|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
163-698 |
0e+00 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 973.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 163 KRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCR 242
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 243 ANVIVVDTQKQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEVPEEALDAIIDTQQPNQCCVLVYTSG 322
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 323 TTGNPKGVMLSQDN-----------------------------------------------------------GTLVNTL 343
Cdd:cd05933 161 TTGMPKGVMLSHDNitwtakaasqhmdlrpatvgqesvvsylplshiaaqildiwlpikvggqvyfaqpdalkGTLVKTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 344 REVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPSNDLKPFTS-RLADYLVLARVRQALGFA 422
Cdd:cd05933 241 REVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFyRLAKKLVFKKVRKALGLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 423 KCQKNFYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGIGEICLWGR 502
Cdd:cd05933 321 RCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 503 TIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISSAMLIGDQ 582
Cdd:cd05933 401 HVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGDK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 583 RKFLSMLLTLKCTLNPETSEPTDNLTEQAVEFCQRVGSKASTVSEIVGQKDEAVYQAIHEGIQRVNANAAARPYHIQKWA 662
Cdd:cd05933 481 RKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKWV 560
|
570 580 590
....*....|....*....|....*....|....*.
gi 1958794461 663 ILERDFSISGGELGPTMKLKRLTVLEKYKDIIDSFY 698
Cdd:cd05933 561 ILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
140-701 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 536.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 140 PYTVHQMFYEALDKYGNLSALGFKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG 219
Cdd:COG1022 10 ADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 220 GIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEV-P 298
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGLRDDPRLLSLDELLALGREVaD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 299 EEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDN------------------------------------------ 336
Cdd:COG1022 170 PAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNllsnarallerlplgpgdrtlsflplahvfertvsyyalaag 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 337 ---------GTLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPSNDLKPFTSR-- 405
Cdd:COG1022 250 atvafaespDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLAGKSPSLLLRlk 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 406 --LADYLVLARVRQALG----FAKCqknfyGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVV 479
Cdd:COG1022 330 haLADKLVFSKLREALGgrlrFAVS-----GGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 480 PGCRVKLvnqDADGigEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPP 559
Cdd:COG1022 405 PGVEVKI---AEDG--EILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 560 VPIEEAVKmELPIISSAMLIGDQRKFLSMLLtlkcTLNPETseptdnlteqAVEFCQRVGSKASTVSEIVgqKDEAVYQA 639
Cdd:COG1022 480 QPIENALK-ASPLIEQAVVVGDGRPFLAALI----VPDFEA----------LGEWAEENGLPYTSYAELA--QDPEVRAL 542
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794461 640 IHEGIQRVNANaAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKDIIDSFYQEQ 701
Cdd:COG1022 543 IQEEVDRANAG-LSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
168-683 |
9.49e-130 |
|
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: 391.57 E-value: 9.49e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 168 WERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 247
Cdd:cd05907 3 WQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 248 VDTqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealdaiidtqqPNQCCVLVYTSGTTGNP 327
Cdd:cd05907 83 VED------------------------------------------------------------PDDLATIIYTSGTTGRP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 328 KGVMLSQDN----------------------------------------------------GTLVNTLREVEPTSHMGVP 355
Cdd:cd05907 103 KGVMLSHRNilsnalalaerlpategdrhlsflplahvferraglyvpllagariyfassaETLLDDLSEVRPTVFLAVP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 356 RVWEKIMERIQEVAAQSGfiRRKMLLWAmsvtleqnltcpsndlkpftsrladylVLARVRqalgFAKCqknfyGAAPMT 435
Cdd:cd05907 183 RVWEKVYAAIKVKAVPGL--KRKLFDLA---------------------------VGGRLR----FAAS-----GGAPLP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 436 AETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQdadgiGEICLWGRTIFMGYLNMEDKT 515
Cdd:cd05907 225 AELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD-----GEILVRGPNVMLGYYKNPEAT 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 516 HEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVKMElPIISSAMLIGDQRKFLSMLLTLKCt 595
Cdd:cd05907 300 AEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PLISQAVVIGDGRPFLVALIVPDP- 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 596 lnpetseptdnltEQAVEFCQRVGSKASTVSEIVgqKDEAVYQAIHEGIQRVNAnAAARPYHIQKWAILERDFSISGGEL 675
Cdd:cd05907 378 -------------EALEAWAEEHGIAYTDVAELA--ANPAVRAEIEAAVEAANA-RLSRYEQIKKFLLLPEPFTIENGEL 441
|
....*...
gi 1958794461 676 GPTMKLKR 683
Cdd:cd05907 442 TPTLKLKR 449
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
147-552 |
3.94e-86 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 277.27 E-value: 3.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 147 FYEALDKYGNLSALGFkrkDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIY 226
Cdd:pfam00501 1 LERQAARTPDKTALEV---GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 227 TTSSPEACQYIAHDCRANVIVVDTQKQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEVPEEAldaii 306
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPP----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 307 dtqQPNQCCVLVYTSGTTGNPKGVMLSQDNgtLVNTLREVEPTSHMGVPRVWEK----------IMERIQEVAA------ 370
Cdd:pfam00501 153 ---DPDDLAYIIYTSGTTGKPKGVMLTHRN--LVANVLSIKRVRPRGFGLGPDDrvlstlplfhDFGLSLGLLGpllaga 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 371 ----QSGFIRRKMLLWAMSVTlEQNLTCpsndlKPFTSRLADYLVLARVRQALGFAKCQKNFYGAAPMTAETQRFFLGLN 446
Cdd:pfam00501 228 tvvlPPGFPALDPAALLELIE-RYKVTV-----LYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 447 IR-LYAGYGLSESTGP---HFMSSPYNYRLYSSGRVVPGCRVKLVNQD-----ADG-IGEICLWGRTIFMGYLNMEDKTH 516
Cdd:pfam00501 302 GGaLVNGYGLTETTGVvttPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtgepvPPGePGELCVRGPGVMKGYLNDPELTA 381
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958794461 517 EAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITA 552
Cdd:pfam00501 382 EAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
168-690 |
1.84e-80 |
|
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: 266.98 E-value: 1.84e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 168 WERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 247
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 248 VDTQKQLEKILKIWKDLPHLKAVVIYQeppPKKMAN-----VYTMEELIELGQEVPE---EALDAIIDTQQPNQCCVLVY 319
Cdd:cd17641 89 AEDEEQVDKLLEIADRIPSVRYVIYCD---PRGMRKyddprLISFEDVVALGRALDRrdpGLYEREVAAGKGEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 320 TSGTTGNPKGVMLSQDN----------------------------------------------------GTLVNTLREVE 347
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNflghcaaylaadplgpgdeyvsvlplpwigeqmysvgqalvcgfivnfpeepETMMEDLREIG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 348 PTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSV---TLEQNLTCPSNDLK-PFTSRLADYLVLARVRQALGFAK 423
Cdd:cd17641 246 PTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLglrALDRGKRGRPVSLWlRLASWLADALLFRPLRDRLGFSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 424 CQKNFYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNqdadgIGEICLWGRT 503
Cdd:cd17641 326 LRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDE-----VGEILVRSPG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 504 IFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVKMElPIISSAMLIGDQR 583
Cdd:cd17641 401 VFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFS-PYIAEAVVLGAGR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 584 KFLSMLLtlkctlnpetseptdNLTEQAV-EFCQRVGSKASTVSEIVGQkdEAVYQAIHEGIQRVNANAAArPYHIQKWA 662
Cdd:cd17641 480 PYLTAFI---------------CIDYAIVgKWAEQRGIAFTTYTDLASR--PEVYELIRKEVEKVNASLPE-AQRIRRFL 541
|
570 580
....*....|....*....|....*...
gi 1958794461 663 ILERDFSISGGELGPTMKLKRLTVLEKY 690
Cdd:cd17641 542 LLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
167-698 |
6.38e-73 |
|
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: 245.97 E-value: 6.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 167 KWERISYYQYYLIARKVAKGFLKLGLER--AHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRAN 244
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 245 VIVVDtqkqlekilkiwKDLphlkavviyqepppkkmaNVYTMEELIELGQEVPEEALDAiidtqQPNQCCVLVYTSGTT 324
Cdd:cd05927 82 IVFCD------------AGV------------------KVYSLEEFEKLGKKNKVPPPPP-----KPEDLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 325 GNPKGVMLSQ--------------------------------------------------------DNGTLVNTLREVEP 348
Cdd:cd05927 127 GNPKGVMLTHgnivsnvagvfkileilnkinptdvyisylplahifervvealflyhgakigfysgDIRLLLDDIKALKP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 349 TSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSvTLEQNLtcpsNDLKPFTSRLADYLVLARVRQALGfAKCQKNF 428
Cdd:cd05927 207 TVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALN-YKLAEL----RSGVVRASPFWDKLVFNKIKQALG-GNVRLML 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 429 YGAAPMTAETQRFFLG-LNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLV-----NQDADGI---GEICL 499
Cdd:cd05927 281 TGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVdvpemNYDAKDPnprGEVCI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 500 WGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIeEAVKMELPIISSAMLI 579
Cdd:cd05927 361 RGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKI-ENIYARSPFVAQIFVY 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 580 GDQRKflSMLLtlkCTLNPEtseptdnlTEQAVEFCQRVGSKASTVSEIVgqKDEAVYQAIHEGIQRVNANAAARPYHIQ 659
Cdd:cd05927 440 GDSLK--SFLV---AIVVPD--------PDVLKEWAASKGGGTGSFEELC--KNPEVKKAILEDLVRLGKENGLKGFEQV 504
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1958794461 660 KWAILERD-FSISGGELGPTMKLKRLTVLEKYKDIIDSFY 698
Cdd:cd05927 505 KAIHLEPEpFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
143-580 |
5.42e-64 |
|
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: 219.30 E-value: 5.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 143 VHQMFYEALDKYGNLSALgfkrKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIV 222
Cdd:COG0318 1 LADLLRRAAARHPDRPAL----VFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 223 TGIYTTSSPEACQYIAHDCRANVIVvdtqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeeal 302
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALV------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 303 daiidtqqpnqCCVLVYTSGTTGNPKGVMLSQDN-------------------------------------------GTL 339
Cdd:COG0318 102 -----------TALILYTSGTTGRPKGVMLTHRNllanaaaiaaalgltpgdvvlvalplfhvfgltvgllapllagATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 340 V-----------NTLREVEPTSHMGVPRVWEKIMERiqevaaqsgfirrkmllwamsvtleqnltcpsndlkpftSRLAD 408
Cdd:COG0318 171 VllprfdpervlELIERERVTVLFGVPTMLARLLRH---------------------------------------PEFAR 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 409 YLvLARVRQAlgfakcqknFYGAAPMTAET-QRFFLGLNIRLYAGYGLSEsTGPHFMSSPYNY---RLYSSGRVVPGCRV 484
Cdd:COG0318 212 YD-LSSLRLV---------VSGGAPLPPELlERFEERFGVRIVEGYGLTE-TSPVVTVNPEDPgerRPGSVGRPLPGVEV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 485 KLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTHEAIDsEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENV 557
Cdd:COG0318 281 RIV--DEDGrelppgeVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENV 356
|
490 500
....*....|....*....|...
gi 1958794461 558 PPVPIEEAVkMELPIISSAMLIG 580
Cdd:COG0318 357 YPAEVEEVL-AAHPGVAEAAVVG 378
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
171-580 |
1.11e-60 |
|
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: 211.30 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 171 ISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDt 250
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 251 QKQLEKILKIWKDLPHLKAVVIYqEPPPKKMANVYTMEElIELGQEVPEEALDAIIDtqqPNQCCVLVYTSGTTGNPKGV 330
Cdd:cd05911 90 PDGLEKVKEAAKELGPKDKIIVL-DDKPDGVLSIEDLLS-PTLGEEDEDLPPPLKDG---KDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 331 MLSQDNgtlvntlrevePTSHMGVPRVWEKIMERIQEVAA-------QSGFIrrkMLLWAMSVTLEQnLTCPSNDLKPFT 403
Cdd:cd05911 165 CLSHRN-----------LIANLSQVQTFLYGNDGSNDVILgflplyhIYGLF---TTLASLLNGATV-IIMPKFDSELFL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 404 SRLADYlvlaRVR-------QALGFAKC---QKN--------FYGAAPMTAETQRFF--LGLNIRLYAGYGLSESTGPHF 463
Cdd:cd05911 230 DLIEKY----KITflylvppIAAALAKSpllDKYdlsslrviLSGGAPLSKELQELLakRFPNATIKQGYGMTETGGILT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 464 MSSPYNYRLYSSGRVVPGCRVKLVNQDA------DGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDG 537
Cdd:cd05911 306 VNPDGDDKPGSVGRLLPNVEAKIVDDDGkdslgpNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958794461 538 FLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISSAMLIG 580
Cdd:cd05911 386 YLYIVDRKKEL-IKYKGFQVAPAEL-EAVLLEHPGVADAAVIG 426
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
169-683 |
1.68e-54 |
|
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: 194.11 E-value: 1.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGG--IVTGiyTTSSPEACQYIAHDCRANVI 246
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAvdVVRG--SDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 247 VVDTQkqlekilkiwkdlphlkavviyqeppPKKMAnvytmeelielgqevpeealdaiidtqqpnqccVLVYTSGTTGN 326
Cdd:cd17640 82 VVEND--------------------------SDDLA---------------------------------TIIYTSGTTGN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 327 PKGVMLSQDN--------------------------------------------------GTLVNTLREVEPTSHMGVPR 356
Cdd:cd17640 103 PKGVMLTHANllhqirslsdivppqpgdrflsilpiwhsyersaeyfifacgcsqaytsiRTLKDDLKRVKPHYIVSVPR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 357 VWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnltcpsndlkpftsrladyLVLARVRQALGfakcqknfyGAAPMTA 436
Cdd:cd17640 183 LWESLYSGIQKQVSKSSPIKQFLFLFF--------------------------LSGGIFKFGIS---------GGGALPP 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 437 ETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGI------GEICLWGRTIFMGYLN 510
Cdd:cd17640 228 HVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekGIVWVRGPQVMKGYYK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 511 MEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISSAMLIGDQRKFLSMLL 590
Cdd:cd17640 308 NPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEAL-MRSPFIEQIMVVGQDQKRLGALI 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 591 TlkctlnPetseptdNLTEQAVEFCQRVGSKASTVSEIVGQKDE-AVYQaiHEGIQRVNANAAARPY-HIQKWAILErDF 668
Cdd:cd17640 387 V------P-------NFEELEKWAKESGVKLANDRSQLLASKKVlKLYK--NEIKDEISNRPGFKSFeQIAPFALLE-EP 450
|
570
....*....|....*
gi 1958794461 669 SISGGELGPTMKLKR 683
Cdd:cd17640 451 FIENGEMTQTMKIKR 465
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
140-580 |
1.91e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 195.02 E-value: 1.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 140 PYTVHQMFYEALDKYGNLSALGFKRKdkweRISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG 219
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYFDGR----RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 220 GIVTGIYTTSSPEACQYIAHDCRANVIVVDTQ--KQLEKILKiwkDLPHLKAVVIYQEPPPK-KMANVYTMEELIElGQe 296
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAAILP---QLPTVRTVIVEGDGPAApLAPEVGEYEELLA-AA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 297 vPEEALDAIIDtqqPNQCCVLVYTSGTTGNPKGVMLSQDNGTL----VNTLREVEPTS---------------------H 351
Cdd:PRK06187 156 -SDTFDFPDID---ENDAAAMLYTSGTTGHPKGVVLSHRNLFLhslaVCAWLKLSRDDvylvivpmfhvhawglpylalM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 352 MGVPRVwekIMERIQ--EVAAQsgfIRRK-------------MLLwamsvtleQNLTCPSNDLkpftsrladylvlARVR 416
Cdd:PRK06187 232 AGAKQV---IPRRFDpeNLLDL---IETErvtfffavptiwqMLL--------KAPRAYFVDF-------------SSLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 417 QALgfakcqknfYGAAPMTAETQRFFLG-LNIRLYAGYGLSESTG-------PHFMSSPYNYRlYSSGRVVPGCRVKLVN 488
Cdd:PRK06187 285 LVI---------YGGAALPPALLREFKEkFGIDLVQGYGMTETSPvvsvlppEDQLPGQWTKR-RSAGRPLPGVEARIVD 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 489 QD-----ADG--IGEICLWGRTIFMGYLNMEDKTHEAIDSeGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVP 561
Cdd:PRK06187 355 DDgdelpPDGgeVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIIS-GGENIYPRE 432
|
490
....*....|....*....
gi 1958794461 562 IEEAVkMELPIISSAMLIG 580
Cdd:PRK06187 433 LEDAL-YGHPAVAEVAVIG 450
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
137-583 |
7.17e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 190.50 E-value: 7.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 137 TQLPYTVHQMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTV 216
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGD----QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 217 FAGGIVTGIYTTSSPEACQYIAHDCRANVIVVdTQKQLEKILKIWKDLPHLKAVVIYQEPPPK-KMANVYTMEELIELGQ 295
Cdd:PRK07656 77 KAGAVVVPLNTRYTADEAAYILARGDAKALFV-LGLFLGVDYSATTRLPALEHVVICETEEDDpHTEKMKTFTDFLAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 296 EVPEEAldaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQDNgTLVN--------TLRE------VEPTSH-MGVPRVW-- 358
Cdd:PRK07656 156 PAERAP------EVDPDDVADILFTSGTTGRPKGAMLTHRQ-LLSNaadwaeylGLTEgdrylaANPFFHvFGYKAGVna 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 359 ----------------EKIMERIQEvaaqsgfirRKMLLWAMSVTLEQNLtcpsndlkpFTSRLADYLVLARVRQALGfa 422
Cdd:PRK07656 229 plmrgatilplpvfdpDEVFRLIET---------ERITVLPGPPTMYNSL---------LQHPDRSAEDLSSLRLAVT-- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 423 kcqknfyGAAPMTAE-TQRFFLGLNIRLYA-GYGLSESTGPHFMSSPYNYRL---YSSGRVVPGCRVKLVNQDADGI--- 494
Cdd:PRK07656 289 -------GAASMPVAlLERFESELGVDIVLtGYGLSEASGVTTFNRLDDDRKtvaGTIGTAIAGVENKIVNELGEEVpvg 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 495 --GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPI 572
Cdd:PRK07656 362 evGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIV-GGFNVYPAEVEE-VLYEHPA 439
|
490
....*....|...
gi 1958794461 573 ISSAMLIG--DQR 583
Cdd:PRK07656 440 VAEAAVIGvpDER 452
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
313-629 |
1.01e-50 |
|
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: 179.79 E-value: 1.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 313 QCCVLVYTSGTTGNPKGVMLSQDNgTLVNT--------LREVE------PTSHMGV------------------PRVWEK 360
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRN-LLAAAaalaasggLTEGDvflstlPLFHIGGlfgllgallaggtvvllpKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 361 IMERIQEVaaqsgfirrkmllwamSVTLeqnLTCPsndlkPFtsrLADYLVLARVRQALGFAKCQKNFYGAAPMTAETQR 440
Cdd:cd04433 80 ALELIERE----------------KVTI---LLGV-----PT---LLARLLKAPESAGYDLSSLRALVSGGAPLPPELLE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 441 FFLGL-NIRLYAGYGLSESTGPHFMSSPYN--YRLYSSGRVVPGCRVKLVNQD-----ADGIGEICLWGRTIFMGYLNME 512
Cdd:cd04433 133 RFEEApGIKLVNGYGLTETGGTVATGPPDDdaRKPGSVGRPVPGVEVRIVDPDggelpPGEIGELVVRGPSVMKGYWNNP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 513 DKThEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISSAMLIG--DQRkfLSMLL 590
Cdd:cd04433 213 EAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAVLL-GHPGVAEAAVVGvpDPE--WGERV 287
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958794461 591 TLKCTLNPetsePTDNLTEQAVEFCQRVGSKASTVSEIV 629
Cdd:cd04433 288 VAVVVLRP----GADLDAEELRAHVRERLAPYKVPRRVV 322
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
180-689 |
2.22e-49 |
|
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: 180.74 E-value: 2.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 180 ARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTqkqlekiLK 259
Cdd:cd05932 16 ARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK-------LD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 260 IWKDLPHLKA--VVIYQEPPPKKMANVYTMEELIELGQEVPEEAldaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQDN- 336
Cdd:cd05932 89 DWKAMAPGVPegLISISLPPPSAANCQYQWDDLIAQHPPLEERP------TRFPEQLATLIYTSGTTGQPKGVMLTFGSf 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 337 ---------------------------------------------------GTLVNTLREVEPTSHMGVPRVWEKIMERI 365
Cdd:cd05932 163 awaaqagiehigteendrmlsylplahvtervfveggslyggvlvafaeslDTFVEDVQRARPTLFFSVPRLWTKFQQGV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 366 QEVAAQSgfiRRKMLLWAmsvtleqnltcpsndlkPFTSRladyLVLARVRQALGFAKCQKNFYGAAPMTAETQRFF--L 443
Cdd:cd05932 243 QDKIPQQ---KLNLLLKI-----------------PVVNS----LVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWYrsL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 444 GLNIrlYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQdadgiGEICLWGRTIFMGYLNMEDKTHEAIDSEG 523
Cdd:cd05932 299 GLNI--LEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSPALMMGYYKDPEATAEAFTADG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 524 WLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISSAMLIGDQrkfLSMLLTLkCTLNPETSEP 603
Cdd:cd05932 372 FLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKL-AEHDRVEMVCVIGSG---LPAPLAL-VVLSEEARLR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 604 TDNLTEQAVEfcqrvgskastvseivgqkdeavyQAIHEGIQRVnaNAAARPY-HIQKWAILERDFSISGGELGPTMKLK 682
Cdd:cd05932 447 ADAFARAELE------------------------ASLRAHLARV--NSTLDSHeQLAGIVVVKDPWSIDNGILTPTLKIK 500
|
....*..
gi 1958794461 683 RlTVLEK 689
Cdd:cd05932 501 R-NVLEK 506
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
169-580 |
1.08e-48 |
|
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: 177.03 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 248
Cdd:cd17631 19 RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLFD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DTqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealdaiidtqqpnqcCVLVYTSGTTGNPK 328
Cdd:cd17631 99 DL----------------------------------------------------------------ALLMYTSGTTGRPK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 329 GVMLSQDN--GTLVNTLRE-----------VEPTSHMG------VPRVW---EKIMERIQEVAAQSGFIRRKML--LWAM 384
Cdd:cd17631 115 GAMLTHRNllWNAVNALAAldlgpddvllvVAPLFHIGglgvftLPTLLrggTVVILRKFDPETVLDLIERHRVtsFFLV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 385 SVTLEQNLTCPsndlkpftsRLADYlVLARVRQALgfakcqknfYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFM 464
Cdd:cd17631 195 PTMIQALLQHP---------RFATT-DLSSLRAVI---------YGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 465 SSPYNYR--LYSSGRVVPGCRVKLVNQD-----ADGIGEICLWGRTIFMGYLNMEDKTHEAIDsEGWLHTGDMGRLDDDG 537
Cdd:cd17631 256 LSPEDHRrkLGSAGRPVFFVEVRIVDPDgrevpPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDG 334
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958794461 538 FLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:cd17631 335 YLYIVDRKKDMIIS-GGENVYPAEVEDVL-YEHPAVAEVAVIG 375
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
171-683 |
1.73e-48 |
|
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: 178.18 E-value: 1.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 171 ISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDT 250
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 251 QKqlekilkiwKDLphlkavviyqepppkkmanvytmeelielgqevpeealdaiidtqqpnqcCVLVYTSGTTGNPKGV 330
Cdd:cd17639 86 KP---------DDL--------------------------------------------------ACIMYTSGSTGNPKGV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 331 MLSQDN-----------------------------------------------G-----TLVNT--------LREVEPTS 350
Cdd:cd17639 107 MLTHGNlvagiaglgdrvpellgpddrylaylplahifelaaenvclyrggtiGygsprTLTDKskrgckgdLTEFKPTL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 351 HMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLtcpsndlKPFTSRLADYLVLARVRQALGfAKCQKNFYG 430
Cdd:cd17639 187 MVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALK-------EGPGTPLLDELVFKKVRAALG-GRLRYMLSG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 431 AAPMTAETQRFflgLNI---RLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGI--------GEICL 499
Cdd:cd17639 259 GAPLSADTQEF---LNIvlcPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYstdkppprGEILI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 500 WGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENvppVPIE--EAVKMELPIISSAM 577
Cdd:cd17639 336 RGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEY---IALEklESIYRSNPLVNNIC 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 578 LIGDQRKflSMLLTLKCTlnpetseptdnlTEQAVE-FCQRVGSKASTVSEIVgqKDEAVYQAIHEGIQRVNANAAARPY 656
Cdd:cd17639 413 VYADPDK--SYPVAIVVP------------NEKHLTkLAEKHGVINSEWEELC--EDKKLQKAVLKSLAETARAAGLEKF 476
|
570 580
....*....|....*....|....*...
gi 1958794461 657 HI-QKWAILERDFSISGGELGPTMKLKR 683
Cdd:cd17639 477 EIpQGVVLLDEEWTPENGLVTAAQKLKR 504
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
174-589 |
1.78e-48 |
|
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: 177.25 E-value: 1.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 174 YQYYLIARKVAK--GFLKL-GLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIahdcranvivvdt 250
Cdd:cd05914 8 LTYKDLADNIAKfaLLLKInGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHI------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 251 qkqlekilkiwkdLPHLKAVVIYqepppkkmanvytmeelielgqevpeealdaiidTQQPNQCCVLVYTSGTTGNPKGV 330
Cdd:cd05914 75 -------------LNHSEAKAIF----------------------------------VSDEDDVALINYTSGTTGNSKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 331 MLSQDN-GTLVNTLREVE------------PTSHM-------------GVPRVWekiMERIQE--VAAQSgFIRRKMLLw 382
Cdd:cd05914 108 MLTYRNiVSNVDGVKEVVllgkgdkilsilPLHHIypltftlllpllnGAHVVF---LDKIPSakIIALA-FAQVTPTL- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 383 AMSVTLE-----QNLTCPSNDLKPFTSRLADYLVLARVRQALgFAKCQKNFYGA--------APMTAETQRFFLGLNIRL 449
Cdd:cd05914 183 GVPVPLViekifKMDIIPKLTLKKFKFKLAKKINNRKIRKLA-FKKVHEAFGGNikefviggAKINPDVEEFLRTIGFPY 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 450 YAGYGLSEsTGPHFMSSPYN-YRLYSSGRVVPGCRVKLVNQD-ADGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHT 527
Cdd:cd05914 262 TIGYGMTE-TAPIISYSPPNrIRLGSAGKVIDGVEVRIDSPDpATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHT 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794461 528 GDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIE-EAVKMELPIISsamLIGDQRKFLSML 589
Cdd:cd05914 341 GDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEaKINNMPFVLES---LVVVQEKKLVAL 400
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
145-580 |
2.68e-44 |
|
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: 165.43 E-value: 2.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 145 QMFYEALDKYGNLSALGFKrkDKWerISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 224
Cdd:cd05936 3 DLLEEAARRFPDKTALIFM--GRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 225 IYTTSSPEACQYIAHDCRANVIVVDTQkqLEKILKIWKDLPhlkavviyqepppkkmanvytmeelieLGQEVPEEALda 304
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAVS--FTDLLAAGAPLG---------------------------ERVALTPEDV-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 305 iidtqqpnqcCVLVYTSGTTGNPKGVMLSQDNgTLVNTL--REVEPTSHMGVPRVwekimeriqeVAAQS-----GFIRR 377
Cdd:cd05936 128 ----------AVLQYTSGTTGVPKGAMLTHRN-LVANALqiKAWLEDLLEGDDVV----------LAALPlfhvfGLTVA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 378 KMLLWAM--SVTLEQNLTcPSNDLK-----PFTSRLA-----DYLVLARVRQALGFAKCQKNFYGAAPMTAETQRFFLGL 445
Cdd:cd05936 187 LLLPLALgaTIVLIPRFR-PIGVLKeirkhRVTIFPGvptmyIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEEL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 446 -NIRLYAGYGLSEsTGP--HFMSSPYNYRLYSSGRVVPGCRVKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDKTHE 517
Cdd:cd05936 266 tGVPIVEGYGLTE-TSPvvAVNPLDGPRKPGSIGIPLPGTEVKIVDDDgeelPPGeVGELWVRGPQVMKGYWNRPEETAE 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794461 518 AIDsEGWLHTGDMGRLDDDGFLYITGRLKELIItAGGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:cd05936 345 AFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGFNVYPREVEEVL-YEHPAVAEAAVVG 404
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
146-703 |
4.92e-44 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 168.28 E-value: 4.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 146 MFYEALDKYGNLSALGFK-----RKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGG 220
Cdd:PLN02614 50 VFRMSVEKYPNNPMLGRReivdgKPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 221 IVTGIYTTSSPEACQYIAHDCRANVIVVDTQKqlekILKIWKDLP----HLKAVVIYQ--EPPPKKMAN-----VYTMEE 289
Cdd:PLN02614 130 YCVPLYDTLGAGAVEFIISHSEVSIVFVEEKK----ISELFKTCPnsteYMKTVVSFGgvSREQKEEAEtfglvIYAWDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 290 LIELGQEVPEEaldaiIDTQQPNQCCVLVYTSGTTGNPKGVMLSQ----------------------------------- 334
Cdd:PLN02614 206 FLKLGEGKQYD-----LPIKKKSDICTIMYTSGTTGDPKGVMISNesivtliagvirllksanaaltvkdvylsylplah 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 335 ----------------------DNGTLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLeQNL 392
Cdd:PLN02614 281 ifdrvieecfiqhgaaigfwrgDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKF-GNM 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 393 TCPSNDLKpfTSRLADYLVLARVRQALGfAKCQKNFYGAAPMTAETQRFflglnIRLYA------GYGLSESTGPHFMSS 466
Cdd:PLN02614 360 KKGQSHVE--ASPLCDKLVFNKVKQGLG-GNVRIILSGAAPLASHVESF-----LRVVAcchvlqGYGLTESCAGTFVSL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 467 PYNYRLYSS-GRVVPGCRVKL-----VNQDADGI---GEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDG 537
Cdd:PLN02614 432 PDELDMLGTvGPPVPNVDIRLesvpeMEYDALAStprGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNG 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 538 FLYITGRLKELIITAGGENVPPVPIEEaVKMELPIISSAMLIGDQrkFLSMLLTLKctlNPETSEPTDNLTEQAVE---- 613
Cdd:PLN02614 511 SMKIIDRKKNIFKLSQGEYVAVENIEN-IYGEVQAVDSVWVYGNS--FESFLVAIA---NPNQQILERWAAENGVSgdyn 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 614 -FCQRVGSKASTVSEIVGQKDEavyqaihegiQRVNANAAARPYHIQKWAI-LERDFsisggeLGPTMKLKRLTVLEKYK 691
Cdd:PLN02614 585 aLCQNEKAKEFILGELVKMAKE----------KKMKGFEIIKAIHLDPVPFdMERDL------LTPTFKKKRPQLLKYYQ 648
|
650
....*....|..
gi 1958794461 692 DIIDSFYQEQKQ 703
Cdd:PLN02614 649 SVIDEMYKTTNE 660
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
170-580 |
1.44e-43 |
|
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: 164.33 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 249
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 250 TQkQLEKILkiwkdlPHLKAVVIYQEPPPKKMANVytmeeliELGQEVPEEALDAIIDTQqpNQCCVLVYTSGTTGNPKG 329
Cdd:cd05904 112 AE-LAEKLA------SLALPVVLLDSAEFDSLSFS-------DLLFEADEAEPPVVVIKQ--DDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 330 VMLSQDNgtLVNTLREVEptshmgvpRVWEKIMERIQ---------EVAAQSGFIRRKMLLWAMSVTLeqnltcPSNDLK 400
Cdd:cd05904 176 VMLTHRN--LIAMVAQFV--------AGEGSNSDSEDvflcvlpmfHIYGLSSFALGLLRLGATVVVM------PRFDLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 401 PFTSRLADY----------LVLARVRQALG----FAKCQKNFYGAAPMTAETQRFFLGL--NIRLYAGYGLSESTGP--- 461
Cdd:cd05904 240 ELLAAIERYkvthlpvvppIVLALVKSPIVdkydLSSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvam 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 462 HFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGI------GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDD 535
Cdd:cd05904 320 CFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESlppnqtGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDE 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958794461 536 DGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISSAMLIG 580
Cdd:cd05904 400 DGYLFIVDRLKEL-IKYKGFQVAPAEL-EALLLSHPEILDAAVIP 442
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
142-700 |
2.34e-42 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 163.35 E-value: 2.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 142 TVHQMFYEALDKYGNLSALGFKRKD-------KWerISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVG 214
Cdd:PLN02736 45 TLHDNFVYAVETFRDYKYLGTRIRVdgtvgeyKW--MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 215 TVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKqLEKILKIWKDLPHLKAVVIYQ-------EPPPKKMANVYTM 287
Cdd:PLN02736 123 CSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQT-LNTLLSCLSEIPSVRLIVVVGgadeplpSLPSGTGVEIVTY 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 288 EELIELGQEVPEEALdaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQ--------------------------------- 334
Cdd:PLN02736 202 SKLLAQGRSSPQPFR-----PPKPEDVATICYTSGTTGTPKGVVLTHgnlianvagsslstkfypsdvhisylplahiye 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 335 -------------------DNGTLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTlEQNLtcp 395
Cdd:PLN02736 277 rvnqivmlhygvavgfyqgDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAK-KQAL--- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 396 SNDLKPftSRLADYLVLARVRQALGfAKCQKNFYGAAPMTAETQRFflgLNI----RLYAGYGLSESTGPhfmSSPYNYR 471
Cdd:PLN02736 353 ENGKNP--SPMWDRLVFNKIKAKLG-GRVRFMSSGASPLSPDVMEF---LRIcfggRVLEGYGMTETSCV---ISGMDEG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 472 LYSSGRV---VPGCRVKLV--------NQDAD-GIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFL 539
Cdd:PLN02736 424 DNLSGHVgspNPACEVKLVdvpemnytSEDQPyPRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRL 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 540 YITGRLKELIITAGGENVPPVPIEEaVKMELPIISSAMLIGDQrkFLSMLLTLkCTLNPETSEPtdnlteqaveFCQRVG 619
Cdd:PLN02736 504 KIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKFVAQCFVYGDS--LNSSLVAV-VVVDPEVLKA----------WAASEG 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 620 SKASTVSEIVgqKDEAVYQAIHEGIQRVNANAAARPYHIQKWAILERD-FSISGGELGPTMKLKRLTVLEKYKDIIDSFY 698
Cdd:PLN02736 570 IKYEDLKQLC--NDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEpFTVENGLLTPTFKVKRPQAKAYFAKAISDMY 647
|
..
gi 1958794461 699 QE 700
Cdd:PLN02736 648 AE 649
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
142-564 |
1.23e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 159.59 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 142 TVHQMFYEALDKYGNLSALGFKRKDKweRISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWffsaVGTVFA--- 218
Cdd:PRK08315 17 TIGQLLDRTAARYPDREALVYRDQGL--RWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEW----VLTQFAtak 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 219 -GGIVTGIYTTSSPEACQYIAH--DCRANVIV--------VDTQKQLEKILKIW-------KDLPHLKAVVIYQEPPPKK 280
Cdd:PRK08315 91 iGAILVTINPAYRLSELEYALNqsGCKALIAAdgfkdsdyVAMLYELAPELATCepgqlqsARLPELRRVIFLGDEKHPG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 281 ManvYTMEELIELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDN------------------------ 336
Cdd:PRK08315 171 M---LNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNilnngyfigeamklteedrlcipv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 337 ----------GTL------------------VNTLREVEP---TSHMGVPrvwekIMeriqevaaqsgFIrrkmllwAMs 385
Cdd:PRK08315 248 plyhcfgmvlGNLacvthgatmvypgegfdpLATLAAVEEercTALYGVP-----TM-----------FI-------AE- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 386 vtLEQ------NL-----------TCPSNdlkpftsrladylVLARVRQALGfakcqknfygaapMTAETqrfflglnIr 448
Cdd:PRK08315 304 --LDHpdfarfDLsslrtgimagsPCPIE-------------VMKRVIDKMH-------------MSEVT--------I- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 449 lyaGYGLSESTGPHFMSS---PYNYRLYSSGRVVPGCRVKLVNQDADGI------GEICLWGRTIFMGYLNMEDKTHEAI 519
Cdd:PRK08315 347 ---AYGMTETSPVSTQTRtddPLEKRVTTVGRALPHLEVKIVDPETGETvprgeqGELCTRGYSVMKGYWNDPEKTAEAI 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1958794461 520 DSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEE 564
Cdd:PRK08315 424 DADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIEE 467
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
142-699 |
4.94e-40 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 156.51 E-value: 4.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 142 TVHQMFYEALDKYGNLSALGFKR-KD------KWEriSYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVG 214
Cdd:PLN02430 43 TAWDIFSKSVEKYPDNKMLGWRRiVDgkvgpyMWK--TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 215 TVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKQLEKILKIWKDLPHLKAVVIYQEPPPK---KMANV----YTM 287
Cdd:PLN02430 121 CAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLKAIVSFTSVTEEesdKASQIgvktYSW 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 288 EELIELGQEVPEEaldaiIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNGTL---------------------------- 339
Cdd:PLN02430 201 IDFLHMGKENPSE-----TNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATfvrgvdlfmeqfedkmthddvylsflpl 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 340 -------------------------VNTLR----EVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKM--------LLW 382
Cdd:PLN02430 276 ahildrmieeyffrkgasvgyyhgdLNALRddlmELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIfnalykykLAW 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 383 amsvtleQNLTCPSNDLKPftsrLADYLVLARVRQALGfAKCQKNFYGAAPMTAETQRFflgLNIR----LYAGYGLSES 458
Cdd:PLN02430 356 -------MNRGYSHKKASP----MADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEF---LRVTscafVVQGYGLTET 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 459 TGPHFMSSPYNYRLYSSGRVVPGC---RVKLVNQ---DADG---IGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGD 529
Cdd:PLN02430 421 LGPTTLGFPDEMCMLGTVGAPAVYnelRLEEVPEmgyDPLGeppRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGD 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 530 MGRLDDDGFLYITGRLKELIITAGGENVpPVPIEEAVKMELPIISSAMLIGDQrkFLSMLLTLkCTLNPETSEP---TDN 606
Cdd:PLN02430 500 IGEILPNGVLKIIDRKKNLIKLSQGEYV-ALEYLENVYGQNPIVEDIWVYGDS--FKSMLVAV-VVPNEENTNKwakDNG 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 607 LTEQAVEFCQRVGSKASTVSEivgqkdeavyqaihegIQRVNANAAARPYHIQKWAILE-RDFSISGGELGPTMKLKRLT 685
Cdd:PLN02430 576 FTGSFEELCSLPELKEHILSE----------------LKSTAEKNKLRGFEYIKGVILEtKPFDVERDLVTATLKKRRNN 639
|
650
....*....|....
gi 1958794461 686 VLEKYKDIIDSFYQ 699
Cdd:PLN02430 640 LLKYYQVEIDEMYR 653
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
145-702 |
8.27e-39 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 153.07 E-value: 8.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 145 QMFYEALDKYGNLSALGFK-----RKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG 219
Cdd:PLN02861 47 QFFSDAVKKYPNNQMLGRRqvtdsKVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 220 GIVTGIYTTSSPEACQYIAHDCRANVIVVdtqkQLEKILKIWKDLP----HLKAVVIY-------QEPPPKKMANVYTME 288
Cdd:PLN02861 127 ITYVPLYDTLGANAVEFIINHAEVSIAFV----QESKISSILSCLPkcssNLKTIVSFgdvsseqKEEAEELGVSCFSWE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 289 ELIELGQevpeeaLDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQ---------------------------------- 334
Cdd:PLN02861 203 EFSLMGS------LDCELPPKQKTDICTIMYTSGTTGEPKGVILTNraiiaevlstdhllkvtdrvateedsyfsylpla 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 335 -----------------------DNGTLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLeQN 391
Cdd:PLN02861 277 hvydqvietyciskgasigfwqgDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKL-GN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 392 LT--CPSNDLKPFTSRLadylVLARVRQALGfAKCQKNFYGAAPMTAETQRFFLGLNIR-LYAGYGLSESTGPHFMSSPY 468
Cdd:PLN02861 356 LRkgLKQEEASPRLDRL----VFDKIKEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCGGCFTSIAN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 469 NYRLYSS-GRVVPGCRVKLVNQDADGI--------GEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFL 539
Cdd:PLN02861 431 VFSMVGTvGVPMTTIEARLESVPEMGYdalsdvprGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAM 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 540 YITGRLKELIITAGGENVpPVPIEEAVKMELPIISSAMLIGDQrkFLSMLLTLkctLNPEtseptdnltEQAVEFCQRVG 619
Cdd:PLN02861 510 KIIDRKKNIFKLSQGEYV-AVENLENTYSRCPLIASIWVYGNS--FESFLVAV---VVPD---------RQALEDWAANN 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 620 SKASTVSEIVgqKDEAVYQAIHEGIQRVNANAAARPYHIQKWAILERD-FSISGGELGPTMKLKRLTVLEKYKDIIDSFY 698
Cdd:PLN02861 575 NKTGDFKSLC--KNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNpFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
....
gi 1958794461 699 QEQK 702
Cdd:PLN02861 653 SEAK 656
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
145-580 |
1.10e-37 |
|
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: 147.67 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 145 QMFYeALDKYGNLS-ALGFKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVt 223
Cdd:cd17642 19 QLHK-AMKRYASVPgTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGV- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 224 giyttsSPEACQYIAHDCRANV------IVVDTQKQLEKILKIWKDLPHLKAVVI---------YQEpppkkmanvytME 288
Cdd:cd17642 97 ------APTNDIYNERELDHSLniskptIVFCSKKGLQKVLNVQKKLKIIKTIIIldskedykgYQC-----------LY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 289 ELIELGQEVPEEALDAIIDT-QQPNQCCVLVYTSGTTGNPKGVMLSQDNgtLVNTLreveptSHMGVPRVWEKIMER--- 364
Cdd:cd17642 160 TFITQNLPPGFNEYDFKPPSfDRDEQVALIMNSSGSTGLPKGVQLTHKN--IVARF------SHARDPIFGNQIIPDtai 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 365 IQEVAAQSGFirrkmllwAMSVTLeQNLTC-------PSNDLKPFTSRLADYLVLARVRQALGFAKCQK----NFY---- 429
Cdd:cd17642 232 LTVIPFHHGF--------GMFTTL-GYLICgfrvvlmYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKstlvDKYdlsn 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 430 ------GAAPMTAET-----QRFflGLN-IRlyAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGI--- 494
Cdd:cd17642 303 lheiasGGAPLSKEVgeavaKRF--KLPgIR--QGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTlgp 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 495 ---GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIeEAVKMELP 571
Cdd:cd17642 379 nerGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSL-IKYKGYQVPPAEL-ESILLQHP 456
|
....*....
gi 1958794461 572 IISSAMLIG 580
Cdd:cd17642 457 KIFDAGVAG 465
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
169-566 |
1.44e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 145.51 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 248
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DTqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealdaiidtqqpnqcCVLVYTSGTTGNPK 328
Cdd:cd05934 82 DP----------------------------------------------------------------ASILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 329 GVMLSQDNGTL-------VNTLRE------VEPTSHMG------VPRVWEKIMERIQEVAAQSGF---IRRKMLLWA--- 383
Cdd:cd05934 98 GVVITHANLTFagyysarRFGLGEddvyltVLPLFHINaqavsvLAALSVGATLVLLPRFSASRFwsdVRRYGATVTnyl 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 384 ---MSVTLEQnltcpsndlkPFTSRLADylvlARVRQAlgfakcqknfYGAAPMTAETQRFFLGLNIRLYAGYGLSESTG 460
Cdd:cd05934 178 gamLSYLLAQ----------PPSPDDRA----HRLRAA----------YGAPNPPELHEEFEERFGVRLLEGYGMTETIV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 461 PhFMSSPYNYRLYSS-GRVVPGCRVKLVNQD----ADG-IGEICL---WGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMG 531
Cdd:cd05934 234 G-VIGPRDEPRRPGSiGRPAPGYEVRIVDDDgqelPAGePGELVIrglRGWGFFKGYYNMPEATAEAM-RNGWFHTGDLG 311
|
410 420 430
....*....|....*....|....*....|....*
gi 1958794461 532 RLDDDGFLYITGRLKELiITAGGENVPPVPIEEAV 566
Cdd:cd05934 312 YRDADGFFYFVDRKKDM-IRRRGENISSAEVERAI 345
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
132-564 |
1.60e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 147.61 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 132 LEPFCTQlpyTVHQMFYEALDKYGNLSALGFKRKDKweRISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFS 211
Cdd:PRK12583 12 DKPLLTQ---TIGDAFDATVARFPDREALVVRHQAL--RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 212 AVGTVFAGGIVTGIYTTSSPEACQY-IAH-DCRAnVIVVDTQKQ------LEKILK----------IWKDLPHLKAVVIY 273
Cdd:PRK12583 87 QFATARIGAILVNINPAYRASELEYaLGQsGVRW-VICADAFKTsdyhamLQELLPglaegqpgalACERLPELRGVVSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 274 QEPPPKKMANvytMEELIELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDN----------------- 336
Cdd:PRK12583 166 APAPPPGFLA---WHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNilnngyfvaeslglteh 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 337 -------------GTLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQsgfirRKMLLWAMSVTLEQNLTCPSndlkpft 403
Cdd:PRK12583 243 drlcvpvplyhcfGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEE-----RCTALYGVPTMFIAELDHPQ------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 404 srladylvlarvRQALGFAKCQKNFYGAAPMTAETQRFFLG-LNI-RLYAGYGLSESTGPHFMSS---PYNYRLYSSGRV 478
Cdd:PRK12583 311 ------------RGNFDLSSLRTGIMAGAPCPIEVMRRVMDeMHMaEVQIAYGMTETSPVSLQTTaadDLERRVETVGRT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 479 VPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIIT 551
Cdd:PRK12583 379 QPHLEVKVV--DPDGatvprgeIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIR 456
|
490
....*....|...
gi 1958794461 552 aGGENVPPVPIEE 564
Cdd:PRK12583 457 -GGENIYPREIEE 468
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
170-580 |
1.70e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 147.05 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQyyLIAR--KVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 247
Cdd:PRK06188 37 RLTYGQ--LADRisRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 248 VDTQKQLEKILKIWKDLPHLKAVViyqepppkKMANVYTMEELIELGQEVPEEALDAIIDTQQPNqccVLVYTSGTTGNP 327
Cdd:PRK06188 115 VDPAPFVERALALLARVPSLKHVL--------TLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIA---GLAYTGGTTGKP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 328 KGVMLSQDNGTLVNTL----RE---------VEPTSHMGVPRVWEKIMeRIQEVAAQSGF--------IRRKMLLWAMSV 386
Cdd:PRK06188 184 KGVMGTHRSIATMAQIqlaeWEwpadprflmCTPLSHAGGAFFLPTLL-RGGTVIVLAKFdpaevlraIEEQRITATFLV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 387 tleqnltcPSndlkpFTSRLADYlvlARVRQAlGFAKCQKNFYGAAPMT----AET-QRF---FLGLnirlyagYGLSE- 457
Cdd:PRK06188 263 --------PT-----MIYALLDH---PDLRTR-DLSSLETVYYGASPMSpvrlAEAiERFgpiFAQY-------YGQTEa 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 458 -------STGPHFMSSPYnyRLYSSGRVVPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTHEAIdSEG 523
Cdd:PRK06188 319 pmvitylRKRDHDPDDPK--RLTSCGRPTPGLRVALL--DEDGrevaqgeVGEICVRGPLVMDGYWNRPEETAEAF-RDG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794461 524 WLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:PRK06188 394 WLHTGDVAREDEDGFYYIVDRKKDMIVT-GGFNVFPREVEDVL-AEHPAVAQVAVIG 448
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
138-580 |
2.33e-37 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 148.18 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 138 QLPYTVHQMFYEALDKYGNLSALGF----KRKDKWERISYYQyyLIAR--KVAKGFLKLGLERAHSVAILGFNSPEwffs 211
Cdd:PRK07529 22 DLPASTYELLSRAAARHPDAPALSFlldaDPLDRPETWTYAE--LLADvtRTANLLHSLGVGPGDVVAFLLPNLPE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 212 AVGTVFAG---GIVTGIYTTSSPEAcqyIAHDCR-ANVIVVDTQKQLEKIlKIWKD-------LPHLKAVVIY----QEP 276
Cdd:PRK07529 96 THFALWGGeaaGIANPINPLLEPEQ---IAELLRaAGAKVLVTLGPFPGT-DIWQKvaevlaaLPELRTVVEVdlarYLP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 277 PPKKMAnvytmEELIELGQEVPEEALDAIIDTQQ-----------PNQCCVLVYTSGTTGNPKGVMLSQDN----GTLVN 341
Cdd:PRK07529 172 GPKRLA-----VPLIRRKAHARILDFDAELARQPgdrlfsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGNevanAWLGA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 342 TLREVEPTS---------HMG-----------------------------VPRVWeKIMERIQeVAAQSGfirrkmLLWA 383
Cdd:PRK07529 247 LLLGLGPGDtvfcglplfHVNallvtglaplargahvvlatpqgyrgpgvIANFW-KIVERYR-INFLSG------VPTV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 384 MSVTLEqnltCPSNdlkpftsrladylvlARVRQALGFAKCqknfyGAAPMTAETQRFFLG-LNIRLYAGYGLSESTGPH 462
Cdd:PRK07529 319 YAALLQ----VPVD---------------GHDISSLRYALC-----GAAPLPVEVFRRFEAaTGVRIVEGYGLTEATCVS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 463 FMSSPYN-YRLYSSGRVVPGCRVKLVNQDADG----------IGEICLWGRTIFMGYLNmEDKTHEAIDSEGWLHTGDMG 531
Cdd:PRK07529 375 SVNPPDGeRRIGSVGLRLPYQRVRVVILDDAGrylrdcavdeVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLG 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1958794461 532 RLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:PRK07529 454 RIDADGYFWLTGRAKDLIIR-GGHNIDPAAIEEAL-LRHPAVALAAAVG 500
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
148-615 |
7.97e-35 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 139.86 E-value: 7.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 148 YEALDKYgnlsALGfkRKDK----WE-------RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTV 216
Cdd:COG0365 12 YNCLDRH----AEG--RGDKvaliWEgedgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 217 FAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD--------TQKQLEKILKIWKDLPHLKAVVIYQEP-PPKKMANVYTM 287
Cdd:COG0365 86 RIGAVHSPVFPGFGAEALADRIEDAEAKVLITAdgglrggkVIDLKEKVDEALEELPSLEHVIVVGRTgADVPMEGDLDW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 288 EELIEL-GQEVPEEALDAiidtqqpNQCCVLVYTSGTTGNPKGVMLSQdNGTLVNTLREVEptSHMGV-P--RVWekime 363
Cdd:COG0365 166 DELLAAaSAEFEPEPTDA-------DDPLFILYTSGTTGKPKGVVHTH-GGYLVHAATTAK--YVLDLkPgdVFW----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 364 riqeVAAQSGFIrrkMLLW----------AMSVTLEQNLTCPSNDlkpftsRLADYLVLARVrqalgfakcqKNFYGAA- 432
Cdd:COG0365 231 ----CTADIGWA---TGHSyivygpllngATVVLYEGRPDFPDPG------RLWELIEKYGV----------TVFFTAPt 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 433 -----------------------------PMTAETQRFFL-GLNIRLYAGYGLSEsTGPHFMSSPYNYRLY--SSGRVVP 480
Cdd:COG0365 288 airalmkagdeplkkydlsslrllgsagePLNPEVWEWWYeAVGVPIVDGWGQTE-TGGIFISNLPGLPVKpgSMGKPVP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 481 GCRVKLVnqDADG-------IGEICL---W-GrtIFMGYLNMEDKTHEAI--DSEGWLHTGDMGRLDDDGFLYITGRLKE 547
Cdd:COG0365 367 GYDVAVV--DEDGnpvppgeEGELVIkgpWpG--MFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDD 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 548 LIITAgGENVPPVPIEEAVkMELPIISSAMLIG--DQRKFLSMLLTlkCTLNPETsEPTDNLTEQAVEFC 615
Cdd:COG0365 443 VINVS-GHRIGTAEIESAL-VSHPAVAEAAVVGvpDEIRGQVVKAF--VVLKPGV-EPSDELAKELQAHV 507
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
185-701 |
1.82e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 140.11 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 185 KGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKqLEKILKIWKD- 263
Cdd:PTZ00216 136 RGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKN-VPNLLRLMKSg 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 264 -LPHlkAVVIY--QEPPPKKMAN--VYTMEELIELGQEvpeEALDAIIDTQQPNQCCVLV-YTSGTTGNPKGVM------ 331
Cdd:PTZ00216 215 gMPN--TTIIYldSLPASVDTEGcrLVAWTDVVAKGHS---AGSHHPLNIPENNDDLALImYTSGTTGDPKGVMhthgsl 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 332 -----------------------------------LSQDN-----------G---TLVNT-------LREVEPTSHMGVP 355
Cdd:PTZ00216 290 tagilaledrlndligppeedetycsylplahimeFGVTNiflargaligfGsprTLTDTfarphgdLTEFRPVFLIGVP 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 356 RVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnltcpsndlkpFTSRLA-----------DYLVLARVRQALGfAKC 424
Cdd:PTZ00216 370 RIFDTIKKAVEAKLPPVGSLKRRVFDHA------------------YQSRLRalkegkdtpywNEKVFSAPRAVLG-GRV 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 425 QKNFYGAAPMTAETQRFF---LGLNIRlyaGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVnqDADGI------- 494
Cdd:PTZ00216 431 RAMLSGGGPLSAATQEFVnvvFGMVIQ---GWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLL--DTEEYkhtdtpe 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 495 --GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENvppVPIE--EAVKMEL 570
Cdd:PTZ00216 506 prGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEY---IALEalEALYGQN 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 571 PIISS---AMLIGDQRKFLSMLLtlkctlnpetseptdnLTEQ--AVEFCQRVGSKAsTVSEIVgqKDEAVYQAIHEGIQ 645
Cdd:PTZ00216 583 ELVVPngvCVLVHPARSYICALV----------------LTDEakAMAFAKEHGIEG-EYPAIL--KDPEFQKKATESLQ 643
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794461 646 RVNANAAARPYHIQKWA-ILERDFSISGGELGPTMKLKRLTVLEKYKDIIDSFYQEQ 701
Cdd:PTZ00216 644 ETARAAGRKSFEIVRHVrVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFADE 700
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
172-580 |
3.39e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 134.72 E-value: 3.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 172 SYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTG---IYTtsSPEAC-QYIAhdCRANVIV 247
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTanpFYT--PAEIAkQAKA--SGAKLII 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 248 vdTQKQ-LEKIlkiwKDLPHLKAVVIYQ-EPPPKKMAnvytmeELIELGQEVPEEALDAIIDtqqPNQCCVLVYTSGTTG 325
Cdd:PLN02246 128 --TQSCyVDKL----KGLAEDDGVTVVTiDDPPEGCL------HFSELTQADENELPEVEIS---PDDVVALPYSSGTTG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 326 NPKGVMLSQ-------------DNGTLVNTLREVE----PTSHM-------------GVPRVwekIMERIqEVAAQSGFI 375
Cdd:PLN02246 193 LPKGVMLTHkglvtsvaqqvdgENPNLYFHSDDVIlcvlPMFHIyslnsvllcglrvGAAIL---IMPKF-EIGALLELI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 376 RRKMLLWAMSVtleqnltcPSNDLKPFTSRLADYLVLARVRQALGfakcqknfyGAAPMTAETQRFFLGL--NIRLYAGY 453
Cdd:PLN02246 269 QRHKVTIAPFV--------PPIVLAIAKSPVVEKYDLSSIRMVLS---------GAAPLGKELEDAFRAKlpNAVLGQGY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 454 GLSEStGP------HFMSSPYNYRLYSSGRVVPGCRVKLVNQDAdGI-------GEICLWGRTIFMGYLNMEDKTHEAID 520
Cdd:PLN02246 332 GMTEA-GPvlamclAFAKEPFPVKSGSCGTVVRNAELKIVDPET-GAslprnqpGEICIRGPQIMKGYLNDPEATANTID 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 521 SEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGEnVPPVPIeEAVKMELPIISSAMLIG 580
Cdd:PLN02246 410 KDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQ-VAPAEL-EALLISHPSIADAAVVP 467
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
167-699 |
4.06e-33 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 136.01 E-value: 4.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 167 KWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVI 246
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 247 VVDtQKQLEKILKIWKDLPHLKAVVIYQEPPPK------KMAN--VYTMEELIELGQEVPEEAldaiiDTQQPNQCCVLV 318
Cdd:PLN02387 183 ICD-SKQLKKLIDISSQLETVKRVIYMDDEGVDsdsslsGSSNwtVSSFSEVEKLGKENPVDP-----DLPSPNDIAVIM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 319 YTSGTTGNPKGVMLSQDN------------------------------------------------G---TLVNT----- 342
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNivatvagvmtvvpklgkndvylaylplahilelaaesvmaavgaaigyGsplTLTDTsnkik 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 343 ------LREVEPTSHMGVPRVWEKIMERIQE-VAAQSG---------FIRRKMLL---WAMSVTLEqnltcpsndlkpft 403
Cdd:PLN02387 337 kgtkgdASALKPTLMTAVPAILDRVRDGVRKkVDAKGGlakklfdiaYKRRLAAIegsWFGAWGLE-------------- 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 404 SRLADYLVLARVRQALG----FAKCqknfyGAAPMTAETQRFflgLNIRLYA----GYGLSES-TGPHFMsspyNYRLYS 474
Cdd:PLN02387 403 KLLWDALVFKKIRAVLGgrirFMLS-----GGAPLSGDTQRF---INICLGApigqGYGLTETcAGATFS----EWDDTS 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 475 SGRV---VPGCRVKLVNQDADGI---------GEICLWGRTIFMGYLNMEDKTHEA--IDSEG--WLHTGDMGRLDDDGF 538
Cdd:PLN02387 471 VGRVgppLPCCYVKLVSWEEGGYlisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGC 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 539 LYITGRLKELIITAGGENVPPVPIEEAVkMELPIISSAMLIGDqrKFLSMLLTLKCTlnpetseptdnlTEQAVE-FCQR 617
Cdd:PLN02387 551 LEIIDRKKDIVKLQHGEYVSLGKVEAAL-SVSPYVDNIMVHAD--PFHSYCVALVVP------------SQQALEkWAKK 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 618 VGSKASTVSEIVgQKDEAVYQaIHEGIQRVNANAAARPYHI-QKWAILERDFSISGGELGPTMKLKRLTVLEKYKDIIDS 696
Cdd:PLN02387 616 AGIDYSNFAELC-EKEEAVKE-VQQSLSKAAKAARLEKFEIpAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKK 693
|
...
gi 1958794461 697 FYQ 699
Cdd:PLN02387 694 LYE 696
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
170-583 |
1.96e-32 |
|
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: 130.58 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQYYLIARKVAKGFLKLGLERAHSVAilgFNSPEWFFSAV---GTVFAGGIVTGIYTTSSPEACQYIAHDCRANVI 246
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVA---FQLPNWWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 247 VVDTqkqlekilkiwkdlphlkavviyqepppkkmanvytmeeliELGQEVPEealdaiidtQQPNQCCVLVYTSGTTGN 326
Cdd:cd05903 78 VVPE-----------------------------------------RFRQFDPA---------AMPDAVALLLFTSGTTGE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 327 PKGVMLSQdNGTLVNTLREVEptsHMGVPrvWEKIMERIQEVAAQSGFIRRKMLL----------------WAMSVTLEQ 390
Cdd:cd05903 108 PKGVMHSH-NTLSASIRQYAE---RLGLG--PGDVFLVASPMAHQTGFVYGFTLPlllgapvvlqdiwdpdKALALMREH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 391 NLTCpSNDLKPFtsrLADylvLARVRQALGFAKCQKNFYGAAPMT---AETQRFFLGLNIRLYAGYGLSEStgPHFMSS- 466
Cdd:cd05903 182 GVTF-MMGATPF---LTD---LLNAVEEAGEPLSRLRTFVCGGATvprSLARRAAELLGAKVCSAYGSTEC--PGAVTSi 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 467 ---PYNYRLYSSGRVVPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTHEAiDSEGWLHTGDMGRLDDD 536
Cdd:cd05903 253 tpaPEDRRLYTDGRPLPGVEIKVV--DDTGatlapgvEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDED 329
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1958794461 537 GFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG--DQR 583
Cdd:cd05903 330 GYLRITGRSKDIIIR-GGENIPVLEVEDLL-LGHPGVIEAAVVAlpDER 376
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
169-582 |
8.82e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 129.98 E-value: 8.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFL-KLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 247
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 248 VDTQKQlEKILKIWKdlphlkavVIYQEPPpkkmanvytmeelieLGQEVPEEALDA-IIDTQQPNQ--CCVLVYTSGTT 324
Cdd:PRK06839 106 VEKTFQ-NMALSMQK--------VSYVQRV---------------ISITSLKEIEDRkIDNFVEKNEsaSFIICYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 325 GNPKGVMLSQDNG--TLVNTLREVEPTS-----------HMG-----------------VPRVWE--KIMERIQEvaaqs 372
Cdd:PRK06839 162 GKPKGAVLTQENMfwNALNNTFAIDLTMhdrsivllplfHIGgiglfafptlfaggviiVPRKFEptKALSMIEK----- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 373 gfirrKMLLWAMSV-TLEQNLTCPSNDLKPftsrladylVLARVRQalgfakcqknFY-GAAPMTAETQRFFLGLNIRLY 450
Cdd:PRK06839 237 -----HKVTVVMGVpTIHQALINCSKFETT---------NLQSVRW----------FYnGGAPCPEELMREFIDRGFLFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 451 AGYGLSESTGPHFMSSPYNYR--LYSSGRVVPGCRVKLVNQDAD-----GIGEICLWGRTIFMGYLNMEDKTHEAIdSEG 523
Cdd:PRK06839 293 QGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIDENKNkvevgEVGELLIRGPNVMKEYWNRPDATEETI-QDG 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794461 524 WLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISSAMLIGDQ 582
Cdd:PRK06839 372 WLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQVIN-KLSDVYEVAVVGRQ 428
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
180-583 |
1.84e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 129.48 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 180 ARKVAKGFLKLGLERAHSVAilgFNSPEWF-FSAV--GTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQ-KQ-- 253
Cdd:PRK06087 59 ASRLANWLLAKGIEPGDRVA---FQLPGWCeFTIIylACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLfKQtr 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 254 -LEKILKIWKDLPHLKAVVIYQEPPPKkmANVYTMEELIELGqevpeEALDAIIDTQQPNQCCVLvYTSGTTGNPKGVML 332
Cdd:PRK06087 136 pVDLILPLQNQLPQLQQIVGVDKLAPA--TSSLSLSQIIADY-----EPLTTAITTHGDELAAVL-FTSGTEGLPKGVML 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 333 SQDNgtlvntLREVEPTSHMGVPRVWEKIMERIQEVAAQSGF---IRRKMLLWAMSVTLE-------------QNLTCpS 396
Cdd:PRK06087 208 THNN------ILASERAYCARLNLTWQDVFMMPAPLGHATGFlhgVTAPFLIGARSVLLDiftpdaclalleqQRCTC-M 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 397 NDLKPFTsrladYLVLARVRQ------ALGFAKCqknfyGAAPMTAETQRFFLGLNIRLYAGYGLSESTgPHFM---SSP 467
Cdd:PRK06087 281 LGATPFI-----YDLLNLLEKqpadlsALRFFLC-----GGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVvnlDDP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 468 YNYRLYSSGRVVPGCRVKLVNQDADGI-----GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYIT 542
Cdd:PRK06087 350 LSRFMHTDGYAAAGVEIKVVDEARKTLppgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKIT 429
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958794461 543 GRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG--DQR 583
Cdd:PRK06087 430 GRKKDIIVR-GGENISSREVEDIL-LQHPKIHDACVVAmpDER 470
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
313-582 |
4.45e-31 |
|
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: 126.79 E-value: 4.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 313 QCCVLVYTSGTTGNPKGVMLSQDNgtLVNTLREVEPTSHMGVPRVWEKIMErIQEVAAQSgfIRRKMLLWAMSVTLEQNL 392
Cdd:TIGR01923 112 QIATLMFTSGTTGKPKAVPHTFRN--HYASAVGSKENLGFTEDDNWLLSLP-LYHISGLS--ILFRWLIEGATLRIVDKF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 393 TCPSNDLKPFTSRLADyLV---LARV-RQALGFAKCQKNFYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSP- 467
Cdd:TIGR01923 187 NQLLEMIANERVTHIS-LVptqLNRLlDEGGHNENLRKILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVTTATPe 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 468 -YNYRLySSGRVVPGCRVKLVNQDADGIGEICLWGRTIFMGYLNMEDKThEAIDSEGWLHTGDMGRLDDDGFLYITGRLK 546
Cdd:TIGR01923 266 mLHARP-DVGRPLAGREIKIKVDNKEGHGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRD 343
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958794461 547 ELIITaGGENVPPVPIEEAVKmELPIISSAMLIGDQ 582
Cdd:TIGR01923 344 DLIIS-GGENIYPEEIETVLY-QHPGIQEAVVVPKP 377
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
168-567 |
5.43e-31 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 128.13 E-value: 5.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 168 WERISYYQYYLIARKVAKGFLKLGlERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEA---CQYIAHDCRAN 244
Cdd:cd05931 22 EETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 245 VIVVDTqkqlekilkiwkdlPHLKAVVIYQEPPPKKMAnvytmeelieLGQEVPEEALDAIIDTQQPNQC-----CVLVY 319
Cdd:cd05931 101 VVLTTA--------------AALAAVRAFAASRPAAGT----------PRLLVVDLLPDTSAADWPPPSPdpddiAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 320 TSGTTGNPKGVMLSQDNgtLVNTLR------EVEPTSHM----------------------GVPRVWekiMeriqevaAQ 371
Cdd:cd05931 157 TSGSTGTPKGVVVTHRN--LLANVRqirrayGLDPGDVVvswlplyhdmgligglltplysGGPSVL---M-------SP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 372 SGFIRRKML-LWAMSvtlEQNLTC---PsN---DL--KPFTSRLADYLVLARVRQALgfakcqkNfyGAAPMTAET-QRF 441
Cdd:cd05931 225 AAFLRRPLRwLRLIS---RYRATIsaaP-NfayDLcvRRVRDEDLEGLDLSSWRVAL-------N--GAEPVRPATlRRF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 442 ---FLGLNIR---LYAGYGLSEST--------GPHFMS------------------SPYNYRLYSSGRVVPGCRVKLVNQ 489
Cdd:cd05931 292 aeaFAPFGFRpeaFRPSYGLAEATlfvsggppGTGPVVlrvdrdalagravavaadDPAARELVSCGRPLPDQEVRIVDP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 490 D------ADGIGEICLWGRTIFMGYLNMEDKTHE------AIDSEGWLHTGDMGRLDDdGFLYITGRLKELIITAgGENV 557
Cdd:cd05931 372 EtgrelpDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLGFLHD-GELYITGRLKDLIIVR-GRNH 449
|
490
....*....|
gi 1958794461 558 PPVPIEEAVK 567
Cdd:cd05931 450 YPQDIEATAE 459
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
132-580 |
9.15e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 127.46 E-value: 9.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 132 LEPFCTQLPYTV-------HQMFYEALDKYGNLSALGFKRKDkwerISYYQYYLIARKVAKGFLKLGLERAHSVAILGFN 204
Cdd:PRK06710 8 LKSYPEEIPSTIsydiqplHKYVEQMASRYPEKKALHFLGKD----ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 205 SPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV-----------VDTQKQLEKIL--KIWKDLPHLKAVv 271
Cdd:PRK06710 84 CPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnVQSATKIEHVIvtRIADFLPFPKNL- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 272 IYQEPPPKKMANVYTMEE--LIELGQEVPEE---ALDAIIDTQqpNQCCVLVYTSGTTGNPKGVMLSQDNgTLVNTLrev 346
Cdd:PRK06710 163 LYPFVQKKQSNLVVKVSEseTIHLWNSVEKEvntGVEVPCDPE--NDLALLQYTGGTTGFPKGVMLTHKN-LVSNTL--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 347 eptshMGVPRVWeKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQN---LTCPSNDLK--------------PFTSRLADY 409
Cdd:PRK06710 237 -----MGVQWLY-NCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGykmVLIPKFDMKmvfeaikkhkvtlfPGAPTIYIA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 410 LVLARVRQALGFAKCQKNFYGAAPMTAETQRFFLGLNI-RLYAGYGLSEStgphfmsSPYNYRLYSSGRVVPGcRVKLVN 488
Cdd:PRK06710 311 LLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGgKLVEGYGLTES-------SPVTHSNFLWEKRVPG-SIGVPW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 489 QDADG---------------IGEICLWGRTIFMGYLNMEDKThEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIItAG 553
Cdd:PRK06710 383 PDTEAmimsletgealppgeIGEIVVKGPQIMKGYWNKPEET-AAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIV-AS 460
|
490 500
....*....|....*....|....*..
gi 1958794461 554 GENVPPVPIEEaVKMELPIISSAMLIG 580
Cdd:PRK06710 461 GFNVYPREVEE-VLYEHEKVQEVVTIG 486
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
166-616 |
3.18e-30 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 125.17 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 166 DKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANV 245
Cdd:cd05959 25 DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 246 IVVDTQ--KQLEKILKiwKDLPHLKAVVIYQEPPPKKMANVYTmeelielgQEVPEEALDAIIDTQQPNQCCVLVYTSGT 323
Cdd:cd05959 105 VVVSGElaPVLAAALT--KSEHTLVVLIVSGGAGPEAGALLLA--------ELVAAEAEQLKPAATHADDPAFWLYSSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 324 TGNPKGVMLSQDNGTLV------NTLREVEPTSHMGVPRVWekimeriqeVAAQSGfirrKMLLWAMSVtleqNLTCPSN 397
Cdd:cd05959 175 TGRPKGVVHLHADIYWTaelyarNVLGIREDDVCFSAAKLF---------FAYGLG----NSLTFPLSV----GATTVLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 398 DLKPFTSRLADYLVlaRVRQALgfakcqknFYGA----APMTAE---TQRFFLGLNIRLYAGYGLSESTGP--------- 461
Cdd:cd05959 238 PERPTPAAVFKRIR--RYRPTV--------FFGVptlyAAMLAApnlPSRDLSSLRLCVSAGEALPAEVGErwkarfgld 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 462 -----------H-FMSS-PYNYRLYSSGRVVPGCRVKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDSEg 523
Cdd:cd05959 308 ildgigstemlHiFLSNrPGRVRYGTTGKPVPGYEVELRDEDggdvADGePGELYVRGPSSATMYWNNRDKTRDTFQGE- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 524 WLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIEEAVkMELPIISSAMLIG---DQRkflsmLLTLKC--TLNP 598
Cdd:cd05959 387 WTRTGDKYVRDDDGFYTYAGRADDM-LKVSGIWVSPFEVESAL-VQHPAVLEAAVVGvedEDG-----LTKPKAfvVLRP 459
|
490
....*....|....*...
gi 1958794461 599 ETsEPTDNLTEQAVEFCQ 616
Cdd:cd05959 460 GY-EDSEALEEELKEFVK 476
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
418-613 |
6.96e-30 |
|
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: 121.43 E-value: 6.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 418 ALGFAKCqknfyGAAPMTAET-QRFFLGLNIRLYAGYGLSESTGPHFMSSPYN-YRLYSSGRVVPGCRVKLVNQDADG-- 493
Cdd:cd05944 122 SLRFAMS-----GAAPLPVELrARFEDATGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGLRLPYARVRIKVLDGVGrl 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 494 --------IGEICLWGRTIFMGYLNMEDKTHEAIDsEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEA 565
Cdd:cd05944 197 lrdcapdeVGEICVAGPGVFGGYLYTEGNKNAFVA-DGWLNTGDLGRLDADGYLFITGRAKDLIIR-GGHNIDPALIEEA 274
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958794461 566 VkMELPIISSAMLIGDQRKFLSMLLTLKCTLNPETSEPTDNLTEQAVE 613
Cdd:cd05944 275 L-LRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARD 321
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
171-580 |
6.04e-29 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 121.27 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 171 ISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDT 250
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 251 QKqlekilkiwkDLPHLKAVVIYQePPPKKMANVYTMEELI----ELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGN 326
Cdd:cd05926 95 GE----------LGPASRAASKLG-LAILELALDVGVLIRApsaeSLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 327 PKGVMLSQDNgtLVNTLREVEPTSHMGvprvwekimeriqevAAQSGFIRRKM-----LLWAMSVTLEQ--NLTCPSN-D 398
Cdd:cd05926 164 PKGVPLTHRN--LAASATNITNTYKLT---------------PDDRTLVVMPLfhvhgLVASLLSTLAAggSVVLPPRfS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 399 LKPFTSRLADY-------------LVLAR-------VRQALGFAKCqknfyGAAPMTAET----QRFFlglNIRLYAGYG 454
Cdd:cd05926 227 ASTFWPDVRDYnatwytavptihqILLNRpepnpesPPPKLRFIRS-----CSASLPPAVlealEATF---GAPVLEAYG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 455 LSESTgpHFMSS----PYNYRLYSSGRVVpGCRVKLVNQDAD-----GIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWL 525
Cdd:cd05926 299 MTEAA--HQMTSnplpPGPRKPGSVGKPV-GVEVRILDEDGEilppgVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWF 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1958794461 526 HTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISSAMLIG 580
Cdd:cd05926 376 RTGDLGYLDADGYLFLTGRIKELINR-GGEKISPLEVDG-VLLSHPAVLEAVAFG 428
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
159-580 |
8.69e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 120.45 E-value: 8.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 159 ALGFKRKDkwerISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIA 238
Cdd:PRK03640 20 AIEFEEKK----VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 239 HDCRANVIVVD---TQKQLEKILKIWKDLPhlkavviyQEPppkkmanvytmEELIELGQEVPEEALDAIIdtqqpnqcc 315
Cdd:PRK03640 96 DDAEVKCLITDddfEAKLIPGISVKFAELM--------NGP-----------KEEAEIQEEFDLDEVATIM--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 316 vlvYTSGTTGNPKGVMLSQDN------GTLVNT-LRE------VEPTSHMgvprvwekimeriqevaaqSGF-IRRKMLL 381
Cdd:PRK03640 148 ---YTSGTTGKPKGVIQTYGNhwwsavGSALNLgLTEddcwlaAVPIFHI-------------------SGLsILMRSVI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 382 WAMSVTLEQNLtcpsnDLKPFTSRLADYLV---------LARVRQALGFAKCQKNFY------GAAPMT--AETQRFflg 444
Cdd:PRK03640 206 YGMRVVLVEKF-----DAEKINKLLQTGGVtiisvvstmLQRLLERLGEGTYPSSFRcmllggGPAPKPllEQCKEK--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 445 lNIRLYAGYGLSEsTGPHFMSSPYNY---RLYSSGRVVPGCRVKLVNQDADG----IGEICLWGRTIFMGYLNMEDKTHE 517
Cdd:PRK03640 278 -GIPVYQSYGMTE-TASQIVTLSPEDaltKLGSAGKPLFPCELKIEKDGVVVppfeEGEIVVKGPNVTKGYLNREDATRE 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794461 518 AIDSeGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISSAMLIG 580
Cdd:PRK03640 356 TFQD-GWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEI-EEVLLSHPGVAEAGVVG 415
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
169-580 |
8.83e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 120.76 E-value: 8.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 248
Cdd:PRK06145 26 QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DtqKQLEKILKiwkdLPHLKAVViyqepppkKMANVYTMEELIELGQEVPEEALDAiidtqqPNQCCVLVYTSGTTGNPK 328
Cdd:PRK06145 106 D--EEFDAIVA----LETPKIVI--------DAAAQADSRRLAQGGLEIPPQAAVA------PTDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 329 GVMLSQDNG-------------TLVNTLREVEPTSHMG------VPRVWEKIMERIQ---EVAAQSGFIRRKMLL--WAM 384
Cdd:PRK06145 166 GVMHSYGNLhwksidhvialglTASERLLVVGPLYHVGafdlpgIAVLWVGGTLRIHrefDPEAVLAAIERHRLTcaWMA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 385 SVTLEQNLTCPSNDlkpftsrladylvlarvRQALG-FAKCqknfYGAAPMTAETQ-RFFLGL--NIRLYAGYGLSES-T 459
Cdd:PRK06145 246 PVMLSRVLTVPDRD-----------------RFDLDsLAWC----IGGGEKTPESRiRDFTRVftRARYIDAYGLTETcS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 460 GPHFMSSPYNY-RLYSSGRVVPGCRVKLVNQDADGI-----GEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRL 533
Cdd:PRK06145 305 GDTLMEAGREIeKIGSTGRALAHVEIRIADGAGRWLppnmkGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYL 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958794461 534 DDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:PRK06145 384 DEEGFLYLTDRKKDMIIS-GGENIASSEVERVI-YELPEVAEAAVIG 428
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
169-580 |
9.63e-29 |
|
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: 120.81 E-value: 9.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSP---EWFFSAVGtvfAGGIVTGIYTTSSPEACQYIAHDCRANV 245
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHrhlELYYAVPG---MGAVLHTINPRLFPEQIAYIINHAEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 246 IVVDtqKQLEKILKIWKD-LPHLKAVVIYQ---EPPPKKMANVYTMEELIElgQEVPEEALDAIidtqQPNQCCVLVYTS 321
Cdd:cd12119 101 VFVD--RDFLPLLEAIAPrLPTVEHVVVMTddaAMPEPAGVGVLAYEELLA--AESPEYDWPDF----DENTAAAICYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 322 GTTGNPKGVMLSQ--------------------------------------------------------DNGTLVNTLRE 345
Cdd:cd12119 173 GTTGNPKGVVYSHrslvlhamaalltdglglsesdvvlpvvpmfhvnawglpyaaamvgaklvlpgpylDPASLAELIER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 346 VEPTSHMGVPRVWEkimeriqevaaqsgfirrkMLLwamsvtleQNLTCPSNDLKPftsrladylvLARVrqALGfakcq 425
Cdd:cd12119 253 EGVTFAAGVPTVWQ-------------------GLL--------DHLEANGRDLSS----------LRRV--VIG----- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 426 knfyGAAP----MTAetqrfFLGLNIRLYAGYGLSE-------STGPHFMS-----SPYNYRLySSGRVVPGCRVKLVNQ 489
Cdd:cd12119 289 ----GSAVprslIEA-----FEERGVRVIHAWGMTEtsplgtvARPPSEHSnlsedEQLALRA-KQGRPVPGVELRIVDD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 490 D-----ADG--IGEICLWGRTIFMGYLNMEDKThEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPI 562
Cdd:cd12119 359 DgrelpWDGkaVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKDV-IKSGGEWISSVEL 436
|
490
....*....|....*...
gi 1958794461 563 EEAVkMELPIISSAMLIG 580
Cdd:cd12119 437 ENAI-MAHPAVAEAAVIG 453
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
435-615 |
4.92e-28 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 115.44 E-value: 4.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 435 TAET-QRFFLGLNIRLYAGYGLSESTGPHFMSsPYNYRLYSSGRVVPGCRVKLVNQD-----ADGIGEICLWGRTIFMGY 508
Cdd:cd17637 124 APETiQRFEETTGATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVDDNdrpvpAGETGEIVVRGPLVFQGY 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 509 LNMEDKTHEAIDsEGWLHTGDMGRLDDDGFLYITGRL--KELIITaGGENVPPVPIEEAVkMELPIISSAMLIGDQRKFL 586
Cdd:cd17637 203 WNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPAEVEKVI-LEHPAIAEVCVIGVPDPKW 279
|
170 180 190
....*....|....*....|....*....|
gi 1958794461 587 SMLLTLKCTLNPETSeptdnLTEQAV-EFC 615
Cdd:cd17637 280 GEGIKAVCVLKPGAT-----LTADELiEFV 304
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
169-580 |
5.81e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 118.50 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 248
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DTQ--KQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVytmeelIELGQEVPEEALDAIIDTQQPNQccvLVYTSGTTGN 326
Cdd:PRK08316 115 DPAlaPTAEAALALLPVDTLILSLVLGGREAPGGWLDF------ADWAEAGSVAEPDVELADDDLAQ---ILYTSGTESL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 327 PKGVMLSQD-----------------NGTLVNTLrevePTSH---MGV---PRVW-------------EKIMERIQEVAA 370
Cdd:PRK08316 186 PKGAMLTHRaliaeyvscivagdmsaDDIPLHAL----PLYHcaqLDVflgPYLYvgatnvildapdpELILRTIEAERI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 371 QSGFIrrKMLLWamsVTLeqnLTCPSNDlkpfTSRLadylvlarvrQALgfakcQKNFYGAAPMTAE-----TQRFflgL 445
Cdd:PRK08316 262 TSFFA--PPTVW---ISL---LRHPDFD----TRDL----------SSL-----RKGYYGASIMPVEvlkelRERL---P 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 446 NIRLYAGYGLSEsTGP-HFMSSPYNY--RLYSSGRVVPGCRVKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDKTHE 517
Cdd:PRK08316 312 GLRFYNCYGQTE-IAPlATVLGPEEHlrRPGSAGRPVLNVETRVVDDDgndvAPGeVGEIVHRSPQLMLGYWDDPEKTAE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794461 518 AIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:PRK08316 391 AF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKT-GGENVASREVEEAL-YTHPAVAEVAVIG 450
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
316-580 |
6.80e-28 |
|
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: 116.68 E-value: 6.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 316 VLVYTSGTTGNPKGVMLSQDN------GTLVNT-LRE------VEPTSHMgvprvwekimeriqevaaqSGF-IRRKMLL 381
Cdd:cd05912 81 TIMYTSGTTGKPKGVQQTFGNhwwsaiGSALNLgLTEddnwlcALPLFHI-------------------SGLsILMRSVI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 382 WAMSVTLEQNLtcpsnDLKPFTSRLADYLV---------LARVRQALGfAKCQKNF----YGAAPMTAETQRFFLGLNIR 448
Cdd:cd05912 142 YGMTVYLVDKF-----DAEQVLHLINSGKVtiisvvptmLQRLLEILG-EGYPNNLrcilLGGGPAPKPLLEQCKEKGIP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 449 LYAGYGLSEsTGPHFMSSPYNY---RLYSSGRVVPGCRVKLVN--QDADGIGEICLWGRTIFMGYLNMEDKTHEAIDSeG 523
Cdd:cd05912 216 VYQSYGMTE-TCSQIVTLSPEDalnKIGSAGKPLFPVELKIEDdgQPPYEVGEILLKGPNVTKGYLNRPDATEESFEN-G 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794461 524 WLHTGDMGRLDDDGFLYITGRLKELIItAGGENVPPVPIEEAVKmELPIISSAMLIG 580
Cdd:cd05912 294 WFKTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEVLL-SHPAIKEAGVVG 348
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
142-580 |
1.95e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 117.09 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 142 TVHQMFYEALDKYGNLSALGFK-RKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGG 220
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALIFEsSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 221 IVTGIYTTSSPEACQYIAHDCRANVIVVDtqkqlEKILKIWKDLPH-----LKAVVIYQEPPPKkMANVYTMEEL----- 290
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTS-----AQFYPMYRQIQQedatpLRHICLTRVALPA-DDGVSSFTQLkaqqp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 291 IELGQEVPEEALD-AIIdtqqpnqccvlVYTSGTTGNPKGVMLSQDN-------GTLVNTLRE------VEPTSHMGvpr 356
Cdd:PRK08008 162 ATLCYAPPLSTDDtAEI-----------LFTSGTTSRPKGVVITHYNlrfagyySAWQCALRDddvyltVMPAFHID--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 357 vwekimerIQEVAAQSGFIrrkmlLWAMSVTLEQNltcpsnDLKPFTSRLADYLvlARVRQALgfakcqknfygaaPM-- 434
Cdd:PRK08008 228 --------CQCTAAMAAFS-----AGATFVLLEKY------SARAFWGQVCKYR--ATITECI-------------PMmi 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 435 -------TAETQR--------FFLGL------------NIRLYAGYGLSESTGPHFMSSPYNYRLYSS-GRVVPGCRVKL 486
Cdd:PRK08008 274 rtlmvqpPSANDRqhclrevmFYLNLsdqekdafeerfGVRLLTSYGMTETIVGIIGDRPGDKRRWPSiGRPGFCYEAEI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 487 VNQD-----ADGIGEICLWG---RTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRlKELIITAGGENVP 558
Cdd:PRK08008 354 RDDHnrplpAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDR-RCNMIKRGGENVS 432
|
490 500
....*....|....*....|..
gi 1958794461 559 PVPIEEAVkMELPIISSAMLIG 580
Cdd:PRK08008 433 CVELENII-ATHPKIQDIVVVG 453
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
146-584 |
2.36e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 117.41 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 146 MFYEALDKYGNLSALGFKRKdkweRISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEwffsAVGTVFA----GGI 221
Cdd:PRK05605 37 LYDNAVARFGDRPALDFFGA----TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQ----HIVAFYAvlrlGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 222 VT---GIYTTSSPEAcQYIAHDCRAnVIVVDtqKQLEKILKIWKDLPhLKAVV----IYQEPPPKKMA------NVYTME 288
Cdd:PRK05605 109 VVehnPLYTAHELEH-PFEDHGARV-AIVWD--KVAPTVERLRRTTP-LETIVsvnmIAAMPLLQRLAlrlpipALRKAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 289 EliELGQEVP-----EEALDA-------IIDTQQPNQCCV--LVYTSGTTGNPKGVMLSQDNgtLVNTLReveptshMGv 354
Cdd:PRK05605 184 A--ALTGPAPgtvpwETLVDAaiggdgsDVSHPRPTPDDValILYTSGTTGKPKGAQLTHRN--LFANAA-------QG- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 355 pRVWEKIMERIQEV----------------AAQSGFIRRKMLLWA---MSVTLEQNLTCPSNDLkPFTSRLADYLVLARV 415
Cdd:PRK05605 252 -KAWVPGLGDGPERvlaalpmfhaygltlcLTLAVSIGGELVLLPapdIDLILDAMKKHPPTWL-PGVPPLYEKIAEAAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 416 RQALGFAKCQKNFYGAAPMTAETQRFFLGL-NIRLYAGYGLSEsTGPHFMSSPYN--YRLYSSGRVVPGCRVKLVNQD-- 490
Cdd:PRK05605 330 ERGVDLSGVRNAFSGAMALPVSTVELWEKLtGGLLVEGYGLTE-TSPIIVGNPMSddRRPGYVGVPFPDTEVRIVDPEdp 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 491 ----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEA 565
Cdd:PRK05605 409 detmPDGeEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEEV 486
|
490
....*....|....*....
gi 1958794461 566 VKmELPIISSAMLIGDQRK 584
Cdd:PRK05605 487 LR-EHPGVEDAAVVGLPRE 504
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
315-565 |
2.75e-27 |
|
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: 113.19 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 315 CVLVYTSGTTGNPKGVMLSQDNGT------------------LVNTlrevePTSHM-GVPRVWekimeRIQEVAAQSGFI 375
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLasaaglhsrlgfgggdswLLSL-----PLYHVgGLAILV-----RSLLAGAELVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 376 RRKmllWAMSVTLEQNLTCpsndlkpFTSrladyLV---LARVRQALGFAKCQKNF----YGAAPMTAETQRFFLGLNIR 448
Cdd:cd17630 73 ERN---QALAEDLAPPGVT-------HVS-----LVptqLQRLLDSGQGPAALKSLravlLGGAPIPPELLERAADRGIP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 449 LYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQdadgiGEICLWGRTIFMGYLNMEdkTHEAIDSEGWLHTG 528
Cdd:cd17630 138 LYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----GEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTK 210
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958794461 529 DMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEA 565
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAA 246
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
311-580 |
6.64e-27 |
|
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: 112.76 E-value: 6.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 311 PNQCCVLVYTSGTTGNPKGVMLSQDN----------------------------------GTL----------------- 339
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNivnngyfigerlglteqdrlcipvplfhcfgsvlGVLaclthgatmvfpspsfd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 340 -VNTLREVEP---TSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnlTCPSNdlkpftsrladylVLARV 415
Cdd:cd05917 81 pLAVLEAIEKekcTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGA---------PCPPE-------------LMKRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 416 RQALGFAKCQknfygaapmtaetqrfflglnirlyAGYGLSESTGPHFMSS---PYNYRLYSSGRVVPGCRVKLVNQDAD 492
Cdd:cd05917 139 IEVMNMKDVT-------------------------IAYGMTETSPVSTQTRtddSIEKRVNTVGRIMPHTEAKIVDPEGG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 493 GI------GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAV 566
Cdd:cd05917 194 IVppvgvpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENIYPREIEEFL 272
|
330
....*....|....
gi 1958794461 567 kMELPIISSAMLIG 580
Cdd:cd05917 273 -HTHPKVSDVQVVG 285
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
168-700 |
1.81e-26 |
|
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: 114.45 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 168 WERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG---GIVTGIYTTSSPE--ACQYIAHDCR 242
Cdd:cd05921 23 WRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGvpaAPVSPAYSLMSQDlaKLKHLFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 243 ANVIVVDTQKQLEKILKIwKDLPHLKAVVIYQEPPPKkmaNVYTMEELIElgqEVPEEALDAIIDTQQPNQCCVLVYTSG 322
Cdd:cd05921 103 PGLVFAQDAAPFARALAA-IFPLGTPLVVSRNAVAGR---GAISFAELAA---TPPTAAVDAAFAAVGPDTVAKFLFTSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 323 TTGNPKGV------------MLSQ---------------------------------DNGTL---------------VNT 342
Cdd:cd05921 176 STGLPKAVintqrmlcanqaMLEQtypffgeeppvlvdwlpwnhtfggnhnfnlvlyNGGTLyiddgkpmpggfeetLRN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 343 LREVEPTSHMGVPRVWEKI---MERiQEVAAQSGFIRRKMLLWAmSVTLEQNltcpsndlkpftsrladylVLARVrQAL 419
Cdd:cd05921 256 LREISPTVYFNVPAGWEMLvaaLEK-DEALRRRFFKRLKLMFYA-GAGLSQD-------------------VWDRL-QAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 420 GFAKCqknfygaapmtaetqrfflGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVnqDADGIGEICL 499
Cdd:cd05921 314 AVATV-------------------GERIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV--PSGGKYEVRV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 500 WGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDD-----GfLYITGRLKELIITAGGENVPPVPIE-EAVKMELPII 573
Cdd:cd05921 373 KGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADPddpakG-LVFDGRVAEDFKLASGTWVSVGPLRaRAVAACAPLV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 574 SSAMLIGDQRKFLSMLLTLkctlnpetseptdNLTEqavefCQR-VGSKASTVSEIVgqKDEAVYQAIHEGIQRVNANAA 652
Cdd:cd05921 452 HDAVVAGEDRAEVGALVFP-------------DLLA-----CRRlVGLQEASDAEVL--RHAKVRAAFRDRLAALNGEAT 511
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1958794461 653 ARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKDIIDSFYQE 700
Cdd:cd05921 512 GSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
169-573 |
4.96e-26 |
|
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: 112.76 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLeRAHSVAILGFNSPEWFFSAV-GTVFAGGI-----VTGIYTTSSPEacqyIAHDCR 242
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLGL-RPGDSVILQFDDNEDFIPAFwACVLAGFVpapltVPPTYDEPNAR----LRKLRH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 243 A-----NVIVVDTQKQLEKILKIWKDLPHLKAVVIyqepppkkmanvytmeelielgqeVPEEALDAIIDT----QQPNQ 313
Cdd:cd05906 113 IwqllgSPVVLTDAELVAEFAGLETLSGLPGIRVL------------------------SIEELLDTAADHdlpqSRPDD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 314 CCVLVYTSGTTGNPKGVMLSQDN------GTLVN---TLREVE----PTSHMGVprvwekIME--------RIQEVAAQS 372
Cdd:cd05906 169 LALLMLTSGSTGFPKAVPLTHRNilarsaGKIQHnglTPQDVFlnwvPLDHVGG------LVElhlravylGCQQVHVPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 373 GFIRRKMLLW-------AMSVTLEQN--LTCPSNDLKPFTSRLADylvLARVRQALGfakcqknfyGAAPMTAETQRFFL 443
Cdd:cd05906 243 EEILADPLRWldlidryRVTITWAPNfaFALLNDLLEEIEDGTWD---LSSLRYLVN---------AGEAVVAKTIRRLL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 444 ------GLNIR-LYAGYGLSES-TGPHFMSSPYNY------RLYSSGRVVPGCRVKLVNQDADG-----IGEICLWGRTI 504
Cdd:cd05906 311 rllepyGLPPDaIRPAFGMTETcSGVIYSRSFPTYdhsqalEFVSLGRPIPGVSMRIVDDEGQLlpegeVGRLQVRGPVV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794461 505 FMGYLNMEDKTHEAIDSEGWLHTGDMGRLdDDGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPII 573
Cdd:cd05906 391 TKGYYNNPEANAEAFTEDGWFRTGDLGFL-DNGNLTITGRTKDTIIV-NGVNYYSHEIEAAVE-EVPGV 456
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
181-579 |
8.39e-26 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 112.38 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 181 RKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDtQKQLEKILKI 260
Cdd:PLN02330 66 RRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN-DTNYGKVKGL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 261 wkDLPhlkaVVIYQEpppKKMANVYTMEELIELGQEVPEEALDAIIdtqQPNQCCVLVYTSGTTGNPKGVMLSQDN--GT 338
Cdd:PLN02330 145 --GLP----VIVLGE---EKIEGAVNWKELLEAADRAGDTSDNEEI---LQTDLCALPFSSGTTGISKGVMLTHRNlvAN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 339 LVNTLREVEPTS-------------HM-GVPRVWEKIMERIQEVAAQSGFIRRKML--LWAMSVTLEQnlTCPSNDLKPF 402
Cdd:PLN02330 213 LCSSLFSVGPEMigqvvtlglipffHIyGITGICCATLRNKGKVVVMSRFELRTFLnaLITQEVSFAP--IVPPIILNLV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 403 TSRLADYLVLARVrqalgfaKCQKNFYGAAPMTAETQRFFLGL--NIRLYAGYGLSES---TGPHfmSSPYN----YRLY 473
Cdd:PLN02330 291 KNPIVEEFDLSKL-------KLQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHsciTLTH--GDPEKghgiAKKN 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 474 SSGRVVPGCRVKLVNQDA------DGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKE 547
Cdd:PLN02330 362 SVGFILPNLEVKFIDPDTgrslpkNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKE 441
|
410 420 430
....*....|....*....|....*....|..
gi 1958794461 548 LIITAGGEnVPPVPIeEAVKMELPIISSAMLI 579
Cdd:PLN02330 442 LIKYKGFQ-VAPAEL-EAILLTHPSVEDAAVV 471
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
315-580 |
8.49e-26 |
|
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: 110.84 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 315 CVLVYTSGTTGNPKGVMLSQDN-GTLVNTLRE------------VEPTSHM-GV------PRVWEKIMERIQEVAAQSGF 374
Cdd:cd05941 92 ALILYTSGTTGRPKGVVLTHANlAANVRALVDawrwteddvllhVLPLHHVhGLvnallcPLFAGASVEFLPKFDPKEVA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 375 IRRkmllWAMSVTLeqnltcpsndlkpFT------SRLADYLVLARVRQALGFAKCQKNFY----GAAPMTAETQRFFLG 444
Cdd:cd05941 172 ISR----LMPSITV-------------FMgvptiyTRLLQYYEAHFTDPQFARAAAAERLRlmvsGSAALPVPTLEEWEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 445 LN-IRLYAGYGLSEsTGphfM--SSPYN--YRLYSSGRVVPGCRVKLVNQ------DADGIGEICLWGRTIFMGYLNMED 513
Cdd:cd05941 235 ITgHTLLERYGMTE-IG---MalSNPLDgeRRPGTVGMPLPGVQARIVDEetgeplPRGEVGEIQVRGPSVFKEYWNKPE 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794461 514 KTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:cd05941 311 ATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVL-LAHPGVSECAVIG 376
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
170-566 |
9.51e-26 |
|
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: 111.24 E-value: 9.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 249
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 250 TQKQLEKILKIWKDlphlkavviyqEPPPkkmanvytmeelielgqEVPEEALDAIidtqqpnqccVLVYTSGTTGNPKG 329
Cdd:cd12118 109 REFEYEDLLAEGDP-----------DFEW-----------------IPPADEWDPI----------ALNYTSGTTGRPKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 330 VMLSQdNGTLVNTLREVEpTSHMGVPRV--WEKIMER------IQEVAAQSG--FIRRKM---LLWAM----SVT----- 387
Cdd:cd12118 151 VVYHH-RGAYLNALANIL-EWEMKQHPVylWTLPMFHcngwcfPWTVAAVGGtnVCLRKVdakAIYDLiekhKVThfcga 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 388 ---LEQNLTCPSNDLKPFTsrladylvlARVRQALGfakcqknfyGAAP---MTAETQRfflgLNIRLYAGYGLSESTGP 461
Cdd:cd12118 229 ptvLNMLANAPPSDARPLP---------HRVHVMTA---------GAPPpaaVLAKMEE----LGFDVTHVYGLTETYGP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 462 HF----------MSSPYNYRLYS-SG---------RVVPGCRVKLVNQDADGIGEICLWGRTIFMGYLNMEDKTHEAIdS 521
Cdd:cd12118 287 ATvcawkpewdeLPTEERARLKArQGvryvgleevDVLDPETMKPVPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-R 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958794461 522 EGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAV 566
Cdd:cd12118 366 GGWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEGVL 409
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
169-583 |
1.78e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 108.22 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAilgFNSPEWF-FSAVgtVFAG---GIVTG----IYTTSspEACQYIAHd 240
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVS---CQLPNWWeFTVL--YLACsriGAVLNplmpIFRER--ELSFMLKH- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 241 CRANVIVV-------DTQKQLEKILKiwkDLPHLKAVVIYQEPPPKKMANVytmeeLIELGQEVpEEALDAIIDTQQ--P 311
Cdd:PRK13295 126 AESKVLVVpktfrgfDHAAMARRLRP---ELPALRHVVVVGGDGADSFEAL-----LITPAWEQ-EPDAPAILARLRpgP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 312 NQCCVLVYTSGTTGNPKGVMLSQDngTLVNTLREV---------------EPTSH-------MGVPRVWEK--IMERIQE 367
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTAN--TLMANIVPYaerlglgaddvilmaSPMAHqtgfmygLMMPVMLGAtaVLQDIWD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 368 VAAQSGFIRRKMLLWAMSVTleqnltcpsndlkPFtsrLADylvLARVRQALGFAKCQ-KNFY--GAA--PMTAETQRFF 442
Cdd:PRK13295 275 PARAAELIRTEGVTFTMAST-------------PF---LTD---LTRAVKESGRPVSSlRTFLcaGAPipGALVERARAA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 443 LGLNIrlYAGYGLSES---TGpHFMSSPYNYRLYSSGRVVPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNME 512
Cdd:PRK13295 336 LGAKI--VSAWGMTENgavTL-TKLDDPDERASTTDGCPLPGVEVRVV--DADGaplpagqIGRLQVRGCSNFGGYLKRP 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794461 513 DKTheAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISSAMLIG--DQR 583
Cdd:PRK13295 411 QLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEI-EALLYRHPAIAQVAIVAypDER 479
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
287-583 |
2.90e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 106.81 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 287 MEELIELGQEVPEEALD--AIIDTQQPNqccVLVYTSGTTGNPKGVMLSQDN--GTLVN--TLREVEPTSHMGVPRVWEK 360
Cdd:PRK09088 111 VEDLAAFIASADALEPAdtPSIPPERVS---LILFTSGTSGQPKGVMLSERNlqQTAHNfgVLGRVDAHSSFLCDAPMFH 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 361 IMERIQEVaaqsgfirRKMLLWAMSVTLeqnltcpSNDLKPFTS--RLAD-------YLVLARVRQAL----GFAKCQKN 427
Cdd:PRK09088 188 IIGLITSV--------RPVLAVGGSILV-------SNGFEPKRTlgRLGDpalgithYFCVPQMAQAFraqpGFDAAALR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 428 -----FYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMS---SPYNYRLYSSGRVVPGCRVKLVNQDADGI----- 494
Cdd:PRK09088 253 hltalFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGTVFGMSvdcDVIRAKAGAAGIPTPTVQTRVVDDQGNDCpagvp 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 495 GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIIS 574
Cdd:PRK09088 333 GELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFIS-GGENVYPAEI-EAVLADHPGIR 410
|
330
....*....|.
gi 1958794461 575 SAMLIG--DQR 583
Cdd:PRK09088 411 ECAVVGmaDAQ 421
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
142-580 |
1.17e-23 |
|
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: 105.25 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 142 TVHQMFYEALDKYGNLSALgfkrKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGI 221
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATAL----VHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 222 VTGIYTTSSPEACQYIAHDCRANVIVVdTQKQLEKILKIWKDLPHLKAVVIYQEPPPKKM----ANVYTMEELIELGQEV 297
Cdd:TIGR03098 77 FVPINPLLKAEQVAHILADCNVRLLVT-SSERLDLLHPALPGCHDLRTLIIVGDPAHASEghpgEEPASWPKLLALGDAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 298 PeeALDAIidtqQPNQCCVLvYTSGTTGNPKGVMLSQDN----GTLVNTLREVEPTshmgvprvwekimERIQEV---AA 370
Cdd:TIGR03098 156 P--PHPVI----DSDMAAIL-YTSGSTGRPKGVVLSHRNlvagAQSVATYLENRPD-------------DRLLAVlplSF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 371 QSGFirrKMLLWAM----SVTLEQNLTcPSNDLK--------------PFTSRLADYLVLARVRQALGFAkcqKNFYGAA 432
Cdd:TIGR03098 216 DYGF---NQLTTAFyvgaTVVLHDYLL-PRDVLKalekhgitglaavpPLWAQLAQLDWPESAAPSLRYL---TNSGGAM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 433 P--MTAETQRFFlgLNIRLYAGYGLSEStgphFMSS---P--YNYRLYSSGRVVPGCRVKLVNQDAD-----GIGEICLW 500
Cdd:TIGR03098 289 PraTLSRLRSFL--PNARLFLMYGLTEA----FRSTylpPeeVDRRPDSIGKAIPNAEVLVLREDGSecapgEEGELVHR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 501 GRTIFMGYLNMEDKTHEAI------DSEGWLH-----TGDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEEAVkME 569
Cdd:TIGR03098 363 GALVAMGYWNDPEKTAERFrplppfPGELHLPelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVA-YA 440
|
490
....*....|.
gi 1958794461 570 LPIISSAMLIG 580
Cdd:TIGR03098 441 TGLVAEAVAFG 451
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
279-583 |
1.38e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 105.67 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 279 KKMANVYTMEELIELGQEVPEEALDAIIDTQQP-NQCCVLVYTSGTTGNPKGVMLSqdNGTLVNTLREVEPTSHMGVPRv 357
Cdd:PRK12492 173 KKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGlDDIAVLQYTGGTTGLAKGAMLT--HGNLVANMLQVRACLSQLGPD- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 358 WEKIMERIQEVAAQS-------GFIRRKMllwAMSVTLEQN--LTCPsNDLKPFTSRLADY-----LVLARVRQAL---- 419
Cdd:PRK12492 250 GQPLMKEGQEVMIAPlplyhiyAFTANCM---CMMVSGNHNvlITNP-RDIPGFIKELGKWrfsalLGLNTLFVALmdhp 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 420 GFAKCQ------KNFYGAAPMTAETQRFFLGLNIRLYAGYGLSEsTGPHFMSSPYN--YRLYSSGRVVPGCRVKLVNQDA 491
Cdd:PRK12492 326 GFKDLDfsalklTNSGGTALVKATAERWEQLTGCTIVEGYGLTE-TSPVASTNPYGelARLGTVGIPVPGTALKVIDDDG 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 492 DGI-----GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGeNVPPVPIEEAV 566
Cdd:PRK12492 405 NELplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF-NVYPNEIEDVV 483
|
330
....*....|....*....
gi 1958794461 567 kMELPIISSAMLIG--DQR 583
Cdd:PRK12492 484 -MAHPKVANCAAIGvpDER 501
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
170-580 |
2.59e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 104.35 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQYYLIARKVAKGFLKLglerAHSVailgfNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 249
Cdd:PRK07470 41 RVDALAAALAARGVRKGDRIL----VHSR-----NCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 250 TQKQlEKILKIWKDLPHLKAVVIYQEPPpkkMANVYtmEELI--ELGQEVPeealDAIIDTQQPnqcCVLVYTSGTTGNP 327
Cdd:PRK07470 112 ADFP-EHAAAVRAASPDLTHVVAIGGAR---AGLDY--EALVarHLGARVA----NAAVDHDDP---CWFFFTSGTTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 328 KGVMLS--------------------QDNGTLVntlreVEPTSH-------MGVPRVWEKIM---ERIqEVAAQSGFIRR 377
Cdd:PRK07470 179 KAAVLThgqmafvitnhladlmpgttEQDASLV-----VAPLSHgagihqlCQVARGAATVLlpsERF-DPAEVWALVER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 378 kmllWAMSvtleqNL-TCPSnDLK-----PFTSRlADYLVLARVrqalgfakcqknFYGAAPMTAETQRFFLG-LNIRLY 450
Cdd:PRK07470 253 ----HRVT-----NLfTVPT-ILKmlvehPAVDR-YDHSSLRYV------------IYAGAPMYRADQKRALAkLGKVLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 451 AGYGLSESTG------PHFMSS---PyNYRLYSSGRVVPGCRVKLvnQDADG-------IGEICLWGRTIFMGYLNMEDK 514
Cdd:PRK07470 310 QYFGLGEVTGnitvlpPALHDAedgP-DARIGTCGFERTGMEVQI--QDDEGrelppgeTGEICVIGPAVFAGYYNNPEA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794461 515 THEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKMElPIISSAMLIG 580
Cdd:PRK07470 387 NAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYIS-GGSNVYPREIEEKLLTH-PAVSEVAVLG 449
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
171-615 |
4.03e-23 |
|
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: 102.93 E-value: 4.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 171 ISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDT 250
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 251 qkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealDAIidtqqpnqcCVLVYTSGTTGNPKGV 330
Cdd:cd05919 91 ----------------------------------------------------DDI---------AYLLYSSGTTGPPKGV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 331 MLSQDNgtlvntlreveptsHMGVPRVWEKIMERIQEvaAQSGFIRRKMLL-WAM--SVT--LEQNLTCPSNDLKPFTSR 405
Cdd:cd05919 110 MHAHRD--------------PLLFADAMAREALGLTP--GDRVFSSAKMFFgYGLgnSLWfpLAVGASAVLNPGWPTAER 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 406 LADYLVLARVRQALGFAkcqkNFYGAA-PMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSS------------------ 466
Cdd:cd05919 174 VLATLARFRPTVLYGVP----TFYANLlDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHfggpildgigatevghif 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 467 ----PYNYRLYSSGRVVPGCRVKLVNQD-----ADGIGEICLWGRTIFMGYLNMEDKThEAIDSEGWLHTGDMGRLDDDG 537
Cdd:cd05919 250 lsnrPGAWRLGSTGRPVPGYEIRLVDEEghtipPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADG 328
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794461 538 FLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIGDQRkfLSMLLTLKCTLNPET-SEPTDNLTEQAVEFC 615
Cdd:cd05919 329 WYTHAGRADDMLKV-GGQWVSPVEVESLI-IQHPAVAEAAVVAVPE--STGLSRLTAFVVLKSpAAPQESLARDIHRHL 403
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
181-580 |
4.63e-23 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 103.73 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 181 RKVAKGFLKLGLERAHSVAILGFNSP---EWFFsAVgtVFAGGIVTGI-YTTSSPEACQYIAHdCRANVIVVDTQKQLEK 256
Cdd:PLN02860 43 LSLAAGLLRLGLRNGDVVAIAALNSDlylEWLL-AV--ACAGGIVAPLnYRWSFEEAKSAMLL-VRPVMLVTDETCSSWY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 257 ILKIWKDLPHLKAVVIYQEPPPKK---MANVYTMEELIELGQEVPEEALdaiidTQQPNQCCVLVYTSGTTGNPKGVMLS 333
Cdd:PLN02860 119 EELQNDRLPSLMWQVFLESPSSSVfifLNSFLTTEMLKQRALGTTELDY-----AWAPDDAVLICFTSGTTGRPKGVTIS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 334 QdNGTLVNTLREV--------------EPTSHM-GVPRVWEKIMeriqeVAAQSGFIRRKMLLWAMSVTLEQNLTCpsnd 398
Cdd:PLN02860 194 H-SALIVQSLAKIaivgygeddvylhtAPLCHIgGLSSALAMLM-----VGACHVLLPKFDAKAALQAIKQHNVTS---- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 399 LKPFTSRLADYLVLARVRQA-LGFAKCQKNFYGAAPMTAE----TQRFFlgLNIRLYAGYGLSES-TGPHFM-------- 464
Cdd:PLN02860 264 MITVPAMMADLISLTRKSMTwKVFPSVRKILNGGGSLSSRllpdAKKLF--PNAKLFSAYGMTEAcSSLTFMtlhdptle 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 465 ----SSPYNYRLYSS----------GRVVPGCRVKLVNQDADGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDM 530
Cdd:PLN02860 342 spkqTLQTVNQTKSSsvhqpqgvcvGKPAPHVELKIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDI 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958794461 531 GRLDDDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISSAMLIG 580
Cdd:PLN02860 422 GWIDKAGNLWLIGRSNDRIKT-GGENVYPEEV-EAVLSQHPGVASVVVVG 469
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
317-583 |
5.31e-23 |
|
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: 100.65 E-value: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 317 LVYTSGTTGNPKGVMLSQ-----------DNGTLVNTLRE--VEPTSH-MGVPRVWEKIMERIQEVAAQSGFIRRKMLlw 382
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHrqtlraaaawaDCADLTEDDRYliINPFFHtFGYKAGIVACLLTGATVVPVAVFDVDAIL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 383 aMSVTLEQNLTCPSndlKP--FTSRLA----DYLVLARVRQALGfakcqknfyGAA---PMTAETQRFFLGLNIRLYAgY 453
Cdd:cd17638 83 -EAIERERITVLPG---PPtlFQSLLDhpgrKKFDLSSLRAAVT---------GAAtvpVELVRRMRSELGFETVLTA-Y 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 454 GLSEStGPHFMSSPYNYRL---YSSGRVVPGCRVKLVNQdadgiGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDM 530
Cdd:cd17638 149 GLTEA-GVATMCRPGDDAEtvaTTCGRACPGFEVRIADD-----GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDV 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958794461 531 GRLDDDGFLYITGRLKELIItAGGENVPPVPIEEAVkMELPIISSAMLIG--DQR 583
Cdd:cd17638 223 GELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGAL-AEHPGVAQVAVIGvpDER 275
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
213-584 |
1.72e-22 |
|
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: 101.64 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 213 VGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVvdTQKQLEKILKIWKDLPHLK-AVVIYQEpppKKMANVYTMEEL- 290
Cdd:cd05909 49 FALALSGKVPVMLNYTAGLRELRACIKLAGIKTVL--TSKQFIEKLKLHHLFDVEYdARIVYLE---DLRAKISKADKCk 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 291 IELGQEVPEEALDAI--IDTQQPNQCCVLVYTSGTTGNPKGVMLSQDN--GTLVNTLREVEPTS-----------H---- 351
Cdd:cd05909 124 AFLAGKFPPKWLLRIfgVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNllANVEQITAIFDPNPedvvfgalpffHsfgl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 352 ---------MGVPRVW-------EKIMERIQEvaaqsgfiRRKMLLWAMSVTLEQnltcpsndlkpftsrladylvLARV 415
Cdd:cd05909 204 tgclwlpllSGIKVVFhpnpldyKKIPELIYD--------KKATILLGTPTFLRG---------------------YARA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 416 RQALGFAKCQKNFYGAAPMTAETQRFFLGL-NIRLYAGYGLSESTGPHFMSSP-YNYRLYSSGRVVPGCRVKLVNQDAD- 492
Cdd:cd05909 255 AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISVNTPqSPNKEGTVGRPLPGMEVKIVSVETHe 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 493 --GIGE---ICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIEEAVK 567
Cdd:cd05909 335 evPIGEgglLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRF-AKIAGEMVSLEAIEDILS 412
|
410
....*....|....*....
gi 1958794461 568 MELPI--ISSAMLIGDQRK 584
Cdd:cd05909 413 EILPEdnEVAVVSVPDGRK 431
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
146-580 |
1.33e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 99.20 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 146 MFYEALDKY-----GNLSALGFKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGG 220
Cdd:PRK04319 44 IAYEAIDRHadggrKDKVALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 221 IVTGIYTTSSPEACQYIAHDCRANVIVVdTQKQLEKilKIWKDLPHLKAVVIYQEPppkkmanVYTMEELIELGQEVPEE 300
Cdd:PRK04319 124 IVGPLFEAFMEEAVRDRLEDSEAKVLIT-TPALLER--KPADDLPSLKHVLLVGED-------VEEGPGTLDFNALMEQA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 301 ALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQD-------NGTLVNTLRE------------VEPTSH-------MGV 354
Cdd:PRK04319 194 SDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNamlqhyqTGKYVLDLHEddvywctadpgwVTGTSYgifapwlNGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 355 ----------PRVWEKIMERiQEV----AAQSGFirrKMLlwaMSVTLEqnltcpsndlkpftsrLADYLVLARVRQALG 420
Cdd:PRK04319 274 tnvidggrfsPERWYRILED-YKVtvwyTAPTAI---RML---MGAGDD----------------LVKKYDLSSLRHILS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 421 FAKcqknfygaaPMTAETQRFflG---LNIRLYAGYGLSEsTGPHFMSspyNY-----RLYSSGRVVPGCRVKLVNQDAD 492
Cdd:PRK04319 331 VGE---------PLNPEVVRW--GmkvFGLPIHDNWWMTE-TGGIMIA---NYpamdiKPGSMGKPLPGIEAAIVDDQGN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 493 G-----IGEICL---WgRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEE 564
Cdd:PRK04319 396 ElppnrMGNLAIkkgW-PSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVES 472
|
490
....*....|....*.
gi 1958794461 565 AVkMELPIISSAMLIG 580
Cdd:PRK04319 473 KL-MEHPAVAEAGVIG 487
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
170-563 |
1.82e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 98.88 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQYYLIARKVAkGFL--KLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 247
Cdd:PRK08314 35 AISYRELLEEAERLA-GYLqqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 248 VdTQKQLEKILKIWKDLPhLKAVVIYQ----------EPPPKKMANVYTMEELIELGQEVPEEALDAIID----TQQPNQ 313
Cdd:PRK08314 114 V-GSELAPKVAPAVGNLR-LRHVIVAQysdylpaepeIAVPAWLRAEPPLQALAPGGVVAWKEALAAGLAppphTAGPDD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 314 CCVLVYTSGTTGNPKGVM-----------LSQD--NGTLVNTLREVEPTSH-------------MG-----VPRvWEKim 362
Cdd:PRK08314 192 LAVLPYTSGTTGVPKGCMhthrtvmanavGSVLwsNSTPESVVLAVLPLFHvtgmvhsmnapiyAGatvvlMPR-WDR-- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 363 eriqEVAAQsgFIRR-KMLLW----AMSVTLeqnLTCPsndlkpftsRLADYlVLARVRQALGfakcqknfyGAAPM-TA 436
Cdd:PRK08314 269 ----EAAAR--LIERyRVTHWtnipTMVVDF---LASP---------GLAER-DLSSLRYIGG---------GGAAMpEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 437 ETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSG--------RVV-PgcrVKLVNQDADGIGEICLWGRTIFMG 507
Cdd:PRK08314 321 VAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGiptfgvdaRVIdP---ETLEELPPGEVGEIVVHGPQVFKG 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794461 508 YLNMEDKTHEA---IDSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIE 563
Cdd:PRK08314 398 YWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRM-INASGFKVWPAEVE 455
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
168-701 |
2.98e-21 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 98.41 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 168 WERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIyttsSPeacQY--IAHD----- 240
Cdd:PRK08180 67 WRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV----SP---AYslVSQDfgklr 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 241 -----CRANVIVVDTQKQLEKILKIwKDLPHLKAVVIYQEPPPKKmanVYTMEELIELGqevPEEALDAIIDTQQPNQCC 315
Cdd:PRK08180 140 hvlelLTPGLVFADDGAAFARALAA-VVPADVEVVAVRGAVPGRA---ATPFAALLATP---PTAAVDAAHAAVGPDTIA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 316 VLVYTSGTTGNPKGV------------MLSQ----------------------------------------DNG------ 337
Cdd:PRK08180 213 KFLFTSGSTGLPKAVinthrmlcanqqMLAQtfpflaeeppvlvdwlpwnhtfggnhnlgivlynggtlyiDDGkptpgg 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 338 ---TLVNtLREVEPTSHMGVPRVWEkimeriqevaaqsgfirrkMLLWAmsvtLEQNltcpsndlkpftSRLADYLvLAR 414
Cdd:PRK08180 293 fdeTLRN-LREISPTVYFNVPKGWE-------------------MLVPA----LERD------------AALRRRF-FSR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 415 VRQAlgfakcqknFYGAAPMTAET----QRF---FLGLNIRLYAGYGLSEsTGPHFMSSpyNYRLYSSGRV---VPGCRV 484
Cdd:PRK08180 336 LKLL---------FYAGAALSQDVwdrlDRVaeaTCGERIRMMTGLGMTE-TAPSATFT--TGPLSRAGNIglpAPGCEV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 485 KLVnqDADGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDD-----GFLYiTGRLKELIITAGGE--NV 557
Cdd:PRK08180 404 KLV--PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVDPadperGLMF-DGRIAEDFKLSSGTwvSV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 558 PPVPIeEAVKMELPIISSAMLIGDQRKFLSMLLTLKctlnpetseptdnlteqaVEFCQRVGSKASTVSEIVGQKDEAVY 637
Cdd:PRK08180 481 GPLRA-RAVSAGAPLVQDVVITGHDRDEIGLLVFPN------------------LDACRRLAGLLADASLAEVLAHPAVR 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794461 638 QAIHEGIQRVNANAAARPYHIQKWAILERDFSISGGELgpTMK--LKRLTVLEKYKDIIDSFYQEQ 701
Cdd:PRK08180 542 AAFRERLARLNAQATGSSTRVARALLLDEPPSLDAGEI--TDKgyINQRAVLARRAALVEALYADE 605
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
317-580 |
1.23e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 95.71 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 317 LVYTSGTTGNPKGVMLSQDNgTLVN--TLREVeptshmgvprvWekimeriqevaaqsGFIRRKMLLW------------ 382
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGN-LLSNalTLVDY-----------W--------------RFTPDDVLIHalpifhthglfv 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 383 AMSVTL---EQNLTCPSNDLKPFTSRLADYLVLARV---------RQALGFAKCQKN--FY-GAAPMTAETQRFF---LG 444
Cdd:PRK07514 215 ATNVALlagASMIFLPKFDPDAVLALMPRATVMMGVptfytrllqEPRLTREAAAHMrlFIsGSAPLLAETHREFqerTG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 445 LNI--RlyagYGLSEsTGphfM--SSPYN--YRLYSSGRVVPGCRVKLVNQD------ADGIGEICLWGRTIFMGYLNME 512
Cdd:PRK07514 295 HAIleR----YGMTE-TN---MntSNPYDgeRRAGTVGFPLPGVSLRVTDPEtgaelpPGEIGMIEVKGPNVFKGYWRMP 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794461 513 DKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKmELP-IISSAmLIG 580
Cdd:PRK07514 367 EKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIIS-GGYNVYPKEVEGEID-ELPgVVESA-VIG 432
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
170-565 |
6.31e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 93.86 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 249
Cdd:PRK08162 43 RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 250 TQKQlEKILKIWKDLPHLKAVVI-YQEPPPKKMANVYTM--EELIELGQ-----EVPEEALDAIidtqqpnqccVLVYTS 321
Cdd:PRK08162 123 TEFA-EVAREALALLPGPKPLVIdVDDPEYPGGRFIGALdyEAFLASGDpdfawTLPADEWDAI----------ALNYTS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 322 GTTGNPKGV--------MLSQDN----------------------------------GTLVnTLREVEPtshmgvprvwE 359
Cdd:PRK08162 192 GTTGNPKGVvyhhrgayLNALSNilawgmpkhpvylwtlpmfhcngwcfpwtvaaraGTNV-CLRKVDP----------K 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 360 KIMERIQE--VAAQSGF-IRRKMLLWAmsvtleqnltcPSNDLKPFtsrlaDYLVLARVRqalgfakcqknfyGAAP--- 433
Cdd:PRK08162 261 LIFDLIREhgVTHYCGApIVLSALINA-----------PAEWRAGI-----DHPVHAMVA-------------GAAPpaa 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 434 MTAETQRfflgLNIRLYAGYGLSESTGP--------HFMSSPYNYRLYSSGR------VVPGCRV------KLVNQDADG 493
Cdd:PRK08162 312 VIAKMEE----IGFDLTHVYGLTETYGPatvcawqpEWDALPLDERAQLKARqgvrypLQEGVTVldpdtmQPVPADGET 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794461 494 IGEICLWGRTIFMGYLNMEDKTHEAIDSeGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEA 565
Cdd:PRK08162 388 IGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVEDV 457
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
169-580 |
7.78e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 93.75 E-value: 7.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLK-LGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 247
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 248 VDTQKqLEKilkiwkdLPHLKAVVI-------YQEPPPKKMANVYTMEELIELGQEVPEEALDAiidtqqpnqcCVLVYT 320
Cdd:PLN02574 145 TSPEN-VEK-------LSPLGVPVIgvpenydFDSKRIEFPKFYELIKEDFDFVPKPVIKQDDV----------AAIMYS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 321 SGTTGNPKGVMLSQDNgtLVNTLR-----EVEPTSHMGVPRVWEKIMERIQeVAAQSGFIRRKMLLWAMSVTLEQnltCP 395
Cdd:PLN02574 207 SGTTGASKGVVLTHRN--LIAMVElfvrfEASQYEYPGSDNVYLAALPMFH-IYGLSLFVVGLLSLGSTIVVMRR---FD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 396 SNDLKPFTSR-------LADYLVLARVRQALGFA----KCQKNFY-GAAPMTAETQRFFLGL--NIRLYAGYGLSEST-- 459
Cdd:PLN02574 281 ASDMVKVIDRfkvthfpVVPPILMALTKKAKGVCgevlKSLKQVScGAAPLSGKFIQDFVQTlpHVDFIQGYGMTESTav 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 460 GPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDA------DGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRL 533
Cdd:PLN02574 361 GTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTgcllppGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYF 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958794461 534 DDDGFLYITGRLKElIITAGGENVPPVPIeEAVKMELPIISSAMLIG 580
Cdd:PLN02574 441 DEDGYLYIVDRLKE-IIKYKGFQIAPADL-EAVLISHPEIIDAAVTA 485
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
180-571 |
2.84e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 91.68 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 180 ARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV--VDTQKQLEKI 257
Cdd:PRK12406 21 AARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIahADLLHGLASA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 258 LKiwkdlPHLKAVVIyqePPPKKMANVYTMEE--------LIELGQEVPEEALDAIIDTQQPNQccvLVYTSGTTGNPKG 329
Cdd:PRK12406 101 LP-----AGVTVLSV---PTPPEIAAAYRISPalltppagAIDWEGWLAQQEPYDGPPVPQPQS---MIYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 330 VmlsqdngtlvntlREVEPTShmgvprvwEKIMERIQEVAAQSGFIRRkmllwamSVTLeqnLTCP-----SNDLKPFTS 404
Cdd:PRK12406 170 V-------------RRAAPTP--------EQAAAAEQMRALIYGLKPG-------IRAL---LTGPlyhsaPNAYGLRAG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 405 RLADYLVL-----------------------------------ARVRQALGFAKCQKNFYGAAPMTAETQRFFL---GLN 446
Cdd:PRK12406 219 RLGGVLVLqprfdpeellqlierhrithmhmvptmfirllklpEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIewwGPV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 447 IrlYAGYGLSESTGPHFMSSP-YNYRLYSSGRVVPGCRVKLVnqDADG-------IGEIC--LWGRTIFMgYLNMEDKTH 516
Cdd:PRK12406 299 I--YEYYGSTESGAVTFATSEdALSHPGTVGKAAPGAELRFV--DEDGrplpqgeIGEIYsrIAGNPDFT-YHNKPEKRA 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1958794461 517 EaIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELP 571
Cdd:PRK12406 374 E-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEI-EAVLHAVP 425
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
172-580 |
3.59e-19 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 90.47 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 172 SYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQ 251
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 252 kqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealdaiiDTqqpnqcCVLVYTSGTTGNPKGVm 331
Cdd:cd05972 82 -------------------------------------------------------DP------ALIYFTSGTTGLPKGV- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 332 lsqdngtlVNTLREvePTSHMGVPRVWEKIMER-IQEVAAQSGFIrrKMLL------WAMSVT----------------- 387
Cdd:cd05972 100 --------LHTHSY--PLGHIPTAAYWLGLRPDdIHWNIADPGWA--KGAWssffgpWLLGATvfvyegprfdaerilel 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 388 LEQ----NLTCPSNDLKPFTSRLADYLVLARVRQALGfakcqknfyGAAPMTAETQRFF---LGLNIRlyAGYGLSESTG 460
Cdd:cd05972 168 LERygvtSFCGPPTAYRMLIKQDLSSYKFSHLRLVVS---------AGEPLNPEVIEWWraaTGLPIR--DGYGQTETGL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 461 PHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGI-----GEICLWGRTI--FMGYLNMEDKTHEAIdSEGWLHTGDMGRL 533
Cdd:cd05972 237 TVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELppgeeGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYR 315
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958794461 534 DDDGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:cd05972 316 DEDGYFWFVGRADDIIKSS-GYRIGPFEVESAL-LEHPAVAEAAVVG 360
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
317-564 |
5.13e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 88.86 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 317 LVYTSGTTGNPKGVMLS--------------QDNGTLVNTLREVEPTSHMGvpRVWEKIMERIQEVAAQSG--FIRRKML 380
Cdd:cd17635 6 VIFTSGTTGEPKAVLLAnktffavpdilqkeGLNWVVGDVTYLPLPATHIG--GLWWILTCLIHGGLCVTGgeNTTYKSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 381 LWAMSVTLEQNLTCPSNDLKPFTSRLADYLVLARVRQALGFAkcqknfyGAAPMTAETQRFFLGLNIRLYAGYGLSESTG 460
Cdd:cd17635 84 FKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYG-------GSRAIAADVRFIEATGLTNTAQVYGLSETGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 461 PHFMssPYNYRLY---SSGRVVPGCRVKLVNQDA-----DGIGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGR 532
Cdd:cd17635 157 ALCL--PTDDDSIeinAVGRPYPGVDVYLAATDGiagpsASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGE 233
|
250 260 270
....*....|....*....|....*....|..
gi 1958794461 533 LDDDGFLYITGRLKElIITAGGENVPPVPIEE 564
Cdd:cd17635 234 RREDGFLFITGRSSE-SINCGGVKIAPDEVER 264
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
181-580 |
1.47e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 89.45 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 181 RKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQkqLEKILKI 260
Cdd:PRK07786 53 AALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA--LAPVATA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 261 WKDL-PHLKAVVIYQEPPPkkmANVYTMEELIELGQEVPeealdAIIDTqqPNQCCVLV-YTSGTTGNPKGVMLSQDN-- 336
Cdd:PRK07786 131 VRDIvPLLSTVVVAGGSSD---DSVLGYEDLLAEAGPAH-----APVDI--PNDSPALImYTSGTTGRPKGAVLTHANlt 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 337 ---GTLVNTLREVEPTS--HMGVPrvwekimerIQEVAAqSGFIRRKMLLWAMSVTLeqnltcPSNDLKPftSRLADylV 411
Cdd:PRK07786 201 gqaMTCLRTNGADINSDvgFVGVP---------LFHIAG-IGSMLPGLLLGAPTVIY------PLGAFDP--GQLLD--V 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 412 LARVRQALGF-------AKC------QKNF------YGAAPMT-------AETqrfFLGLNIrlYAGYGLSEstgphfMS 465
Cdd:PRK07786 261 LEAEKVTGIFlvpaqwqAVCaeqqarPRDLalrvlsWGAAPASdtllrqmAAT---FPEAQI--LAAFGQTE------MS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 466 sPYN---------YRLYSSGRVVPGCRVKLVNQDADG-----IGEICLWGRTIFMGYLNMEDKTHEAIDSeGWLHTGDMG 531
Cdd:PRK07786 330 -PVTcmllgedaiRKLGSVGKVIPTVAARVVDENMNDvpvgeVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLV 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1958794461 532 RLDDDGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISSAMLIG 580
Cdd:PRK07786 408 RQDEEGYVWVVDRKKDMIIS-GGENIYCAEVEN-VLASHPDIVEVAVIG 454
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
446-580 |
1.49e-18 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 87.08 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 446 NIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGIGEICLWGRTIFMGYLNMEdktheAIDSEGWL 525
Cdd:cd17633 136 KANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGG-----FSNPDGWM 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958794461 526 HTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISSAMLIG 580
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLK-AIPGIEEAIVVG 263
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
316-581 |
2.51e-18 |
|
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: 88.27 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 316 VLVYTSGTTGNPKGVMLSQDNgtlvntlreveptshmgvprvwekIMERIQEVAAQSGFIRRKMLLWAMSVT-------L 388
Cdd:cd05922 121 LLLYTSGSTGSPKLVRLSHQN------------------------LLANARSIAEYLGITADDRALTVLPLSydyglsvL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 389 EQNLTCPSNDLKPFTSRLADYLV-LARVRQALGFAKCQKNF-----YGAAPMTAETQRFF-----------------LGL 445
Cdd:cd05922 177 NTHLLRGATLVLTNDGVLDDAFWeDLREHGATGLAGVPSTYamltrLGFDPAKLPSLRYLtqaggrlpqetiarlreLLP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 446 NIRLYAGYGLSESTG------PHFMSSpynyRLYSSGRVVPGCRVKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDK 514
Cdd:cd05922 257 GAQVYVMYGQTEATRrmtylpPERILE----KPGSIGLAIPGGEFEILDDDgtptPPGePGEIVHRGPNVMKGYWNDPPY 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794461 515 THEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISSAMLIGD 581
Cdd:cd05922 333 RRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAAA-RSIGLIIEAAAVGL 397
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
170-566 |
3.06e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 88.51 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYT-TSSPEACQYIAhdcranvivv 248
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQpTPRTDLAVWAE---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DTQKQLEKIlkiwkdlpHLKAVVI---YQEPPP---KKMANVYTMEELIELGQEVPEEALDAIIDTQQpnqccvlvYTSG 322
Cdd:PRK07768 99 DTLRVIGMI--------GAKAVVVgepFLAAAPvleEKGIRVLTVADLLAADPIDPVETGEDDLALMQ--------LTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 323 TTGNPKGVMLSQDNgtLVNTLR--------EVE--------PTSH-MG------VPrvwekiMERIQEVAAQS--GFIRR 377
Cdd:PRK07768 163 STGSPKAVQITHGN--LYANAEamfvaaefDVEtdvmvswlPLFHdMGmvgfltVP------MYFGAELVKVTpmDFLRD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 378 KmLLWAMSVTLEQ-NLTCPSNdlkpFTsrladYLVLARV--RQA---------LGFAKCqknfyGAAPMTAETQRFFL-- 443
Cdd:PRK07768 235 P-LLWAELISKYRgTMTAAPN----FA-----YALLARRlrRQAkpgafdlssLRFALN-----GAEPIDPADVEDLLda 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 444 ----GLNIR-LYAGYGLSEST----------GPHF----------------MSSPYNYRLYSSGRVVPGCRVKLVNQD-- 490
Cdd:PRK07768 300 garfGLRPEaILPAYGMAEATlavsfspcgaGLVVdevdadllaalrravpATKGNTRRLATLGPPLPGLEVRVVDEDgq 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794461 491 ---ADGIGEICLWGRTIFMGYLNMeDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAV 566
Cdd:PRK07768 380 vlpPRGVGVIELRGESVTPGYLTM-DGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIM-AGRNIYPTDIERAA 456
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
171-568 |
6.18e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 87.62 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 171 ISYYQYYLIARKVAKGFL-KLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV- 248
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVi 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 ------------DTQ-KQ-----LEKILKIWKD------LPHLKAVViyqepPPKKMANVYTMEELIELGQEVPEEALDA 304
Cdd:PRK08751 131 dnfgttvqqviaDTPvKQvittgLGDMLGFPKAalvnfvVKYVKKLV-----PEYRINGAIRFREALALGRKHSMPTLQI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 305 iidtqQPNQCCVLVYTSGTTGNPKGVMLSQDNG-----------TLVNTLREVEPTSHMGVPR-----------VWEKI- 361
Cdd:PRK08751 206 -----EPDDIAFLQYTGGTTGVAKGAMLTHRNLvanmqqahqwlAGTGKLEEGCEVVITALPLyhifaltanglVFMKIg 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 362 --MERIQEVAAQSGFIR-----RKMLLWAMSVTLEQNLTCPSNDLKPFTSrladylvlarVRQALGfakcqknfYGAAPM 434
Cdd:PRK08751 281 gcNHLISNPRDMPGFVKelkktRFTAFTGVNTLFNGLLNTPGFDQIDFSS----------LKMTLG--------GGMAVQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 435 TAETQRFFLGLNIRLYAGYGLSEsTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADG-------IGEICLWGRTIFMG 507
Cdd:PRK08751 343 RSVAERWKQVTGLTLVEAYGLTE-TSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGtvlaigeIGELCIKGPQVMKG 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794461 508 YLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGeNVPPVPIEEAVKM 568
Cdd:PRK08751 422 YWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGF-NVYPNEIEDVIAM 481
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
140-586 |
8.41e-18 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 87.11 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 140 PYTVHQMFYEALDKYGNLSALGFKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG 219
Cdd:PRK06018 9 PLLCHRIIDHAARIHGNREVVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 220 GIVTGIYTTSSPEACQYIAHDCRANVIVVDTQ--KQLEKILKiwkDLPHLKAVVIYQEP---PPKKMANVYTMEELIElg 294
Cdd:PRK06018 89 AICHTVNPRLFPEQIAWIINHAEDRVVITDLTfvPILEKIAD---KLPSVERYVVLTDAahmPQTTLKNAVAYEEWIA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 295 qevpEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNGTL---------------VNTLREVEPTSH-------M 352
Cdd:PRK06018 164 ----EADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRSNVLhalmanngdalgtsaADTMLPVVPLFHanswgiaF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 353 GVPRVWEKIM-----------------ERIQEVAAQSGFIrrKMLLWAMSvtlEQNLTCPsnDLKpftsrladylvlarv 415
Cdd:PRK06018 240 SAPSMGTKLVmpgakldgasvyelldtEKVTFTAGVPTVW--LMLLQYME---KEGLKLP--HLK--------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 416 rqalgfakcqKNFYGAAPMTAETQRFFLGLNIRLYAGYGLSEST--------GPHFMSSPYNYRL---YSSGRVVPGCRV 484
Cdd:PRK06018 298 ----------MVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSplgtlaalKPPFSKLPGDARLdvlQKQGYPPFGVEM 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 485 KLVNQDA-----DG--IGEICLWGRTIFMGYLNMEDkthEAIDSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENV 557
Cdd:PRK06018 368 KITDDAGkelpwDGktFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKD-VIKSGGEWI 443
|
490 500 510
....*....|....*....|....*....|....*.
gi 1958794461 558 PPVPIEE-AVKMelPIISSAMLIG------DQRKFL 586
Cdd:PRK06018 444 SSIDLENlAVGH--PKVAEAAVIGvyhpkwDERPLL 477
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
169-566 |
9.64e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 87.12 E-value: 9.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 248
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DTQkQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEVPEEALdaiidtqQPNQCCVLVYTSGTTGNPK 328
Cdd:PRK06155 125 EAA-LLAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAV-------QPGDTAAILYTSGTTGPSK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 329 GVMLSQ-----------------DNGTLVNTLrevePTSHMGVPRVWEKIM---------ERIqevaAQSGF---IRRK- 378
Cdd:PRK06155 197 GVCCPHaqfywwgrnsaedleigADDVLYTTL----PLFHTNALNAFFQALlagatyvlePRF----SASGFwpaVRRHg 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 379 ----MLLWAM-SVTLEQNLTCPSNDlkpftsrladylvlARVRQALGfakcqknfyGAAPmTAETQRFFLGLNIRLYAGY 453
Cdd:PRK06155 269 atvtYLLGAMvSILLSQPARESDRA--------------HRVRVALG---------PGVP-AALHAAFRERFGVDLLDGY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 454 GLSESTGPhFMSSPYNYRLYSSGRVVPGCRVKLVNQD-----ADGIGEICLWGRTIFM---GYLNMEDKTHEAIDSEgWL 525
Cdd:PRK06155 325 GSTETNFV-IAVTHGSQRPGSMGRLAPGFEARVVDEHdqelpDGEPGELLLRADEPFAfatGYFGMPEKTVEAWRNL-WF 402
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1958794461 526 HTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEEAV 566
Cdd:PRK06155 403 HTGDRVVRDADGWFRFVDRIKD-AIRRRGENISSFEVEQVL 442
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
170-578 |
9.76e-18 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 87.38 E-value: 9.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 249
Cdd:PLN03102 39 RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 250 TQ-----KQLEKILKIWKDLPHLKAVVIYQEPPPKK-MANVYTMEELIELGQEVPEeALDAIIDTQQPNQCCVLVYTSGT 323
Cdd:PLN03102 119 RSfeplaREVLHLLSSEDSNLNLPVIFIHEIDFPKRpSSEELDYECLIQRGEPTPS-LVARMFRIQDEHDPISLNYTSGT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 324 TGNPKGVMLSQdNGTLVNTLREVePTSHMGVPRV--WEKIMERIQ------EVAAQSGfirrkmllwaMSVTLeQNLTCP 395
Cdd:PLN03102 198 TADPKGVVISH-RGAYLSTLSAI-IGWEMGTCPVylWTLPMFHCNgwtftwGTAARGG----------TSVCM-RHVTAP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 396 ----SNDLKPFTSRLADYLVLARVRQALGFAKCQKN-----FYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSS 466
Cdd:PLN03102 265 eiykNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSgpvhvLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 467 --------PYNYRLYSSGRvvPGCRV--------------KLVNQDADGIGEICLWGRTIFMGYLNMEDKTHEAIdSEGW 524
Cdd:PLN03102 345 wqdewnrlPENQQMELKAR--QGVSIlgladvdvknketqESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGW 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958794461 525 LHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKMELPIISSAML 578
Cdd:PLN03102 422 LNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEVENVLYKYPKVLETAVV 474
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
104-675 |
1.17e-17 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 87.13 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 104 PEKARAASLDASEEALwttradGRVRLRLepfcTQLPYTVhqmfyeaLDKYGNLSALGFKRKDK--------------WE 169
Cdd:cd17632 2 PQFAAAAPLEAVTEAI------RRPGLRL----AQIIATV-------MTGYADRPALGQRATELvtdpatgrttlrllPR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 R--ISYYQYYLIARKVAKGF-LKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVI 246
Cdd:cd17632 65 FetITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 247 VVDTQkQLEKILKIWKDLPHLKAVVIY----------------QEPPPKKMANVYTMEELIELGQEVPEEALDAIIDTQQ 310
Cdd:cd17632 145 AVSAE-HLDLAVEAVLEGGTPPRLVVFdhrpevdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 311 PnqCCVLVYTSGTTGNPKGVM-------------------------------LSQDNG---------------------- 337
Cdd:cd17632 224 P--LALLIYTSGSTGTPKGAMyterlvatfwlkvssiqdirppasitlnfmpMSHIAGrislygtlarggtayfaaasdm 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 338 -TLVNTLREVEPTSHMGVPRVWEKIMERIQEVaaqsgfIRRKMLLWAMSVTLEQNltcpsndlkpftsrladylVLARVR 416
Cdd:cd17632 302 sTLFDDLALVRPTELFLVPRVCDMLFQRYQAE------LDRRSVAGADAETLAER-------------------VKAELR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 417 QALGFAKCQKNFYGAAPMTAETQRFFLG-LNIRLYAGYGLSESTGphfmsspynyrLYSSGRVV--PGCRVKLVNQDADG 493
Cdd:cd17632 357 ERVLGGRLLAAVCGSAPLSAEMKAFMESlLDLDLHDGYGSTEAGA-----------VILDGVIVrpPVLDYKLVDVPELG 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 494 I---------GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGD-MGRLDDDGFLYITgRLKELIITAGGENVpPVPIE 563
Cdd:cd17632 426 YfrtdrphprGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDvMAELGPDRLVYVD-RRNNVLKLSQGEFV-TVARL 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 564 EAVKMELPIISSAMLIGD-QRKFLSMLLTlkctlnpetsePTDNlteqavefcqrvgskastvsEIVGQKDEAVYQAIHE 642
Cdd:cd17632 504 EAVFAASPLVRQIFVYGNsERAYLLAVVV-----------PTQD--------------------ALAGEDTARLRAALAE 552
|
650 660 670
....*....|....*....|....*....|....
gi 1958794461 643 GIQRVNANAAARPYHIQKWAILERD-FSISGGEL 675
Cdd:cd17632 553 SLQRIAREAGLQSYEIPRDFLIETEpFTIANGLL 586
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
448-576 |
2.12e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 85.88 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 448 RLYAGYGLSESTgPHFMSSPYNYRLY--SSGRVVPGCRVKLVNQDA-----DGIGEICLWGRTIFMGYLNMEDKTHEAId 520
Cdd:PRK08974 352 YLLEGYGLTECS-PLVSVNPYDLDYYsgSIGLPVPSTEIKLVDDDGnevppGEPGELWVKGPQVMLGYWQRPEATDEVI- 429
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794461 521 SEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGeNVPPVPIEEAVKMELPIISSA 576
Cdd:PRK08974 430 KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGF-NVYPNEIEDVVMLHPKVLEVA 484
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
279-566 |
2.12e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 85.97 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 279 KKMANVYTMEELIEL------GQEVPEEALDAiidtqQPNQCCVLVYTSGTTGNPKGVMLSQDNgtLVNTLREVEPTshM 352
Cdd:PRK05677 173 KKMVPAYHLPQAVKFndalakGAGQPVTEANP-----QADDVAVLQYTGGTTGVAKGAMLTHRN--LVANMLQCRAL--M 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 353 GVprvweKIMERIQEVAAQ------SGFIRRKMllwAMSVTLEQNLTCPS-NDLKPFTSRLADYLVLARVR--------- 416
Cdd:PRK05677 244 GS-----NLNEGCEILIAPlplyhiYAFTFHCM---AMMLIGNHNILISNpRDLPAMVKELGKWKFSGFVGlntlfvalc 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 417 -----QALGFAKCQKNFYGAAPMTAETQRFFLGL-NIRLYAGYGLSEsTGPHFMSSPYNY-RLYSSGRVVPGCRVKLVNQ 489
Cdd:PRK05677 316 nneafRKLDFSALKLTLSGGMALQLATAERWKEVtGCAICEGYGMTE-TSPVVSVNPSQAiQVGTIGIPVPSTLCKVIDD 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 490 DAD-----GIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGeNVPPVPIEE 564
Cdd:PRK05677 395 DGNelplgEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGF-NVYPNELED 473
|
..
gi 1958794461 565 AV 566
Cdd:PRK05677 474 VL 475
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
198-544 |
4.87e-17 |
|
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: 83.85 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 198 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKQLEKIlkiWKDLPHLkavviyqepp 277
Cdd:TIGR01733 28 VAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLA---GLVLPVI---------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 278 pkkmanVYTMEELIELGQEVPEEALDAiiDTQQPNQCCVLvYTSGTTGNPKGVMLSQDNgtLVNTLReveptshmgvPRV 357
Cdd:TIGR01733 95 ------LLDPLELAALDDAPAPPPPDA--PSGPDDLAYVI-YTSGSTGRPKGVVVTHRS--LVNLLA----------WLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 358 WEKIMERIQEVAAQSGFirrkmllwAMSVTLEQNLTC----------PSNDLKPFTSRLADYL-------------VLAR 414
Cdd:TIGR01733 154 RRYGLDPDDRVLQFASL--------SFDASVEEIFGAllagatlvvpPEDEERDDAALLAALIaehpvtvlnltpsLLAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 415 VRQALGFAKC--QKNFYGAAPMTAET-QRF-FLGLNIRLYAGYGLSEST----------GPHFMSSPYNYrlyssGRVVP 480
Cdd:TIGR01733 226 LAAALPPALAslRLVILGGEALTPALvDRWrARGPGARLINLYGPTETTvwstatlvdpDDAPRESPVPI-----GRPLA 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794461 481 GCRVKLVNQD-----ADGIGEICLWGRTIFMGYLNMEDKTHEAI--------DSEGWLHTGDMGRLDDDGFLYITGR 544
Cdd:TIGR01733 301 NTRLYVLDDDlrpvpVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGR 377
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
169-618 |
4.96e-17 |
|
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: 84.07 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFL-KLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 247
Cdd:cd05958 9 REWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 248 VDtqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeEALDAIIDTqqpnqcCVLVYTSGTTGNP 327
Cdd:cd05958 89 CA--------------------------------------------------HALTASDDI------CILAFTSGTTGAP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 328 KGVM------LSQDNGTLVNTLREVEPTSHMGVPRVWekimeriqevaaqSGFIRRKMLLWAMSV-----TLEQnlTCPS 396
Cdd:cd05958 113 KATMhfhrdpLASADRYAVNVLRLREDDRFVGSPPLA-------------FTFGLGGVLLFPFGVgasgvLLEE--ATPD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 397 NDL------KP---FTSRLADYLVLARVRQA----LGFAKCQKNfyGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHF 463
Cdd:cd05958 178 LLLsaiaryKPtvlFTAPTAYRAMLAHPDAAgpdlSSLRKCVSA--GEALPAALHRAWKEATGIPIIDGIGSTEMFHIFI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 464 MSSPYNYRLYSSGRVVPGCRVKLVnqDADG-------IGEICLWGRTifmGYLNMEDKTHEAIDSEGWLHTGDMGRLDDD 536
Cdd:cd05958 256 SARPGDARPGATGKPVPGYEAKVV--DDEGnpvpdgtIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 537 GFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIGDQRKFLSMLLTLKCTLNPETSePTDNLTEQAVEFCQ 616
Cdd:cd05958 331 GYFRHQGRSDDMIVS-GGYNIAPPEVEDVL-LQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVI-PGPVLARELQDHAK 407
|
..
gi 1958794461 617 RV 618
Cdd:cd05958 408 AH 409
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
169-615 |
6.53e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 84.36 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFfsavgTVFAGGIVTGIYTTS-----SPEACQYIAHDCRA 243
Cdd:PRK13391 23 EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYL-----EVCWAAERSGLYYTCvnshlTPAEAAYIVDDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 244 NVIVVdTQKQLEKILKIWKDLPHLKAVVIYQEPPpkkmanvyTMEELIELgqevpEEALDAIIDTQQPNQC--CVLVYTS 321
Cdd:PRK13391 98 RALIT-SAAKLDVARALLKQCPGVRHRLVLDGDG--------ELEGFVGY-----AEAVAGLPATPIADESlgTDMLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 322 GTTGNPKGVmlsqdngtlVNTLREVEPTSHMGVPRVWEKiMERIQEVAA--------QSGFIRRKMLLWAMSVTL----- 388
Cdd:PRK13391 164 GTTGRPKGI---------KRPLPEQPPDTPLPLTAFLQR-LWGFRSDMVylspaplyHSAPQRAVMLVIRLGGTVivmeh 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 389 ---EQNLTC------PSNDLKP--FtSRLadyLVLAR-VRQALGFAKCQKNFYGAAPMTAETQRFFL---GLNIRLYagY 453
Cdd:PRK13391 234 fdaEQYLALieeygvTHTQLVPtmF-SRM---LKLPEeVRDKYDLSSLEVAIHAAAPCPPQVKEQMIdwwGPIIHEY--Y 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 454 GLSESTGPHFMSSP-YNYRLYSSGRVVPGcrvKLVNQDADG-------IGEICLWGRTIFMgYLNMEDKTHEAIDSEG-W 524
Cdd:PRK13391 308 AATEGLGFTACDSEeWLAHPGTVGRAMFG---DLHILDDDGaelppgePGTIWFEGGRPFE-YLNDPAKTAEARHPDGtW 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 525 LHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG--DQrkflSMLLTLKCTLNP-ETS 601
Cdd:PRK13391 384 STVGDIGYVDEDGYLYLTDRAAFMIIS-GGVNIYPQEAENLL-ITHPKVADAAVFGvpNE----DLGEEVKAVVQPvDGV 457
|
490
....*....|....
gi 1958794461 602 EPTDNLTEQAVEFC 615
Cdd:PRK13391 458 DPGPALAAELIAFC 471
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
296-544 |
7.32e-17 |
|
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: 83.73 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 296 EVPEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQDNgtLVNTLREveptshmgvprVWEKIMERIQEV 368
Cdd:cd05930 70 SYPAERLAYILeDSGaklvltDPDDLAYVIYTSGSTGKPKGVMVEHRG--LVNLLLW-----------MQEAYPLTPGDR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 369 AAQS---GFIrrkMLLWAMSVTLEQN--LTCPSNDLKPFTSRLADYLVLARVR-------------QALGFAKCQ--KNF 428
Cdd:cd05930 137 VLQFtsfSFD---VSVWEIFGALLAGatLVVLPEEVRKDPEALADLLAEEGITvlhltpsllrlllQELELAALPslRLV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 429 Y-GAAPMTAETQRFFLGL--NIRLYAGYGLSEST-GPHFMSSPYNYRLYSS---GRVVPGCRVKLVNQD----ADG-IGE 496
Cdd:cd05930 214 LvGGEALPPDLVRRWRELlpGARLVNLYGPTEATvDATYYRVPPDDEEDGRvpiGRPIPNTRVYVLDENlrpvPPGvPGE 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958794461 497 ICLWGRTIFMGYLNMEDKTHEAI-----DSEGWLH-TGDMGRLDDDGFLYITGR 544
Cdd:cd05930 294 LYIGGAGLARGYLNRPELTAERFvpnpfGPGERMYrTGDLVRWLPDGNLEFLGR 347
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
145-544 |
7.67e-17 |
|
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: 83.51 E-value: 7.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 145 QMFYEALDKYGNLSALgfkrKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 224
Cdd:cd17653 1 DAFERIAAAHPDAVAV----ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 225 IYTTSSPEACQYIAHDCRANVIVVDTQkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealda 304
Cdd:cd17653 77 LDAKLPSARIQAILRTSGATLLLTTDS----------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 305 iidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNgtLVNTLREVEPTSHMGVPRvwekimeRIQEVAAqSGFirrKMLLWAM 384
Cdd:cd17653 104 ------PDDLAYIIFTSGSTGIPKGVMVPHRG--VLNYVSQPPARLDVGPGS-------RVAQVLS-IAF---DACIGEI 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 385 SVTLEQNLT-CPSNDLKPFTS--RLADYL-----VLARVRQAlGFAKCQKNFYGAAPMTAETQRFFLGlNIRLYAGYGLS 456
Cdd:cd17653 165 FSTLCNGGTlVLADPSDPFAHvaRTVDALmstpsILSTLSPQ-DFPNLKTIFLGGEAVPPSLLDRWSP-GRRLYNAYGPT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 457 ESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQD-----ADGIGEICLWGRTIFMGYLNMEDKT----HEAIDSEGWLH- 526
Cdd:cd17653 243 ECTISSTMTELLPGQPVTIGKPIPNSTCYILDADlqpvpEGVVGEICISGVQVARGYLGNPALTaskfVPDPFWPGSRMy 322
|
410
....*....|....*....
gi 1958794461 527 -TGDMGRLDDDGFLYITGR 544
Cdd:cd17653 323 rTGDYGRWTEDGGLEFLGR 341
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
172-614 |
1.01e-16 |
|
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: 83.32 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 172 SYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVvdtq 251
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 252 kqlekilkiwkdlphlkavviyqepppkkmanvyTMEELIElgqevpeealdaiidTQQPNQCCVLVYTSGTTGNPKGVM 331
Cdd:cd05969 78 ----------------------------------TTEELYE---------------RTDPEDPTLLHYTSGTTGTPKGVL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 332 LSQD-------NGTLVNTLREVEPTSHMGVPR--------VWEKIMERIQEVAAQSGF--------IRR-KMLLWAMSVT 387
Cdd:cd05969 109 HVHDamifyyfTGKYVLDLHPDDIYWCTADPGwvtgtvygIWAPWLNGVTNVVYEGRFdaeswygiIERvKVTVWYTAPT 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 388 LEQNLTcpsndlkpftsRLADYLVLARVRQALGFAKCqknfyGAAPMTAETQRFFLG-LNIRLYAGYGLSEsTGPHFMSs 466
Cdd:cd05969 189 AIRMLM-----------KEGDELARKYDLSSLRFIHS-----VGEPLNPEAIRWGMEvFGVPIHDTWWQTE-TGSIMIA- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 467 pyNY-----RLYSSGRVVPGCRVKLVNQDADGI-----GEICL---WgRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRL 533
Cdd:cd05969 251 --NYpcmpiKPGSMGKPLPGVKAAVVDENGNELppgtkGILALkpgW-PSMFRGIWNDEERYKNSF-IDGWYLTGDLAYR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 534 DDDGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISSAMLIGDQRKFLSMLLTLKCTLNPETsEPTDNLTEQAVE 613
Cdd:cd05969 327 DEDGYFWFVGRADDIIKTS-GHRVGPFEVESAL-MEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF-EPSDELKEEIIN 403
|
.
gi 1958794461 614 F 614
Cdd:cd05969 404 F 404
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
168-700 |
1.13e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 83.94 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 168 WERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTTSSPE--ACQYIAHDCR 242
Cdd:PRK12582 78 WRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHDhaKLKHLFDLVK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 243 ANVIVVDTQKQLEKILKIwkdLPHLKAVVIYQEPPPKKMANVytmeELIELGQEVPEEALDAIIDTQQPNQCCVLVYTSG 322
Cdd:PRK12582 158 PRVVFAQSGAPFARALAA---LDLLDVTVVHVTGPGEGIASI----AFADLAATPPTAAVAAAIAAITPDTVAKYLFTSG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 323 TTGNPKGVMLSQ----DNGTLVNTLREVEPTSHMGV-----PrvWEKIMeriqevAAQSGFirrKMLLWA---------- 383
Cdd:PRK12582 231 STGMPKAVINTQrmmcANIAMQEQLRPREPDPPPPVsldwmP--WNHTM------GGNANF---NGLLWGggtlyiddgk 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 384 ----MSVTLEQNLTcpsnDLKP--FTSRLADYLVLARVRQ---ALG---FAKCQKNFYGAAPMT----AETQRFFL---G 444
Cdd:PRK12582 300 plpgMFEETIRNLR----EISPtvYGNVPAGYAMLAEAMEkddALRrsfFKNLRLMAYGGATLSddlyERMQALAVrttG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 445 LNIRLYAGYGLSE----STGPHFMSSpynyRLYSSGRVVPGCRVKLVNqdadgIG---EICLWGRTIFMGYLNMEDKTHE 517
Cdd:PRK12582 376 HRIPFYTGYGATEtaptTTGTHWDTE----RVGLIGLPLPGVELKLAP-----VGdkyEVRVKGPNVTPGYHKDPELTAA 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 518 AIDSEGWLHTGDMGR-LDDD----GfLYITGRLKELIITAGGE--NVPPVPIeEAVKMELPIISSAMLIGDQRKFLSMLl 590
Cdd:PRK12582 447 AFDEEGFYRLGDAARfVDPDdpekG-LIFDGRVAEDFKLSTGTwvSVGTLRP-DAVAACSPVIHDAVVAGQDRAFIGLL- 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 591 tlkCTLNPETseptdnlteqavefCQR-VGSKASTVSEIVgqKDEAVYQAIHEGIQRVNANAAARPYHIQKWAILERDFS 669
Cdd:PRK12582 524 ---AWPNPAA--------------CRQlAGDPDAAPEDVV--KHPAVLAILREGLSAHNAEAGGSSSRIARALLMTEPPS 584
|
570 580 590
....*....|....*....|....*....|.
gi 1958794461 670 ISGGELGPTMKLKRLTVLEKYKDIIDSFYQE 700
Cdd:PRK12582 585 IDAGEITDKGYINQRAVLERRAALVERLYAE 615
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
169-566 |
1.78e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 82.97 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 248
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DTQ--KQLEKILKIWKD------LPHLKAVVIYQEPPPKKMA-----NVYTMEELIELGQevPEEALdaiidtQQPN--- 312
Cdd:PLN02479 124 DQEffTLAEEALKILAEkkkssfKPPLLIVIGDPTCDPKSLQyalgkGAIEYEKFLETGD--PEFAW------KPPAdew 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 313 QCCVLVYTSGTTGNPKGVMLSQDNGTLVNtlreveptshMGVPRVWEkimerIQEVAAQ---------SGFIrrkmLLWA 383
Cdd:PLN02479 196 QSIALGYTSGTTASPKGVVLHHRGAYLMA----------LSNALIWG-----MNEGAVYlwtlpmfhcNGWC----FTWT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 384 MSVTLEQNLTCPSNDLKPFTSRLADYLVL-----ARVRQALGFAKCQKNFY-----------GAAP----MTAETQRFFl 443
Cdd:PLN02479 257 LAALCGTNICLRQVTAKAIYSAIANYGVThfcaaPVVLNTIVNAPKSETILplprvvhvmtaGAAPppsvLFAMSEKGF- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 444 glniRLYAGYGLSESTGPHFM--------SSPYNYRLYSSGR------------VVPGCRVKLVNQDADGIGEICLWGRT 503
Cdd:PLN02479 336 ----RVTHTYGLSETYGPSTVcawkpewdSLPPEEQARLNARqgvryiglegldVVDTKTMKPVPADGKTMGEIVMRGNM 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794461 504 IFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAV 566
Cdd:PLN02479 412 VMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIIS-GGENISSLEVENVV 472
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
446-566 |
4.18e-16 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 82.66 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 446 NIRLYAGYGLSESTG------PHFMSSPYNY----RLYSSGRVVPGCRVKLVNQD-----ADGI-GEICLWGRTIFMGYL 509
Cdd:PRK08633 923 GIRILEGYGATETSPvasvnlPDVLAADFKRqtgsKEGSVGMPLPGVAVRIVDPEtfeelPPGEdGLILIGGPQVMKGYL 1002
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794461 510 NMEDKTHEAI---DSEGWLHTGDMGRLDDDGFLYITGRLKEL--IitaGGENVPPVPIEEAV 566
Cdd:PRK08633 1003 GDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFakI---GGEMVPLGAVEEEL 1061
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
166-580 |
6.47e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 81.13 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 166 DKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANV 245
Cdd:PRK07788 70 DERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 246 IVVDtQKQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEVPEEALdaiidtqqPNQCCVLVYTSGTTG 325
Cdd:PRK07788 150 LVYD-DEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKP--------PKPGGIVILTSGTTG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 326 NPKGVMLSqdngtlvntlrevEPTShmgvPRVWEKIMERI----QEVAAQS-------GFirrkmLLWAMSVTLEQNLTC 394
Cdd:PRK07788 221 TPKGAPRP-------------EPSP----LAPLAGLLSRVpfraGETTLLPapmfhatGW-----AHLTLAMALGSTVVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 395 -----PSNDLKPFTSRLADYLVLARV---RQ-ALGFAKCQKN--------FYGAAPMTAET-QRFFLGLNIRLYAGYGls 456
Cdd:PRK07788 279 rrrfdPEATLEDIAKHKATALVVVPVmlsRIlDLGPEVLAKYdtsslkiiFVSGSALSPELaTRALEAFGPVLYNLYG-- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 457 eSTGPHFMS--SPYNYRLYSS--GRVVPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKthEAIDseGWL 525
Cdd:PRK07788 357 -STEVAFATiaTPEDLAEAPGtvGRPPKGVTVKIL--DENGnevprgvVGRIFVGNGFPFEGYTDGRDK--QIID--GLL 429
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1958794461 526 HTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISSAMLIG 580
Cdd:PRK07788 430 SSGDVGYFDEDGLLFVDGRDDDMIVS-GGENVFPAEVEDLLA-GHPDVVEAAVIG 482
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
315-580 |
7.68e-16 |
|
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: 79.27 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 315 CVLVYTSGTTGNPKGVMLSQDN-----------------------------GTLVNTLrevePTSHMG-----VPRV-WE 359
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQAllaqalvlavlqaidegtvflnsgplfhiGTLMFTL----ATFHAGgtnvfVRRVdAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 360 KIMERIQEVAAQSGFIrrkmllwaMSVTLEQNLTCPSNDLKPFTSrladylvLARVRQALGFAkcqknfygaAPMTAETQ 439
Cdd:cd17636 79 EVLELIEAERCTHAFL--------LPPTIDQIVELNADGLYDLSS-------LRSSPAAPEWN---------DMATVDTS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 440 RFFLGLnirlyAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDK 514
Cdd:cd17636 135 PWGRKP-----GGYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrevPDGeVGEIVARGPTVMAGYWNRPEV 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794461 515 THEAIDSeGWLHTGDMGRLDDDGFLYITGRlKELIITAGGENVPPVPIEEAVKmELPIISSAMLIG 580
Cdd:cd17636 210 NARRTRG-GWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYPAEVERCLR-QHPAVADAAVIG 272
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
316-583 |
8.05e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 79.70 E-value: 8.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 316 VLVYTSGTTGNPKGVMLSQDNgtlvntLREVEPTSH--MGVPRVWEKIMERIQeVAAQSGFIRRkmlLWAMSVTLEQNLT 393
Cdd:PRK07824 39 LVVATSGTTGTPKGAMLTAAA------LTASADATHdrLGGPGQWLLALPAHH-IAGLQVLVRS---VIAGSEPVELDVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 394 cPSNDLKPFTSRLAD------Y--LVLARVRQALG-------FAKCQKNFYGAAPMTAETQRFFLGLNIRLYAGYGLSES 458
Cdd:PRK07824 109 -AGFDPTALPRAVAElgggrrYtsLVPMQLAKALDdpaataaLAELDAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSET 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 459 TGphfmSSPYNyrlyssGRVVPGCRVKLVNqdadgiGEICLWGRTIFMGYLNMEDktHEAIDSEGWLHTGDMGRLDDdGF 538
Cdd:PRK07824 188 SG----GCVYD------GVPLDGVRVRVED------GRIALGGPTLAKGYRNPVD--PDPFAEPGWFRTDDLGALDD-GV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958794461 539 LYITGRLKElIITAGGENVPPVPIEEAVkMELPIISSAMLIG--DQR 583
Cdd:PRK07824 249 LTVLGRADD-AISTGGLTVLPQVVEAAL-ATHPAVADCAVFGlpDDR 293
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
192-580 |
1.25e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 80.03 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 192 LERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKQLEKILKIWKDLpHLKAVV 271
Cdd:PRK07787 42 VAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPAPDDPAGLPHVPVRL-HARSWH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 272 IYQEPPPKKMAnvytmeeLIelgqevpeealdaiidtqqpnqccvlVYTSGTTGNPKGVMLSQ-------D--------- 335
Cdd:PRK07787 121 RYPEPDPDAPA-------LI--------------------------VYTSGTTGPPKGVVLSRraiaadlDalaeawqwt 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 336 -NGTLVN----------------TLREVEPTSHMGVPRVwekimeriqEVAAQSGFIRRKML-----LWamsvtleqnlt 393
Cdd:PRK07787 168 aDDVLVHglplfhvhglvlgvlgPLRIGNRFVHTGRPTP---------EAYAQALSEGGTLYfgvptVW----------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 394 cpsndlkpftSRLADYLVLARvrqALGFAKCQKNfyGAAPM--------TAETQRfflglniRLYAGYGLSES------- 458
Cdd:PRK07787 228 ----------SRIAADPEAAR---ALRGARLLVS--GSAALpvpvfdrlAALTGH-------RPVERYGMTETlitlstr 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 459 -TGPHfmsspynyRLYSSGRVVPGCRVKLVNQD-----ADG--IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDM 530
Cdd:PRK07787 286 aDGER--------RPGWVGLPLAGVETRLVDEDggpvpHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDV 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958794461 531 GRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:PRK07787 358 AVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETAL-LGHPGVREAAVVG 406
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
170-580 |
1.45e-15 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 79.45 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVd 249
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 250 tqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielGQEVPEEALdaiidtqqpnqccvLVYTSGTTGNPKG 329
Cdd:cd05935 80 --------------------------------------------GSELDDLAL--------------IPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 330 VMLSQ-------------DNGTLVNTLREVEPTSH-------MGVPRVWEK---IMERIQEVAAQSGFIRRKMLLWAMSV 386
Cdd:cd05935 102 CMHTHfsaaanalqsavwTGLTPSDVILACLPLFHvtgfvgsLNTAVYVGGtyvLMARWDRETALELIEKYKVTFWTNIP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 387 TLEQNLTcpsNDLKPFTSRLADYLVLARvrqalgfakcqknfyGAAPM-TAETQRFFLGLNIRLYAGYGLSESTGPHFMS 465
Cdd:cd05935 182 TMLVDLL---ATPEFKTRDLSSLKVLTG---------------GGAPMpPAVAEKLLKLTGLRFVEGYGLTETMSQTHTN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 466 SPYNYRLYSSGrvVPGCRVKLVNQDA-DGI-------GEICLWGRTIFMGYLNMEDKTHEA---IDSEGWLHTGDMGRLD 534
Cdd:cd05935 244 PPLRPKLQCLG--IP*FGVDARVIDIeTGRelppnevGEIVVRGPQIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMD 321
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958794461 535 DDGFLYITGRLKELIITAGGEnVPPVPIeEAVKMELPIISSAMLIG 580
Cdd:cd05935 322 EEGYFFFVDRVKRMINVSGFK-VWPAEV-EAKLYKHPAI*EVCVIS 365
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
121-569 |
4.39e-15 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 78.89 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 121 TTRADGRVRlRLEPFCTqlpytvhqmFYEALDkYGNLSALGFKRKD-KWERISYYQYYLI---ARKVAKGFLKLGLERAH 196
Cdd:PRK09192 7 TPTTSSLPR-RYADFPT---------LVEALD-YAALGEAGMNFYDrRGQLEEALPYQTLrarAEAGARRLLALGLKPGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 197 SVAILGFNSPEW---FFSAVgtvFAGG------IVTGIyttSSPEAcqYIAH------DCRANVIVVDtqkqlekilKIW 261
Cdd:PRK09192 76 RVALIAETDGDFveaFFACQ---YAGLvpvplpLPMGF---GGRES--YIAQlrgmlaSAQPAAIITP---------DEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 262 KDLphLKAVVIYQEPPpkkmaNVYTMEELIELgqevpeEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQdnGTLVN 341
Cdd:PRK09192 139 LPW--VNEATHGNPLL-----HVLSHAWFKAL------PEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITH--RALMA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 342 TLR-------EVEPTS---------H-MGV------PrvwekimeriqeVAAQ--------SGFIRRKmLLW-------- 382
Cdd:PRK09192 204 NLRaishdglKVRPGDrcvswlpfyHdMGLvgflltP------------VATQlsvdylptRDFARRP-LQWldlisrnr 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 383 ---AMSVTLEQNLtCPsndLKPFTSRLADyLVLARVRQAlGFakcqknfyGAAPMTAETQRFF------LGLNIRLY-AG 452
Cdd:PRK09192 271 gtiSYSPPFGYEL-CA---RRVNSKDLAE-LDLSCWRVA-GI--------GADMIRPDVLHQFaeafapAGFDDKAFmPS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 453 YGLSEST------------------------GPHFMSSPYNYRLYSS----GRVVPGCRVKLVNQDAD-----GIGEICL 499
Cdd:PRK09192 337 YGLAEATlavsfsplgsgivveevdrdrleyQGKAVAPGAETRRVRTfvncGKALPGHEIEIRNEAGMplperVVGHICV 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 500 WGRTIFMGYLNMEDkTHEAIDSEGWLHTGDMGRLDDdGFLYITGRLKELIITaGGENVPPVPIEEAVKME 569
Cdd:PRK09192 417 RGPSLMSGYFRDEE-SQDVLAADGWLDTGDLGYLLD-GYLYITGRAKDLIII-NGRNIWPQDIEWIAEQE 483
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
170-583 |
7.05e-15 |
|
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: 77.93 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSP-EACQYIAHDCRANVIVV 248
Cdd:cd05923 28 RLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAaELAELIERGEMTAAVIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DTQKQLEKILKiwkdlphlkavviyqepppkKMANVYTMEELIELGqeVPEEALDAIIDTQ-QPNQCCVLVYTSGTTGNP 327
Cdd:cd05923 108 VDAQVMDAIFQ--------------------SGVRVLALSDLVGLG--EPESAGPLIEDPPrEPEQPAFVFYTSGTTGLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 328 KGVMLSQdngtlvntlREVEPtshmgvprvwekimeRIQEVAAQSG--FIRRKMLLWAMSV------------TLEQNLT 393
Cdd:cd05923 166 KGAVIPQ---------RAAES---------------RVLFMSTQAGlrHGRHNVVLGLMPLyhvigffavlvaALALDGT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 394 -CPSNDLKP----------------FTSRLADYLV---------LARVRQaLGFAkcqknfyGAAPMTAETQRFFLGLNI 447
Cdd:cd05923 222 yVVVEEFDPadalklieqervtslfATPTHLDALAaaaefaglkLSSLRH-VTFA-------GATMPDAVLERVNQHLPG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 448 RLYAGYGLSESTGPHFMSSPYNYR-----LYSSGRVVP--GCRVKLVNQDADGIGEICLWGRTIFMGYLNMEDKTHEAId 520
Cdd:cd05923 294 EKVNIYGTTEAMNSLYMRDARTGTemrpgFFSEVRIVRigGSPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKKL- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958794461 521 SEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKMElPIISSAMLIG--DQR 583
Cdd:cd05923 373 QDGWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHPSEIERVLSRH-PGVTEVVVIGvaDER 435
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
180-565 |
1.24e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 76.87 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 180 ARKVAKGFLKLGLERAHSVAILGFNSPEWFfsavgTVFAGGIVTGIYTT------SSPEAcQYIAHDCRANVIVVDtQKQ 253
Cdd:PRK08276 21 SNRLAHGLRALGLREGDVVAILLENNPEFF-----EVYWAARRSGLYYTpinwhlTAAEI-AYIVDDSGAKVLIVS-AAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 254 LEKILKIWKDLP-HLKAVVIYQEPPPkkmanvytmeelielGQEVPEEALDAIIDTQQPNQC--CVLVYTSGTTGNPKGV 330
Cdd:PRK08276 94 ADTAAELAAELPaGVPLLLVVAGPVP---------------GFRSYEEALAAQPDTPIADETagADMLYSSGTTGRPKGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 331 mlsqdngtlvntLREVEPTshmgvprvwekimeRIQEVAAQ-SGFIRRKM-------------------LLWAMSV---- 386
Cdd:PRK08276 159 ------------KRPLPGL--------------DPDEAPGMmLALLGFGMyggpdsvylspaplyhtapLRFGMSAlalg 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 387 -TL--------EQNL--------TCpsNDLKP--FTsRLadyLVLAR-VRQALGFAKCQKNFYGAAPMTAETQRFFL--- 443
Cdd:PRK08276 213 gTVvvmekfdaEEALalieryrvTH--SQLVPtmFV-RM---LKLPEeVRARYDVSSLRVAIHAAAPCPVEVKRAMIdww 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 444 GLNIRLYagYGLSESTGPHFMSS------PYnyrlySSGRVVPGcRVKLVNQDADGI--GEIclwGrTIFM-------GY 508
Cdd:PRK08276 287 GPIIHEY--YASSEGGGVTVITSedwlahPG-----SVGKAVLG-EVRILDEDGNELppGEI---G-TVYFemdgypfEY 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794461 509 LNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEA 565
Cdd:PRK08276 355 HNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIIS-GGVNIYPQEIENL 410
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
296-545 |
1.30e-14 |
|
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: 76.52 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 296 EVPEEALDAIIDTQQP-------NQCCVLVYTSGTTGNPKGVMLSQDNgtLVNTLReveptsHMgvprVWEKIMERIQEV 368
Cdd:cd05945 74 SSPAERIREILDAAKPalliadgDDNAYIIFTSGSTGRPKGVQISHDN--LVSFTN------WM----LSDFPLGPGDVF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 369 AAQSGF-IRRKMLLWAMSVTLEQNLTCPSNDLKPFTSRLADYLV---------------LARVRQALgfakCQKN----- 427
Cdd:cd05945 142 LNQAPFsFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAehgitvwvstpsfaaMCLLSPTF----TPESlpslr 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 428 ---FYG---AAPMTAETQRFFLGLNIrlYAGYGLSESTG--------PHFMSSpyNYRLYSsGRVVPGCRVKLVNQDAD- 492
Cdd:cd05945 218 hflFCGevlPHKTARALQQRFPDARI--YNTYGPTEATVavtyievtPEVLDG--YDRLPI-GYAKPGAKLVILDEDGRp 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 493 ----GIGEICLWGRTIFMGYLNMEDKTHEA---IDSEGWLHTGDMGRLDDDGFLYITGRL 545
Cdd:cd05945 293 vppgEKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRLEADGLLFYRGRL 352
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
309-569 |
1.90e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 76.37 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 309 QQPNQCCVLVYTSGTTGNPKGVMLSQDNgtLVNTLREVE---------------PTSH-MG------VPrvweKIMERIQ 366
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHEN--LVHNMFAILnstewktkdrilswmPLTHdMGliafhlAP----LIAGMNQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 367 EVAAQSGFIRRKML-LWAMSVTLEQNLTCPSNDLKPFTSRLADYLV----LARVRQALGfakcqknfyGAAPMTAETQRF 441
Cdd:cd05908 177 YLMPTRLFIRRPILwLKKASEHKATIVSSPNFGYKYFLKTLKPEKAndwdLSSIRMILN---------GAEPIDYELCHE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 442 FL------GLNIR-LYAGYGLSEST--------GPHFM--------------------SSPYNYRLYSSGRVVPGCRVKL 486
Cdd:cd05908 248 FLdhmskyGLKRNaILPVYGLAEASvgaslpkaQSPFKtitlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIRI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 487 VNQDADG-----IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGrLDDDGFLYITGRLKELIITaGGENVPPVP 561
Cdd:cd05908 328 CDEDNKIlpdgyIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKDIIFV-NGQNVYPHD 405
|
....*....
gi 1958794461 562 IEE-AVKME 569
Cdd:cd05908 406 IERiAEELE 414
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
171-584 |
2.58e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 76.32 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 171 ISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV-- 248
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVwp 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 -----DTQKQLEKILKiwKDLPHLKAVVIYQE-----PPPKKMANVytmeelIELGQEVPEEALDAIIDTQQPNQCCVLV 318
Cdd:PRK06164 116 gfkgiDFAAILAAVPP--DALPPLRAIAVVDDaadatPAPAPGARV------QLFALPDPAPPAAAGERAADPDAGALLF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 319 YTSGTTGNPKGVMLSQDngTLVNTLREV------EPTS---------------------HMGVPRVWEKIME-------- 363
Cdd:PRK06164 188 TTSGTTSGPKLVLHRQA--TLLRHARAIaraygyDPGAvllaalpfcgvfgfstllgalAGGAPLVCEPVFDaartaral 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 364 ---RIQEVAAQSGFIRRkmllwaMSVTLEQNLTCPSNDL---KPFTSRLADYLVLARVRqalgfakcqknfygAAPMTae 437
Cdd:PRK06164 266 rrhRVTHTFGNDEMLRR------ILDTAGERADFPSARLfgfASFAPALGELAALARAR--------------GVPLT-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 438 tqrfflGLnirlyagYGLSE-----STGPhfMSSPYNYRLYSSGRVV-PGCRVKLVNQDADGI------GEICLWGRTIF 505
Cdd:PRK06164 324 ------GL-------YGSSEvqalvALQP--ATDPVSVRIEGGGRPAsPEARVRARDPQDGALlpdgesGEIEIRAPSLM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 506 MGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDG-FLYITgRLKElIITAGGENVPPVPIEEAVKmELPIISSAMLIGDQRK 584
Cdd:PRK06164 389 RGYLDNPDATARALTDDGYFRTGDLGYTRGDGqFVYQT-RMGD-SLRLGGFLVNPAEIEHALE-ALPGVAAAQVVGATRD 465
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
169-583 |
2.82e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 76.08 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTtssPEACQYIAHDCRANV 245
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyrYV---EDELRYLLDDSDAVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 246 IVVDTQkQLEKILKIWKDLPHLK-AVVIYQEPPPKKMANVYTMEELIELG---QEVPEEALDAIIdtqqpnqccvLVYTS 321
Cdd:PRK07798 104 LVYERE-FAPRVAEVLPRLPKLRtLVVVEDGSGNDLLPGAVDYEDALAAGspeRDFGERSPDDLY----------LLYTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 322 GTTGNPKGVMLSQDNgtlvntLREV--EPTSHMGVPRVweKIMERIQEVAAQSGFIRRKML--------LWAMSVTLEQN 391
Cdd:PRK07798 173 GTTGMPKGVMWRQED------IFRVllGGRDFATGEPI--EDEEELAKRAAAGPGMRRFPApplmhgagQWAAFAALFSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 392 LTCPSNDLKPF----TSRLAD---YLVLARVRQAlgFAK------CQKNFY----------GAAPMTAETQRFFLGL--N 446
Cdd:PRK07798 245 QTVVLLPDVRFdadeVWRTIErekVNVITIVGDA--MARplldalEARGPYdlsslfaiasGGALFSPSVKEALLELlpN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 447 IRLYAGYGLSEsTGphFMSSPYNyrlySSG-------RVVPGCRVKLVNQD-------ADGIGEICLWGRtIFMGYLNME 512
Cdd:PRK07798 323 VVLTDSIGSSE-TG--FGGSGTV----AKGavhtggpRFTIGPRTVVLDEDgnpvepgSGEIGWIARRGH-IPLGYYKDP 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794461 513 DKTHEA---IDSEGWLHTGDMGRLDDDGFLYITGRlKELIITAGGENVPPVPIEEAVKMElPIISSAMLIG--DQR 583
Cdd:PRK07798 395 EKTAETfptIDGVRYAIPGDRARVEADGTITLLGR-GSVCINTGGEKVFPEEVEEALKAH-PDVADALVVGvpDER 468
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
474-566 |
5.66e-14 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 74.65 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 474 SSGRVVPGCRVKLVNQDadgIGEICLWGRTIFMGYLNmedkthEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaG 553
Cdd:PRK07445 284 SSGQVLPHAQITIPANQ---TGNITIQAQSLALGYYP------QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-G 353
|
90
....*....|...
gi 1958794461 554 GENVPPVPIEEAV 566
Cdd:PRK07445 354 GENVYPAEVEAAI 366
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
452-568 |
3.52e-13 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 72.75 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 452 GYGLSEsTGPHFMSSPYNYRLYSS--GRVVPGCRVKLvnQDADG-------IGEICLWGRTIFMGYLNMEDKTHEAIDSE 522
Cdd:PRK07059 358 GYGLSE-TSPVATCNPVDATEFSGtiGLPLPSTEVSI--RDDDGndlplgePGEICIRGPQVMAGYWNRPDETAKVMTAD 434
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1958794461 523 GWLHTGDMGRLDDDGFLYITGRLKELIITAGGeNVPPVPIEEAVKM 568
Cdd:PRK07059 435 GFFRTGDVGVMDERGYTKIVDRKKDMILVSGF-NVYPNEIEEVVAS 479
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
415-580 |
4.82e-13 |
|
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: 72.02 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 415 VRQALGFAKCQKNFYGAAPMTAETQRFFLGL-NIRLYAGYGLSESTGPHFMSS------PYnyrlySSGRVVPGcRVKLV 487
Cdd:cd05929 237 VRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWgGPIIWEYYGGTEGQGLTIINGeewlthPG-----SVGRAVLG-KVHIL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 488 nqDADG-------IGEICLWGRTIFMgYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPV 560
Cdd:cd05929 311 --DEDGnevppgeIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIIS-GGVNIYPQ 386
|
170 180
....*....|....*....|
gi 1958794461 561 PIEEAVkMELPIISSAMLIG 580
Cdd:cd05929 387 EIENAL-IAHPKVLDAAVVG 405
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
306-555 |
4.99e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 72.44 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 306 IDTQQPNQCCVLVYTSGTTGNPKGVMLSQDN--GTLV-----NTLREVEPTSHM-------------------------- 352
Cdd:PTZ00342 298 IQNEDPDFITSIVYTSGTSGKPKGVMLSNKNlyNTVVplckhSIFKKYNPKTHLsylpishiyerviaylsfmlggtini 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 353 ---------------------GVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPSNDLKPFTSrladylV 411
Cdd:PTZ00342 378 wskdinyfskdiynskgnilaGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILSLRKSNNNGGFSKFLEGITH------I 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 412 LARVRQALGfAKCQKNFYGAAPMTAETQR-FFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYS-SGRVVPGCRVKLVN- 488
Cdd:PTZ00342 452 SSKIKDKVN-PNLEVILNGGGKLSPKIAEeLSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESiGGPISPNTKYKVRTw 530
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794461 489 -----QDADGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGE 555
Cdd:PTZ00342 531 etykaTDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGE 602
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
479-584 |
5.05e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 72.00 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 479 VPGCRVKLVNQDADGI------GEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITA 552
Cdd:PRK06178 393 VPGTEFKICDFETGELlplgaeGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
90 100 110
....*....|....*....|....*....|....*
gi 1958794461 553 GGENVPPvpiE-EAVKMELPIISSAMLIG--DQRK 584
Cdd:PRK06178 472 GMSVFPS---EvEALLGQHPAVLGSAVVGrpDPDK 503
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
310-584 |
5.86e-13 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 72.69 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 310 QPNQCCVLVYTSGTTGNPKGVMLSQDNgtlvntlreveptshmgvprvwekIMERIQEVAAQSGFIRRKMLLWAMSVTLE 389
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRN------------------------LLANRAQVAARIDFSPEDKVFNALPVFHS 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 390 QNLTC---------------PSndlkPFTSRLADYLVL-----------------ARVRQALGFAKCQKNFYGAAPMTAE 437
Cdd:PRK06814 847 FGLTGglvlpllsgvkvflyPS----PLHYRIIPELIYdtnatilfgtdtflngyARYAHPYDFRSLRYVFAGAEKVKEE 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 438 TQRFFL-GLNIRLYAGYGLSEsTGPHF-MSSPYNYRLYSSGRVVPGCRVKLvnQDADGI---GEICLWGRTIFMGYLNME 512
Cdd:PRK06814 923 TRQTWMeKFGIRILEGYGVTE-TAPVIaLNTPMHNKAGTVGRLLPGIEYRL--EPVPGIdegGRLFVRGPNVMLGYLRAE 999
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958794461 513 DK-THEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIEEAVKMELP-IISSAMLIGDQRK 584
Cdd:PRK06814 1000 NPgVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRF-AKIAGEMISLAAVEELAAELWPdALHAAVSIPDARK 1071
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
169-580 |
5.97e-13 |
|
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: 71.31 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 248
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DtqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqEVPEEALdaiidtqqpnqccvLVYTSGTTGNPK 328
Cdd:cd05971 85 D----------------------------------------------GSDDPAL--------------IIYTSGTTGPPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 329 GVM--------------LSQDN-----------------GTLVNTLRevePTSHMGVPRVWEKiMERIQEVAAQSgfirr 377
Cdd:cd05971 105 GALhahrvllghlpgvqFPFNLfprdgdlywtpadwawiGGLLDVLL---PSLYFGVPVLAHR-MTKFDPKAALD----- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 378 kmLLWAMSVTleqNLTCPSNDLKPFtSRLADYLVLARVR-QALGFAkcqknfyGAAPMTAETQRFFLGLNIRLYAGYGLS 456
Cdd:cd05971 176 --LMSRYGVT---TAFLPPTALKMM-RQQGEQLKHAQVKlRAIATG-------GESLGEELLGWAREQFGVEVNEFYGQT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 457 ES---TGPHfmSSPYNYRLYSSGRVVPGCRVKLVNQDA-----DGIGEICLwgRT----IFMGYLNMEDKThEAIDSEGW 524
Cdd:cd05971 243 ECnlvIGNC--SALFPIKPGSMGKPIPGHRVAIVDDNGtplppGEVGEIAV--ELpdpvAFLGYWNNPSAT-EKKMAGDW 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794461 525 LHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:cd05971 318 LLTGDLGRKDSDGYFWYVGRDDD-VITSSGYRIGPAEIEECL-LKHPAVLMAAVVG 371
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
182-566 |
9.98e-13 |
|
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: 70.99 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 182 KVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTgiyttssPEACQYIAHDcranvIVVDTQK-QLEKILKI 260
Cdd:cd05970 59 KTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAI-------PATHQLTAKD-----IVYRIESaDIKMIVAI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 261 WKDlphlkavvIYQEPPPKKMANVYTMEELIELGQEVPE--EALDAIIDTQQP-------------NQCCVLVYTSGTTG 325
Cdd:cd05970 127 AED--------NIPEEIEKAAPECPSKPKLVWVGDPVPEgwIDFRKLIKNASPdferptansypcgEDILLVYFSSGTTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 326 NPKgvMLSQDNgtlvntlreVEPTSHMGVPRVWEKIMER-IQEVAAQSGfirrkmllWAMSV--TLEQNLTCPSN----D 398
Cdd:cd05970 199 MPK--MVEHDF---------TYPLGHIVTAKYWQNVREGgLHLTVADTG--------WGKAVwgKIYGQWIAGAAvfvyD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 399 LKPFT-----SRLADYLVLA----------RVRQALG---FAKCQKNFYGAAPMTAET-QRFFLGLNIRLYAGYGLSE-- 457
Cdd:cd05970 260 YDKFDpkallEKLSKYGVTTfcapptiyrfLIREDLSrydLSSLRYCTTAGEALNPEVfNTFKEKTGIKLMEGFGQTEtt 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 458 ---STGPHFMSSPYnyrlySSGRVVPGCRVKLVNQDADGI-----GEICLwgRT-------IFMGYLNMEDKTHEAIdSE 522
Cdd:cd05970 340 ltiATFPWMEPKPG-----SMGKPAPGYEIDLIDREGRSCeageeGEIVI--RTskgkpvgLFGGYYKDAEKTAEVW-HD 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958794461 523 GWLHTGDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEEAV 566
Cdd:cd05970 412 GYYHTGDAAWMDEDGYLWFVGRTDDLIKSS-GYRIGPFEVESAL 454
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
414-563 |
1.51e-12 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 70.69 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 414 RVRQALGFAK-CqknfygAAPMTAET----QRFFLGlniRLYAGYGLSESTgpHFMSSPynyRLYSSGR-----VVPG-- 481
Cdd:PRK05852 292 RKPAALRFIRsC------SAPLTAETaqalQTEFAA---PVVCAFGMTEAT--HQVTTT---QIEGIGQtenpvVSTGlv 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 482 -----CRVKLVNQD-----ADGIGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELiIT 551
Cdd:PRK05852 358 grstgAQIRIVGSDglplpAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKEL-IN 435
|
170
....*....|..
gi 1958794461 552 AGGENVPPVPIE 563
Cdd:PRK05852 436 RGGEKISPERVE 447
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
137-580 |
1.96e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.42 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 137 TQLPYTVHQMFYEALDKygNLSALGFKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTV 216
Cdd:PRK05857 10 PQLPSTVLDRVFEQARQ--QPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 217 FAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKQLEkilkiwkdlphlkavviyQEPPPKKMANVYTMEELIELGQE 296
Cdd:PRK05857 88 KLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMA------------------SSAVPEALHSIPVIAVDIAAVTR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 297 VPEEALDAIIDTQQPN----QCCVLVYTSGTTGNPKGVMLSqdNGTLV---NTLREVE----------------PTSHMG 353
Cdd:PRK05857 150 ESEHSLDAASLAGNADqgseDPLAMIFTSGTTGEPKAVLLA--NRTFFavpDILQKEGlnwvtwvvgettysplPATHIG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 354 vpRVWEKIMERIQEVAAQSGFiRRKMLLWAMSVTLEQNLTCpsndLKP-FTSRLADYLVLARVR-QALGFAKcqknfYGA 431
Cdd:PRK05857 228 --GLWWILTCLMHGGLCVTGG-ENTTSLLEILTTNAVATTC----LVPtLLSKLVSELKSANATvPSLRLVG-----YGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 432 APMTAETQRFFLGLNIRLYAGYGLSEsTGPHFMSSPYNYRLYSS------GRVVPGCRVKLvnQDADGIGEIC------- 498
Cdd:PRK05857 296 SRAIAADVRFIEATGVRTAQVYGLSE-TGCTALCLPTDDGSIVKieagavGRPYPGVDVYL--AATDGIGPTApgagpsa 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 499 ----LWGRTI--FMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPP---------VP-I 562
Cdd:PRK05857 373 sfgtLWIKSPanMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPdevdriaegVSgV 450
|
490
....*....|....*...
gi 1958794461 563 EEAVKMELPIISSAMLIG 580
Cdd:PRK05857 451 REAACYEIPDEEFGALVG 468
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
446-580 |
2.06e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 69.81 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 446 NIRLYAGYGLSESTGPHFMSSPYNYRLYSS-GRVVPGCRVKLVNQD-----ADGIGEICLWGRTIFMGYLNmEDKTHEAI 519
Cdd:PRK07638 279 YAKLYEFYGASELSFVTALVDEESERRPNSvGRPFHNVQVRICNEAgeevqKGEIGTVYVKSPQFFMGYII-GGVLAREL 357
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958794461 520 DSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISSAMLIG 580
Cdd:PRK07638 358 NADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIES-VLHEHPAVDEIVVIG 416
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
439-583 |
7.96e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 68.10 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 439 QRFFLGLNIRLYAGYGLSEsTGPHFMSSPYNYRLY--SSGRVVPGCRVKLVNQDADGIGEIcLWGRTIFMGYLNMEDKT- 515
Cdd:PRK13383 310 QRFMDTYGDILYNGYGSTE-VGIGALATPADLRDApeTVGKPVAGCPVRILDRNNRPVGPR-VTGRIFVGGELAGTRYTd 387
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794461 516 ---HEAIDseGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKMElPIISSAMLIG--DQR 583
Cdd:PRK13383 388 gggKAVVD--GMTSTGDMGYLDNAGRLFIVGREDDMIIS-GGENVYPRAVENALAAH-PAVADNAVIGvpDER 456
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
227-612 |
8.98e-12 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 68.25 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 227 TTSSPEACQYIAHDCRANVIVVDtQKQLEKILKIWKDLPHLKAVVIYQEPPPKkmanvYTMEELIE--LGQEVPeealda 304
Cdd:PRK13382 125 TSFAGPALAEVVTREGVDTVIYD-EEFSATVDRALADCPQATRIVAWTDEDHD-----LTVEVLIAahAGQRPE------ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 305 iidtQQPNQCCVLVYTSGTTGNPKGVmlsqdngtlvntlREVEPtshmGVPRVWEKIMERIQEVAAQSGFIRRKML-LWA 383
Cdd:PRK13382 193 ----PTGRKGRVILLTSGTTGTPKGA-------------RRSGP----GGIGTLKAILDRTPWRAEEPTVIVAPMFhAWG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 384 MS-VTLEQNLTCPSNDLKPFtsRLADYLVLARVRQALGFAKCQKNFYGAAPMTAETQRFFLGLNIRLYAGYGlsESTGPH 462
Cdd:PRK13382 252 FSqLVLAASLACTIVTRRRF--DPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASG--SRMRPD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 463 ----FMS--SPYNYRLYSS---------------------GRVVPGCRVKLVNQD----ADG-IGEICLWGRTIFMGYLN 510
Cdd:PRK13382 328 vviaFMDqfGDVIYNNYNAteagmiatatpadlraapdtaGRPAEGTEIRILDQDfrevPTGeVGTIFVRNDTQFDGYTS 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 511 MEDK-THEaidseGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG-DQRKFLSM 588
Cdd:PRK13382 408 GSTKdFHD-----GFMASGDVGYLDENGRLFVVGRDDEMIVS-GGENVYPIEVEKTL-ATHPDVAEAAVIGvDDEQYGQR 480
|
410 420 430
....*....|....*....|....*....|.
gi 1958794461 589 L-----LTLKCTLNPET--SEPTDNLTEQAV 612
Cdd:PRK13382 481 LaafvvLKPGASATPETlkQHVRDNLANYKV 511
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
309-553 |
5.72e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 65.89 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 309 QQPNQCCVLVYTSGTTGNPKGVMLSQdNGTLVNtlreveptshmgvprvwekiMERIQEVA---AQSGFIRRKMLLWA-- 383
Cdd:PRK08043 362 QQPEDAALILFTSGSEGHPKGVVHSH-KSLLAN--------------------VEQIKTIAdftPNDRFMSALPLFHSfg 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 384 MSVTLEQNLTC-------PSndlkPFTSRLADYLVL-----------------ARVRQALGFAKCQKNFYGAAPMTAETQ 439
Cdd:PRK08043 421 LTVGLFTPLLTgaevflyPS----PLHYRIVPELVYdrnctvlfgtstflgnyARFANPYDFARLRYVVAGAEKLQESTK 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 440 RFFLG-LNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNqdADGI---GEICLWGRTIFMGYLNMED-- 513
Cdd:PRK08043 497 QLWQDkFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLS--VPGIeqgGRLQLKGPNIMNGYLRVEKpg 574
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958794461 514 --KTHEAIDSEG-----WLHTGDMGRLDDDGFLYITGRLKELIITAG 553
Cdd:PRK08043 575 vlEVPTAENARGemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
317-544 |
6.27e-11 |
|
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: 65.44 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 317 LVYTSGTTGNPKGVMLSqdNGTLVNTLREVEPTSHMGvPRvwekimERIQEVAAqSGFirrKMLLWAMSVTL--EQNLTC 394
Cdd:cd17651 141 VIYTSGSTGRPKGVVMP--HRSLANLVAWQARASSLG-PG------ARTLQFAG-LGF---DVSVQEIFSTLcaGATLVL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 395 PSNDLKPFTSRLADYLVLARVR---------QALGFAKCQKNFYGAA-----------PMTAETQRFFLGL-NIRLYAGY 453
Cdd:cd17651 208 PPEEVRTDPPALAAWLDEQRISrvflptvalRALAEHGRPLGVRLAAlrylltggeqlVLTEDLREFCAGLpGLRLHNHY 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 454 GLSEStgpHFMSS------PYNYRLYSS-GRVVPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTHEAI 519
Cdd:cd17651 288 GPTET---HVVTAlslpgdPAAWPAPPPiGRPIDNTRVYVL--DAALrpvppgvPGELYIGGAGLARGYLNRPELTAERF 362
|
250 260 270
....*....|....*....|....*....|.
gi 1958794461 520 DSEGWL------HTGDMGRLDDDGFLYITGR 544
Cdd:cd17651 363 VPDPFVpgarmyRTGDLARWLPDGELEFLGR 393
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
430-565 |
6.79e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 65.17 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 430 GAAPMTAETQRFflGLNIR-LYAGYGLSESTGPHFMSSP---------------YNYRLYSSGRVVPGCRVKLVNQDAD- 492
Cdd:PRK05851 288 GFERFATAMAPF--GFDAGaAAPSYGLAESTCAVTVPVPgiglrvdevttddgsGARRHAVLGNPIPGMEVRISPGDGAa 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794461 493 -----GIGEICLWGRTIFMGYLNmedktHEAIDSEGWLHTGDMGRLDDDGfLYITGRLKELIITAgGENVPPVPIEEA 565
Cdd:PRK05851 366 gvagrEIGEIEIRGASMMSGYLG-----QAPIDPDDWFPTGDLGYLVDGG-LVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
304-579 |
9.19e-11 |
|
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: 64.70 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 304 AIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQdnGTLVNTLREVEPTSHMG----------------VPRVWEKIME---- 363
Cdd:cd17649 86 GLLLTHHPRQLAYVIYTSGSTGTPKGVAVSH--GPLAAHCQATAERYGLTpgdrelqfasfnfdgaHEQLLPPLICgacv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 364 --RIQEVAAQSGFIRRKMLLWAMSVTleqnltcpsnDLKP-FTSRLADYL--VLARVRQALGfakcQKNFYGAApMTAET 438
Cdd:cd17649 164 vlRPDELWASADELAEMVRELGVTVL----------DLPPaYLQQLAEEAdrTGDGRPPSLR----LYIFGGEA-LSPEL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 439 QRFFLGLNIRLYAGYGLSES--TGPHFMSSPYNYRLYSS---GRVVPGCRVKLVNQDA-----DGIGEICLWGRTIFMGY 508
Cdd:cd17649 229 LRRWLKAPVRLFNAYGPTEAtvTPLVWKCEAGAARAGASmpiGRPLGGRSAYILDADLnpvpvGVTGELYIGGEGLARGY 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794461 509 LNMEDKTHEAI-----DSEG--WLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIEEAVkMELPIISSAMLI 579
Cdd:cd17649 309 LGRPELTAERFvpdpfGAPGsrLYRTGDLARWRDDGVIEYLGRVDHQ-VKIRGFRIELGEIEAAL-LEHPGVREAAVV 384
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
169-580 |
9.22e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 248
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DTQkqlekilkiwkdlphLKAVVIYQEPPpkkmanvytMEELIELGQEVP-----EEALDAIID--TQQPnqC-CVLVYT 320
Cdd:PRK13390 103 SAA---------------LDGLAAKVGAD---------LPLRLSFGGEIDgfgsfEAALAGAGPrlTEQP--CgAVMLYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 321 SGTTGNPKGVM-------LSQDNGTLVNTLREV------------EPTSHmGVPRVW---------EKIMERIQEVAAQS 372
Cdd:PRK13390 157 SGTTGFPKGIQpdlpgrdVDAPGDPIVAIARAFydisesdiyyssAPIYH-AAPLRWcsmvhalggTVVLAKRFDAQATL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 373 GFIRRkmllwaMSVTLEQNLtcPSNdlkpFTSRLAdylVLARVRQALGFAKCQKNFYGAAPMTAETQRFFLG-LNIRLYA 451
Cdd:PRK13390 236 GHVER------YRITVTQMV--PTM----FVRLLK---LDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDwLGPIVYE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 452 GYGLSESTGPHFMSSP-YNYRLYSSGRVVPGcrvKLVNQDADG-------IGEICLWGRTIFMGYLNMEDKTHEAIDSEG 523
Cdd:PRK13390 301 YYSSTEAHGMTFIDSPdWLAHPGSVGRSVLG---DLHICDDDGnelpagrIGTVYFERDRLPFRYLNDPEKTAAAQHPAH 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794461 524 --WLHTGDMGRLDDDGFLYITGRlKELIITAGGENVPPVPIEEAVKMElPIISSAMLIG 580
Cdd:PRK13390 378 pfWTTVGDLGSVDEDGYLYLADR-KSFMIISGGVNIYPQETENALTMH-PAVHDVAVIG 434
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
298-544 |
1.95e-10 |
|
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: 63.72 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 298 PEEALDAIID--------TQQPNQCCVLVYTSGTTGNPKGVMLSQdnGTLVNTLR------EVEPTS------------- 350
Cdd:cd05918 84 PLQRLQEILQdtgakvvlTSSPSDAAYVIFTSGSTGKPKGVVIEH--RALSTSALahgralGLTSESrvlqfasytfdvs 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 351 ---------HMG---VPRvwEKimERIQEVAaqsGFIRRKMLLWAMsvtleqnLTcPSndlkpfTSRLAD--------YL 410
Cdd:cd05918 162 ileifttlaAGGclcIPS--EE--DRLNDLA---GFINRLRVTWAF-------LT-PS------VARLLDpedvpslrTL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 411 VLarvrqalgfakcqknfyGAAPMTAETQRFFLGlNIRLYAGYGLSESTgphfMSSPYNYRLYSS-----GRVVpGCRVK 485
Cdd:cd05918 221 VL-----------------GGEALTQSDVDTWAD-RVRLINAYGPAECT----IAATVSPVVPSTdprniGRPL-GATCW 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958794461 486 LVNQD-------ADGIGEICLWGRTIFMGYLNMEDKTHEA-IDSEGWLH------------TGDMGRLDDDGFLYITGR 544
Cdd:cd05918 278 VVDPDnhdrlvpIGAVGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGR 356
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
170-580 |
2.55e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 63.57 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 170 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 249
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 250 TQKqLEKILKIWKDLPHLKAVVIyqepppkkMANVYTMEElielgQEVPEEALDAIIDTQQP---------NQCCVLVYT 320
Cdd:PRK07008 119 LTF-LPLVDALAPQCPNVKGWVA--------MTDAAHLPA-----GSTPLLCYETLVGAQDGdydwprfdeNQASSLCYT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 321 SGTTGNPKGVMLSQDNGTL---------------------------VNT----------------------------LRE 345
Cdd:PRK07008 185 SGTTGNPKGALYSHRSTVLhaygaalpdamglsardavlpvvpmfhVNAwglpysapltgaklvlpgpdldgkslyeLIE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 346 VEP-TSHMGVPRVWEKIMERIQEVAAQSGFIRRkmllwamsvTLEQNLTCPSNDLKPFTsrlADYLVlaRVRQALGfakc 424
Cdd:PRK07008 265 AERvTFSAGVPTVWLGLLNHMREAGLRFSTLRR---------TVIGGSACPPAMIRTFE---DEYGV--EVIHAWG---- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 425 qknfygaapMTAETQrffLGLNIRLYAGY-GLSESTGPHfmsspynyRLYSSGRVVPGCRVKLVNQDA-----DGI--GE 496
Cdd:PRK07008 327 ---------MTEMSP---LGTLCKLKWKHsQLPLDEQRK--------LLEKQGRVIYGVDMKIVGDDGrelpwDGKafGD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 497 ICLWGRTIFMGYLNMEDKTHeaidSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEEaVKMELPIISSA 576
Cdd:PRK07008 387 LQVRGPWVIDRYFRGDASPL----VDGWFPTGDVATIDADGFMQITDRSKD-VIKSGGEWISSIDIEN-VAVAHPAVAEA 460
|
....
gi 1958794461 577 MLIG 580
Cdd:PRK07008 461 ACIA 464
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
169-579 |
5.10e-10 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 62.49 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVv 248
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 dTQKQLEKILKIWKDLPHLKAVVIYQEPPPkkmanvytmeeliELGQEVPEEALDAIIdtqqpnqccvlvYTSGTTGNPK 328
Cdd:cd17656 91 -TQRHLKSKLSFNKSTILLEDPSISQEDTS-------------NIDYINNSDDLLYII------------YTSGTTGKPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 329 GVMLSQDNgtLVNTLrEVEPTsHMGVPRvwekiMERIQEVAAQSGFIRRKMLLWAMsvTLEQNLTCPSNDLKPFTSRLAD 408
Cdd:cd17656 145 GVQLEHKN--MVNLL-HFERE-KTNINF-----SDKVLQFATCSFDVCYQEIFSTL--LSGGTLYIIREETKRDVEQLFD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 409 YL----------------VLARVRQALG-FAKCQKNFYGAAP---MTAETQRFFLGLNIRLYAGYGLSES---TGPHFMS 465
Cdd:cd17656 214 LVkrhnievvflpvaflkFIFSEREFINrFPTCVKHIITAGEqlvITNEFKEMLHEHNVHLHNHYGPSEThvvTTYTINP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 466 SPYNYRLYSSGRVVPGCRVKLVNQDAD-----GIGEICLWGRTIFMGYLNMEDKTHEAI-----DSEGWLH-TGDMGRLD 534
Cdd:cd17656 294 EAEIPELPPIGKPISNTWIYILDQEQQlqpqgIVGELYISGASVARGYLNRQELTAEKFfpdpfDPNERMYrTGDLARYL 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958794461 535 DDGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISSAMLI 579
Cdd:cd17656 374 PDGNIEFLGRADHQ-VKIRGYRIELGEI-EAQLLNHPGVSEAVVL 416
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
145-544 |
5.40e-10 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 62.35 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 145 QMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 224
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFED----QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 225 IYTTSSPEACQYIAHDCRANVIVvdTQKqlekilkiwkdlpHLKAVVIYQEpppkkmANVYTMEELIelgQEVPEEALDA 304
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILL--TQS-------------HLQPPIAFIG------LIDLLDEDTI---YHEESENLEP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 305 IIdtqQPNQCCVLVYTSGTTGNPKGVMLSQDNGT-LVNTLREVEPTS-HMGVPR---------VWEKIMERIqevAAQSG 373
Cdd:cd17655 133 VS---KSDDLAYVIYTSGSTGKPKGVMIEHRGVVnLVEWANKVIYQGeHLRVALfasisfdasVTEIFASLL---SGNTL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 374 FIRRKMLLWA----MSVTLEQNLTCPsnDLKPftsrlaDYLVLARVRQALGFAKCQKNFYGAAPMTAETQRFFL---GLN 446
Cdd:cd17655 207 YIVRKETVLDgqalTQYIRQNRITII--DLTP------AHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIelfGTN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 447 IRLYAGYGLSEST--------GPHFMSSPY--------NYRLY---SSGRVVPgcrvklvnqdaDGI-GEICLWGRTIFM 506
Cdd:cd17655 279 PTITNAYGPTETTvdasiyqyEPETDQQVSvpigkplgNTRIYildQYGRPQP-----------VGVaGELYIGGEGVAR 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958794461 507 GYLNMEDKT------HEAIDSEGWLHTGDMGRLDDDGFLYITGR 544
Cdd:cd17655 348 GYLNRPELTaekfvdDPFVPGERMYRTGDLARWLPDGNIEFLGR 391
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
169-582 |
5.98e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 62.39 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFL-KLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQY-IAH-DCRanv 245
Cdd:PRK07867 27 SFTSWREHIRGSAARAAALRaRLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARdIAHaDCQ--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 246 IVVDTQKQLEKILKIWKDLPHLkavviyqepppkkmaNVYTME--ELIELGQEVPEEALDAiidtqQPNQCCVLVYTSGT 323
Cdd:PRK07867 104 LVLTESAHAELLDGLDPGVRVI---------------NVDSPAwaDELAAHRDAEPPFRVA-----DPDDLFMLIFTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 324 TGNPKGVMLSQDN----GTLVNTLREVEP--TSHMGVPRV--------WekimerIQEVAAQSGF-IRRKmllWAMSVTL 388
Cdd:PRK07867 164 SGDPKAVRCTHRKvasaGVMLAQRFGLGPddVCYVSMPLFhsnavmagW------AVALAAGASIaLRRK---FSASGFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 389 EqnltcpsnDLKPFTSRLADYL------VLAR----------VRQALGfakcqkNfYGAAPMTAETQRFFlglNIRLYAG 452
Cdd:PRK07867 235 P--------DVRRYGATYANYVgkplsyVLATperpddadnpLRIVYG------N-EGAPGDIARFARRF---GCVVVDG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 453 YGLSEsTGPHFMSSPyNYRLYSSGRVVPGcrVKLVNQD------------------ADGIGEIC-LWGRTIFMGYLNMED 513
Cdd:PRK07867 297 FGSTE-GGVAITRTP-DTPPGALGPLPPG--VAIVDPDtgtecppaedadgrllnaDEAIGELVnTAGPGGFEGYYNDPE 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794461 514 KTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIEEAVkMELPIISSAML-------IGDQ 582
Cdd:PRK07867 373 ADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDW-MRVDGENLGTAPIERIL-LRYPDATEVAVyavpdpvVGDQ 445
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
198-582 |
9.32e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 61.58 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 198 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEA-CQYIAH-DCRanVIVVDTQ--KQLEKIlkiwkDLPHLKAVVIY 273
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAAlAADIRRaDCQ--LLVTDAEhrPLLDGL-----DLPGVRVLDVD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 274 QEPPPKKMAnvytmeeliELGQEVPEEALDAiiDTQqpnqcCVLVYTSGTTGNPKGVMLSQdnGTLVntlreveptshmg 353
Cdd:PRK13388 128 TPAYAELVA---------AAGALTPHREVDA--MDP-----FMLIFTSGTTGAPKAVRCSH--GRLA------------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 354 vpRVWEKIMERIQEVAAQSGFIRRK-------MLLWAMSVTLEQNLTCPSN--------DLKPFTSRLADYlvlarVRQA 418
Cdd:PRK13388 177 --FAGRALTERFGLTRDDVCYVSMPlfhsnavMAGWAPAVASGAAVALPAKfsasgfldDVRRYGATYFNY-----VGKP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 419 LGF--AKCQKNFYGAAPMT------------AETQRFFlglNIRLYAGYGLSESTGphFMSSPYNYRLYSSGRVVPGCRV 484
Cdd:PRK13388 250 LAYilATPERPDDADNPLRvafgneasprdiAEFSRRF---GCQVEDGYGSSEGAV--IVVREPGTPPGSIGRGAPGVAI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 485 ------------------KLVNQDaDGIGEIC-LWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRL 545
Cdd:PRK13388 325 ynpetltecavarfdahgALLNAD-EAIGELVnTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRT 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958794461 546 KELiITAGGENVPPVPIeEAVKMELPIISSAML-------IGDQ 582
Cdd:PRK13388 403 ADW-MRVDGENLSAAPI-ERILLRHPAINRVAVyavpderVGDQ 444
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
447-576 |
1.27e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 61.04 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 447 IRLYAGYGLSEstgphfMSSPYNYRLYSS----GRVVPGCRVKLVNqdadgiGEICLWGRTIFMGYLnMEDKTHEAIDSE 522
Cdd:PRK09029 265 IRCWCGYGLTE------MASTVCAKRADGlagvGSPLPGREVKLVD------GEIWLRGASLALGYW-RQGQLVPLVNDE 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958794461 523 GWLHTGDMGRLdDDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISSA 576
Cdd:PRK09029 332 GWFATRDRGEW-QNGELTILGRLDNLFFS-GGEGIQPEEI-ERVINQHPLVQQV 382
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
317-583 |
1.46e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 60.47 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 317 LVYTSGTTGNPKGVMLSQDN-----GTLVNTLREVEPTSHMGVPRvwekimeriqevAAQSGFIRR----------KMLL 381
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDifrmlMGGADFGTGEFTPSEDAHKA------------AAAAAGTVMfpapplmhgtGSWT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 382 WAMSVTLEQNLTCPSNDLKPFTS-RLAD---YLVLARVRQAlgFAK------CQKNFY----------GAAPMTAETQRF 441
Cdd:cd05924 76 AFGGLLGGQTVVLPDDRFDPEEVwRTIEkhkVTSMTIVGDA--MARplidalRDAGPYdlsslfaissGGALLSPEVKQG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 442 FLGL--NIRLYAGYGLSESTgphFMSSPYN-YRLYSSG-RVVPGCRVKLVNQD-------ADGIGEICLWGRtIFMGYLN 510
Cdd:cd05924 154 LLELvpNITLVDAFGSSETG---FTGSGHSaGSGPETGpFTRANPDTVVLDDDgrvvppgSGGVGWIARRGH-IPLGYYG 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794461 511 MEDKTHEA---IDSEGWLHTGDMGRLDDDGFLYITGRlKELIITAGGENVPPVPIEEAVKMElPIISSAMLIG--DQR 583
Cdd:cd05924 230 DEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGR-GSVCINTGGEKVFPEEVEEALKSH-PAVYDVLVVGrpDER 305
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
433-580 |
1.51e-09 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 60.61 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 433 PMTAETQRFF---LGLNIRLYagYGLSESTGP----HFMSSPYnyRLYSSGRVVPGCRVKLVNQDADGIGE--------- 496
Cdd:cd05973 216 PLTPEVIRWFdaaLGVPIHDH--YGQTELGMVlanhHALEHPV--HAGSAGRAMPGWRVAVLDDDGDELGPgepgrlaid 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 497 ----ICLWgrtiFMGYLNMEDKtheAIDSeGWLHTGDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPI 572
Cdd:cd05973 292 iansPLMW----FRGYQLPDTP---AIDG-GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESAL-IEHPA 361
|
....*...
gi 1958794461 573 ISSAMLIG 580
Cdd:cd05973 362 VAEAAVIG 369
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
127-544 |
2.06e-09 |
|
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: 61.03 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 127 RVRLRLEPFCTQLPY----TVHQMFYEALDKYGNLSALGFKRkdkwERISYYQyyLIAR--KVAKGFLKLGLERAHSVAI 200
Cdd:COG1020 458 RQQLLAEWNATAAPYpadaTLHELFEAQAARTPDAVAVVFGD----QSLTYAE--LNARanRLAHHLRALGVGPGDLVGV 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 201 LGFNSPEWFFSAVGTVFAGGIvtgiYT---TSSPEA-CQYIAHDCRANVIVvdTQKQLEKilkiwkDLPHLKAVVIYQEP 276
Cdd:COG1020 532 CLERSLEMVVALLAVLKAGAA----YVpldPAYPAErLAYMLEDAGARLVL--TQSALAA------RLPELGVPVLALDA 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 277 PpkkmanvytmeeliELGQEvPEEALDAIIDTQQPnqCCVLvYTSGTTGNPKGVMLSQDNgtLVNTLREVEPTSHMGvPR 356
Cdd:COG1020 600 L--------------ALAAE-PATNPPVPVTPDDL--AYVI-YTSGSTGRPKGVMVEHRA--LVNLLAWMQRRYGLG-PG 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 357 --------------VWEKIM-------------ERIQEVAAQSGFIRRKmllwamSVTLeQNLTcPSndlkpFTSRLADY 409
Cdd:COG1020 659 drvlqfaslsfdasVWEIFGallsgatlvlappEARRDPAALAELLARH------RVTV-LNLT-PS-----LLRALLDA 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 410 L--VLARVRQALgfakcqknFYGAAPMTAETQRFF-LGLNIRLYAGYGLSEST-----------GPHFMSSPYnyrlyss 475
Cdd:COG1020 726 ApeALPSLRLVL--------VGGEALPPELVRRWRaRLPGARLVNLYGPTETTvdstyyevtppDADGGSVPI------- 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 476 GRVVPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTHEA-------IDSEGWLHTGDMGRLDDDGFLYI 541
Cdd:COG1020 791 GRPIANTRVYVL--DAHLqpvpvgvPGELYIGGAGLARGYLNRPELTAERfvadpfgFPGARLYRTGDLARWLPDGNLEF 868
|
...
gi 1958794461 542 TGR 544
Cdd:COG1020 869 LGR 871
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
140-334 |
2.50e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 60.27 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 140 PYTVHQMFYEALDKYGNLSALGFKRKdkweRISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG 219
Cdd:PRK08279 36 KRSLGDVFEEAAARHPDRPALLFEDQ----SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 220 GIVTGIYTTSSPEAcqyIAHdC----RANVIVV--DTQKQLEKIlkiwkdLPHLKAVVIYQEPPPKKMANVYTMEELIEL 293
Cdd:PRK08279 112 AVVALLNTQQRGAV---LAH-SlnlvDAKHLIVgeELVEAFEEA------RADLARPPRLWVAGGDTLDDPEGYEDLAAA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958794461 294 GQEVPEEALDAiidTQ--QPNQCCVLVYTSGTTGNPKGVMLSQ 334
Cdd:PRK08279 182 AAGAPTTNPAS---RSgvTAKDTAFYIYTSGTTGLPKAAVMSH 221
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
169-545 |
5.12e-09 |
|
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: 59.21 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 248
Cdd:cd12114 11 GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DtqkqlekilkiwkdlphlkavviyqEPPPKKMANVYTMEELIELGQEVPEEALDAiidTQQPNQCCVLVYTSGTTGNPK 328
Cdd:cd12114 91 D-------------------------GPDAQLDVAVFDVLILDLDALAAPAPPPPV---DVAPDDLAYVIFTSGSTGTPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 329 GVMLSQDNgtLVNTLREVepTSHMGV-PRvwekimERIQEVAAqsgfirrkmLLWAMSV-----TLEQ--NLTCPSNDLK 400
Cdd:cd12114 143 GVMISHRA--ALNTILDI--NRRFAVgPD------DRVLALSS---------LSFDLSVydifgALSAgaTLVLPDEARR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 401 PFTSRLADYLVLARVR-----QALGFAKCqkNFYGAAPMTAETQRFFL------GL-----------NIRLYAGYGLSES 458
Cdd:cd12114 204 RDPAHWAELIERHGVTlwnsvPALLEMLL--DVLEAAQALLPSLRLVLlsgdwiPLdlparlralapDARLISLGGATEA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 459 T-----------GPHFMSSPYnyrlyssGRVVPGCRVKLVNQDA----DGI-GEICLWGRTIFMGYLNMEDKTHEA---- 518
Cdd:cd12114 282 SiwsiyhpidevPPDWRSIPY-------GRPLANQRYRVLDPRGrdcpDWVpGELWIGGRGVALGYLGDPELTAARfvth 354
|
410 420
....*....|....*....|....*..
gi 1958794461 519 IDSEGWLHTGDMGRLDDDGFLYITGRL 545
Cdd:cd12114 355 PDGERLYRTGDLGRYRPDGTLEFLGRR 381
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
484-580 |
5.51e-09 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 59.00 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 484 VKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVP 558
Cdd:COG1021 365 VRIVDEDgnpvPPGeVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINR-GGEKIA 443
|
90 100
....*....|....*....|..
gi 1958794461 559 PVPIEEAVkMELPIISSAMLIG 580
Cdd:COG1021 444 AEEVENLL-LAHPAVHDAAVVA 464
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
433-579 |
1.14e-08 |
|
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: 57.96 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 433 PMTAETQRFFLGLNIRlyAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVnqDADGI----GEICL-WGRT---- 503
Cdd:cd05974 214 PEVIEQVRRAWGLTIR--DGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALL--DPDGApateGEVALdLGDTrpvg 289
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958794461 504 IFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEEAVkMELPIISSAMLI 579
Cdd:cd05974 290 LMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADD-VFKSSDYRISPFELESVL-IEHPAVAEAAVV 362
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
292-554 |
4.40e-08 |
|
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: 56.31 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 292 ELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSqdNGTL---VNTLREVEPTSHMGVprvwekimeriqEV 368
Cdd:cd05910 65 NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYR--HGTFaaqIDALRQLYGIRPGEV------------DL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 369 AAQSGFIRRKMLLWAMSVTLEQNLTCPSN-DLKPFTSRLADY---------LVLARV-----RQALGFAKCQKNFYGAAP 433
Cdd:cd05910 131 ATFPLFALFGPALGLTSVIPDMDPTRPARaDPQKLVGAIRQYgvsivfgspALLERVarycaQHGITLPSLRRVLSAGAP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 434 MTAET-QRF--FLGLNIRLYAGYGLSE-----STGPHFMSS-----PYNYRLYSSGRVVPGCRVKLVNQDAD-------- 492
Cdd:cd05910 211 VPIALaARLrkMLSDEAEILTPYGATEalpvsSIGSRELLAtttaaTSGGAGTCVGRPIPGVRVRIIEIDDEpiaewddt 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958794461 493 ------GIGEICLWGRTIFMGYLNMEDKTHEA-ID--SEGWLH-TGDMGRLDDDGFLYITGRLKELIITAGG 554
Cdd:cd05910 291 lelprgEIGEITVTGPTVTPTYVNRPVATALAkIDdnSEGFWHrMGDLGYLDDEGRLWFCGRKAHRVITTGG 362
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
143-545 |
5.48e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.50 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 143 VHQMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIV 222
Cdd:PRK12316 3059 VHRLFEEQVERTPDAVALAFGE----QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAY 3134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 223 TGIYTTSSPEACQYIAHDCRANVIVvdTQKQLEkilkiwkdLPHLKAVVIYqepppkkmanvytmeeLIELGQEVPEEAL 302
Cdd:PRK12316 3135 VPLDPEYPEERLAYMLEDSGAQLLL--SQSHLR--------LPLAQGVQVL----------------DLDRGDENYAEAN 3188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 303 DAIIDTqqPNQCCVLVYTSGTTGNPKGVMLSQdnGTLVNTLREVEPTSHMGV-PRVWEK--------IMERIQEVAAQSG 373
Cdd:PRK12316 3189 PAIRTM--PENLAYVIYTSGSTGKPKGVGIRH--SALSNHLCWMQQAYGLGVgDRVLQFttfsfdvfVEELFWPLMSGAR 3264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 374 FIRRKMLLWAMSVTLEQNLTCPSNDLKPFT-SRLADYLVLARVRQALGFAKCQKNfyGAAPMTAETQRFFLGLniRLYAG 452
Cdd:PRK12316 3265 VVLAGPEDWRDPALLVELINSEGVDVLHAYpSMLQAFLEEEDAHRCTSLKRIVCG--GEALPADLQQQVFAGL--PLYNL 3340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 453 YGLSEST--GPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDAD-----GIGEICLWGRTIFMGYLNMEDKTHEAI------ 519
Cdd:PRK12316 3341 YGPTEATitVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEpvpvgALGELYLGGEGLARGYHNRPGLTAERFvpdpfv 3420
|
410 420
....*....|....*....|....*.
gi 1958794461 520 DSEGWLHTGDMGRLDDDGFLYITGRL 545
Cdd:PRK12316 3421 PGERLYRTGDLARYRADGVIEYIGRV 3446
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
472-580 |
7.34e-08 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 55.41 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 472 LYSSGR-VVPGCRVKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRL 545
Cdd:cd05920 307 IHTQGRpMSPDDEIRVVDEEgnpvPPGeEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRI 386
|
90 100 110
....*....|....*....|....*....|....*
gi 1958794461 546 KELiITAGGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:cd05920 387 KDQ-INRGGEKIAAEEVENLL-LRHPAVHDAAVVA 419
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
471-566 |
9.20e-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: 55.40 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 471 RLYSSGRVVPGCRVKLVNQD-----ADGIGEICLwGRTIFMGYLNMEDKTHEAI------DSEGWLHTGDMGRLDDDGFL 539
Cdd:cd05967 409 KAGSPGKPVPGYQVQVLDEDgepvgPNELGNIVI-KLPLPPGCLLTLWKNDERFkklylsKFPGYYDTGDAGYKDEDGYL 487
|
90 100 110
....*....|....*....|....*....|..
gi 1958794461 540 YITGRLKELIITAG-----GEnvppvpIEEAV 566
Cdd:cd05967 488 FIMGRTDDVINVAGhrlstGE------MEESV 513
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
472-573 |
1.10e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.56 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 472 LYSSGRVVPGCRVKLVNQD-----ADG-IGEICLWGRTIFMGYL-NMED--KTHEAIDSEGWLHTGDMGRLDDdGFLYIT 542
Cdd:PRK05691 369 LMSCGRSQPGHAVLIVDPQslevlGDNrVGEIWASGPSIAHGYWrNPEAsaKTFVEHDGRTWLRTGDLGFLRD-GELFVT 447
|
90 100 110
....*....|....*....|....*....|.
gi 1958794461 543 GRLKELIITAgGENVPPVPIEEAVKMELPII 573
Cdd:PRK05691 448 GRLKDMLIVR-GHNLYPQDIEKTVEREVEVV 477
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
474-573 |
1.28e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 54.75 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 474 SSGRVVPGCRVKLVNQDA-----DG-IGEICLWGRTIFMGYLNMEDKTHE------------------AIDSEGWLHTGD 529
Cdd:PRK12476 403 SCGQVARSQWAVIVDPDTgaelpDGeVGEIWLHGDNIGRGYWGRPEETERtfgaklqsrlaegshadgAADDGTWLRTGD 482
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958794461 530 MGrLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKMELPII 573
Cdd:PRK12476 483 LG-VYLDGELYITGRIADLIVI-DGRNHYPQDIEATVAEASPMV 524
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
143-545 |
1.65e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.96 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 143 VHQMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIV 222
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALAFGE----ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 223 TGIYTTSSPEACQYIAHDCRANVIVvdTQKQLEKILkiwkDLPHLKAVVIYQEPPPkkmanvytmeELIELGQEVPEEAL 302
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGVQLLL--SQSHLGRKL----PLAAGVQVLDLDRPAA----------WLEGYSEENPGTEL 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 303 DaiidtqqPNQCCVLVYTSGTTGNPKGVMLSqdNGTLVNTLREVEPTSHMGVPR-------------VWE---KIMERIQ 366
Cdd:PRK12316 653 N-------PENLAYVIYTSGSTGKPKGAGNR--HRALSNRLCWMQQAYGLGVGDtvlqktpfsfdvsVWEffwPLMSGAR 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 367 EVAAQSGFIRRKMLLWAMSVTLEQNLtcpsndLKPFTSRLADYLVLARVRQALGFAKCqkNFYGAA-PMTAETQRFFLGL 445
Cdd:PRK12316 724 LVVAAPGDHRDPAKLVELINREGVDT------LHFVPSMLQAFLQDEDVASCTSLRRI--VCSGEAlPADAQEQVFAKLP 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 446 NIRLYAGYGLSEST--GPHFMSSPYNYRLYSSGRVVPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTH 516
Cdd:PRK12316 796 QAGLYNLYGPTEAAidVTHWTCVEEGGDSVPIGRPIANLACYIL--DANLepvpvgvLGELYLAGRGLARGYHGRPGLTA 873
|
410 420 430
....*....|....*....|....*....|....*
gi 1958794461 517 EA------IDSEGWLHTGDMGRLDDDGFLYITGRL 545
Cdd:PRK12316 874 ERfvpspfVAGERMYRTGDLARYRADGVIEYAGRI 908
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
433-605 |
1.75e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.65 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 433 PMTAETQRFFLGlNIRLYAGYGLSEsTGPHFMSSPYN-YRLYSSGRVVPGCRVKLVNQDADGIG---EICLW--GRTIFM 506
Cdd:PRK06060 274 LGLAERLMEFFG-GIPILDGIGSTE-VGQTFVSNRVDeWRLGTLGRVLPPYEIRVVAPDGTTAGpgvEGDLWvrGPAIAK 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 507 GYLNMEDKTheaIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIGdQRKFL 586
Cdd:PRK06060 352 GYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVI-GGVNVDPREVERLI-IEDEAVAEAAVVA-VREST 425
|
170
....*....|....*....
gi 1958794461 587 SMlLTLKCTLNPETSEPTD 605
Cdd:PRK06060 426 GA-STLQAFLVATSGATID 443
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
167-580 |
2.19e-07 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 54.01 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 167 KWeriSYYQYYLIARKVAKGFLKL-GLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTgiyttssPEACQYIAHD----- 240
Cdd:cd05928 41 KW---SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFI-------PGTIQLTAKDilyrl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 241 --CRANVIVVDtQKQLEKILKIWKDLPHLKAVVIYQEPPPKKMANvytmeeLIELGQEVPEEALDAIIDTQQPnqcCVLV 318
Cdd:cd05928 111 qaSKAKCIVTS-DELAPEVDSVASECPSLKTKLLVSEKSRDGWLN------FKELLNEASTEHHCVETGSQEP---MAIY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 319 YTSGTTGNPKGVMLSQDN---GTLVNT--LREVEP------TSHMG-VPRVWEKIMEriQEVAAQSGFIRRkMLLWAMSV 386
Cdd:cd05928 181 FTSGTTGSPKMAEHSHSSlglGLKVNGryWLDLTAsdimwnTSDTGwIKSAWSSLFE--PWIQGACVFVHH-LPRFDPLV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 387 TLEQNLTCPsndLKPFTSRLADYLVLarVRQALG---FAKCQKNFYGAAPMTAETQ---RFFLGLNIrlYAGYGLSEsTG 460
Cdd:cd05928 258 ILKTLSSYP---ITTFCGAPTVYRML--VQQDLSsykFPSLQHCVTGGEPLNPEVLekwKAQTGLDI--YEGYGQTE-TG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 461 ------------PHFM---SSPYNYRLYS-SGRVVP-------GCRVKLVNqdadgigEICLwgrtiFMGYLNMEDKTHE 517
Cdd:cd05928 330 licanfkgmkikPGSMgkaSPPYDVQIIDdNGNVLPpgtegdiGIRVKPIR-------PFGL-----FSGYVDNPEKTAA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794461 518 AIDSEGWLhTGDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:cd05928 398 TIRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSS-GYRIGPFEVESAL-IEHPAVVESAVVS 457
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
491-558 |
5.40e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 52.81 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 491 ADG-IGEICLWGRTIFMGYLNMEDKTHEAID-----------SEG------WLHTGDMGRLDDdGFLYITGRLKELIITA 552
Cdd:PRK07769 414 PDGqIGEIWLHGNNIGTGYWGKPEETAATFQnilksrlseshAEGapddalWVRTGDYGVYFD-GELYITGRVKDLVIID 492
|
....*.
gi 1958794461 553 GGENVP 558
Cdd:PRK07769 493 GRNHYP 498
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
112-353 |
6.09e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.42 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 112 LDASEEAlwttRADGRVRLRLEPFCTQLpyTVHQMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLG 191
Cdd:PRK12316 1980 LDAGERQ----RILADWDRTPEAYPRGP--GVHQRIAEQAARAPEAIAVVFGD----QHLSYAELDSRANRLAHRLRARG 2049
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 192 LERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTqkqlekilkiwkdlpHLKAvv 271
Cdd:PRK12316 2050 VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR---------------HLLE-- 2112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 272 iyQEPPPKKMAN--VYTMEELIELGQEVPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQdnGTLVNTLREVEPT 349
Cdd:PRK12316 2113 --RLPLPAGVARlpLDRDAEWADYPDTAPAVQLA-------GENLAYVIYTSGSTGLPKGVAVSH--GALVAHCQAAGER 2181
|
....
gi 1958794461 350 SHMG 353
Cdd:PRK12316 2182 YELS 2185
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
190-580 |
6.32e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 52.48 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 190 LGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDtQKQLEKILKIWKDLPHLKA 269
Cdd:PRK05620 59 LGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKECPCVRA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 270 VVIYQEPPPKKMA-------NVYTMEELIElGQ-------EVPEEALDAIidtqqpnqcCvlvYTSGTTGNPKGVMLSQD 335
Cdd:PRK05620 138 VVFIGPSDADSAAahmpegiKVYSYEALLD-GRstvydwpELDETTAAAI---------C---YSTGTTGAPKGVVYSHR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 336 NGTLVN-TLREVE--------------PTSHM---GVPrvwekimeriqeVAAqsgfirrkmllWaMSVTleqNLTCPSN 397
Cdd:PRK05620 205 SLYLQSlSLRTTDslavthgesflccvPIYHVlswGVP------------LAA-----------F-MSGT---PLVFPGP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 398 DLKPftSRLADYLVLARVRQALG--------FAKCQKN----------FYGAAP-----MTAETQRFflGLNIrlYAGYG 454
Cdd:PRK05620 258 DLSA--PTLAKIIATAMPRVAHGvptlwiqlMVHYLKNppermslqeiYVGGSAvppilIKAWEERY--GVDV--VHVWG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 455 LSESTGPHFMSSP---------YNYRlYSSGRVVPGCRVKLVNqdaDG---------IGEICLWGRTIFMGYLNME---- 512
Cdd:PRK05620 332 MTETSPVGTVARPpsgvsgearWAYR-VSQGRFPASLEYRIVN---DGqvmestdrnEGEIQVRGNWVTASYYHSPteeg 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 513 ------------DKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEEAVkMELPIISSAMLIG 580
Cdd:PRK05620 408 ggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARD-VIRSGGEWIYSAQLENYI-MAAPEVVECAVIG 485
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
144-599 |
1.20e-06 |
|
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: 51.40 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 144 HQMFYEALDKYGNLSALGFkRKDKWeriSYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVT 223
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVD-RGQSL---TYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 224 GIYTTSSPEACQYIAHDCRANVIVvdtqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeeald 303
Cdd:cd17645 77 PIDPDYPGERIAYMLADSSAKILL-------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 304 aiidtQQPNQCCVLVYTSGTTGNPKGVMLSQDNgtLVNTLREVEPTSHMGvprvwekiMERIQEVAAQSGFirrKMLLWA 383
Cdd:cd17645 101 -----TNPDDLAYVIYTSGSTGLPKGVMIEHHN--LVNLCEWHRPYFGVT--------PADKSLVYASFSF---DASAWE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 384 M--SVTLEQNLTCPSNDLKPFTSRLADYLVLARVRQALGFAKCQKNFygaapMTAETQRFFLGLN------------IRL 449
Cdd:cd17645 163 IfpHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQF-----MQLDNQSLRVLLTggdklkkierkgYKL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 450 YAGYGLSESTgphFMSSPY----NYRLYSSGRVVPGCRVKLVNQD----ADGI-GEICLWGRTIFMGYLNMEDKT----- 515
Cdd:cd17645 238 VNNYGPTENT---VVATSFeidkPYANIPIGKPIDNTRVYILDEAlqlqPIGVaGELCIAGEGLARGYLNRPELTaekfi 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 516 -HEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIEEAVkMELPIISSAMLI----GDQRKFLSMLL 590
Cdd:cd17645 315 vHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ-VKIRGYRIEPGEIEPFL-MNHPLIELAAVLakedADGRKYLVAYV 392
|
....*....
gi 1958794461 591 TLKCTLNPE 599
Cdd:cd17645 393 TAPEEIPHE 401
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
198-353 |
1.92e-06 |
|
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: 50.75 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 198 VAILGFNSPEWFFSAVGTVFAGGIvtgiYTTSSPEA----CQYIAHDCRANVIVVDTqkqlekilkiwkDLPHLkavviY 273
Cdd:cd12116 40 VAVYLPRSARLVAAMLAVLKAGAA----YVPLDPDYpadrLRYILEDAEPALVLTDD------------ALPDR-----L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 274 QEPPPkkmanvytmeeLIELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNgtLVNTLREVEPTSHMG 353
Cdd:cd12116 99 PAGLP-----------VLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRN--LVNFLHSMRERLGLG 165
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
484-567 |
1.93e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.10 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 484 VKLVNQD------ADGIGEICLWGRTIFMGYLNMEDKTHEAID------SEG-----WLHTGDMGRLDDDGfLYITGRLK 546
Cdd:PRK05850 381 VRIVDPDtciecpAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpSPGtpegpWLRTGDLGFISEGE-LFIVGRIK 459
|
90 100
....*....|....*....|.
gi 1958794461 547 ELIITAgGENVPPVPIEEAVK 567
Cdd:PRK05850 460 DLLIVD-GRNHYPDDIEATIQ 479
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
112-341 |
2.47e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 51.32 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 112 LDASEealwttRADGRVRLRLEPFcTQLPYTVHQMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLG 191
Cdd:PRK12467 490 LDAEE------RARELVRWNAPAT-EYAPDCVHQLIEAQARQHPERPALVFGE----QVLSYAELNRQANRLAHVLIAAG 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 192 LERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDcrANVIVVDTQKQLEKILKIWKDLPhlkaVV 271
Cdd:PRK12467 559 VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDD--SGVRLLLTQSHLLAQLPVPAGLR----SL 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 272 IYQEPPPkkmanvytmeELIELGQEVPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSqdNGTLVN 341
Cdd:PRK12467 633 CLDEPAD----------LLCGYSGHNPEVALD-------PDNLAYVIYTSGSTGQPKGVAIS--HGALAN 683
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
291-545 |
3.49e-06 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 50.13 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 291 IELGQEVPEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQDngTLVN----TLREVEPTSHMGVprvwe 359
Cdd:cd17644 78 VPLDPNYPQERLTYILeDAQisvlltQPENLAYVIYTSGSTGKPKGVMIEHQ--SLVNlshgLIKEYGITSSDRV----- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 360 KIMERIQ-EVAAQSGFIrrkMLLWAMSVTLEQNLTCPsnDLKPFTSRLADY--------------LVLARVRQAL-GFAK 423
Cdd:cd17644 151 LQFASIAfDVAAEEIYV---TLLSGATLVLRPEEMRS--SLEDFVQYIQQWqltvlslppaywhlLVLELLLSTIdLPSS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 424 CQKNFYGAA---PMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSS-----GRVVPGCRVKLVNQDADGI- 494
Cdd:cd17644 226 LRLVIVGGEavqPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNItsvpiGRPIANTQVYILDENLQPVp 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958794461 495 ----GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLH--------TGDMGRLDDDGFLYITGRL 545
Cdd:cd17644 306 vgvpGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRI 368
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
487-617 |
4.05e-06 |
|
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: 50.12 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 487 VNQDADGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIeEAV 566
Cdd:cd05915 353 VPKDGKALGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKD-LIKSGGEWISSVDL-ENA 430
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958794461 567 KMELPIISSAMLIG--DQRKFLSMLLTLKCTlNPETSEptdnltEQAVEFCQR 617
Cdd:cd05915 431 LMGHPKVKEAAVVAipHPKWQERPLAVVVPR-GEKPTP------EELNEHLLK 476
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
169-334 |
5.51e-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: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLK-LGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 247
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 248 VDT--QKQLEKILkiwkdlPHLKA--VVIYQEPPPkkmANVYTMEELIELGQEVPEEALDAIIDTQQ-PNQCCVLVYTSG 322
Cdd:cd05938 84 VAPelQEAVEEVL------PALRAdgVSVWYLSHT---SNTEGVISLLDKVDAASDEPVPASLRAHVtIKSPALYIYTSG 154
|
170
....*....|..
gi 1958794461 323 TTGNPKGVMLSQ 334
Cdd:cd05938 155 TTGLPKAARISH 166
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
476-554 |
8.02e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 49.13 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 476 GRVVPGCRVKLVN---------QD-----ADGIGEICLWGRTIFMGYLNMEDKTHEA--IDSEG--WLHTGDMGRLDDDG 537
Cdd:PRK09274 355 GRPVDGVEVRIIAisdapipewDDalrlaTGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQG 434
|
90
....*....|....*..
gi 1958794461 538 FLYITGRLKELIITAGG 554
Cdd:PRK09274 435 RLWFCGRKAHRVETAGG 451
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
148-617 |
8.28e-06 |
|
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: 49.11 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 148 YEALDKY----GNLSALGFKRKD--KWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGI 221
Cdd:cd17634 56 ANALDRHlrenGDRTAIIYEGDDtsQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 222 VTGIYTTSSPEACQYIAHDCRANVIV-----------VDTQKQLEKILKIWKDLPHlKAVVIYQEPPPKKM--ANVYTME 288
Cdd:cd17634 136 HSVIFGGFAPEAVAGRIIDSSSRLLItadggvragrsVPLKKNVDDALNPNVTSVE-HVIVLKRTGSDIDWqeGRDLWWR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 289 ELIElgqEVPEEALDAIIDTQQPnqcCVLVYTSGTTGNPKGVmLSQDNGTLVNTLREVEPTSHMGVPRVWEKIMErIQEV 368
Cdd:cd17634 215 DLIA---KASPEHQPEAMNAEDP---LFILYTSGTTGKPKGV-LHTTGGYLVYAATTMKYVFDYGPGDIYWCTAD-VGWV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 369 AAQSGFIRRKMLLWAMSVTLEQNLTCPSNDL-----------KPFTSRLADYLVLARVRQAL-GFAKCQKNFYGAA--PM 434
Cdd:cd17634 287 TGHSYLLYGPLACGATTLLYEGVPNWPTPARmwqvvdkhgvnILYTAPTAIRALMAAGDDAIeGTDRSSLRILGSVgePI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 435 TAETQRFF---LGLNIRLYAGYGLSESTGpHFMSSP----YNYRLYSSGRVVPGCRVKLVN-----QDADGIGEICL--- 499
Cdd:cd17634 367 NPEAYEWYwkkIGKEKCPVVDTWWQTETG-GFMITPlpgaIELKAGSATRPVFGVQPAVVDneghpQPGGTEGNLVItdp 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 500 W-GRTifMGYLNMEDKTHEAIDS--EGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEEAVKMElPIISSA 576
Cdd:cd17634 446 WpGQT--RTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDD-VINVAGHRLGTAEIESVLVAH-PKVAEA 521
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1958794461 577 MLIGDQRKFLSMLLTLKCTLNPETsEPTDNLTEQAVEFCQR 617
Cdd:cd17634 522 AVVGIPHAIKGQAPYAYVVLNHGV-EPSPELYAELRNWVRK 561
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
180-336 |
1.10e-05 |
|
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: 48.35 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 180 ARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVvdTQKQLEKILk 259
Cdd:cd12117 32 ANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL--TDRSLAGRA- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794461 260 iwkdLPHLKAVVIYQEPPPKkmanvytmeelielGQEVPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDN 336
Cdd:cd12117 109 ----GGLEVAVVIDEALDAG--------------PAGNPAVPVS-------PDDLAYVMYTSGSTGRPKGVAVTHRG 160
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
476-545 |
7.99e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 45.66 E-value: 7.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958794461 476 GRVVPGCRVKLVNQDAD-----GIGEICLWGRTIFMGYLNMEDKTHEA---IDSEGWLHTGDMGRLdDDGFLYITGRL 545
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTklpdgEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGYL-EDGLLFYQGRI 397
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
232-557 |
8.66e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 45.58 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 232 EACQYIAHdcranVIVVDTQKQL-EKILKIWKDLPHLKAVVIYQEPPPKKManvyTMEELIELG--QEVPEEALDAI--I 306
Cdd:PRK06334 107 TACANLVG-----VTHVLTSKQLmQHLAQTHGEDAEYPFSLIYMEEVRKEL----SFWEKCRIGiyMSIPFEWLMRWfgV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 307 DTQQPNQCCVLVYTSGTTGNPKGVMLSQDNgTLVNT---LREVEPTSH------------------------MGVPRVW- 358
Cdd:PRK06334 178 SDKDPEDVAVILFTSGTEKLPKGVPLTHAN-LLANQracLKFFSPKEDdvmmsflppfhaygfnsctlfpllSGVPVVFa 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 359 ------EKIMERIQEVAAqsgfirrkMLLWAMSVTLEQNLTCPSndlKPFTSrladylvLARVRQALGFAKCQKNfygaa 432
Cdd:PRK06334 257 ynplypKKIVEMIDEAKV--------TFLGSTPVFFDYILKTAK---KQESC-------LPSLRFVVIGGDAFKD----- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 433 PMTAETQRFFLglNIRLYAGYGLSESTgP----HFMSSPYNYRLYssGRVVPGCRVKLVNQD------ADGIGEICLWGR 502
Cdd:PRK06334 314 SLYQEALKTFP--HIQLRQGYGTTECS-PvitiNTVNSPKHESCV--GMPIRGMDVLIVSEEtkvpvsSGETGLVLTRGT 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958794461 503 TIFMGYLNmEDKTHEAI--DSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENV 557
Cdd:PRK06334 389 SLFSGYLG-EDFGQGFVelGGETWYVTGDLGYVDRHGELFLKGRLSRF-VKIGAEMV 443
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
310-579 |
1.01e-04 |
|
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: 45.54 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 310 QPNQCCVLVYTSGTTGNPKGVMLSQDNGTlvntlreveptsHMGVprVWekimERIQEVAAQSgfiRRKMLLWAMSVTL- 388
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVA------------HAAH--AW----RREYELDSFP---VRLLQMASFSFDVf 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 389 -----------EQNLTCPsNDLKPFTSRLADYLVLARV------------------RQALGFAKCQKNFYGAAPMTAE-- 437
Cdd:cd17650 150 agdfarsllngGTLVICP-DEVKLDPAALYDLILKSRItlmestpalirpvmayvyRNGLDLSAMRLLIVGSDGCKAQdf 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 438 ---TQRFflGLNIRLYAGYGLSESTgphfMSSPY---------NYRLYSSGRVVPGCRVKLVN-----QDADGIGEICLW 500
Cdd:cd17650 229 ktlAARF--GQGMRIINSYGVTEAT----IDSTYyeegrdplgDSANVPIGRPLPNTAMYVLDerlqpQPVGVAGELYIG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 501 GRTIFMGYLNMEDKTHEAI------DSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGgenvppVPIE----EAVKMEL 570
Cdd:cd17650 303 GAGVARGYLNRPELTAERFvenpfaPGERMYRTGDLARWRADGNVELLGRVDHQVKIRG------FRIElgeiESQLARH 376
|
....*....
gi 1958794461 571 PIISSAMLI 579
Cdd:cd17650 377 PAIDEAVVA 385
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
310-545 |
1.06e-04 |
|
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: 45.34 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 310 QPNQCCVLVYTSGTTGNPKGVMLSQDngTLVNTLREVEptSHMGV---------------PRVWEKIM------------ 362
Cdd:cd17646 136 RPDNLAYVIYTSGSTGRPKGVMVTHA--GIVNRLLWMQ--DEYPLgpgdrvlqktplsfdVSVWELFWplvagarlvvar 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 363 -ERIQEVAAQSGFIRRKmllwamSVTleqnlTCpsnDLKPftSRLADYLVLARVRQAlgfAKCQKNFYGAAPMTAET-QR 440
Cdd:cd17646 212 pGGHRDPAYLAALIREH------GVT-----TC---HFVP--SMLRVFLAEPAAGSC---ASLRRVFCSGEALPPELaAR 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 441 FFLGLNIRLYAGYGLSEST--GPHFMSSPYNYRLYSS-GRVVPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLN 510
Cdd:cd17646 273 FLALPGAELHNLYGPTEAAidVTHWPVRGPAETPSVPiGRPVPNTRLYVL--DDALrpvpvgvPGELYLGGVQLARGYLG 350
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958794461 511 MEDKTHEAI-----DSEGWLH-TGDMGRLDDDGFLYITGRL 545
Cdd:cd17646 351 RPALTAERFvpdpfGPGSRMYrTGDLARWRPDGALEFLGRS 391
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
148-331 |
1.31e-04 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 45.24 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 148 YEALDKygNLSALGFKRKDKWE--------RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEwffsAVGTVFA- 218
Cdd:cd05966 56 YNCLDR--HLKERGDKVAIIWEgdepdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPE----LVIAMLAc 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 219 ---GGIVTGIYTTSSPEACQYIAHDCRANVIV-VDTQKQLEKI--LKIWKD-----LPHLKAVVIYQ----EPPPKKMAN 283
Cdd:cd05966 130 ariGAVHSVVFAGFSAESLADRINDAQCKLVItADGGYRGGKVipLKEIVDealekCPSVEKVLVVKrtggEVPMTEGRD 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958794461 284 VYTMEELIELGQEVPEEALDAiidtQQPnqcCVLVYTSGTTGNPKGVM 331
Cdd:cd05966 210 LWWHDLMAKQSPECEPEWMDS----EDP---LFILYTSGSTGKPKGVV 250
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
298-607 |
1.53e-04 |
|
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: 44.62 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 298 PEEALDAIIDTQQ-------PNQCCVLVYTSGTTGNPKGVMLSQDN------------------GTLVNT-----LREVE 347
Cdd:cd12115 84 PPERLRFILEDAQarlvltdPDDLAYVIYTSGSTGRPKGVAIEHRNaaaflqwaaaafsaeelaGVLASTsicfdLSVFE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 348 ---PTSHMGVPRVWEKIMERIQEVAAQsgfirrkmllwamSVTLEQnlTCPSndlkpFTSRLADYLVLARVRQALGFAkc 424
Cdd:cd12115 164 lfgPLATGGKVVLADNVLALPDLPAAA-------------EVTLIN--TVPS-----AAAELLRHDALPASVRVVNLA-- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 425 qknfygAAPMTAE-TQRFFLGLNI-RLYAGYGLSEST--------GPHFMSSPynyrlySSGRVVPGCRVKLVNQD---- 490
Cdd:cd12115 222 ------GEPLPRDlVQRLYARLQVeRVVNLYGPSEDTtystvapvPPGASGEV------SIGRPLANTQAYVLDRAlqpv 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 491 ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWL------HTGDMGRLDDDGFLYITGRLKELIITAGgenvppVPIE 563
Cdd:cd12115 290 PLGvPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRG------FRIE 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958794461 564 ----EAVKMELPIISSA--MLIGDQ--RKFLSMLLTLKCTLNPETSEPTDNL 607
Cdd:cd12115 364 lgeiEAALRSIPGVREAvvVAIGDAagERRLVAYIVAEPGAAGLVEDLRRHL 415
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
169-345 |
2.24e-04 |
|
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: 44.57 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEwffsAVGTVFAGGIVTGIYTTSSPE---------------- 232
Cdd:cd05943 97 TEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPE----AVVAMLATASIGAIWSSCSPDfgvpgvldrfgqiepk 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 233 ------ACQYIA--HDCRanvivvdtqkqlEKILKIWKDLPHLKAVVI--YQEPPPK----KMANVYTMEELI--ELGQE 296
Cdd:cd05943 173 vlfavdAYTYNGkrHDVR------------EKVAELVKGLPSLLAVVVvpYTVAAGQpdlsKIAKALTLEDFLatGAAGE 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958794461 297 VPEEALDAiidtQQPnqCCVLvYTSGTTGNPKGVMLSQdNGTLVNTLRE 345
Cdd:cd05943 241 LEFEPLPF----DHP--LYIL-YSSGTTGLPKCIVHGA-GGTLLQHLKE 281
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
171-576 |
3.13e-04 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 44.02 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 171 ISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV--- 247
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALItad 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 248 --------VDTQKQLEKILKiwkDLPHLKAVVIYqepppKKMANVYTMEELIELGQEVPEEALDAIIDTQQPNQCCVLVY 319
Cdd:cd05968 172 gftrrgreVNLKEEADKACA---QCPTVEKVVVV-----RHLGNDFTPAKGRDLSYDEEKETAGDGAERTESEDPLMIIY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 320 TSGTTGNPKGVmlsqdngtlVNTlreveptsHMGVPrvwekiMERIQEVAAQSGFIRRKMLLWamsvtleqnltcpsndl 399
Cdd:cd05968 244 TSGTTGKPKGT---------VHV--------HAGFP------LKAAQDMYFQFDLKPGDLLTW----------------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 400 kpFTS---RLADYLVLARVrqALGfakCQKNFYGAAP----------MTAETQRFFLGLN---IRLYAGYG--------- 454
Cdd:cd05968 284 --FTDlgwMMGPWLIFGGL--ILG---ATMVLYDGAPdhpkadrlwrMVEDHEITHLGLSptlIRALKPRGdapvnahdl 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 455 ----LSESTGPHFMSSPYNYRL------------YSSGR----------------------VVPGCRVKLVNQDA----D 492
Cdd:cd05968 357 sslrVLGSTGEPWNPEPWNWLFetvgkgrnpiinYSGGTeisggilgnvlikpikpssfngPVPGMKADVLDESGkparP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 493 GIGEICLWGRTIFM--GYLNMEDKTHEAIDS--EG-WLHtGDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEEAVK 567
Cdd:cd05968 437 EVGELVLLAPWPGMtrGFWRDEDRYLETYWSrfDNvWVH-GDFAYYDEEGYFYILGRSDDTINVA-GKRVGPAEIESVLN 514
|
....*....
gi 1958794461 568 MELPIISSA 576
Cdd:cd05968 515 AHPAVLESA 523
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
298-336 |
3.28e-04 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 43.84 E-value: 3.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958794461 298 PEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQDN 336
Cdd:cd17643 72 PVERIAFILaDSGpsllltDPDDLAYVIYTSGSTGRPKGVVVSHAN 117
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
169-336 |
5.02e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 43.35 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGgivtgiyttsspeaCQYIAhdcranvivV 248
Cdd:PRK04813 26 EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--------------HAYIP---------V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 249 DTQKQLEKILKIwKDLPHLKAVV-IYQEPPPKKMANVYTMEELIELGQEVPEEALDAIIdtqQPNQCCVLVYTSGTTGNP 327
Cdd:PRK04813 83 DVSSPAERIEMI-IEVAKPSLIIaTEELPLEILGIPVITLDELKDIFATGNPYDFDHAV---KGDDNYYIIFTSGTTGKP 158
|
....*....
gi 1958794461 328 KGVMLSQDN 336
Cdd:PRK04813 159 KGVQISHDN 167
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
169-250 |
5.15e-04 |
|
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: 43.11 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958794461 169 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 248
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
..
gi 1958794461 249 DT 250
Cdd:cd05940 82 DA 83
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
311-346 |
7.28e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 39.77 E-value: 7.28e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1958794461 311 PNQCCVLVYTSGTTGNPKGVMLSQdNGTLVNTLREV 346
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQ-RGMLNNQLSKV 3902
|
|
| |
