLEGYG 380
Cdd:PRK12476 297 nFAYEWAAQRG---LPAEG-------DDIDLSNVVLIIG----------SEPVSIDAVTTfnkafapYGLPRTAFKPSYG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 381 MTE-TSGVAS----------------------VNVIGD--NRIGTIGCALPA-------------TELRIAENGEICLKG 422
Cdd:PRK12476 357 IAEaTLFVATiapdaepsvvyldreqlgagraVRVAADapNAVAHVSCGQVArsqwavivdpdtgAELPDGEVGEIWLHG 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 423 PNVFKGYWRKPEKTAE-------------------DIRDGWLYTGDVGrIGDDGAITITGRVKDIIITaGGKNITPAEIE 483
Cdd:PRK12476 437 DNIGRGYWGRPEETERtfgaklqsrlaegshadgaADDGTWLRTGDLG-VYLDGELYITGRIADLIVI-DGRNHYPQDIE 514
|
.
gi 1821015446 484 S 484
Cdd:PRK12476 515 A 515
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
22-499 |
8.18e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 77.61 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 22 WAAKcaeRGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVY 101
Cdd:PRK08279 46 AAAR---HPDRPALLFED----QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 102 TTDSAGQLEYLINDSGSAFLFVEnDEQLDKYLEVQDRVPTIVKVIVFDPKGLRDfshpkVMFLSDLYEIGEKAPDAAERF 181
Cdd:PRK08279 119 TQQRGAVLAHSLNLVDAKHLIVG-EELVEAFEEARADLARPPRLWVAGGDTLDD-----PEGYEDLAAAAAGAPTTNPAS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 182 RieiNASQPEDTRMLIYTSGTTGPPKGAMISHsnMLYQMWAGQ--QVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGS 259
Cdd:PRK08279 193 R---SGVTAKDTAFYIYTSGTTGLPKAAVMSH--MRWLKAMGGfgGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 260 TVNFAESpdtvfdnlrevsphvFTAvPRLWEKiysrvlIMRSEATPFG------RWafdrAMASGAAKLEGKggamHAVw 333
Cdd:PRK08279 268 TLALRRK---------------FSA-SRFWDD------VRRYRATAFQyigelcRY----LLNQPPKPTDRD----HRL- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 334 dflvlrniRQMIGfdrnrrsnTGAAP-ISPDLIRWYGALGVtlLEGYGMTEtSGVASVNVigDNRIGTIG-CALP-ATEL 410
Cdd:PRK08279 317 --------RLMIG--------NGLRPdIWDEFQQRFGIPRI--LEFYAASE-GNVGFINV--FNFDGTVGrVPLWlAHPY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 411 RI--------------------AENGEICL-------KGPnvFKGYwRKPEKTAEDI-RDG------WLYTGD------- 449
Cdd:PRK08279 376 AIvkydvdtgepvrdadgrcikVKPGEVGLligritdRGP--FDGY-TDPEASEKKIlRDVfkkgdaWFNTGDlmrddgf 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1821015446 450 -----VGRIGDdgaitiTGRVKdiiitagGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK08279 453 ghaqfVDRLGD------TFRWK-------GENVATTEVENALSGFPGVEEAVVYG 494
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
53-499 |
1.37e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 76.50 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 53 DRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYcdlAISAAGGIPSGVY--TTDSAG-QLEYLINDSGSAFLFVenDEQL 129
Cdd:PRK07788 82 EQSNALARGLLALGVRAGDGVAVLARNHRGFVL---ALYAAGKVGARIIllNTGFSGpQLAEVAAREGVKALVY--DDEF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 130 DKYLE-VQDRVPTIvKVIVFDPKGLRDfSHPKVMFLSDLYEIGEKAPDAAerfrieinASQPedTRMLIYTSGTTGPPKG 208
Cdd:PRK07788 157 TDLLSaLPPDLGRL-RAWGGNPDDDEP-SGSTDETLDDLIAGSSTAPLPK--------PPKP--GGIVILTSGTTGTPKG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 209 AMISHSNMLYQMwaGQQVLRVDPKDEQLCFL--PLCH---VLERIVSvefpIAVGSTVNFAE--SPDTVFDNLREVSPHV 281
Cdd:PRK07788 225 APRPEPSPLAPL--AGLLSRVPFRAGETTLLpaPMFHatgWAHLTLA----MALGSTVVLRRrfDPEATLEDIAKHKATA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 282 FTAVPrlwekiysrvlIMRSEatpfgrwafdraMASGAAKLEGKggamhavWDFLVLRNIrqmigFdrnrrsnTGAAPIS 361
Cdd:PRK07788 299 LVVVP-----------VMLSR------------ILDLGPEVLAK-------YDTSSLKII-----F-------VSGSALS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 362 PDLI-RWYGALGVTLLEGYGMTETSgVASVNVIGDNRI--GTIGCALPATELRI----------AENGEICLKGPNVFKG 428
Cdd:PRK07788 337 PELAtRALEAFGPVLYNLYGSTEVA-FATIATPEDLAEapGTVGRPPKGVTVKIldengnevprGVVGRIFVGNGFPFEG 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821015446 429 YWRKPEKtaeDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK07788 416 YTDGRDK---QIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVS-GGENVFPAEVEDLLAGHPDVVEAAVIG 482
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
47-507 |
1.48e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 76.71 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 47 SWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFVenD 126
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT--D 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 127 EQLDKYLE-VQDRVPTIVKVIVFDpkglrDFSH-PKVMFLSDL-YEIGEKAPDAAERFrieinASQPEDTRM-LIYTSGT 202
Cdd:PRK06018 119 LTFVPILEkIADKLPSVERYVVLT-----DAAHmPQTTLKNAVaYEEWIAEADGDFAW-----KTFDENTAAgMCYTSGT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 203 TGPPKGAMISH-SNMLYQMWAGQ-QVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESPD--TVFDNLREVS 278
Cdd:PRK06018 189 TGDPKGVLYSHrSNVLHALMANNgDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPGAKLDgaSVYELLDTEK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 279 PHVFTAVPRLWEkiysrVLIMRSEATPFGRWAFDRAMASGAAKLEGkggamhavwdflvlrnirqmigfdrnrrsntgaa 358
Cdd:PRK06018 269 VTFTAGVPTVWL-----MLLQYMEKEGLKLPHLKMVVCGGSAMPRS---------------------------------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 359 pispdLIRWYGALGVTLLEGYGMTETSGVASVNVI--------GDNRIG---TIGCALPATELRIAEN------------ 415
Cdd:PRK06018 310 -----MIKAFEDMGVEVRHAWGMTEMSPLGTLAALkppfsklpGDARLDvlqKQGYPPFGVEMKITDDagkelpwdgktf 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 GEICLKGPNVFKGYWRKPEKTAEDirDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRLKFSPFISDA 495
Cdd:PRK06018 385 GRLKVRGPAVAAAYYRVDGEILDD--DGFFDTGDVATIDAYGYMRITDRSKD-VIKSGGEWISSIDLENLAVGHPKVAEA 461
|
490
....*....|....*...
gi 1821015446 496 VVIG------DRRKYLTV 507
Cdd:PRK06018 462 AVIGvyhpkwDERPLLIV 479
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
176-484 |
8.80e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 74.21 E-value: 8.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 176 DAAERFRIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMwagQQVLR--------VDPKDEQLC-FLPLCHVLE 246
Cdd:PRK05850 145 DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANF---EQLMSdyfgdtggVPPPDTTVVsWLPFYHDMG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 247 RIVSVEFPIAVG------STVNFAESPDTVFDNLREvSPHVFTAVPRlwekiysrvlimrseatpfgrWAFDRAMA-SGA 319
Cdd:PRK05850 222 LVLGVCAPILGGcpavltSPVAFLQRPARWMQLLAS-NPHAFSAAPN---------------------FAFELAVRkTSD 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 320 AKLEGkggamhavwdfLVLRNIRQMI-GFDRN-----RRSNTGAAP--ISPDLIR-WYGALGVTLlegYGMTETSGVASV 390
Cdd:PRK05850 280 DDMAG-----------LDLGGVLGIIsGSERVhpatlKRFADRFAPfnLRETAIRpSYGLAEATV---YVATREPGQPPE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 391 NVIGD-------------NRIGT--IGCALP-ATELRI------AEN-----GEICLKGPNVFKGYWRKPEKTAE----D 439
Cdd:PRK05850 346 SVRFDyeklsaghakrceTGGGTplVSYGSPrSPTVRIvdpdtcIECpagtvGEIWVHGDNVAAGYWQKPEETERtfgaT 425
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1821015446 440 IRDG--------WLYTGDVGRIgDDGAITITGRVKDIIITAgGKNITPAEIES 484
Cdd:PRK05850 426 LVDPspgtpegpWLRTGDLGFI-SEGELFIVGRIKDLLIVD-GRNHYPDDIEA 476
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
18-498 |
1.14e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.81 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 18 VVKLWAAKCAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGG-- 95
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPALVFGD----QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGay 3172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 96 IPSGV-YTTDsagQLEYLINDSGSAFLFVEND--EQLDkylevqdrVPTIVKVIVFDpkglrdfshpkvmfLSDLYEIGE 172
Cdd:PRK12467 3173 VPLDPeYPRE---RLAYMIEDSGVKLLLTQAHllEQLP--------APAGDTALTLD--------------RLDLNGYSE 3227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 173 KAPDaaerfrieiNASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHvlerIVSVE 252
Cdd:PRK12467 3228 NNPS---------TRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSF----DGAQE 3294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 253 ---FPIAVGSTVnfaespdTVFDNlrevspHVFTAvPRLWEKI-YSRVLIMrseatpfgrwAFDRAMASGAAKlEGKGGA 328
Cdd:PRK12467 3295 rflWTLICGGCL-------VVRDN------DLWDP-EELWQAIhAHRISIA----------CFPPAYLQQFAE-DAGGAD 3349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 329 MHAVwdflvlrnirqmigfdrnRRSNTGAAPISPDLIRWYGAL--GVTLLEGYGMTETSGVASV-NVIGDNRIGT----I 401
Cdd:PRK12467 3350 CASL------------------DIYVFGGEAVPPAAFEQVKRKlkPRGLTNGYGPTEAVVTVTLwKCGGDAVCEApyapI 3411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 402 GCALPATELRIAEN----------GEICLKGPNVFKGYWRKPEKTAE-------DIRDGWLY-TGDVGRIGDDGAITITG 463
Cdd:PRK12467 3412 GRPVAGRSIYVLDGqlnpvpvgvaGELYIGGVGLARGYHQRPSLTAErfvadpfSGSGGRLYrTGDLARYRADGVIEYLG 3491
|
490 500 510
....*....|....*....|....*....|....*
gi 1821015446 464 RVkDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK12467 3492 RI-DHQVKIRGFRIELGEIEARLLQHPSVREAVVL 3525
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
23-586 |
1.22e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 23 AAKCAERGDATAHREKDfgiwqayswsdwyDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLycdLAISAAggIPSGVYT 102
Cdd:PRK13390 15 AVIVAETGEQVSYRQLD-------------DDSAALARVLYDAGLRTGDVVALLSDNSPEAL---VVLWAA--LRSGLYI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 103 TD-----SAGQLEYLINDSGSAFLFVEndEQLDKyLEVQDRVPTIVKvIVFDPK--GLRDFShpkvmflSDLYEIGekaP 175
Cdd:PRK13390 77 TAinhhlTAPEADYIVGDSGARVLVAS--AALDG-LAAKVGADLPLR-LSFGGEidGFGSFE-------AALAGAG---P 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 176 DAAErfrieinasQPEDTRMLiYTSGTTGPPKG---------------AMISHSNMLYQmwagqqvlrVDPKDEQLCFLP 240
Cdd:PRK13390 143 RLTE---------QPCGAVML-YSSGTTGFPKGiqpdlpgrdvdapgdPIVAIARAFYD---------ISESDIYYSSAP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 241 LCHVLE-RIVSVEFpiAVGSTVNFAESPDTVfDNLREVSPHVFTAVpRLWEKIYSRVLIMRSEAtpfgRWAFDramasga 319
Cdd:PRK13390 204 IYHAAPlRWCSMVH--ALGGTVVLAKRFDAQ-ATLGHVERYRITVT-QMVPTMFVRLLKLDADV----RTRYD------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 320 akLEGKGGAMHAvwdflvlrnirqmigfdrnrrsntgAAPISPD----LIRWygaLGVTLLEGYGMTETSGVASVNV--- 392
Cdd:PRK13390 269 --VSSLRAVIHA-------------------------AAPCPVDvkhaMIDW---LGPIVYEYYSSTEAHGMTFIDSpdw 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 393 ------IGDNRIGTIG-CALPATELRIAENGEICLKGPNVFKGYWRKPEKTAEDIRDG---WLYTGDVGRIGDDGAITIT 462
Cdd:PRK13390 319 lahpgsVGRSVLGDLHiCDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLA 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 463 GRvKDIIITAGGKNITPAEIESRLKFSPFISDAVVIGdrrkyltvlimidqenvekyaqdhqIPFSDFASLTRApqVVDL 542
Cdd:PRK13390 399 DR-KSFMIISGGVNIYPQETENALTMHPAVHDVAVIG-------------------------VPDPEMGEQVKA--VIQL 450
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1821015446 543 IDGV------VRE-VNTHFAQVEQIKYFRLIDILltaedDEL--TPTMKLKRG 586
Cdd:PRK13390 451 VEGIrgsdelARElIDYTRSRIAHYKAPRSVEFV-----DELprTPTGKLVKG 498
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
356-483 |
1.18e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.42 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 356 GAAPISPDlIRWYGALGVTLLEGYGMTETsGVASVNVIGDN----RI--GTIGCALPATELRIAEN-------------- 415
Cdd:PRK05857 295 GSRAIAAD-VRFIEATGVRTAQVYGLSET-GCTALCLPTDDgsivKIeaGAVGRPYPGVDVYLAATdgigptapgagpsa 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 --GEICLKGPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIE 483
Cdd:PRK05857 373 sfGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPDEVD 441
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
196-507 |
1.25e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 70.51 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 196 LIYTSGTTGPPKGAMISH-SNMLYQMWAG-QQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIaVGSTVNFAeSPD----T 269
Cdd:PRK07008 181 LCYTSGTTGNPKGALYSHrSTVLHAYGAAlPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLP-GPDldgkS 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 270 VFDnLREVSPHVFTA-VPRLWEKIYSRvliMRSEATPFGrwAFDRAMASGAAklegkggamhavwdflvlrnirqmigfd 348
Cdd:PRK07008 259 LYE-LIEAERVTFSAgVPTVWLGLLNH---MREAGLRFS--TLRRTVIGGSA---------------------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 349 rnrrsntgaAPisPDLIRWYG-ALGVTLLEGYGMTETSGVASVNVI--------GDNRIGTI---GCALPATELRIAEN- 415
Cdd:PRK07008 305 ---------CP--PAMIRTFEdEYGVEVIHAWGMTEMSPLGTLCKLkwkhsqlpLDEQRKLLekqGRVIYGVDMKIVGDd 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 -----------GEICLKGPNVFKGYWRKpekTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIES 484
Cdd:PRK07008 374 grelpwdgkafGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDVATIDADGFMQITDRSKD-VIKSGGEWISSIDIEN 449
|
330 340
....*....|....*....|....*....
gi 1821015446 485 RLKFSPFISDAVVIG------DRRKYLTV 507
Cdd:PRK07008 450 VAVAHPAVAEAACIAcahpkwDERPLLVV 478
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
373-518 |
1.40e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 70.19 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 373 VTLLEGYGMTETSGVASV---------NVIGD--NRIGTIGCALPATELRIAENGEICLKGPNVFKGYWRKPEKTAEDIR 441
Cdd:PRK07638 280 AKLYEFYGASELSFVTALvdeeserrpNSVGRpfHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 442 DGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIGDRRKY---LTVLIMIDQENVEK 518
Cdd:PRK07638 360 DGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIESVLHEHPAVDEIVVIGVPDSYwgeKPVAIIKGSATKQQ 438
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
15-499 |
1.85e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 70.06 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 15 ADTVVKLWAAKCAERGDATAHREKDfgiwqaYSWSDWYDRSQAIGMGLIELGLTRGTP-VSILSEDNKEWLYCDLAISAA 93
Cdd:PRK13388 2 RDTIAQLLRDRAGDDTIAVRYGDRT------WTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 94 GGIPSGVYTTDSAGQLEYLIndsgsaflfvendeqldKYLEVQdrvptivkVIVFDPKG---LRDFSHPKVMFL-SDLYE 169
Cdd:PRK13388 76 GYVLVGLNTTRRGAALAADI-----------------RRADCQ--------LLVTDAEHrplLDGLDLPGVRVLdVDTPA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 170 IGEKAPDAAERfrIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLyqMWAGQQVLRVDPKDEQLCFL--PLCHVlER 247
Cdd:PRK13388 131 YAELVAAAGAL--TPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLA--FAGRALTERFGLTRDDVCYVsmPLFHS-NA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 248 IVSVEFP-IAVGSTVnfaespdtvfdnlreVSPHVFTAvprlwekiySRVL--IMRSEATPF---GRwafdrAMASGAAK 321
Cdd:PRK13388 206 VMAGWAPaVASGAAV---------------ALPAKFSA---------SGFLddVRRYGATYFnyvGK-----PLAYILAT 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 322 LEGKGGAMHAvwdflvLRnirqmIGFdrnrrsNTGAAPisPDLIRWYGALGVTLLEGYGMTEtsGVASVNVIGDNRIGTI 401
Cdd:PRK13388 257 PERPDDADNP------LR-----VAF------GNEASP--RDIAEFSRRFGCQVEDGYGSSE--GAVIVVREPGTPPGSI 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 402 GCALPA---------TELRIAE--------N-----GEICLK-GPNVFKGYWRKPEKTAEDIRDGWLYTGDVGRIGDDGA 458
Cdd:PRK13388 316 GRGAPGvaiynpetlTECAVARfdahgallNadeaiGELVNTaGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGW 395
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1821015446 459 ITITGRVKDiIITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK13388 396 IYFAGRTAD-WMRVDGENLSAAPIERILLRHPAINRVAVYA 435
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
191-499 |
2.05e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 68.95 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 191 EDTRMLIYTSGTTGPPKGAMISHSNmLYQMWAG------------QQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAV- 257
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQED-IFRMLMGgadfgtgeftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 258 -GSTVNFaesPDTVFDN---LREVSPHVFTAVPRLWEkIYSRVLImrsEATPFGRwAFD----RAMASGAAKLEgkggam 329
Cdd:cd05924 82 gGQTVVL---PDDRFDPeevWRTIEKHKVTSMTIVGD-AMARPLI---DALRDAG-PYDlsslFAISSGGALLS------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 330 havwdflvlRNIRQmigfdrnrrsntGAAPISPDLirwygalgvTLLEGYGMTETSGVAS-VNVIGDNRIGTIGCALPAT 408
Cdd:cd05924 148 ---------PEVKQ------------GLLELVPNI---------TLVDAFGSSETGFTGSgHSAGSGPETGPFTRANPDT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 409 EL----------------RIAENGEICLkgpnvfkGYWRKPEKTAEDIR--DG--WLYTGDVGRIGDDGAITITGRvKDI 468
Cdd:cd05924 198 VVldddgrvvppgsggvgWIARRGHIPL-------GYYGDEAKTAETFPevDGvrYAVPGDRATVEADGTVTLLGR-GSV 269
|
330 340 350
....*....|....*....|....*....|.
gi 1821015446 469 IITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05924 270 CINTGGEKVFPEEVEEALKSHPAVYDVLVVG 300
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
22-498 |
6.61e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 68.00 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 22 WAAKCAERgdaTAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGG--IPSG 99
Cdd:PRK04813 11 FAQTQPDF---PAYDYLG----EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHayIPVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 100 VYTtdSAGQLEYLINDSGSAFLFVENDEQLDkylevQDRVPTIVkvivfdpkglrdfshpkvmfLSDLYEIGEKAPDAae 179
Cdd:PRK04813 84 VSS--PAERIEMIIEVAKPSLIIATEELPLE-----ILGIPVIT--------------------LDELKDIFATGNPY-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 180 rfrIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNML-YQMWAgqqvLRVDPKDEQLCFL---PLCHVLerivSVE--F 253
Cdd:PRK04813 135 ---DFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVsFTNWM----LEDFALPEGPQFLnqaPYSFDL----SVMdlY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 254 P-IAVGSTVNfaespdtvfdnlreVSPHVFTAVPRLwekiysrvLIMRSEATPFGRW----AF-DraMAsgaaklegkgg 327
Cdd:PRK04813 204 PtLASGGTLV--------------ALPKDMTANFKQ--------LFETLPQLPINVWvstpSFaD--MC----------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 328 amhavwdfLVLRNirqmigFDRNRRsntgaapisPDLIRWY--G-ALGV----TLLE---------GYGMTETSG-VASV 390
Cdd:PRK04813 249 --------LLDPS------FNEEHL---------PNLTHFLfcGeELPHktakKLLErfpsatiynTYGPTEATVaVTSI 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 391 NVIGD-----NRIgTIGCALPATELRI----------AENGEICLKGPNVFKGYWRKPEKTAEDI--RDG-WLY-TGDVG 451
Cdd:PRK04813 306 EITDEmldqyKRL-PIGYAKPDSPLLIideegtklpdGEQGEIVISGPSVSKGYLNNPEKTAEAFftFDGqPAYhTGDAG 384
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1821015446 452 RIgDDGAITITGRVkDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK04813 385 YL-EDGLLFYQGRI-DFQIKLNGYRIELEEIEQNLRQSSYVESAVVV 429
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
356-498 |
8.94e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 67.59 E-value: 8.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 356 GAAPISPDLIRWYGALGVTLLEGYGMTET-SGVASVNVigDNRIGtIGCALPATELRIaENGEICLKGPNVFKGYWRKPE 434
Cdd:PRK09029 248 GGAAIPVELTEQAEQQGIRCWCGYGLTEMaSTVCAKRA--DGLAG-VGSPLPGREVKL-VDGEIWLRGASLALGYWRQGQ 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821015446 435 KTAEDIRDGWLYTGDVGRIgDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK09029 324 LVPLVNDEGWFATRDRGEW-QNGELTILGRLDNLFFS-GGEGIQPEEIERVINQHPLVQQVFVV 385
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
170-474 |
1.14e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 67.10 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 170 IGEKAPDAaerFrieINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIV 249
Cdd:cd05910 70 LQEAEPDA---F---IGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPAL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 250 SVEFPI-AVGSTVNFAESPDTVFDNLREVSPHVFTAVPRLWEKIYS------------RVLIMRSEATPFGRWAFDRAMA 316
Cdd:cd05910 144 GLTSVIpDMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARycaqhgitlpslRRVLSAGAPVPIALAARLRKML 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 317 SGAAKLEGKGGAMHAVwdflvlrnIRQMIGfDRNRRSNTGAAPIspdlirwygalgvtllEGYGMTETSGVASVNV---- 392
Cdd:cd05910 224 SDEAEILTPYGATEAL--------PVSSIG-SRELLATTTAATS----------------GGAGTCVGRPIPGVRVriie 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 393 IGDNRIGTIG--CALPATELriaenGEICLKGPNVFKGYWRKPEKTA-EDIRDG----WLYTGDVGRIGDDGAITITGRV 465
Cdd:cd05910 279 IDDEPIAEWDdtLELPRGEI-----GEITVTGPTVTPTYVNRPVATAlAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRK 353
|
....*....
gi 1821015446 466 KDIIITAGG 474
Cdd:cd05910 354 AHRVITTGG 362
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
188-514 |
1.42e-11 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 66.81 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 188 SQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFlplchvlerivsvefpiavgSTVNFAESp 267
Cdd:cd17645 101 TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVY--------------------ASFSFDAS- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 268 dtvfdnLREVSPHVFtavprlwekIYSRVLIMRSEAtpfgRWAFDRamasgaakLEGKGGAMHAVWDFLVLRNIRQMIGF 347
Cdd:cd17645 160 ------AWEIFPHLT---------AGAALHVVPSER----RLDLDA--------LNDYFNQEGITISFLPTGAAEQFMQL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 348 DRN--RRSNTGAapispDLIRWYGALGVTLLEGYGMTETSGVASV-------------NVIGDNRIGTIGCALPATELRI 412
Cdd:cd17645 213 DNQslRVLLTGG-----DKLKKIERKGYKLVNNYGPTENTVVATSfeidkpyanipigKPIDNTRVYILDEALQLQPIGV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 413 AenGEICLKGPNVFKGYWRKPEKTAED-IRDGW-----LY-TGDVGRIGDDGAITITGRVkDIIITAGGKNITPAEIESR 485
Cdd:cd17645 288 A--GELCIAGEGLARGYLNRPELTAEKfIVHPFvpgerMYrTGDLAKFLPDGNIEFLGRL-DQQVKIRGYRIEPGEIEPF 364
|
330 340 350
....*....|....*....|....*....|...
gi 1821015446 486 LKFSPFISDAVVI----GDRRKYLTVLIMIDQE 514
Cdd:cd17645 365 LMNHPLIELAAVLakedADGRKYLVAYVTAPEE 397
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
47-499 |
1.62e-11 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 67.09 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 47 SWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLycdLAISAAGGIPSGVYttdsagqleyLINDS--GSAFLFVE 124
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFV---EALLAANRIGADIL----------LLNTSfaGPALAEVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 125 NDEQLDKYLEVQDRVPTIVKVIVFDPKGLRDFSHPKvmflSDLYEIGEKAPDAAERFRIEinaSQPEDTRMLIYTSGTTG 204
Cdd:PRK13382 137 TREGVDTVIYDEEFSATVDRALADCPQATRIVAWTD----EDHDLTVEVLIAAHAGQRPE---PTGRKGRVILLTSGTTG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 205 PPKGAmiSHSnmlyqmwagqqvlrvDPKDeqlcFLPLCHVLERIvsvefPIAvgstvnfAESPdtvfdnlrevsphVFTA 284
Cdd:PRK13382 210 TPKGA--RRS---------------GPGG----IGTLKAILDRT-----PWR-------AEEP-------------TVIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 285 VPRLWEKIYSRVLIMRSEATPF-GRWAFDramASGAAKLEGKGGAMHAVWDFLVLRNIRQMIGFDRNRRSNTG----AA- 358
Cdd:PRK13382 244 APMFHAWGFSQLVLAASLACTIvTRRRFD---PEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSlrfaAAs 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 359 --PISPDLIR-WYGALGVTLLEGYGMTETSGVASVNViGDNR--IGTIGCALPATELRI----------AENGEICLKGP 423
Cdd:PRK13382 321 gsRMRPDVVIaFMDQFGDVIYNNYNATEAGMIATATP-ADLRaaPDTAGRPAEGTEIRIldqdfrevptGEVGTIFVRND 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821015446 424 NVFKGYwrkPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK13382 400 TQFDGY---TSGSTKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVS-GGENVYPIEVEKTLATHPDVAEAAVIG 471
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
199-483 |
2.17e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 66.33 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 199 TSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLC-FLPLCH------VLERIVSvEFPIAVGSTVNFAESPDTVF 271
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCsWLPLYHdmglafLLTAALA-GAPLWLAPTTAFSASPFRWL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 272 DNLREvSPHVFTAVPRLwekIYSrvLIMRseatpFGRWAFDRAMasGAAKLEGKGGamhavwdflvlrnirQMIGFDRNR 351
Cdd:PRK05851 239 SWLSD-SRATLTAAPNF---AYN--LIGK-----YARRVSDVDL--GALRVALNGG---------------EPVDCDGFE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 352 RSNTGAAPISPDLirwyGALgvtlLEGYGMTETSGVASVNVIGD---------------NRIGTIGCALPATELRIA--- 413
Cdd:PRK05851 291 RFATAMAPFGFDA----GAA----APSYGLAESTCAVTVPVPGIglrvdevttddgsgaRRHAVLGNPIPGMEVRISpgd 362
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821015446 414 --------ENGEICLKGPNVFKGYwrkpeKTAEDIR-DGWLYTGDVGRIGDDGaITITGRVKDIIITAgGKNITPAEIE 483
Cdd:PRK05851 363 gaagvagrEIGEIEIRGASMMSGY-----LGQAPIDpDDWFPTGDLGYLVDGG-LVVCGRAKELITVA-GRNIFPTEIE 434
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
44-514 |
1.38e-10 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 63.65 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 44 QAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLFV 123
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 124 ENdeqldkylevqdrvptivkvivfdpkglrdfsHPKVMFLSDLYEIGEKAPDAAERFRIEINASQPEDTRM-LIYTSGT 202
Cdd:cd17656 92 QR--------------------------------HLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLyIIYTSGT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 203 TGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCF----LPLCHvlERIVSVefpIAVGSTVNFAESpdtvfDNLREVs 278
Cdd:cd17656 140 TGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFatcsFDVCY--QEIFST---LLSGGTLYIIRE-----ETKRDV- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 279 PHVFTAVPR-----------LWEKIYSrvliMRSEATPFGRwAFDRAMASGaaklegkggamhavwdflvlrniRQMIgf 347
Cdd:cd17656 209 EQLFDLVKRhnievvflpvaFLKFIFS----EREFINRFPT-CVKHIITAG-----------------------EQLV-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 348 drnrrsntgaapISPDLIRWYGALGVTLLEGYGMTETSGVASVNVIGDNRIGT---IGCALPATELRIAEN--------- 415
Cdd:cd17656 259 ------------ITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPElppIGKPISNTWIYILDQeqqlqpqgi 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 416 -GEICLKGPNVFKGYWRKPEKTAEDI------RDGWLY-TGDVGRIGDDGAITITGRVkDIIITAGGKNITPAEIESRLK 487
Cdd:cd17656 327 vGELYISGASVARGYLNRQELTAEKFfpdpfdPNERMYrTGDLARYLPDGNIEFLGRA-DHQVKIRGYRIELGEIEAQLL 405
|
490 500 510
....*....|....*....|....*....|.
gi 1821015446 488 FSPFISDAVVI----GDRRKYLTVLIMIDQE 514
Cdd:cd17656 406 NHPGVSEAVVLdkadDKGEKYLCAYFVMEQE 436
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
192-499 |
3.72e-10 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 62.37 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 192 DTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFAESpdtvf 271
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKK----- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 272 dnlrevsphvFTAvPRLWEKiysrvlIMRSEATPFGRWA-FDRAMASGAAKLEGKGgamHavwdflvlrNIRQMIGfdrn 350
Cdd:cd05940 157 ----------FSA-SNFWDD------IRKYQATIFQYIGeLCRYLLNQPPKPTERK---H---------KVRMIFG---- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 351 rrsNTGAAPISPDLIRWYGAlgVTLLEGYGMTETSgVASVNVigDNRIGTIGCALPATELRIA--------ENGE----- 417
Cdd:cd05940 204 ---NGLRPDIWEEFKERFGV--PRIAEFYAATEGN-SGFINF--FGKPGAIGRNPSLLRKVAPlalvkydlESGEpirda 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 418 --ICLKGP--------------NVFKGYWRKPEKTAEDIR------DGWLYTGDVGRIGDDGAITITGRVKDiIITAGGK 475
Cdd:cd05940 276 egRCIKVPrgepgllisrinplEPFDGYTDPAATEKKILRdvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGD-TFRWKGE 354
|
330 340
....*....|....*....|....
gi 1821015446 476 NITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05940 355 NVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
356-486 |
5.95e-10 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 61.93 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 356 GAAPISPDLIRWYGA-LGVTLLEGYGMTEtsGVasVNVI----GDNRI-GTIGCAL-PATELRIA----------ENGEI 418
Cdd:PRK10946 308 GGARLSETLARRIPAeLGCQLQQVFGMAE--GL--VNYTrlddSDERIfTTQGRPMsPDDEVWVAdadgnplpqgEVGRL 383
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 419 CLKGPNVFKGYWRKPEKTAE--DiRDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRL 486
Cdd:PRK10946 384 MTRGPYTFRGYYKSPQHNASafD-ANGFYCSGDLVSIDPDGYITVVGREKD-QINRGGEKIAAEEIENLL 451
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
46-499 |
6.35e-10 |
|
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: 61.68 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEwlYCDLAISA--AGGIPSGVYTTDSAGQLEYLINDSGSAFLFV 123
Cdd:cd05915 25 TTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFR--HLEAYFAVpgMGAVLHTANPRLSPKEIAYILNHAEDKVLLF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 124 ENDeqldkYLEVQDRVPTIVKVIVFDPKglrdfSHPKVMFLSDLYEIGEkaPDaaerFRiEINASQPEDTRMLIYTSGTT 203
Cdd:cd05915 103 DPN-----LLPLVEAIRGELKTVQHFVV-----MDEKAPEGYLAYEEAL--GE----EA-DPVRVPERAACGMAYTTGTT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 204 GPPKGAMISHSNMLYQMWAG--QQVLRVDPKDEQLCFLPLCHVLE--RIVSVEFPIAVGSTVNFAESPDTVFDNLREVSP 279
Cdd:cd05915 166 GLPKGVVYSHRALVLHSLAAslVDGTALSEKDVVLPVVPMFHVNAwcLPYAATLVGAKQVLPGPRLDPASLVELFDGEGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 280 HVFTAVPRLWEKIYSrvliMRSEATPFGRWAFdRAMASGAAKLEgkggamhAVWDFLVLRNIRQMIGFDRNRRSNTGAAP 359
Cdd:cd05915 246 TFTAGVPTVWLALAD----YLESTGHRLKTLR-RLVVGGSAAPR-------SLIARFERMGVEVRQGYGLTETSPVVVQN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 360 IspdlirWygalgvtLLEGYGMTETSGVASVNVIGDNRIGTIGCALPATELRIAENGE----ICLKGPNVFKGYWRKPEK 435
Cdd:cd05915 314 F------V-------KSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEA 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821015446 436 T-AEDIRDGWLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05915 381 TrSALTPDGFFRTGDIAVWDEEGYVEIKDRLKD-LIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
27-499 |
6.00e-09 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 58.80 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 27 AERGDATA-HREKD-FGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTD 104
Cdd:TIGR02188 68 EARPDKVAiIWEGDePGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 105 SAGQLEYLINDSGSAFLfVENDEQL--DKYLEVQDRV-------PTIVK-VIVFDPKGL--------RDFshpkvmflsD 166
Cdd:TIGR02188 148 SAEALADRINDAGAKLV-ITADEGLrgGKVIPLKAIVdealekcPVSVEhVLVVRRTGNpvvpwvegRDV---------W 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 167 LYEIGEKAPD--AAERFrieinasQPEDTRMLIYTSGTTGPPKGAMisHSNMLYQMWA---GQQVLRVDPKDEQLCFLPL 241
Cdd:TIGR02188 218 WHDLMAKASAycEPEPM-------DSEDPLFILYTSGSTGKPKGVL--HTTGGYLLYAamtMKYVFDIKDGDIFWCTADV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 242 CHVLERIVSVEFPIAVG-STVNFAESPDTvfdnlrevsPHvftaVPRLWEKIYS-RVLIMRSEATPFgrwafdRA-MASG 318
Cdd:TIGR02188 289 GWITGHSYIVYGPLANGaTTVMFEGVPTY---------PD----PGRFWEIIEKhKVTIFYTAPTAI------RAlMRLG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 319 AAKLEGkggamhavWDFLVLRnirqMIGfdrnrrsnTGAAPISPDLIRWY----GALGVTLLEGYGMTETSG--VASVNV 392
Cdd:TIGR02188 350 DEWVKK--------HDLSSLR----LLG--------SVGEPINPEAWMWYykvvGKERCPIVDTWWQTETGGimITPLPG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 393 IGDNRIGTIGCALPATELRI-----------AENGEICLKG--PNVFKGYWRKPE---KTAEDIRDGWLYTGDVGRIGDD 456
Cdd:TIGR02188 410 ATPTKPGSATLPFFGIEPAVvdeegnpvegpGEGGYLVIKQpwPGMLRTIYGDHErfvDTYFSPFPGYYFTGDGARRDKD 489
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1821015446 457 GAITITGRVKDIIITAgGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:TIGR02188 490 GYIWITGRVDDVINVS-GHRLGTAEIESALVSHPAVAEAAVVG 531
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
175-517 |
1.19e-08 |
|
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: 57.41 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 175 PDAAERFRIEINASQ-----PEDTRMLIYTSGTTGPPKGAMISHSNMLYqmwagqqvLRVD---------PKDEQLCFLP 240
Cdd:cd17648 73 PDERIQFILEDTGARvvitnSTDLAYAIYTSGTTGKPKGVLVEHGSVVN--------LRTSlseryfgrdNGDEAVLFFS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 241 ---LCHVLERIVsvefpIAV--GSTvnfaespdtvfdnLREVSPHVFTAVPRLWEKIYSRVLIMRSeATPFGRWAFDRAM 315
Cdd:cd17648 145 nyvFDFFVEQMT-----LALlnGQK-------------LVVPPDEMRFDPDRFYAYINREKVTYLS-GTPSVLQQYDLAR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 316 ASGAAKLEGKGGAMHAVwdflVLRNIRQmiGFdrnrrsntgAAPIspdlirwygalgvtlLEGYGMTETSgVASVNVI-- 393
Cdd:cd17648 206 LPHLKRVDAAGEEFTAP----VFEKLRS--RF---------AGLI---------------INAYGPTETT-VTNHKRFfp 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 394 GDNRI-GTIGCALPATELRIAEN----------GEICLKGPNVFKGYWRKPEKTAE-----------DIRDG---WLY-T 447
Cdd:cd17648 255 GDQRFdKSLGRPVRNTKCYVLNDamkrvpvgavGELYLGGDGVARGYLNRPELTAErflpnpfqteqERARGrnaRLYkT 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821015446 448 GDVGRIGDDGAITITGRvKDIIITAGGKNITPAEIESRLKFSPFISDAVVI---------GDRRKYLTVLIMIDQENVE 517
Cdd:cd17648 335 GDLVRWLPSGELEYLGR-NDFQVKIRGQRIEPGEVEAALASYPGVRECAVVakedasqaqSRIQKYLVGYYLPEPGHVP 412
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
29-499 |
1.67e-08 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 57.33 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 29 RGDATA--HREKDFGIWQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSA 106
Cdd:cd05967 64 RGDQIAliYDSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 107 GQLEYLINDSGSAFLF-----------VENDEQLDKYLEVQDRVPtiVKVIVFD--------PKGLRDFshpkvmflsDL 167
Cdd:cd05967 144 KELASRIDDAKPKLIVtascgiepgkvVPYKPLLDKALELSGHKP--HHVLVLNrpqvpadlTKPGRDL---------DW 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 168 YEIGEKAPdaaerfRIEINASQPEDTRMLIYTSGTTGPPKG--------AMISHSNM--LYQM------WAGQQVLRVdP 231
Cdd:cd05967 213 SELLAKAE------PVDCVPVAATDPLYILYTSGTTGKPKGvvrdngghAVALNWSMrnIYGIkpgdvwWAASDVGWV-V 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 232 KDEQLCFLPLCHVLerivsvefpiavgSTVNFAESPDTVFDnlrevsPHVFTavpRLWEKiySRVLIMRSEATPFgrwaf 311
Cdd:cd05967 286 GHSYIVYGPLLHGA-------------TTVLYEGKPVGTPD------PGAFW---RVIEK--YQVNALFTAPTAI----- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 312 dRAMasgaaKLEGKGGAMHAVWDFLVLRNIrqmigfdrnrrsNTGAAPISPDLIRWY-GALGVTLLEGYGMTETSGVASV 390
Cdd:cd05967 337 -RAI-----RKEDPDGKYIKKYDLSSLRTL------------FLAGERLDPPTLEWAeNTLGVPVIDHWWQTETGWPITA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 391 NVIG----DNRIGTIGCALPATELRI----------AENGEICLKGP---NVFKGYWRKPEKTAE---DIRDGWLYTGDV 450
Cdd:cd05967 399 NPVGleplPIKAGSPGKPVPGYQVQVldedgepvgpNELGNIVIKLPlppGCLLTLWKNDERFKKlylSKFPGYYDTGDA 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1821015446 451 GRIGDDGAITITGRVKDIIITAGGKnITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05967 479 GYKDEDGYLFIMGRTDDVINVAGHR-LSTGEMEESVLSHPAVAECAVVG 526
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
156-497 |
4.23e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 56.59 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 156 FSH-PKVMFLSdlYEIGEKAPDAAERFRieinaSQPEDTRMLIYTSGTTGPPKGAMISHS---NMLYQMwagQQVLRVDP 231
Cdd:PRK10252 569 FADvPDLTSLC--YNAPLAPQGAAPLQL-----SQPHHTAYIIFTSGSTGRPKGVMVGQTaivNRLLWM---QNHYPLTA 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 232 KDEqlcflplchVLERI-----VSV-EF--PIAVGSTVNFAEsPDTVFDnlrevsphvftavPRLWEKIYSRVLIMRSEA 303
Cdd:PRK10252 639 DDV---------VLQKTpcsfdVSVwEFfwPFIAGAKLVMAE-PEAHRD-------------PLAMQQFFAEYGVTTTHF 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 304 TPFGRWAFDRAMASGAAKlegkggamhavwdflvlRNIRQMigfdrnRRSNTGAAPISPDLIR-WYGALGVTLLEGYGMT 382
Cdd:PRK10252 696 VPSMLAAFVASLTPEGAR-----------------QSCASL------RQVFCSGEALPADLCReWQQLTGAPLHNLYGPT 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 383 EtsgvASVNVI-----GDNRIGTIGCALPA------TELRIAEN----------GEICLKGPNVFKGYWRKPEKTAED-I 440
Cdd:PRK10252 753 E----AAVDVSwypafGEELAAVRGSSVPIgypvwnTGLRILDArmrpvppgvaGDLYLTGIQLAQGYLGRPDLTASRfI 828
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821015446 441 RD-----GWLY-TGDVGRIGDDGAITITGRvKDIIITAGGKNITPAEIESRLKFSPFISDAVV 497
Cdd:PRK10252 829 ADpfapgERMYrTGDVARWLDDGAVEYLGR-SDDQLKIRGQRIELGEIDRAMQALPDVEQAVT 890
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
19-505 |
1.20e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 19 VKLWAAKCAERGDATAHREKDfgiwQAYSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGgips 98
Cdd:PRK05691 3723 VRLFEAQVAAHPQRIAASCLD----QQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAG---- 3794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 99 gvyttdsAGqleYLINDSGSAflfvenDEQLDKYLEvQDRVPTIV--------KVIVFDpkGLRDFSHPKVMFLSDLyEI 170
Cdd:PRK05691 3795 -------AG---YLPLDPGLP------AQRLQRIIE-LSRTPVLVcsaacreqARALLD--ELGCANRPRLLVWEEV-QA 3854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 171 GEKAPDAAERFrieinaSQPEDTRMLIYTSGTTGPPKGAMISHSNMLyqmwagqqvlrvdpkDEQLCFLPLCHVLERIV- 249
Cdd:PRK05691 3855 GEVASHNPGIY------SGPDNLAYVIYTSGSTGLPKGVMVEQRGML---------------NNQLSKVPYLALSEADVi 3913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 250 ----SVEFPIAV---------GSTVN-----FAESPDTVFDNLREVSPHVFTAVPRLwekiysrvlimrseatpfgrwaF 311
Cdd:PRK05691 3914 aqtaSQSFDISVwqflaaplfGARVEivpnaIAHDPQGLLAHVQAQGITVLESVPSL----------------------I 3971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 312 DRAMASGAAKLEGkggamhavwdflvlrnIRQMIgfdrnrrsNTGAApISPDLIR-W---YGALGvtLLEGYGMTETSG- 386
Cdd:PRK05691 3972 QGMLAEDRQALDG----------------LRWML--------PTGEA-MPPELARqWlqrYPQIG--LVNAYGPAECSDd 4024
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 387 VASVNV-----------IG----DNRIGTIGCALPATELriAENGEICLKGPNVFKGYWRKPEKTAEDI----------R 441
Cdd:PRK05691 4025 VAFFRVdlastrgsylpIGsptdNNRLYLLDEALELVPL--GAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgapgeR 4102
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821015446 442 dgwLY-TGDVGRIGDDGAITITGRVkDIIITAGGKNITPAEIESRLKFSPFISDAVVI---GDRRKYL 505
Cdd:PRK05691 4103 ---LYrTGDLARRRSDGVLEYVGRI-DHQVKIRGYRIELGEIEARLHEQAEVREAAVAvqeGVNGKHL 4166
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
366-499 |
1.54e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 54.23 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 366 RWYGALGVTLLEGYGMTETsGVASVNVIGDNRIG--TIGCALPATELRIAE----------NGEICLKGPNVFKGYwrkP 433
Cdd:PRK13383 311 RFMDTYGDILYNGYGSTEV-GIGALATPADLRDApeTVGKPVAGCPVRILDrnnrpvgprvTGRIFVGGELAGTRY---T 386
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821015446 434 EKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIIITaGGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK13383 387 DGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIIS-GGENVYPRAVENALAAHPAVADNAVIG 451
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
185-486 |
3.40e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 53.28 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 185 INASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFA 264
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 265 ESPdtvfdnlreVSPhvftavprlwEKIYSrvLIMRSEATPFGRWA--FDRAMAsgAAKlegKGGAMHAVWDFLVlrnir 342
Cdd:PRK06334 257 YNP---------LYP----------KKIVE--MIDEAKVTFLGSTPvfFDYILK--TAK---KQESCLPSLRFVV----- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 343 qmIGFDRNRRS-NTGAAPISPDlirwygalgVTLLEGYGMTETSGVASVNVIGDNRIGT-IGCALPATELRI-------- 412
Cdd:PRK06334 306 --IGGDAFKDSlYQEALKTFPH---------IQLRQGYGTTECSPVITINTVNSPKHEScVGMPIRGMDVLIvseetkvp 374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821015446 413 ---AENGEICLKGPNVFKGYWRKPEKTAEDIRDG--WLYTGDVGRIGDDGAITITGRVKDiIITAGGKNITPAEIESRL 486
Cdd:PRK06334 375 vssGETGLVLTRGTSLFSGYLGEDFGQGFVELGGetWYVTGDLGYVDRHGELFLKGRLSR-FVKIGAEMVSLEALESIL 452
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
188-499 |
3.65e-07 |
|
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: 52.82 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 188 SQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTVNFA--- 264
Cdd:cd05937 84 VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSrkf 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 265 ----------ESPDTVFDNLREV---------SP----HVFTAV------PRLWEKIYSRVLI------MRSEATPFGRW 309
Cdd:cd05937 164 sasqfwkdvrDSGATIIQYVGELcryllstppSPydrdHKVRVAwgnglrPDIWERFRERFNVpeigefYAATEGVFALT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 310 AFDRAmASGAAKLEGKGGAMHavwdfLVLRNIRQMIGFDRN-----RRSNTGAAPISPdlirwygalgvtllegygmTET 384
Cdd:cd05937 244 NHNVG-DFGAGAIGHHGLIRR-----WKFENQVVLVKMDPEtddpiRDPKTGFCVRAP-------------------VGE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 385 SGVASVNVIGDNRIGTIGC--ALPATELRIAEngeiclkgpNVF-KG--YWRKPEKTAEDiRDGWLYTGDvgRIGDdgai 459
Cdd:cd05937 299 PGEMLGRVPFKNREAFQGYlhNEDATESKLVR---------DVFrKGdiYFRTGDLLRQD-ADGRWYFLD--RLGD---- 362
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1821015446 460 tiTGRVKdiiitagGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05937 363 --TFRWK-------SENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
186-498 |
4.31e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.25 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 186 NASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLplchvlerivsvefpiavgsTVNFAe 265
Cdd:PRK05691 2328 FLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFY--------------------SINFD- 2386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 266 spdtvfdnlrevsphvfTAVPRLWEKIYS--RVlIMRSEatpfGRWAFD------RAMASGAAKLEGKGGAMHAVWdfLV 337
Cdd:PRK05691 2387 -----------------AASERLLVPLLCgaRV-VLRAQ----GQWGAEeicqliREQQVSILGFTPSYGSQLAQW--LA 2442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 338 LRN----IRQMIgfdrnrrsnTGAAPISPD-LIRWYGALGVTLL-EGYGMTET--------------SGVASV---NVIG 394
Cdd:PRK05691 2443 GQGeqlpVRMCI---------TGGEALTGEhLQRIRQAFAPQLFfNAYGPTETvvmplaclapeqleEGAASVpigRVVG 2513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 395 DnRIGTIGCA----LPAtelriAENGEICLKGPNVFKGYWRKPEKTAE-------DIRDGWLY-TGDVGRIGDDGAITIT 462
Cdd:PRK05691 2514 A-RVAYILDAdlalVPQ-----GATGELYVGGAGLAQGYHDRPGLTAErfvadpfAADGGRLYrTGDLVRLRADGLVEYV 2587
|
330 340 350
....*....|....*....|....*....|....*.
gi 1821015446 463 GRVkDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK05691 2588 GRI-DHQVKIRGFRIELGEIESRLLEHPAVREAVVL 2622
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
46-221 |
4.36e-07 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 53.04 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 46 YSWSDWYDRSQAIGMGLIELGLTRGTPVSILSEDNKEWLYCDLAISAAGGI---------PSGVytTDSAGQLE--YLIN 114
Cdd:cd05943 99 VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIwsscspdfgVPGV--LDRFGQIEpkVLFA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 115 DSGSAFLFVENDeQLDKYLEVQDRVPTIVKVIVFD---PKGLRDFSH-PKVMFLSDLYEIGEKAPDAAERfrieINASQP 190
Cdd:cd05943 177 VDAYTYNGKRHD-VREKVAELVKGLPSLLAVVVVPytvAAGQPDLSKiAKALTLEDFLATGAAGELEFEP----LPFDHP 251
|
170 180 190
....*....|....*....|....*....|.
gi 1821015446 191 edtRMLIYTSGTTGPPKGAMISHSNMLYQMW 221
Cdd:cd05943 252 ---LYILYSSGTTGLPKCIVHGAGGTLLQHL 279
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
176-527 |
7.53e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 51.58 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 176 DAAERFRIEINASQPEDTRMLIYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPI 255
Cdd:PRK08308 86 GESDFTKLEAVNYLAEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 256 AVGSTVNF--AESPDTVFDNLREVSPHVFTAVPRLWEkIYSRVLImrseatpfGRWAFDRAMASGAAklegkggaMHAVW 333
Cdd:PRK08308 166 TRGSKPVIitNKNPKFALNILRNTPQHILYAVPLMLH-ILGRLLP--------GTFQFHAVMTSGTP--------LPEAW 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 334 dFLVLRNIRQMIgFDRNRRSNTGAAPISPDLiRWYGALGVTLLEgygmtetsgvASVNvIGDNRigtigcalpatelriA 413
Cdd:PRK08308 229 -FYKLRERTTYM-MQQYGCSEAGCVSICPDM-KSHLDLGNPLPH----------VSVS-AGSDE---------------N 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 414 ENGEICLKgpnvfkgywrkpektaedIRDGWLYTGDVGRIGDDGAITITGRVKDIIITAgGKNITPAEIESRLKFSPFIS 493
Cdd:PRK08308 280 APEEIVVK------------------MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVS-GLNVYPIEVEDVMLRLPGVQ 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1821015446 494 DAVV-------IGDRRKYLTVL-IMIDQENVEKYAQD----HQIPF 527
Cdd:PRK08308 341 EAVVyrgkdpvAGERVKAKVIShEEIDPVQLREWCIQhlapYQVPH 386
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
372-498 |
2.05e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 372 GVTLLEGYGMTETSgvasVNV--------------IGdNRIGTIGCALPATELRIAENG---EICLKGPNVFKGYWRKPE 434
Cdd:PRK05691 1414 QVQLHNRYGPTETA----INVthwqcqaedgerspIG-RPLGNVLCRVLDAELNLLPPGvagELCIGGAGLARGYLGRPA 1488
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821015446 435 KTAE------DIRDGW-LY-TGDVGRIGDDGAITITGRVkDIIITAGGKNITPAEIESRLKFSPFISDAVVI 498
Cdd:PRK05691 1489 LTAErfvpdpLGEDGArLYrTGDRARWNADGALEYLGRL-DQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL 1559
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
197-261 |
2.14e-06 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 50.50 E-value: 2.14e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821015446 197 IYTSGTTGPPKGAMISHSNMLYQMWAGQQVLRVDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTV 261
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTV 174
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
44-261 |
4.19e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 49.60 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 44 QAYSWSDWYDRSQAIGMGLI-ELGLTRGTPVSILSEDNKEWLYCDLAISAAGGIPSGVYTTDSAGQLEYLINDSGSAFLF 122
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 123 VENDEQlDKYLEVqdrVPTI----VKVIVfdpKGLRDFSHPKVMFLSDLYEIGEKAPDAAERFRIEINasqpeDTRMLIY 198
Cdd:cd05938 84 VAPELQ-EAVEEV---LPALradgVSVWY---LSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIK-----SPALYIY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821015446 199 TSGTTGPPKGAMISHsnmlYQMWAGQQVLR---VDPKDEQLCFLPLCHVLERIVSVEFPIAVGSTV 261
Cdd:cd05938 152 TSGTTGLPKAARISH----LRVLQCSGFLSlcgVTADDVIYITLPLYHSSGFLLGIGGCIELGATC 213
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
443-499 |
4.74e-06 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 49.48 E-value: 4.74e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821015446 443 GWLYTGDVGRIGDDGAITITGRVKDIIITAgGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:cd05966 469 GYYFTGDGARRDEDGYYWITGRVDDVINVS-GHRLGTAEVESALVAHPAVAEAAVVG 524
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
443-499 |
1.60e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 47.83 E-value: 1.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821015446 443 GWLYTGDVGRIGDDGAITITGRVKDIIITAgGKNITPAEIESRLKFSPFISDAVVIG 499
Cdd:PRK00174 483 GMYFTGDGARRDEDGYYWITGRVDDVLNVS-GHRLGTAEIESALVAHPKVAEAAVVG 538
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
191-499 |
6.71e-05 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 46.04 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 191 EDTRMLIYTSGTTGPPKGAM-ISHSNMLYQMWAGQQVLRVDPKDEQLCFLPlCHVLERIVSVEF-PIAVGSTVNFAES-- 266
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLhTTGGYMVYTATTFKYAFDYKPTDVYWCTAD-CGWITGHSYVTYgPMLNGATVLVFEGap 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 267 --PDT--VFDNLREVSPHVFTAVPRLWEKIysrvliMRSEATPFGRWAFDRAMASGAAKLEGKGGAMHavWDFLVLRNIR 342
Cdd:PLN02654 354 nyPDSgrCWDIVDKYKVTIFYTAPTLVRSL------MRDGDEYVTRHSRKSLRVLGSVGEPINPSAWR--WFFNVVGDSR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 343 QMIGfDRNRRSNTGAAPISPDLIRWYGALGVTLLEGYGMTEtsgvasvnVIGDNRigtigcalpATELRIAENGEICLKG 422
Cdd:PLN02654 426 CPIS-DTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQP--------VIVDEK---------GKEIEGECSGYLCVKK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821015446 423 --PNVFK---GYWRKPEKTAEDIRDGWLYTGDVGRIGDDGAITITGRVKDIiITAGGKNITPAEIESRLKFSPFISDAVV 497
Cdd:PLN02654 488 swPGAFRtlyGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDV-INVSGHRIGTAEVESALVSHPQCAEAAV 566
|
..
gi 1821015446 498 IG 499
Cdd:PLN02654 567 VG 568
|
|
| |
