|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
122-716 |
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: 1116.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 122 KRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCR 201
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 202 ANVIVVDTQKQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEVPEEALDAIIDTQQPNQCCVLVYTSG 281
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 282 TTGNPKGVMLSQDNITWTARYGSQAGDIQPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFADPDALKGTLVNTL 361
Cdd:cd05933 161 TTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 362 REVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPSNDLKPFTS-RLADYLVLARVRQALGFA 440
Cdd:cd05933 241 REVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFyRLAKKLVFKKVRKALGLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 441 KCQKNFYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGIGEICLWGR 520
Cdd:cd05933 321 RCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 521 TIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISSAMLIGDQ 600
Cdd:cd05933 401 HVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGDK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 601 RKFLSMLLTLKCTLNPETSEPTDNLTEQAVEFCQRVGSKASTVSEIVGQKDEAVYQAIHEGIQRVNANAAARPYHIQKWA 680
Cdd:cd05933 481 RKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKWV 560
|
570 580 590
....*....|....*....|....*....|....*.
gi 19705503 681 ILERDFSISGGELGPTMKLKRLTVLEKYKDIIDSFY 716
Cdd:cd05933 561 ILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
99-719 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 591.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 99 PYTVHQMFYEALDKYGNLSALGFKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG 178
Cdd:COG1022 10 ADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 179 GIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEV-P 257
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGLRDDPRLLSLDELLALGREVaD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 258 EEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAAQIYDLWt 337
Cdd:COG1022 170 PAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGP----GDRTLSFLPLAHVFERTVSYY- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 338 GIQWGAQVCFA-DPDalkgTLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPSND 416
Cdd:COG1022 245 ALAAGATVAFAeSPD----TLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLAGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 417 LKPFTSR----LADYLVLARVRQALG----FAKCqknfyGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNY 488
Cdd:COG1022 321 SPSLLLRlkhaLADKLVFSKLREALGgrlrFAVS-----GGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 489 RLYSSGRVVPGCRVKLvnqDADgiGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELII 568
Cdd:COG1022 396 RIGTVGPPLPGVEVKI---AED--GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 569 TAGGENVPPVPIEEAVKmELPIISSAMLIGDQRKFLSMLLtlkcTLNPETseptdnlteqAVEFCQRVGSKASTVSEIVg 648
Cdd:COG1022 471 TSGGKNVAPQPIENALK-ASPLIEQAVVVGDGRPFLAALI----VPDFEA----------LGEWAEENGLPYTSYAELA- 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19705503 649 qKDEAVYQAIHEGIQRVNANaAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKDIIDSFYQEQ 719
Cdd:COG1022 535 -QDPEVRALIQEEVDRANAG-LSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
127-701 |
4.17e-152 |
|
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: 449.35 E-value: 4.17e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 127 WERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 206
Cdd:cd05907 3 WQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 207 VDTqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealdaiidtqqPNQCCVLVYTSGTTGNP 286
Cdd:cd05907 83 VED------------------------------------------------------------PDDLATIIYTSGTTGRP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 287 KGVMLSQDNITWTARYGSQAgdIQPAEvqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFADPDAlkgTLVNTLREVEP 366
Cdd:cd05907 103 KGVMLSHRNILSNALALAER--LPATE--GDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAE---TLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 367 TSHMGVPRVWEKIMERIQEVAAQSGfiRRKMLLWAmsvtleqnltcpsndlkpftsrladylVLARVRqalgFAKCqknf 446
Cdd:cd05907 176 TVFLAVPRVWEKVYAAIKVKAVPGL--KRKLFDLA---------------------------VGGRLR----FAAS---- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 447 yGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQdadgiGEICLWGRTIFMGY 526
Cdd:cd05907 219 -GGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD-----GEILVRGPNVMLGY 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 527 LNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVKMElPIISSAMLIGDQRKFLSM 606
Cdd:cd05907 293 YKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PLISQAVVIGDGRPFLVA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 607 LLTLKCtlnpetseptdnltEQAVEFCQRVGSKASTVSEIVgqKDEAVYQAIHEGIQRVNAnAAARPYHIQKWAILERDF 686
Cdd:cd05907 372 LIVPDP--------------EALEAWAEEHGIAYTDVAELA--ANPAVRAEIEAAVEAANA-RLSRYEQIKKFLLLPEPF 434
|
570
....*....|....*
gi 19705503 687 SISGGELGPTMKLKR 701
Cdd:cd05907 435 TIENGELTPTLKLKR 449
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
106-570 |
7.40e-105 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 326.58 E-value: 7.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 106 FYEALDKYGNLSALGFkrkDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIY 185
Cdd:pfam00501 1 LERQAARTPDKTALEV---GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 186 TTSSPEACQYIAHDCRANVIVVDTQKQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEVPEEAldaii 265
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPP----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 266 dtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 345
Cdd:pfam00501 153 ---DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 346 CFADPDALK--GTLVNTLREVEPTSHMGVPRVWEKIMEriqevaaqSGFIRRkmllwamsvtleqnltcpsndlkpftsr 423
Cdd:pfam00501 230 VLPPGFPALdpAALLELIERYKVTVLYGVPTLLNMLLE--------AGAPKR---------------------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 424 ladyLVLARVRQALgfakcqknfYGAAPMTAETQRFFLGLNIR-LYAGYGLSESTGP---HFMSSPYNYRLYSSGRVVPG 499
Cdd:pfam00501 274 ----ALLSSLRLVL---------SGGAPLPPELARRFRELFGGaLVNGYGLTETTGVvttPLPLDEDLRSLGSVGRPLPG 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19705503 500 CRVKLVNQD-----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITA 570
Cdd:pfam00501 341 TEVKIVDDEtgepvPPGePGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
127-708 |
8.83e-93 |
|
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: 300.11 E-value: 8.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 127 WERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 206
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 207 VDTQKQLEKILKIWKDLPHLKAVVIYQeppPKKMAN-----VYTMEELIELGQEVPE---EALDAIIDTQQPNQCCVLVY 278
Cdd:cd17641 89 AEDEEQVDKLLEIADRIPSVRYVIYCD---PRGMRKyddprLISFEDVVALGRALDRrdpGLYEREVAAGKGEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 279 TSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAevqqEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFA-DPDalkgTL 357
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPG----DEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPeEPE----TM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 358 VNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSV---TLEQNLTCPSNDL-KPFTSRLADYLVLARV 433
Cdd:cd17641 238 MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLglrALDRGKRGRPVSLwLRLASWLADALLFRPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 434 RQALGFAKCQKNFYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNqdadgIG 513
Cdd:cd17641 318 RDRLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDE-----VG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 514 EICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVKMElPIISS 593
Cdd:cd17641 393 EILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFS-PYIAE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 594 AMLIGDQRKFLSMLLtlkctlnpetseptdNLTEQAV-EFCQRVGSKASTVSEIVGQkdEAVYQAIHEGIQRVNANAAAr 672
Cdd:cd17641 472 AVVLGAGRPYLTAFI---------------CIDYAIVgKWAEQRGIAFTTYTDLASR--PEVYELIRKEVEKVNASLPE- 533
|
570 580 590
....*....|....*....|....*....|....*.
gi 19705503 673 PYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKY 708
Cdd:cd17641 534 AQRIRRFLLLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
126-716 |
9.07e-86 |
|
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: 280.64 E-value: 9.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 126 KWERISYYQYYLIARKVAKGFLKLGLER--AHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRAN 203
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 204 VIVVDtqkqlekilkiwKDLphlkavviyqepppkkmaNVYTMEELIELGQEVPEEALDAiidtqQPNQCCVLVYTSGTT 283
Cdd:cd05927 82 IVFCD------------AGV------------------KVYSLEEFEKLGKKNKVPPPPP-----KPEDLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 284 GNPKGVMLSQDNITWTARYGSQAGDIQPAEVQQEVVVSYLPLSHIAAQIYdLWTGIQWGAQVCFADPDALKgtLVNTLRE 363
Cdd:cd05927 127 GNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFYSGDIRL--LLDDIKA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 364 VEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSvTLEQNLtcpsNDLKPFTSRLADYLVLARVRQALGfAKCQ 443
Cdd:cd05927 204 LKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALN-YKLAEL----RSGVVRASPFWDKLVFNKIKQALG-GNVR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 444 KNFYGAAPMTAETQRFFLG-LNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLV-----NQDADGI---GE 514
Cdd:cd05927 278 LMLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVdvpemNYDAKDPnprGE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 515 ICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIeEAVKMELPIISSA 594
Cdd:cd05927 358 VCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKI-ENIYARSPFVAQI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 595 MLIGDQRKflSMLLtlkCTLNPEtseptdnlTEQAVEFCQRVGSKASTVSEIVgqKDEAVYQAIHEGIQRVNANAAARPY 674
Cdd:cd05927 437 FVYGDSLK--SFLV---AIVVPD--------PDVLKEWAASKGGGTGSFEELC--KNPEVKKAILEDLVRLGKENGLKGF 501
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 19705503 675 HIQKWAILERD-FSISGGELGPTMKLKRLTVLEKYKDIIDSFY 716
Cdd:cd05927 502 EQVKAIHLEPEpFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
102-598 |
2.68e-79 |
|
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: 260.51 E-value: 2.68e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 102 VHQMFYEALDKYGNLSALgfkrKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIV 181
Cdd:COG0318 1 LADLLRRAAARHPDRPAL----VFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 182 TGIYTTSSPEACQYIAHDCRANVIVvdtqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeeal 261
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALV------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 262 daiidtqqpnqCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAAQIYDLWTGIQW 341
Cdd:COG0318 102 -----------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP----GDVVLVALPLFHVFGLTVGLLAPLLA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 342 GAQ-VCFADPDAlkGTLVNTLREVEPTSHMGVPRVWEKIMERiqevaaqsgfirrkmllwamsvtleqnltcpsndlkpf 420
Cdd:COG0318 167 GATlVLLPRFDP--ERVLELIERERVTVLFGVPTMLARLLRH-------------------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 421 tSRLADYLvLARVRQAlgfakcqknFYGAAPMTAET-QRFFLGLNIRLYAGYGLSEsTGPHFMSSPYNY---RLYSSGRV 496
Cdd:COG0318 207 -PEFARYD-LSSLRLV---------VSGGAPLPPELlERFEERFGVRIVEGYGLTE-TSPVVTVNPEDPgerRPGSVGRP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 497 VPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTHEAIDsEGWLHTGDMGRLDDDGFLYITGRLKELIIT 569
Cdd:COG0318 275 LPGVEVRIV--DEDGrelppgeVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
490 500
....*....|....*....|....*....
gi 19705503 570 aGGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:COG0318 352 -GGENVYPAEVEEVL-AAHPGVAEAAVVG 378
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
128-701 |
1.70e-65 |
|
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: 224.16 E-value: 1.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGG--IVTGiyTTSSPEACQYIAHDCRANVI 205
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAvdVVRG--SDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 206 VVDTQkqlekilkiwkdlphlkavviyqeppPKKMAnvytmeelielgqevpeealdaiidtqqpnqccVLVYTSGTTGN 285
Cdd:cd17640 82 VVEND--------------------------SDDLA---------------------------------TIIYTSGTTGN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 286 PKGVMLSQDNITWTARygsQAGDIQPAEVQQeVVVSYLPLSHIAAQIYDlWTGIQWGAQVCFADPDALKgtlvNTLREVE 365
Cdd:cd17640 103 PKGVMLTHANLLHQIR---SLSDIVPPQPGD-RFLSILPIWHSYERSAE-YFIFACGCSQAYTSIRTLK----DDLKRVK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 366 PTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnltcpsndlkpftsrladyLVLARVRQALGfakcqkn 445
Cdd:cd17640 174 PHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF--------------------------LSGGIFKFGIS------- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 446 fyGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGI------GEICLWG 519
Cdd:cd17640 221 --GGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 520 RTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISSAMLIGD 599
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEAL-MRSPFIEQIMVVGQ 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 600 QRKFLSMLLTlkctlnPetseptdNLTEQAVEFCQRVGSKASTVSEIVGQKDE-AVYQaiHEGIQRVNANAAARPY-HIQ 677
Cdd:cd17640 378 DQKRLGALIV------P-------NFEELEKWAKESGVKLANDRSQLLASKKVlKLYK--NEIKDEISNRPGFKSFeQIA 442
|
570 580
....*....|....*....|....
gi 19705503 678 KWAILErDFSISGGELGPTMKLKR 701
Cdd:cd17640 443 PFALLE-EPFIENGEMTQTMKIKR 465
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
139-707 |
5.27e-65 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 224.27 E-value: 5.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 139 ARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTqkqlekiLK 218
Cdd:cd05932 16 ARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK-------LD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 219 IWKDLPHLKA--VVIYQEPPPKKMANVYTMEELIELGQEVPEEAldaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQDNI 296
Cdd:cd05932 89 DWKAMAPGVPegLISISLPPPSAANCQYQWDDLIAQHPPLEERP------TRFPEQLATLIYTSGTTGQPKGVMLTFGSF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 297 TWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAdpDALKgTLVNTLREVEPTSHMGVPRVW 376
Cdd:cd05932 163 AWAAQAGIEHIGTEE----NDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFA--ESLD-TFVEDVQRARPTLFFSVPRLW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 377 EKIMERIQEVAAQSgfiRRKMLLWAmsvtleqnltcpsndlkPFTSRladyLVLARVRQALGFAKCQKNFYGAAPMTAET 456
Cdd:cd05932 236 TKFQQGVQDKIPQQ---KLNLLLKI-----------------PVVNS----LVKRKVLKGLGLDQCRLAGCGSAPVPPAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 457 QRFF--LGLNIrlYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQdadgiGEICLWGRTIFMGYLNMEDKTH 534
Cdd:cd05932 292 LEWYrsLGLNI--LEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSPALMMGYYKDPEATA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 535 EAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISSAMLIGDQrkfLSMLLTLkCTL 614
Cdd:cd05932 365 EAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKL-AEHDRVEMVCVIGSG---LPAPLAL-VVL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 615 NPETSEPTDNLTEQAVEfcqrvgskastvseivgqkdeavyQAIHEGIQRVnaNAAARPY-HIQKWAILERDFSISGGEL 693
Cdd:cd05932 440 SEEARLRADAFARAELE------------------------ASLRAHLARV--NSTLDSHeQLAGIVVVKDPWSIDNGIL 493
|
570
....*....|....
gi 19705503 694 GPTMKLKRlTVLEK 707
Cdd:cd05932 494 TPTLKIKR-NVLEK 506
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
272-647 |
1.64e-64 |
|
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: 217.54 E-value: 1.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 272 QCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAaQIYDLWTGIQWGAQVCFADPD 351
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTE----GDVFLSTLPLFHIG-GLFGLLGALLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 352 aLKGTLVNTLREVEPTSHMGVPRVWEKIMERIqevaaqsgfirrkmllwamsvtleqnltcpsndlkpftsRLADYlVLA 431
Cdd:cd04433 76 -DPEAALELIEREKVTILLGVPTLLARLLKAP---------------------------------------ESAGY-DLS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 432 RVRQAlgfakcqknFYGAAPMTAETQRFFLGL-NIRLYAGYGLSESTGPHFMSSPYN--YRLYSSGRVVPGCRVKLVNQD 508
Cdd:cd04433 115 SLRAL---------VSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPDDdaRKPGSVGRPVPGVEVRIVDPD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 509 -----ADGIGEICLWGRTIFMGYLNMEDKThEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEA 583
Cdd:cd04433 186 ggelpPGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAV 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19705503 584 VKmELPIISSAMLIG--DQRkfLSMLLTLKCTLNPetsePTDNLTEQAVEFCQRVGSKASTVSEIV 647
Cdd:cd04433 264 LL-GHPGVAEAAVVGvpDPE--WGERVVAVVVLRP----GADLDAEELRAHVRERLAPYKVPRRVV 322
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
130-598 |
4.32e-64 |
|
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: 220.93 E-value: 4.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 130 ISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDt 209
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 210 QKQLEKILKIWKDLPHLKAVVIYqEPPPKKMANVYTMEElIELGQEVPEEALDAIIDtqqPNQCCVLVYTSGTTGNPKGV 289
Cdd:cd05911 90 PDGLEKVKEAAKELGPKDKIIVL-DDKPDGVLSIEDLLS-PTLGEEDEDLPPPLKDG---KDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 290 MLSQDNITWTArygSQAGDIQPAEVQ-QEVVVSYLPLSHIAAQIYDLWTgiqwgaqvcfadpdALKGTLVNTLREVEPts 368
Cdd:cd05911 165 CLSHRNLIANL---SQVQTFLYGNDGsNDVILGFLPLYHIYGLFTTLAS--------------LLNGATVIIMPKFDS-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 369 hmgvprvwEKIMERIQEvaaqsgfiRRKMLLW---AMSVTLEQNLTCPSNDLKPftsrladylvLARVrqalgfakcqkn 445
Cdd:cd05911 226 --------ELFLDLIEK--------YKITFLYlvpPIAAALAKSPLLDKYDLSS----------LRVI------------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 446 FYGAAPMTAETQRFF--LGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDA------DGIGEICL 517
Cdd:cd05911 268 LSGGAPLSKELQELLakRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGkdslgpNEPGEICV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 518 WGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISSAMLI 597
Cdd:cd05911 348 RGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKEL-IKYKGFQVAPAEL-EAVLLEHPGVADAAVI 425
|
.
gi 19705503 598 G 598
Cdd:cd05911 426 G 426
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
133-607 |
3.67e-62 |
|
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: 215.00 E-value: 3.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 133 YQYYLIARKVAK--GFLKL-GLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIahdcranvivvdt 209
Cdd:cd05914 8 LTYKDLADNIAKfaLLLKInGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHI------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 210 qkqlekilkiwkdLPHLKAVVIYqepppkkmanvytmeelielgqevpeealdaiidTQQPNQCCVLVYTSGTTGNPKGV 289
Cdd:cd05914 75 -------------LNHSEAKAIF----------------------------------VSDEDDVALINYTSGTTGNSKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 290 MLSQDNITWTARYGSQAGDIQPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCFADpdALKGTLVNTLREVEPTSH 369
Cdd:cd05914 108 MLTYRNIVSNVDGVKEVVLLGKGDK----ILSILPLHHIYPLTFTLLLPLLNGAHVVFLD--KIPSAKIIALAFAQVTPT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 370 MGVPRVWEkiMERIqevaaqsgfirRKMLlwamsvtleqnlTCPSNDLKPFTSRLADYLVLARVRQALgFAKCQKNFYGA 449
Cdd:cd05914 182 LGVPVPLV--IEKI-----------FKMD------------IIPKLTLKKFKFKLAKKINNRKIRKLA-FKKVHEAFGGN 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 450 --------APMTAETQRFFLGLNIRLYAGYGLSEsTGPHFMSSPYN-YRLYSSGRVVPGCRVKLVNQD-ADGIGEICLWG 519
Cdd:cd05914 236 ikefviggAKINPDVEEFLRTIGFPYTIGYGMTE-TAPIISYSPPNrIRLGSAGKVIDGVEVRIDSPDpATGEGEIIVRG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 520 RTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIE-EAVKMELPIISsamLIG 598
Cdd:cd05914 315 PNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEaKINNMPFVLES---LVV 391
|
....*....
gi 19705503 599 DQRKFLSML 607
Cdd:cd05914 392 VQEKKLVAL 400
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
130-701 |
4.12e-62 |
|
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: 216.31 E-value: 4.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 130 ISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDT 209
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 210 QKqlekilkiwKDLphlkavviyqepppkkmanvytmeelielgqevpeealdaiidtqqpnqcCVLVYTSGTTGNPKGV 289
Cdd:cd17639 86 KP---------DDL--------------------------------------------------ACIMYTSGSTGNPKGV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 290 MLSQDNITwtARYGSQAGDIQPAEVQQEVVVSYLPLSHI---AAQIydlwTGIQWGAQVCFADPDalkgTLVNT------ 360
Cdd:cd17639 107 MLTHGNLV--AGIAGLGDRVPELLGPDDRYLAYLPLAHIfelAAEN----VCLYRGGTIGYGSPR----TLTDKskrgck 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 361 --LREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLtcpsndlKPFTSRLADYLVLARVRQALG 438
Cdd:cd17639 177 gdLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALK-------EGPGTPLLDELVFKKVRAALG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 439 fAKCQKNFYGAAPMTAETQRFflgLNI---RLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGI--- 512
Cdd:cd17639 250 -GRLRYMLSGGAPLSADTQEF---LNIvlcPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYstd 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 513 -----GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENvppVPIE--EAVK 585
Cdd:cd17639 326 kppprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEY---IALEklESIY 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 586 MELPIISSAMLIGDQRKflSMLLTLKCTlnpetseptdnlTEQAVE-FCQRVGSKASTVSEIVgqKDEAVYQAIHEGIQR 664
Cdd:cd17639 403 RSNPLVNNICVYADPDK--SYPVAIVVP------------NEKHLTkLAEKHGVINSEWEELC--EDKKLQKAVLKSLAE 466
|
570 580 590
....*....|....*....|....*....|....*...
gi 19705503 665 VNANAAARPYHI-QKWAILERDFSISGGELGPTMKLKR 701
Cdd:cd17639 467 TARAAGLEKFEIpQGVVLLDEEWTPENGLVTAAQKLKR 504
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
99-598 |
2.87e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 211.58 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 99 PYTVHQMFYEALDKYGNLSALGFKRKdkweRISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG 178
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYFDGR----RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 179 GIVTGIYTTSSPEACQYIAHDCRANVIVVDTQ--KQLEKILKiwkDLPHLKAVVIYQEPPPK-KMANVYTMEELIElGQe 255
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAAILP---QLPTVRTVIVEGDGPAApLAPEVGEYEELLA-AA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 256 vPEEALDAIIDtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAAqiydl 335
Cdd:PRK06187 156 -SDTFDFPDID---ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR----DDVYLVIVPMFHVHA----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 336 WT----GIQWGAQVCFA---DPDalkgTLVNTLREVEPT-SHMgVPRVWEkimeriqevaaqsgfirrkMLLwamsvtle 407
Cdd:PRK06187 223 WGlpylALMAGAKQVIPrrfDPE----NLLDLIETERVTfFFA-VPTIWQ-------------------MLL-------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 408 QNLTCPSNDLkpftsrladylvlARVRQALgfakcqknfYGAAPMTAETQRFFLG-LNIRLYAGYGLSESTG-------P 479
Cdd:PRK06187 271 KAPRAYFVDF-------------SSLRLVI---------YGGAALPPALLREFKEkFGIDLVQGYGMTETSPvvsvlppE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 480 HFMSSPYNYRlYSSGRVVPGCRVKLVNQD-----ADG--IGEICLWGRTIFMGYLNMEDKTHEAIDSeGWLHTGDMGRLD 552
Cdd:PRK06187 329 DQLPGQWTKR-RSAGRPLPGVEARIVDDDgdelpPDGgeVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYID 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 19705503 553 DDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:PRK06187 407 EDGYLYITDRIKDVIIS-GGENIYPRELEDAL-YGHPAVAEVAVIG 450
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
105-721 |
3.28e-57 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 206.41 E-value: 3.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 105 MFYEALDKYGNLSALGFK-----RKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGG 179
Cdd:PLN02614 50 VFRMSVEKYPNNPMLGRReivdgKPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 180 IVTGIYTTSSPEACQYIAHDCRANVIVVDTQKqlekILKIWKDLP----HLKAVVIYQ--EPPPKKMAN-----VYTMEE 248
Cdd:PLN02614 130 YCVPLYDTLGAGAVEFIISHSEVSIVFVEEKK----ISELFKTCPnsteYMKTVVSFGgvSREQKEEAEtfglvIYAWDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 249 LIELGQEVPEEaldaiIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNI-TWTARYGSQAGDIQPAEVQQEVVVSYLPLSH 327
Cdd:PLN02614 206 FLKLGEGKQYD-----LPIKKKSDICTIMYTSGTTGDPKGVMISNESIvTLIAGVIRLLKSANAALTVKDVYLSYLPLAH 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 328 IAAQIYDLWTgIQWGAQVCFADPDAlkGTLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLe 407
Cdd:PLN02614 281 IFDRVIEECF-IQHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKF- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 408 QNLTCPSNDLKpfTSRLADYLVLARVRQALGfAKCQKNFYGAAPMTAETQRFflglnIRLYA------GYGLSESTGPHF 481
Cdd:PLN02614 357 GNMKKGQSHVE--ASPLCDKLVFNKVKQGLG-GNVRIILSGAAPLASHVESF-----LRVVAcchvlqGYGLTESCAGTF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 482 MSSPYNYRLYSS-GRVVPGCRVKL-----VNQDADGI---GEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLD 552
Cdd:PLN02614 429 VSLPDELDMLGTvGPPVPNVDIRLesvpeMEYDALAStprGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQ 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 553 DDGFLYITGRLKELIITAGGENVPPVPIEEaVKMELPIISSAMLIGDQrkFLSMLLTLKctlNPETSEPTDNLTEQAVE- 631
Cdd:PLN02614 508 PNGSMKIIDRKKNIFKLSQGEYVAVENIEN-IYGEVQAVDSVWVYGNS--FESFLVAIA---NPNQQILERWAAENGVSg 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 632 ----FCQRVGSKASTVSEIVGQKDEavyqaihegiQRVNANAAARPYHIQKWAI-LERDFsisggeLGPTMKLKRLTVLE 706
Cdd:PLN02614 582 dynaLCQNEKAKEFILGELVKMAKE----------KKMKGFEIIKAIHLDPVPFdMERDL------LTPTFKKKRPQLLK 645
|
650
....*....|....*
gi 19705503 707 KYKDIIDSFYQEQKQ 721
Cdd:PLN02614 646 YYQSVIDEMYKTTNE 660
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
128-598 |
5.36e-56 |
|
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: 197.45 E-value: 5.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 207
Cdd:cd17631 19 RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLFD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DTqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealdaiidtqqpnqcCVLVYTSGTTGNPK 287
Cdd:cd17631 99 DL----------------------------------------------------------------ALLMYTSGTTGRPK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 288 GVMLSQDNITWTARYGSQAGDIQPAEVQqeVVVsyLPLSHIAA----QIYDLWTGiqwGAQVCFADPDAlkGTLVNTLRE 363
Cdd:cd17631 115 GAMLTHRNLLWNAVNALAALDLGPDDVL--LVV--APLFHIGGlgvfTLPTLLRG---GTVVILRKFDP--ETVLDLIER 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 364 VEPTSHMGVPRVWEKImeriqevaaqsgfirrkmllwamsvtleqnLTCPsndlkpftsRLADYlVLARVRQALgfakcq 443
Cdd:cd17631 186 HRVTSFFLVPTMIQAL------------------------------LQHP---------RFATT-DLSSLRAVI------ 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 444 knfYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYR--LYSSGRVVPGCRVKLVNQD-----ADGIGEIC 516
Cdd:cd17631 220 ---YGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVDPDgrevpPGEVGEIV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 517 LWGRTIFMGYLNMEDKTHEAIDsEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAML 596
Cdd:cd17631 297 VRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVEDVL-YEHPAVAEVAV 373
|
..
gi 19705503 597 IG 598
Cdd:cd17631 374 IG 375
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
101-718 |
9.06e-56 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 201.87 E-value: 9.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 101 TVHQMFYEALDKYGNLSALGFKRKD-------KWerISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVG 173
Cdd:PLN02736 45 TLHDNFVYAVETFRDYKYLGTRIRVdgtvgeyKW--MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 174 TVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKqLEKILKIWKDLPHLKAVVIYQ-------EPPPKKMANVYTM 246
Cdd:PLN02736 123 CSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQT-LNTLLSCLSEIPSVRLIVVVGgadeplpSLPSGTGVEIVTY 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 247 EELIELGQEVPEEALdaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEVQqevvVSYLPLS 326
Cdd:PLN02736 202 SKLLAQGRSSPQPFR-----PPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVH----ISYLPLA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 327 HIAAQIYDLWTgIQWGAQVCFADPDALKgtLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTl 406
Cdd:PLN02736 273 HIYERVNQIVM-LHYGVAVGFYQGDNLK--LMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAK- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 407 EQNLtcpSNDLKPftSRLADYLVLARVRQALGfAKCQKNFYGAAPMTAETQRFflgLNI----RLYAGYGLSESTGPhfm 482
Cdd:PLN02736 349 KQAL---ENGKNP--SPMWDRLVFNKIKAKLG-GRVRFMSSGASPLSPDVMEF---LRIcfggRVLEGYGMTETSCV--- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 483 SSPYNYRLYSSGRV---VPGCRVKLV--------NQDAD-GIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGR 550
Cdd:PLN02736 417 ISGMDEGDNLSGHVgspNPACEVKLVdvpemnytSEDQPyPRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGL 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 551 LDDDGFLYITGRLKELIITAGGENVPPVPIEEaVKMELPIISSAMLIGDQrkFLSMLLTLkCTLNPETSEPtdnlteqav 630
Cdd:PLN02736 497 WLPGGRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKFVAQCFVYGDS--LNSSLVAV-VVVDPEVLKA--------- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 631 eFCQRVGSKASTVSEIVgqKDEAVYQAIHEGIQRVNANAAARPYHIQKWAILERD-FSISGGELGPTMKLKRLTVLEKYK 709
Cdd:PLN02736 564 -WAASEGIKYEDLKQLC--NDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEpFTVENGLLTPTFKVKRPQAKAYFA 640
|
....*....
gi 19705503 710 DIIDSFYQE 718
Cdd:PLN02736 641 KAISDMYAE 649
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
96-601 |
1.78e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 192.43 E-value: 1.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 96 TQLPYTVHQMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTV 175
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGD----QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 176 FAGGIVTGIYTTSSPEACQYIAHDCRANVIVVdTQKQLEKILKIWKDLPHLKAVVIYQEPPPK-KMANVYTMEELIELGQ 254
Cdd:PRK07656 77 KAGAVVVPLNTRYTADEAAYILARGDAKALFV-LGLFLGVDYSATTRLPALEHVVICETEEDDpHTEKMKTFTDFLAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 255 EVPEEAldaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDiqpaevqqeVVVSYLPLSHIa 329
Cdd:PRK07656 156 PAERAP------EVDPDDVADILFTSGTTGRPKGAMLTHRQLLsnaadWAEYLGLTEGD---------RYLAANPFFHV- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 330 aqiydlwtgiqWGAQVCFADPDALKGTLVntlreVEPTSHMgvprvwEKIMERIQEvaaqsgfirRKMLLWAMSVTLEQN 409
Cdd:PRK07656 220 -----------FGYKAGVNAPLMRGATIL-----PLPVFDP------DEVFRLIET---------ERITVLPGPPTMYNS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 410 LtcpsndlkpFTSRLADYLVLARVRQALGfakcqknfyGAAPMTAE-TQRFFLGLNIRLYA-GYGLSESTGPHFMSSPYN 487
Cdd:PRK07656 269 L---------LQHPDRSAEDLSSLRLAVT---------GAASMPVAlLERFESELGVDIVLtGYGLSEASGVTTFNRLDD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 488 YRL---YSSGRVVPGCRVKLVNQDADGI-----GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYI 559
Cdd:PRK07656 331 DRKtvaGTIGTAIAGVENKIVNELGEEVpvgevGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYI 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 19705503 560 TGRLKELIITaGGENVPPVPIEEaVKMELPIISSAMLIG--DQR 601
Cdd:PRK07656 411 VDRKKDMFIV-GGFNVYPAEVEE-VLYEHPAVAEAAVIGvpDER 452
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
104-598 |
9.81e-53 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 189.31 E-value: 9.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 104 QMFYEALDKYGNLSALGFKrkDKWerISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 183
Cdd:cd05936 3 DLLEEAARRFPDKTALIFM--GRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 184 IYTTSSPEACQYIAHDCRANVIVVDTQkqLEKILKIWKDLPhlkavviyqepppkkmanvytmeelieLGQEVPEEALda 263
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAVS--FTDLLAAGAPLG---------------------------ERVALTPEDV-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 264 iidtqqpnqcCVLVYTSGTTGNPKGVMLSQDNITWTARygSQAGDIQPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGA 343
Cdd:cd05936 128 ----------AVLQYTSGTTGVPKGAMLTHRNLVANAL--QIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 344 -QVCFADPDALkgTLVNTLREVEPTSHMGVPRVWEKIMEriqevaaqsgfirrkmllwamsvtleqnltcpsndLKPFTS 422
Cdd:cd05936 196 tIVLIPRFRPI--GVLKEIRKHRVTIFPGVPTMYIALLN-----------------------------------APEFKK 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 423 RLadylvLARVRQALGfakcqknfyGAAPMTAETQRFFLGL-NIRLYAGYGLSEsTGP--HFMSSPYNYRLYSSGRVVPG 499
Cdd:cd05936 239 RD-----FSSLRLCIS---------GGAPLPVEVAERFEELtGVPIVEGYGLTE-TSPvvAVNPLDGPRKPGSIGIPLPG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 500 CRVKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDsEGWLHTGDMGRLDDDGFLYITGRLKELIItAGGEN 574
Cdd:cd05936 304 TEVKIVDDDgeelPPGeVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGFN 381
|
490 500
....*....|....*....|....
gi 19705503 575 VPPVPIEEAVkMELPIISSAMLIG 598
Cdd:cd05936 382 VYPREVEEVL-YEHPAVAEAAVVG 404
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
101-717 |
4.97e-49 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 183.09 E-value: 4.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 101 TVHQMFYEALDKYGNLSALGFKR-KD------KWEriSYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVG 173
Cdd:PLN02430 43 TAWDIFSKSVEKYPDNKMLGWRRiVDgkvgpyMWK--TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 174 TVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKQLEKILKIWKDLPHLKAVVIYQEPPPK---KMANV----YTM 246
Cdd:PLN02430 121 CAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLKAIVSFTSVTEEesdKASQIgvktYSW 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 247 EELIELGQEVPEEaldaiIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTAR----YGSQAGDIQPAEvqqEVVVSY 322
Cdd:PLN02430 201 IDFLHMGKENPSE-----TNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRgvdlFMEQFEDKMTHD---DVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 323 LPLSHIAAQIYDLWTgIQWGAQVCF--ADPDALKgtlvNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKM--- 397
Cdd:PLN02430 273 LPLAHILDRMIEEYF-FRKGASVGYyhGDLNALR----DDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIfna 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 398 -----LLWamsvtleQNLTCPSNDLKPftsrLADYLVLARVRQALGfAKCQKNFYGAAPMTAETQRFflgLNIR----LY 468
Cdd:PLN02430 348 lykykLAW-------MNRGYSHKKASP----MADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEF---LRVTscafVV 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 469 AGYGLSESTGPHFMSSPYNYRLYSSGRVVPGC---RVKLVNQ---DADG---IGEICLWGRTIFMGYLNMEDKTHEAIdS 539
Cdd:PLN02430 413 QGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYnelRLEEVPEmgyDPLGeppRGEICVRGKCLFSGYYKNPELTEEVM-K 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 540 EGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVpPVPIEEAVKMELPIISSAMLIGDQrkFLSMLLTLkCTLNPETS 619
Cdd:PLN02430 492 DGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYV-ALEYLENVYGQNPIVEDIWVYGDS--FKSMLVAV-VVPNEENT 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 620 EP---TDNLTEQAVEFCQRVGSKASTVSEivgqkdeavyqaihegIQRVNANAAARPYHIQKWAILE-RDFSISGGELGP 695
Cdd:PLN02430 568 NKwakDNGFTGSFEELCSLPELKEHILSE----------------LKSTAEKNKLRGFEYIKGVILEtKPFDVERDLVTA 631
|
650 660
....*....|....*....|..
gi 19705503 696 TMKLKRLTVLEKYKDIIDSFYQ 717
Cdd:PLN02430 632 TLKKRRNNLLKYYQVEIDEMYR 653
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
104-720 |
2.24e-48 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 181.19 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 104 QMFYEALDKYGNLSALGFK-----RKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG 178
Cdd:PLN02861 47 QFFSDAVKKYPNNQMLGRRqvtdsKVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 179 GIVTGIYTTSSPEACQYIAHDCRANVIVVdtqkQLEKILKIWKDLP----HLKAVVIY-------QEPPPKKMANVYTME 247
Cdd:PLN02861 127 ITYVPLYDTLGANAVEFIINHAEVSIAFV----QESKISSILSCLPkcssNLKTIVSFgdvsseqKEEAEELGVSCFSWE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 248 ELIELGQevpeeaLDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEVQQE-VVVSYLPLS 326
Cdd:PLN02861 203 EFSLMGS------LDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATEEdSYFSYLPLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 327 HIAAQIYDLWTgIQWGAQVCFADPDALkgTLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTL 406
Cdd:PLN02861 277 HVYDQVIETYC-ISKGASIGFWQGDIR--YLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 407 eQNLT--CPSNDLKPFTSRladyLVLARVRQALGfAKCQKNFYGAAPMTAETQRFFLGLNIR-LYAGYGLSESTGPHFMS 483
Cdd:PLN02861 354 -GNLRkgLKQEEASPRLDR----LVFDKIKEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCGGCFTS 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 484 SPYNYRLYSS-GRVVPGCRVKLVNQDADGI--------GEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDD 554
Cdd:PLN02861 428 IANVFSMVGTvGVPMTTIEARLESVPEMGYdalsdvprGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPN 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 555 GFLYITGRLKELIITAGGENVpPVPIEEAVKMELPIISSAMLIGDQrkFLSMLLTLkctLNPEtseptdnltEQAVEFCQ 634
Cdd:PLN02861 507 GAMKIIDRKKNIFKLSQGEYV-AVENLENTYSRCPLIASIWVYGNS--FESFLVAV---VVPD---------RQALEDWA 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 635 RVGSKASTVSEIVgqKDEAVYQAIHEGIQRVNANAAARPYHIQKWAILERD-FSISGGELGPTMKLKRLTVLEKYKDIID 713
Cdd:PLN02861 572 ANNNKTGDFKSLC--KNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNpFDIERDLITPTFKLKRPQLLKYYKDCID 649
|
....*..
gi 19705503 714 SFYQEQK 720
Cdd:PLN02861 650 QLYSEAK 656
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
128-584 |
1.69e-45 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 168.24 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 207
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DTqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealdaiidtqqpnqcCVLVYTSGTTGNPK 287
Cdd:cd05934 82 DP----------------------------------------------------------------ASILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 288 GVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAqvcfadpdalkgTLVntlreVEPT 367
Cdd:cd05934 98 GVVITHANLTFAGYYSARRFGLGE----DDVYLTVLPLFHINAQAVSVLAALSVGA------------TLV-----LLPR 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 368 SHMGvpRVWEKImeriQEVAAQSGFIRRKMllwaMSVTLEQnltcpsndlkPFTSRLADylvlARVRQAlgfakcqknfY 447
Cdd:cd05934 157 FSAS--RFWSDV----RRYGATVTNYLGAM----LSYLLAQ----------PPSPDDRA----HRLRAA----------Y 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 448 GAAPMTAETQRFFLGLNIRLYAGYGLSESTGPhFMSSPYNYRLYSS-GRVVPGCRVKLVNQD----ADG-IGEICL---W 518
Cdd:cd05934 203 GAPNPPELHEEFEERFGVRLLEGYGMTETIVG-VIGPRDEPRRPGSiGRPAPGYEVRIVDDDgqelPAGePGELVIrglR 281
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19705503 519 GRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIEEAV 584
Cdd:cd05934 282 GWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDM-IRRRGENISSAEVERAI 345
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
144-719 |
2.68e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 172.85 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 144 KGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKqLEKILKIWKD- 222
Cdd:PTZ00216 136 RGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKN-VPNLLRLMKSg 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 223 -LPHlkAVVIY--QEPPPKKMAN--VYTMEELIELGQEvpeEALDAIIDTQQPNQCCVLV-YTSGTTGNPKGVM-----L 291
Cdd:PTZ00216 215 gMPN--TTIIYldSLPASVDTEGcrLVAWTDVVAKGHS---AGSHHPLNIPENNDDLALImYTSGTTGDPKGVMhthgsL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 292 SQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHI----AAQIYdlwtgIQWGAQVCFADPDalkgTLVNT------- 360
Cdd:PTZ00216 290 TAGILALEDRLNDLIGPPEE----DETYCSYLPLAHImefgVTNIF-----LARGALIGFGSPR----TLTDTfarphgd 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 361 LREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnltcpsndlkpFTSRLA-----------DYLV 429
Cdd:PTZ00216 357 LTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHA------------------YQSRLRalkegkdtpywNEKV 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 430 LARVRQALGfAKCQKNFYGAAPMTAETQRFF---LGLNIRlyaGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVn 506
Cdd:PTZ00216 419 FSAPRAVLG-GRVRAMLSGGGPLSAATQEFVnvvFGMVIQ---GWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLL- 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 507 qDADGI---------GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENvpp 577
Cdd:PTZ00216 494 -DTEEYkhtdtpeprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEY--- 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 578 VPIE--EAVKMELPIISS---AMLIGDQRKFLSMLLtlkctlnpetseptdnLTEQ--AVEFCQRVGSKAsTVSEIVgqK 650
Cdd:PTZ00216 570 IALEalEALYGQNELVVPngvCVLVHPARSYICALV----------------LTDEakAMAFAKEHGIEG-EYPAIL--K 630
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 651 DEAVYQAIHEGIQRVNANAAARPYHIQKWA-ILERDFSISGGELGPTMKLKRLTVLEKYKDIIDSFYQEQ 719
Cdd:PTZ00216 631 DPEFQKKATESLQETARAAGRKSFEIVRHVrVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFADE 700
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
129-598 |
9.74e-45 |
|
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: 167.80 E-value: 9.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 208
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 209 TQkQLEKILkiwkdlPHLKAVVIYQEPPPKKMANVytmeeliELGQEVPEEALDAIIDTQqpNQCCVLVYTSGTTGNPKG 288
Cdd:cd05904 112 AE-LAEKLA------SLALPVVLLDSAEFDSLSFS-------DLLFEADEAEPPVVVIKQ--DDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 289 VMLSQDN-ITWTARY-GSQAGDIQPaevqQEVVVSYLPLSHIaaqiydlwtgiqWGAQVCFADPDALKGTLVntlreVep 366
Cdd:cd05904 176 VMLTHRNlIAMVAQFvAGEGSNSDS----EDVFLCVLPMFHI------------YGLSSFALGLLRLGATVV-----V-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 367 tshmgVPR-VWEKIMERIQEVAAQSGFIRRKMLLwAMSvtleqnltcpsndlkpfTSRLADYLVLARVRQALGfakcqkn 445
Cdd:cd05904 233 -----MPRfDLEELLAAIERYKVTHLPVVPPIVL-ALV-----------------KSPIVDKYDLSSLRQIMS------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 446 fyGAAPMTAETQRFFLGL--NIRLYAGYGLSESTGP---HFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGI------GE 514
Cdd:cd05904 283 --GAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESlppnqtGE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 515 ICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISSA 594
Cdd:cd05904 361 LWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKEL-IKYKGFQVAPAEL-EALLLSHPEILDA 438
|
....
gi 19705503 595 MLIG 598
Cdd:cd05904 439 AVIP 442
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
97-598 |
1.18e-44 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 169.75 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 97 QLPYTVHQMFYEALDKYGNLSALGF----KRKDKWERISYYQyyLIAR--KVAKGFLKLGLERAHSVAILGFNSPEwffs 170
Cdd:PRK07529 22 DLPASTYELLSRAAARHPDAPALSFlldaDPLDRPETWTYAE--LLADvtRTANLLHSLGVGPGDVVAFLLPNLPE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 171 AVGTVFAG---GIVTGIYTTSSPEAcqyIAHDCR-ANVIVVDTQKQLEKIlKIWKD-------LPHLKAVVIY----QEP 235
Cdd:PRK07529 96 THFALWGGeaaGIANPINPLLEPEQ---IAELLRaAGAKVLVTLGPFPGT-DIWQKvaevlaaLPELRTVVEVdlarYLP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 236 PPKKMAnvytmEELIELGQEVPEEALDAIIDTQQ-----------PNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGS 304
Cdd:PRK07529 172 GPKRLA-----VPLIRRKAHARILDFDAELARQPgdrlfsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 305 QAGDIQPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFADPDALKGTLVntlreveptshmgVPRVWeKIMERIQ 384
Cdd:PRK07529 247 LLLGLGP----GDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGPGV-------------IANFW-KIVERYR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 385 eVAAQSGfirrkmLLWAMSVTLEqnltCPSNdlkpftsrladylvlARVRQALGFAKCqknfyGAAPMTAETQRFFLG-L 463
Cdd:PRK07529 309 -INFLSG------VPTVYAALLQ----VPVD---------------GHDISSLRYALC-----GAAPLPVEVFRRFEAaT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 464 NIRLYAGYGLSESTGPHFMSSPYN-YRLYSSGRVVPGCRVKLVNQDADG----------IGEICLWGRTIFMGYLNmEDK 532
Cdd:PRK07529 358 GVRIVEGYGLTEATCVSSVNPPDGeRRIGSVGLRLPYQRVRVVILDDAGrylrdcavdeVGVLCIAGPNVFSGYLE-AAH 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19705503 533 THEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:PRK07529 437 NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIR-GGHNIDPAAIEEAL-LRHPAVALAAAVG 500
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
126-717 |
4.14e-44 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 169.14 E-value: 4.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 126 KWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVI 205
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 206 VVDtQKQLEKILKIWKDLPHLKAVVIYQEPPPK------KMAN--VYTMEELIELGQEVPEEAldaiiDTQQPNQCCVLV 277
Cdd:PLN02387 183 ICD-SKQLKKLIDISSQLETVKRVIYMDDEGVDsdsslsGSSNwtVSSFSEVEKLGKENPVDP-----DLPSPNDIAVIM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 278 YTSGTTGNPKGVMLSQDNITWTArygSQAGDIQPAEVQQEVVVSYLPLSHI---AAQIYDLWTG--IQWGAQVCFADPDA 352
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATV---AGVMTVVPKLGKNDVYLAYLPLAHIlelAAESVMAAVGaaIGYGSPLTLTDTSN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 353 --LKGTL--VNTLRevePTSHMGVPRVWEKIMERIQE-VAAQSG---------FIRRKMLL---WAMSVTLEqnltcpsn 415
Cdd:PLN02387 334 kiKKGTKgdASALK---PTLMTAVPAILDRVRDGVRKkVDAKGGlakklfdiaYKRRLAAIegsWFGAWGLE-------- 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 416 dlkpftSRLADYLVLARVRQALG----FAKCqknfyGAAPMTAETQRFflgLNIRLYA----GYGLSES-TGPHFMsspy 486
Cdd:PLN02387 403 ------KLLWDALVFKKIRAVLGgrirFMLS-----GGAPLSGDTQRF---INICLGApigqGYGLTETcAGATFS---- 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 487 NYRLYSSGRV---VPGCRVKLVNQDADGI---------GEICLWGRTIFMGYLNMEDKTHEA--IDSEG--WLHTGDMGR 550
Cdd:PLN02387 465 EWDDTSVGRVgppLPCCYVKLVSWEEGGYlisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQ 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 551 LDDDGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISSAMLIGDqrKFLSMLLTLKCTlnpetseptdnlTEQAV 630
Cdd:PLN02387 545 FHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAAL-SVSPYVDNIMVHAD--PFHSYCVALVVP------------SQQAL 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 631 E-FCQRVGSKASTVSEIVgQKDEAVYQaIHEGIQRVNANAAARPYHI-QKWAILERDFSISGGELGPTMKLKRLTVLEKY 708
Cdd:PLN02387 610 EkWAKKAGIDYSNFAELC-EKEEAVKE-VQQSLSKAAKAARLEKFEIpAKIKLLPEPWTPESGLVTAALKLKREQIRKKF 687
|
....*....
gi 19705503 709 KDIIDSFYQ 717
Cdd:PLN02387 688 KDDLKKLYE 696
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
101-582 |
6.79e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 160.75 E-value: 6.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 101 TVHQMFYEALDKYGNLSALGFKRKDKweRISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWffsaVGTVFA--- 177
Cdd:PRK08315 17 TIGQLLDRTAARYPDREALVYRDQGL--RWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEW----VLTQFAtak 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 178 -GGIVTGIYTTSSPEACQYIAH--DCRANVIV--------VDTQKQLEKILKIW-------KDLPHLKAVVIYQEPPPKK 239
Cdd:PRK08315 91 iGAILVTINPAYRLSELEYALNqsGCKALIAAdgfkdsdyVAMLYELAPELATCepgqlqsARLPELRRVIFLGDEKHPG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 240 ManvYTMEELIELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVV 319
Cdd:PRK08315 171 M---LNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTE----EDRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 320 VSYLPL--------------SHIAAQIYDLWTgiqwgaqvcFaDPDAlkgtlvnTLREVEP---TSHMGVPrvwekIMer 382
Cdd:PRK08315 244 CIPVPLyhcfgmvlgnlacvTHGATMVYPGEG---------F-DPLA-------TLAAVEEercTALYGVP-----TM-- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 383 iqevaaqsgFIrrkmllwAMsvtLEQ------NL-----------TCPSNdlkpftsrladylVLARVRQALGfakcqkn 445
Cdd:PRK08315 300 ---------FI-------AE---LDHpdfarfDLsslrtgimagsPCPIE-------------VMKRVIDKMH------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 446 fygaapMTAETqrfflglnIrlyaGYGLSESTGPHFMSS---PYNYRLYSSGRVVPGCRVKLVNQDADGI------GEIC 516
Cdd:PRK08315 341 ------MSEVT--------I----AYGMTETSPVSTQTRtddPLEKRVTTVGRALPHLEVKIVDPETGETvprgeqGELC 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19705503 517 LWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEE 582
Cdd:PRK08315 403 TRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIEE 467
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
91-582 |
3.90e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 158.40 E-value: 3.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 91 LEPFCTQlpyTVHQMFYEALDKYGNLSALGFKRKDKweRISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFS 170
Cdd:PRK12583 12 DKPLLTQ---TIGDAFDATVARFPDREALVVRHQAL--RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 171 AVGTVFAGGIVTGIYTTSSPEACQY-IAH-DCRAnVIVVDTQKQ------LEKILK----------IWKDLPHLKAVVIY 232
Cdd:PRK12583 87 QFATARIGAILVNINPAYRASELEYaLGQsGVRW-VICADAFKTsdyhamLQELLPglaegqpgalACERLPELRGVVSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 233 QEPPPKKMANvytMEELIELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIqpa 312
Cdd:PRK12583 166 APAPPPGFLA---WHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGL--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 313 eVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFA----DPDAlkgtlvnTLREVEP---TSHMGVPRVWEKIMERIQe 385
Cdd:PRK12583 240 -TEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPneafDPLA-------TLQAVEEercTALYGVPTMFIAELDHPQ- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 386 vaaqsgfiRRKMLLWAMSVTLEQNLTCPSNDLKpftsRLADYLVLARVRQALGFAKcqknfygAAPMTAETQRfflglni 465
Cdd:PRK12583 311 --------RGNFDLSSLRTGIMAGAPCPIEVMR----RVMDEMHMAEVQIAYGMTE-------TSPVSLQTTA------- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 466 rlyagyglsestgphfmSSPYNYRLYSSGRVVPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTHEAID 538
Cdd:PRK12583 365 -----------------ADDLERRVETVGRTQPHLEVKVV--DPDGatvprgeIGELCTRGYSVMKGYWNNPEATAESID 425
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 19705503 539 SEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEE 582
Cdd:PRK12583 426 EDGWMHTGDLATMDEQGYVRIVGRSKDMIIR-GGENIYPREIEE 468
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
129-598 |
4.10e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 148.98 E-value: 4.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQyyLIAR--KVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 206
Cdd:PRK06188 37 RLTYGQ--LADRisRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 207 VDTQKQLEKILKIWKDLPHLKAVViyqepppkKMANVYTMEELIELGQEVPEEALDAIIDTQQPNqccVLVYTSGTTGNP 286
Cdd:PRK06188 115 VDPAPFVERALALLARVPSLKHVL--------TLGPVPDGVDLLAAAAKFGPAPLVAAALPPDIA---GLAYTGGTTGKP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 287 KGVMLSQDNITWTArygsqagDIQPAEVQQEVVVSYL---PLSHIAAqiydlwtgiqwgaqvCFADPDALKGTLVNTLRE 363
Cdd:PRK06188 184 KGVMGTHRSIATMA-------QIQLAEWEWPADPRFLmctPLSHAGG---------------AFFLPTLLRGGTVIVLAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 364 VEPTShmgVPRVWEKimERIQEVaaqsgfirrkMLLWAMSVTLeqnLTCPSndlkpftSRLADYLVLARVrqalgfakcq 443
Cdd:PRK06188 242 FDPAE---VLRAIEE--QRITAT----------FLVPTMIYAL---LDHPD-------LRTRDLSSLETV---------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 444 knFYGAAPMT----AET-QRF---FLGLnirlyagYGLSE--------STGPHFMSSPYnyRLYSSGRVVPGCRVKLVnq 507
Cdd:PRK06188 287 --YYGASPMSpvrlAEAiERFgpiFAQY-------YGQTEapmvitylRKRDHDPDDPK--RLTSCGRPTPGLRVALL-- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 508 DADG-------IGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPI 580
Cdd:PRK06188 354 DEDGrevaqgeVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVT-GGFNVFPREV 431
|
490
....*....|....*...
gi 19705503 581 EEAVkMELPIISSAMLIG 598
Cdd:PRK06188 432 EDVL-AEHPAVAQVAVIG 448
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
128-600 |
2.28e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 146.54 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFL-KLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 206
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 207 VDTQKQlEKILKIWKdlphlkavVIYQEPPpkkmanvytmeelieLGQEVPEEALDA-IIDTQQPNQ--CCVLVYTSGTT 283
Cdd:PRK06839 106 VEKTFQ-NMALSMQK--------VSYVQRV---------------ISITSLKEIEDRkIDNFVEKNEsaSFIICYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 284 GNPKGVMLSQDNITWTARYGSQAGDIQpaevQQEVVVSYLPLSHIAaqiydlwtGIQwgaqvCFADPDALKGTLVNTLRE 363
Cdd:PRK06839 162 GKPKGAVLTQENMFWNALNNTFAIDLT----MHDRSIVLLPLFHIG--------GIG-----LFAFPTLFAGGVIIVPRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 364 VEPTSH------------MGVPRVWEKIMEriqevaaqsgfirrkmllwamsvtleqnltCPSNDLKPFTSrladylvla 431
Cdd:PRK06839 225 FEPTKAlsmiekhkvtvvMGVPTIHQALIN------------------------------CSKFETTNLQS--------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 432 rVRQalgfakcqknFY-GAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYR--LYSSGRVVPGCRVKLVNQD 508
Cdd:PRK06839 266 -VRW----------FYnGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIDEN 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 509 AD-----GIGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEA 583
Cdd:PRK06839 335 KNkvevgEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQV 412
|
490
....*....|....*..
gi 19705503 584 VKmELPIISSAMLIGDQ 600
Cdd:PRK06839 413 IN-KLSDVYEVAVVGRQ 428
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
278-631 |
3.45e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 139.92 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 278 YTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFADPDALKGTL 357
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDP----DDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYRNPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 358 V--NTLREVE---PTSHMGVPRVWEKIMERiqevaaqsgfirrkmllwamsvtleqnltcPSNdlkpftsrlADylvLAR 432
Cdd:cd05944 85 LfdNFWKLVEryrITSLSTVPTVYAALLQV------------------------------PVN---------AD---ISS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 433 VRQALGfakcqknfyGAAPMTAET-QRFFLGLNIRLYAGYGLSESTGPHFMSSPYN-YRLYSSGRVVPGCRVKLVNQDAD 510
Cdd:cd05944 123 LRFAMS---------GAAPLPVELrARFEDATGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGLRLPYARVRIKVLDGV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 511 G----------IGEICLWGRTIFMGYLNMEDKTHEAIDsEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPI 580
Cdd:cd05944 194 GrllrdcapdeVGEICVAGPGVFGGYLYTEGNKNAFVA-DGWLNTGDLGRLDADGYLFITGRAKDLIIR-GGHNIDPALI 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 19705503 581 EEAVkMELPIISSAMLIGDQRKFLSMLLTLKCTLNPETSEPTDNLTEQAVE 631
Cdd:cd05944 272 EEAL-LRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARD 321
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
104-598 |
2.01e-35 |
|
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: 141.13 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 104 QMFYeALDKYGNLS-ALGFKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVt 182
Cdd:cd17642 19 QLHK-AMKRYASVPgTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGV- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 183 giyttsSPEACQYIAHDCRANV------IVVDTQKQLEKILKIWKDLPHLKAVVI---------YQEpppkkmanvytME 247
Cdd:cd17642 97 ------APTNDIYNERELDHSLniskptIVFCSKKGLQKVLNVQKKLKIIKTIIIldskedykgYQC-----------LY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 248 ELIELGQEVPEEALDAIIDT-QQPNQCCVLVYTSGTTGNPKGVMLSQDNITwtARYGSQAGDIQPAEVQQEV-VVSYLPL 325
Cdd:cd17642 160 TFITQNLPPGFNEYDFKPPSfDRDEQVALIMNSSGSTGLPKGVQLTHKNIV--ARFSHARDPIFGNQIIPDTaILTVIPF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 326 SHiaaqiydlwtgiqwgAQVCFAdpdaLKGTLVNTLREVEptshmgVPRVWEKI-MERIQEVAAQSGF-IRRKMLLWAMS 403
Cdd:cd17642 238 HH---------------GFGMFT----TLGYLICGFRVVL------MYKFEEELfLRSLQDYKVQSALlVPTLFAFFAKS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 404 VTLEQnltcpsndlkpftSRLADYLVLARvrqalgfakcqknfyGAAPMTAET-----QRFflGLN-IRlyAGYGLSEST 477
Cdd:cd17642 293 TLVDK-------------YDLSNLHEIAS---------------GGAPLSKEVgeavaKRF--KLPgIR--QGYGLTETT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 478 GPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGI------GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRL 551
Cdd:cd17642 341 SAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTlgpnerGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYY 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19705503 552 DDDGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISSAMLIG 598
Cdd:cd17642 421 DEDGHFFIVDRLKSL-IKYKGYQVPPAEL-ESILLQHPKIFDAGVAG 465
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
127-585 |
1.04e-34 |
|
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: 139.30 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 127 WERISYYQYYLIARKVAKGFLKLGlERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEA---CQYIAHDCRAN 203
Cdd:cd05931 22 EETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 204 VIVVDTqkqlekilkiwkdlPHLKAVVIYQEPPPKKMAnvytmeelieLGQEVPEEALDAIIDTQQPNQC-----CVLVY 278
Cdd:cd05931 101 VVLTTA--------------AALAAVRAFAASRPAAGT----------PRLLVVDLLPDTSAADWPPPSPdpddiAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 279 TSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHiaaqiyDLwtgiqwgaqvcfadpdALKGTLV 358
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDP----GDVVVSWLPLYH------DM----------------GLIGGLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 359 NTLreveptsHMGVPRVWekiMeriqevaAQSGFIRRKML-LWAMSvtlEQNLTC---PsN---DL--KPFTSRLADYLV 429
Cdd:cd05931 211 TPL-------YSGGPSVL---M-------SPAAFLRRPLRwLRLIS---RYRATIsaaP-NfayDLcvRRVRDEDLEGLD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 430 LARVRQALgfakcqkNfyGAAPMTAET-QRF---FLGLNIR---LYAGYGLSEST--------GPHFMS----------- 483
Cdd:cd05931 270 LSSWRVAL-------N--GAEPVRPATlRRFaeaFAPFGFRpeaFRPSYGLAEATlfvsggppGTGPVVlrvdrdalagr 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 484 -------SPYNYRLYSSGRVVPGCRVKLVNQD------ADGIGEICLWGRTIFMGYLNMEDKTHE------AIDSEGWLH 544
Cdd:cd05931 341 avavaadDPAARELVSCGRPLPDQEVRIVDPEtgrelpDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLR 420
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 19705503 545 TGDMGRLDDdGFLYITGRLKELIITAgGENVPPVPIEEAVK 585
Cdd:cd05931 421 TGDLGFLHD-GELYITGRLKDLIIVR-GRNHYPQDIEATAE 459
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
131-598 |
2.09e-34 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 138.19 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 131 SYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTG---IYTtsSPEAC-QYIAhdCRANVIV 206
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTanpFYT--PAEIAkQAKA--SGAKLII 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 207 vdTQKQ-LEKIlkiwKDLPHLKAVVIYQ-EPPPKKMAnvytmeELIELGQEVPEEALDAIIDtqqPNQCCVLVYTSGTTG 284
Cdd:PLN02246 128 --TQSCyVDKL----KGLAEDDGVTVVTiDDPPEGCL------HFSELTQADENELPEVEIS---PDDVVALPYSSGTTG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 285 NPKGVMLSQDN-ITWTArygsqagdiqpaevQQ-------------EVVVSYLPLSHIAAQIYDLWTGIQWGAqvcfadp 350
Cdd:PLN02246 193 LPKGVMLTHKGlVTSVA--------------QQvdgenpnlyfhsdDVILCVLPMFHIYSLNSVLLCGLRVGA------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 351 dalkgTLVntlreveptshmgvprvwekIMERIqEVAAQSGFIRRKMLLWAMSVtleqnltcPSNDLKPFTSRLADYLVL 430
Cdd:PLN02246 252 -----AIL--------------------IMPKF-EIGALLELIQRHKVTIAPFV--------PPIVLAIAKSPVVEKYDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 431 ARVRQALGfakcqknfyGAAPMTAETQRFFLGL--NIRLYAGYGLSEStGP------HFMSSPYNYRLYSSGRVVPGCRV 502
Cdd:PLN02246 298 SSIRMVLS---------GAAPLGKELEDAFRAKlpNAVLGQGYGMTEA-GPvlamclAFAKEPFPVKSGSCGTVVRNAEL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 503 KLVNQDAdGI-------GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGEnV 575
Cdd:PLN02246 368 KIVDPET-GAslprnqpGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQ-V 445
|
490 500
....*....|....*....|...
gi 19705503 576 PPVPIeEAVKMELPIISSAMLIG 598
Cdd:PLN02246 446 APAEL-EALLISHPSIADAAVVP 467
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
128-598 |
3.41e-34 |
|
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: 137.38 E-value: 3.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSP---EWFFSAVGtvfAGGIVTGIYTTSSPEACQYIAHDCRANV 204
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHrhlELYYAVPG---MGAVLHTINPRLFPEQIAYIINHAEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 205 IVVDtqKQLEKILKIWKD-LPHLKAVVIYQ---EPPPKKMANVYTMEELIElgQEVPEEALDAIidtqQPNQCCVLVYTS 280
Cdd:cd12119 101 VFVD--RDFLPLLEAIAPrLPTVEHVVVMTddaAMPEPAGVGVLAYEELLA--AESPEYDWPDF----DENTAAAICYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 281 GTTGNPKGVMLSQDNITWTARYGSQAGDIqpAEVQQEVVVSYLPLSHIAAqiydlW----TGIQWGAQVCFADPDALKGT 356
Cdd:cd12119 173 GTTGNPKGVVYSHRSLVLHAMAALLTDGL--GLSESDVVLPVVPMFHVNA-----WglpyAAAMVGAKLVLPGPYLDPAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 357 LVNTLREVEPTSHMGVPRVWEkimeriqevaaqsgfirrkMLLwamsvtleQNLTCPSNDLKPftsrladylvLARVrqA 436
Cdd:cd12119 246 LAELIEREGVTFAAGVPTVWQ-------------------GLL--------DHLEANGRDLSS----------LRRV--V 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 437 LGfakcqknfyGAAP----MTAetqrfFLGLNIRLYAGYGLSE-------STGPHFMS-----SPYNYRLySSGRVVPGC 500
Cdd:cd12119 287 IG---------GSAVprslIEA-----FEERGVRVIHAWGMTEtsplgtvARPPSEHSnlsedEQLALRA-KQGRPVPGV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 501 RVKLVNQD-----ADG--IGEICLWGRTIFMGYLNMEDKThEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGE 573
Cdd:cd12119 352 ELRIVDDDgrelpWDGkaVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKDV-IKSGGE 429
|
490 500
....*....|....*....|....*
gi 19705503 574 NVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:cd12119 430 WISSVELENAI-MAHPAVAEAAVIG 453
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
130-598 |
6.33e-34 |
|
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: 136.29 E-value: 6.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 130 ISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDT 209
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 210 QKqlekilkiwkDLPHLKAVVIYQePPPKKMANVYTMEELI----ELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGN 285
Cdd:cd05926 95 GE----------LGPASRAASKLG-LAILELALDVGVLIRApsaeSLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 286 PKGVMLSQDNITWTARYGSQAGDIQPAEvqQEVVVsyLPLSHIAAQIYDLWTGIQWGAQVCFadPDALKGTLV-NTLREV 364
Cdd:cd05926 164 PKGVPLTHRNLAASATNITNTYKLTPDD--RTLVV--MPLFHVHGLVASLLSTLAAGGSVVL--PPRFSASTFwPDVRDY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 365 EPTSHMGVPRVWEKIMERIQE----VAAQSGFIRrkmllwamsvtleqnlTCpSNDLKPFTsrladylvlarvrqalgFA 440
Cdd:cd05926 238 NATWYTAVPTIHQILLNRPEPnpesPPPKLRFIR----------------SC-SASLPPAV-----------------LE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 441 KCQKNFygAAPMtaetqrfflglnirlYAGYGLSESTgpHFMSS----PYNYRLYSSGRVVpGCRVKLVNQDAD-----G 511
Cdd:cd05926 284 ALEATF--GAPV---------------LEAYGMTEAA--HQMTSnplpPGPRKPGSVGKPV-GVEVRILDEDGEilppgV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 512 IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPII 591
Cdd:cd05926 344 VGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINR-GGEKISPLEVDG-VLLSHPAV 421
|
....*..
gi 19705503 592 SSAMLIG 598
Cdd:cd05926 422 LEAVAFG 428
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
127-718 |
6.95e-34 |
|
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: 137.18 E-value: 6.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 127 WERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG---GIVTGIYTTSSPE--ACQYIAHDCR 201
Cdd:cd05921 23 WRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGvpaAPVSPAYSLMSQDlaKLKHLFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 202 ANVIVVDTQKQLEKILKIwKDLPHLKAVVIYQEPPPKkmaNVYTMEELIElgqEVPEEALDAIIDTQQPNQCCVLVYTSG 281
Cdd:cd05921 103 PGLVFAQDAAPFARALAA-IFPLGTPLVVSRNAVAGR---GAISFAELAA---TPPTAAVDAAFAAVGPDTVAKFLFTSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 282 TTGNPKGVMLSQDNITwtaryGSQAGDIQPAEVQQE---VVVSYLPLSHIAAQIYD----LWTG----IQWGAQVcfadP 350
Cdd:cd05921 176 STGLPKAVINTQRMLC-----ANQAMLEQTYPFFGEeppVLVDWLPWNHTFGGNHNfnlvLYNGgtlyIDDGKPM----P 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 351 DALKGTLVNtLREVEPTSHMGVPRVWEKI---MERiQEVAAQSGFIRRKMLLWAmSVTLEQNltcpsndlkpftsrlady 427
Cdd:cd05921 247 GGFEETLRN-LREISPTVYFNVPAGWEMLvaaLEK-DEALRRRFFKRLKLMFYA-GAGLSQD------------------ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 428 lVLARVrQALGFAKCqknfygaapmtaetqrfflGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVnq 507
Cdd:cd05921 306 -VWDRL-QALAVATV-------------------GERIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 508 DADGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDD-----GfLYITGRLKELIITAGGENVPPVPIE- 581
Cdd:cd05921 363 PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADPddpakG-LVFDGRVAEDFKLASGTWVSVGPLRa 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 582 EAVKMELPIISSAMLIGDQRKFLSMLLTLkctlnpetseptdNLTEqavefCQR-VGSKASTVSEIVgqKDEAVYQAIHE 660
Cdd:cd05921 442 RAVAACAPLVHDAVVAGEDRAEVGALVFP-------------DLLA-----CRRlVGLQEASDAEVL--RHAKVRAAFRD 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 19705503 661 GIQRVNANAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKDIIDSFYQE 718
Cdd:cd05921 502 RLAALNGEATGSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
105-602 |
8.43e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 137.05 E-value: 8.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 105 MFYEALDKYGNLSALGFKRKdkweRISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEwffsAVGTVFA----GGI 180
Cdd:PRK05605 37 LYDNAVARFGDRPALDFFGA----TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQ----HIVAFYAvlrlGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 181 VT---GIYTTSSPEAcQYIAHDCRAnVIVVDtqKQLEKILKIWKDLPhLKAVV----IYQEPPPKKMA------NVYTME 247
Cdd:PRK05605 109 VVehnPLYTAHELEH-PFEDHGARV-AIVWD--KVAPTVERLRRTTP-LETIVsvnmIAAMPLLQRLAlrlpipALRKAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 248 EliELGQEVP-----EEALDA-------IIDTQQPNQCCV--LVYTSGTTGNPKGVMLSQDNITWTARYGsQA-----GD 308
Cdd:PRK05605 184 A--ALTGPAPgtvpwETLVDAaiggdgsDVSHPRPTPDDValILYTSGTTGKPKGAQLTHRNLFANAAQG-KAwvpglGD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 309 iqpaevQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCFADPDAlkGTLVNTLREVEPTSHMGVPRVWEKIMEriqevA 387
Cdd:PRK05605 261 ------GPERVLAALPMFHAYGLTLCLTLAVSIGGElVLLPAPDI--DLILDAMKKHPPTWLPGVPPLYEKIAE-----A 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 388 AQsgfirrkmllwamsvtlEQNLTcpsndlkpftsrladylvLARVRQAlgfakcqknFYGAAPMTAETQRFFLGL-NIR 466
Cdd:PRK05605 328 AE-----------------ERGVD------------------LSGVRNA---------FSGAMALPVSTVELWEKLtGGL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 467 LYAGYGLSEsTGPHFMSSPYN--YRLYSSGRVVPGCRVKLVNQD------ADG-IGEICLWGRTIFMGYLNMEDKTHEAI 537
Cdd:PRK05605 364 LVEGYGLTE-TSPIIVGNPMSddRRPGYVGVPFPDTEVRIVDPEdpdetmPDGeEGELLVRGPQVFKGYWNRPEETAKSF 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19705503 538 dSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISSAMLIGDQRK 602
Cdd:PRK05605 443 -LDGWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEEVLR-EHPGVEDAAVVGLPRE 504
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
107-633 |
4.94e-33 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 134.47 E-value: 4.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 107 YEALDKYgnlsALGfkRKDK----WE-------RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTV 175
Cdd:COG0365 12 YNCLDRH----AEG--RGDKvaliWEgedgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 176 FAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD--------TQKQLEKILKIWKDLPHLKAVVIYQEP-PPKKMANVYTM 246
Cdd:COG0365 86 RIGAVHSPVFPGFGAEALADRIEDAEAKVLITAdgglrggkVIDLKEKVDEALEELPSLEHVIVVGRTgADVPMEGDLDW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 247 EELIEL-GQEVPEEALDAiidtqqpNQCCVLVYTSGTTGNPKGVMLSQD----NITWTARYGSqagDIQPaevqQEVV-- 319
Cdd:COG0365 166 DELLAAaSAEFEPEPTDA-------DDPLFILYTSGTTGKPKGVVHTHGgylvHAATTAKYVL---DLKP----GDVFwc 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 320 ---------VSYL---PLSHIAAQ-IYDlwtgiqwGAQVcFADPDAlkgtLVNTLREVEPTSHMGVPRVWEKIMERIQEV 386
Cdd:COG0365 232 tadigwatgHSYIvygPLLNGATVvLYE-------GRPD-FPDPGR----LWELIEKYGVTVFFTAPTAIRALMKAGDEP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 387 AAQSgfirrkmllwamsvtleqnltcpsnDLkpftSRLadylvlarvrQALGFAkcqknfygAAPMTAETQRFFL-GLNI 465
Cdd:COG0365 300 LKKY-------------------------DL----SSL----------RLLGSA--------GEPLNPEVWEWWYeAVGV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 466 RLYAGYGLSEsTGPHFMSSPYNYRLY--SSGRVVPGCRVKLVnqDADG-------IGEICL---W-GrtIFMGYLNMEDK 532
Cdd:COG0365 333 PIVDGWGQTE-TGGIFISNLPGLPVKpgSMGKPVPGYDVAVV--DEDGnpvppgeEGELVIkgpWpG--MFRGYWNDPER 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 533 THEAI--DSEGWLHTGDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISSAMLIG--DQRKFLSMLL 608
Cdd:COG0365 408 YRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESAL-VSHPAVAEAAVVGvpDEIRGQVVKA 485
|
570 580
....*....|....*....|....*
gi 19705503 609 TlkCTLNPETsEPTDNLTEQAVEFC 633
Cdd:COG0365 486 F--VVLKPGV-EPSDELAKELQAHV 507
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
125-634 |
9.66e-33 |
|
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: 132.88 E-value: 9.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 125 DKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANV 204
Cdd:cd05959 25 DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 205 IVVDTQ--KQLEKILKiwKDLPHLKAVVIYQEPPPKKMANVYTmeelielgQEVPEEALDAIIDTQQPNQCCVLVYTSGT 282
Cdd:cd05959 105 VVVSGElaPVLAAALT--KSEHTLVVLIVSGGAGPEAGALLLA--------ELVAAEAEQLKPAATHADDPAFWLYSSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 283 TGNPKGVMLSQDNITWTAR-YGSQAGDIQPAevqqEVVVSYLPLSHI----AAQIYDLWTGiqwGAQVCFAD---PDAlk 354
Cdd:cd05959 175 TGRPKGVVHLHADIYWTAElYARNVLGIRED----DVCFSAAKLFFAyglgNSLTFPLSVG---ATTVLMPErptPAA-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 355 gtLVNTLREVEPTSHMGVPRVWekimeriqevAAqsgfirrkMLlwamsvtleQNLTCPSNDLKpftsrladylvlaRVR 434
Cdd:cd05959 246 --VFKRIRRYRPTVFFGVPTLY----------AA--------ML---------AAPNLPSRDLS-------------SLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 435 QALGfakcqknfyGAAPMTAE-----TQRFflGLNIrlYAGYGLSESTgpH-FMSS-PYNYRLYSSGRVVPGCRVKLVNQ 507
Cdd:cd05959 284 LCVS---------AGEALPAEvgerwKARF--GLDI--LDGIGSTEML--HiFLSNrPGRVRYGTTGKPVPGYEVELRDE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 508 D----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDSEgWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIEE 582
Cdd:cd05959 349 DggdvADGePGELYVRGPSSATMYWNNRDKTRDTFQGE-WTRTGDKYVRDDDGFYTYAGRADDM-LKVSGIWVSPFEVES 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 19705503 583 AVkMELPIISSAMLIG---DQRkflsmLLTLKC--TLNPETsEPTDNLTEQAVEFCQ 634
Cdd:cd05959 427 AL-VQHPAVLEAAVVGvedEDG-----LTKPKAfvVLRPGY-EDSEALEEELKEFVK 476
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
128-598 |
1.59e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 132.36 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 207
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DTQ--KQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVytmeelIELGQEVPEEALDAIIDTQQPNQccvLVYTSGTTGN 285
Cdd:PRK08316 115 DPAlaPTAEAALALLPVDTLILSLVLGGREAPGGWLDF------ADWAEAGSVAEPDVELADDDLAQ---ILYTSGTESL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 286 PKGVMLSQDNITWtaRYGSQ--AGDIQPAEVQqevvVSYLPLSHiAAQIY-----DLWTGiqwGAQVCFADPDAlkGTLV 358
Cdd:PRK08316 186 PKGAMLTHRALIA--EYVSCivAGDMSADDIP----LHALPLYH-CAQLDvflgpYLYVG---ATNVILDAPDP--ELIL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 359 NTLREVEPTSHMGVPRVWekimeriqevaaqsgfirrkmllwamsVTLeqnLTCPSNDlkpfTSRLadylvlarvrQALg 438
Cdd:PRK08316 254 RTIEAERITSFFAPPTVW---------------------------ISL---LRHPDFD----TRDL----------SSL- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 439 fakcQKNFYGAAPMTAE-----TQRFflgLNIRLYAGYGLSEsTGP-HFMSSPYNY--RLYSSGRVVPGCRVKLVNQD-- 508
Cdd:PRK08316 289 ----RKGYYGASIMPVEvlkelRERL---PGLRFYNCYGQTE-IAPlATVLGPEEHlrRPGSAGRPVLNVETRVVDDDgn 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 509 --ADG-IGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVk 585
Cdd:PRK08316 361 dvAPGeVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKT-GGENVASREVEEAL- 437
|
490
....*....|...
gi 19705503 586 MELPIISSAMLIG 598
Cdd:PRK08316 438 YTHPAVAEVAVIG 450
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
270-598 |
3.79e-31 |
|
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: 125.08 E-value: 3.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 270 PNQCCVLVYTSGTTGNPKGVMLSQDNITWTARY-GSQAGDiqpaeVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFA 348
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFiGERLGL-----TEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 349 DP--DALKgtlvnTLREVEP---TSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnlTCPSNdlkpftsr 423
Cdd:cd05917 76 SPsfDPLA-----VLEAIEKekcTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGA---------PCPPE-------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 424 ladylVLARVRQALGFAKCQknfygaapmtaetqrfflglnirlyAGYGLSESTGPHFMSS---PYNYRLYSSGRVVPGC 500
Cdd:cd05917 134 -----LMKRVIEVMNMKDVT-------------------------IAYGMTETSPVSTQTRtddSIEKRVNTVGRIMPHT 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 501 RVKLVNQDADGI------GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGEN 574
Cdd:cd05917 184 EAKIVDPEGGIVppvgvpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGEN 262
|
330 340
....*....|....*....|....
gi 19705503 575 VPPVPIEEAVkMELPIISSAMLIG 598
Cdd:cd05917 263 IYPREIEEFL-HTHPKVSDVQVVG 285
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
129-601 |
1.49e-30 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 125.19 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQYYLIARKVAKGFLKLGLERAHSVAilgFNSPEWFFSAV---GTVFAGGIVTGIYTTSSPEACQYIAHDCRANVI 205
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVA---FQLPNWWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 206 VVDTqkqlekilkiwkdlphlkavviyqepppkkmanvytmeeliELGQEVPEealdaiidtQQPNQCCVLVYTSGTTGN 285
Cdd:cd05903 78 VVPE-----------------------------------------RFRQFDPA---------AMPDAVALLLFTSGTTGE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 286 PKGVMLSQDNITWTARYGSQAGDIQPAEVQqeVVVSylPLSHIAAQIYDLWTGIqwgaqvcfadpdaLKGTLVNTLREVE 365
Cdd:cd05903 108 PKGVMHSHNTLSASIRQYAERLGLGPGDVF--LVAS--PMAHQTGFVYGFTLPL-------------LLGAPVVLQDIWD 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 366 PTshmgvprvwekimeriqevaaqsgfirrkmllWAMSVTLEQNLTCpSNDLKPFtsrLADylvLARVRQALGFAKCQKN 445
Cdd:cd05903 171 PD--------------------------------KALALMREHGVTF-MMGATPF---LTD---LLNAVEEAGEPLSRLR 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 446 FYGAAPMT---AETQRFFLGLNIRLYAGYGLSEStgPHFMSS----PYNYRLYSSGRVVPGCRVKLVnqDADG------- 511
Cdd:cd05903 212 TFVCGGATvprSLARRAAELLGAKVCSAYGSTEC--PGAVTSitpaPEDRRLYTDGRPLPGVEIKVV--DDTGatlapgv 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 512 IGEICLWGRTIFMGYLNMEDKTHEAiDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPII 591
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVEDLL-LGHPGV 364
|
490
....*....|..
gi 19705503 592 SSAMLIG--DQR 601
Cdd:cd05903 365 IEAAVVAlpDER 376
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
274-583 |
1.61e-30 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 122.82 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 274 CVLVYTSGTTGNPKGVMLSQDNITWTARygsQAGDIQPAEVQQEVVVSyLPLSHIAAQiYDLWTGIQWGAQVCFADPDAL 353
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAA---GLHSRLGFGGGDSWLLS-LPLYHVGGL-AILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 354 kgtLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFirRKMLLwamsvtleqnltcpsndlkpftsrladylvlarv 433
Cdd:cd17630 78 ---LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSL--RAVLL---------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 434 rqalgfakcqknfyGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQdadgiG 513
Cdd:cd17630 119 --------------GGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----G 179
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 514 EICLWGRTIFMGYLNMEdkTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEA 583
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAA 246
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
274-598 |
2.82e-30 |
|
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: 124.32 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 274 CVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEVQQEVvvsyLPLSHIAAQIYDLWTGIQWGAQVCF-ADPDA 352
Cdd:cd05941 92 ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHV----LPLHHVHGLVNALLCPLFAGASVEFlPKFDP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 353 lkgTLVNTLREVEP-TSHMGVPRVWEKIMERIQEVAAQSGFIRRKmllwamsvtleqnltCPSNdLKPFTSrladylvla 431
Cdd:cd05941 168 ---KEVAISRLMPSiTVFMGVPTIYTRLLQYYEAHFTDPQFARAA---------------AAER-LRLMVS--------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 432 rvrqalgfakcqknfyGAAPMTAETQRFFLGLN-IRLYAGYGLSEsTGphfM--SSPYN--YRLYSSGRVVPGCRVKLVN 506
Cdd:cd05941 220 ----------------GSAALPVPTLEEWEAITgHTLLERYGMTE-IG---MalSNPLDgeRRPGTVGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 507 Q------DADGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPI 580
Cdd:cd05941 280 EetgeplPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEI 359
|
330
....*....|....*...
gi 19705503 581 EEAVkMELPIISSAMLIG 598
Cdd:cd05941 360 ERVL-LAHPGVSECAVIG 376
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
101-598 |
4.24e-30 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 125.18 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 101 TVHQMFYEALDKYGNLSALGFK-RKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGG 179
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALIFEsSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 180 IVTGIYTTSSPEACQYIAHDCRANVIVVDtqkqlEKILKIWKDLPH-----LKAVVIYQEPPPKkMANVYTMEEL----- 249
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTS-----AQFYPMYRQIQQedatpLRHICLTRVALPA-DDGVSSFTQLkaqqp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 250 IELGQEVPEEALD-AIIdtqqpnqccvlVYTSGTTGNPKGVMLSQDNITWTARYGSQagdiQPAEVQQEVVVSYLPLSHI 328
Cdd:PRK08008 162 ATLCYAPPLSTDDtAEI-----------LFTSGTTSRPKGVVITHYNLRFAGYYSAW----QCALRDDDVYLTVMPAFHI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 329 AAQiydlwtgiqwgaqvCFADPDALkgTLVNTLREVEPTShmgVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQ 408
Cdd:PRK08008 227 DCQ--------------CTAAMAAF--SAGATFVLLEKYS---ARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 409 NltcpsndlkpftsrladylvlaRVRQALgfakcqknFYgAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNY 488
Cdd:PRK08008 288 H----------------------CLREVM--------FY-LNLSDQEKDAFEERFGVRLLTSYGMTETIVGIIGDRPGDK 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 489 RLYSS-GRVVPGCRVKLVNQD-----ADGIGEICLWG---RTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYI 559
Cdd:PRK08008 337 RRWPSiGRPGFCYEAEIRDDHnrplpAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYF 416
|
490 500 510
....*....|....*....|....*....|....*....
gi 19705503 560 TGRlKELIITAGGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:PRK08008 417 VDR-RCNMIKRGGENVSCVELENII-ATHPKIQDIVVVG 453
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
91-598 |
4.62e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 125.53 E-value: 4.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 91 LEPFCTQLPYTV-------HQMFYEALDKYGNLSALGFKRKDkwerISYYQYYLIARKVAKGFLKLGLERAHSVAILGFN 163
Cdd:PRK06710 8 LKSYPEEIPSTIsydiqplHKYVEQMASRYPEKKALHFLGKD----ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 164 SPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV-----------VDTQKQLEKIL--KIWKDLPHLKAVv 230
Cdd:PRK06710 84 CPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnVQSATKIEHVIvtRIADFLPFPKNL- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 231 IYQEPPPKKMANVYTMEE--LIELGQEVPEE---ALDAIIDTQqpNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQ 305
Cdd:PRK06710 163 LYPFVQKKQSNLVVKVSEseTIHLWNSVEKEvntGVEVPCDPE--NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 306 AgdIQPAEVQQEVVVSYLPLSHIAAQiydlwtgiqwgaqvcfadpdalkgTLVNTLREVEPTSHMGVPRVWEK-IMERIQ 384
Cdd:PRK06710 241 W--LYNCKEGEEVVLGVLPFFHVYGM------------------------TAVMNLSIMQGYKMVLIPKFDMKmVFEAIK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 385 evaaqsgfiRRKMLLWAMSVTLEQNLtcpsndlkpFTSRLADYLVLARVRQALGfakcqknfyGAAPMTAETQRFFLGLN 464
Cdd:PRK06710 295 ---------KHKVTLFPGAPTIYIAL---------LNSPLLKEYDISSIRACIS---------GSAPLPVEVQEKFETVT 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 465 I-RLYAGYGLSEStgphfmsSPYNYRLYSSGRVVPGcRVKLVNQDADG---------------IGEICLWGRTIFMGYLN 528
Cdd:PRK06710 348 GgKLVEGYGLTES-------SPVTHSNFLWEKRVPG-SIGVPWPDTEAmimsletgealppgeIGEIVVKGPQIMKGYWN 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 529 MEDKThEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIItAGGENVPPVPIEEaVKMELPIISSAMLIG 598
Cdd:PRK06710 420 KPEET-AAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIV-ASGFNVYPREVEE-VLYEHEKVQEVVTIG 486
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
128-598 |
4.77e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 124.61 E-value: 4.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 207
Cdd:PRK06145 26 QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DtqKQLEKILKiwkdLPHLKAVViyqepppkKMANVYTMEELIELGQEVPEEALDAiidtqqPNQCCVLVYTSGTTGNPK 287
Cdd:PRK06145 106 D--EEFDAIVA----LETPKIVI--------DAAAQADSRRLAQGGLEIPPQAAVA------PTDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 288 GVMLSQDNITW-----TARYGSQAGDiqpaevqQEVVVSylPLSHIAAqiYDLwTGIQWGAQvcfadpdalkGTLVNTLR 362
Cdd:PRK06145 166 GVMHSYGNLHWksidhVIALGLTASE-------RLLVVG--PLYHVGA--FDL-PGIAVLWV----------GGTLRIHR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 363 EVEPtshmgvprvwEKIMERIQEvaaqsgfiRRKMLLWAMSVTLEQNLTCPSNDlkpftsrladylvlarvRQALG-FAK 441
Cdd:PRK06145 224 EFDP----------EAVLAAIER--------HRLTCAWMAPVMLSRVLTVPDRD-----------------RFDLDsLAW 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 442 CqknfYGAAPMTAETQ-RFFLGL--NIRLYAGYGLSES-TGPHFMSSPYNY-RLYSSGRVVPGCRVKLVNQDADGI---- 512
Cdd:PRK06145 269 C----IGGGEKTPESRiRDFTRVftRARYIDAYGLTETcSGDTLMEAGREIeKIGSTGRALAHVEIRIADGAGRWLppnm 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 513 -GEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPII 591
Cdd:PRK06145 345 kGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEVERVI-YELPEV 421
|
....*..
gi 19705503 592 SSAMLIG 598
Cdd:PRK06145 422 AEAAVIG 428
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
128-591 |
7.45e-30 |
|
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: 124.70 E-value: 7.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLeRAHSVAILGFNSPEWFFSAV-GTVFAGGI-----VTGIYTTSSPEacqyIAHDCR 201
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLGL-RPGDSVILQFDDNEDFIPAFwACVLAGFVpapltVPPTYDEPNAR----LRKLRH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 202 A-----NVIVVDTQKQLEKILKIWKDLPHLKAVVIyqepppkkmanvytmeelielgqeVPEEALDAIIDT----QQPNQ 272
Cdd:cd05906 113 IwqllgSPVVLTDAELVAEFAGLETLSGLPGIRVL------------------------SIEELLDTAADHdlpqSRPDD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 273 CCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAA----QIYDLWTGIQwgaQVcfa 348
Cdd:cd05906 169 LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTP----QDVFLNWVPLDHVGGlvelHLRAVYLGCQ---QV--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 349 dpdalkgtlvNTlrevePTSHM-GVPRVWEKIMERIQevAAQSgfirrkmllWAMSVTLeqNLTCpsNDLKPFTSRLADy 427
Cdd:cd05906 239 ----------HV-----PTEEIlADPLRWLDLIDRYR--VTIT---------WAPNFAF--ALLN--DLLEEIEDGTWD- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 428 lvLARVRQALGfakcqknfyGAAPMTAETQRFFL------GLNIR-LYAGYGLSES-TGPHFMSSPYNY------RLYSS 493
Cdd:cd05906 288 --LSSLRYLVN---------AGEAVVAKTIRRLLrllepyGLPPDaIRPAFGMTETcSGVIYSRSFPTYdhsqalEFVSL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 494 GRVVPGCRVKLVNQDADG-----IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLdDDGFLYITGRLKELII 568
Cdd:cd05906 357 GRPIPGVSMRIVDDEGQLlpegeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFL-DNGNLTITGRTKDTII 435
|
490 500
....*....|....*....|...
gi 19705503 569 TaGGENVPPVPIEEAVKmELPII 591
Cdd:cd05906 436 V-NGVNYYSHEIEAAVE-EVPGV 456
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
63-693 |
7.90e-30 |
|
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: 125.26 E-value: 7.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 63 PEKARAASLDASEEALwttradGRVRLRLepfcTQLPYTVhqmfyeaLDKYGNLSALGFKRKDK--------------WE 128
Cdd:cd17632 2 PQFAAAAPLEAVTEAI------RRPGLRL----AQIIATV-------MTGYADRPALGQRATELvtdpatgrttlrllPR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 R--ISYYQYYLIARKVAKGF-LKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVI 205
Cdd:cd17632 65 FetITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 206 VVDTQkQLEKILKIWKDLPHLKAVVIY----------------QEPPPKKMANVYTMEELIELGQEVPEEALDAIIDTQQ 269
Cdd:cd17632 145 AVSAE-HLDLAVEAVLEGGTPPRLVVFdhrpevdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 270 PnqCCVLVYTSGTTGNPKGVMLSQDNIT--WTARYGSQAGDIQPAevqqeVVVSYLPLSHIAAQIYdLWTGIQWGAQVCF 347
Cdd:cd17632 224 P--LALLIYTSGSTGTPKGAMYTERLVAtfWLKVSSIQDIRPPAS-----ITLNFMPMSHIAGRIS-LYGTLARGGTAYF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 348 ADPDALKgTLVNTLREVEPTSHMGVPRVWEKIMERIQEVaaqsgfIRRKMLLWAMSVTLEQNltcpsndlkpftsrlady 427
Cdd:cd17632 296 AAASDMS-TLFDDLALVRPTELFLVPRVCDMLFQRYQAE------LDRRSVAGADAETLAER------------------ 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 428 lVLARVRQALGFAKCQKNFYGAAPMTAETQRFFLG-LNIRLYAGYGLSESTGphfmsspynyrLYSSGRVV--PGCRVKL 504
Cdd:cd17632 351 -VKAELRERVLGGRLLAAVCGSAPLSAEMKAFMESlLDLDLHDGYGSTEAGA-----------VILDGVIVrpPVLDYKL 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 505 VNQDADGI---------GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGD-MGRLDDDGFLYITgRLKELIITAGGEN 574
Cdd:cd17632 419 VDVPELGYfrtdrphprGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDvMAELGPDRLVYVD-RRNNVLKLSQGEF 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 575 VpPVPIEEAVKMELPIISSAMLIGD-QRKFLSMLLTlkctlnpetsePTDNlteqavefcqrvgskastvsEIVGQKDEA 653
Cdd:cd17632 498 V-TVARLEAVFAASPLVRQIFVYGNsERAYLLAVVV-----------PTQD--------------------ALAGEDTAR 545
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 19705503 654 VYQAIHEGIQRVNANAAARPYHIQKWAILERD-FSISGGEL 693
Cdd:cd17632 546 LRAALAESLQRIAREAGLQSYEIPRDFLIETEpFTIANGLL 586
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
272-600 |
1.28e-29 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 122.56 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 272 QCCVLVYTSGTTGNPKGVMlsqdnITWTARYGSQAGDIQP-AEVQQEVVVSYLPLSHIAAQIYdLWTGIQWGAQVCFADP 350
Cdd:TIGR01923 112 QIATLMFTSGTTGKPKAVP-----HTFRNHYASAVGSKENlGFTEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 351 DALKGTLVNTlrevEPTSHMG-VPrvwekimeriqevaaqsgfirrKMLLWamsvTLEQNLTCPSndlkpftsrladylv 429
Cdd:TIGR01923 186 FNQLLEMIAN----ERVTHISlVP----------------------TQLNR----LLDEGGHNEN--------------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 430 LARVRqaLGFAKCqknfygAAPMTAETQRfflgLNIRLYAGYGLSESTGPHFMSSP--YNYRLySSGRVVPGCRVKLVNQ 507
Cdd:TIGR01923 221 LRKIL--LGGSAI------PAPLIEEAQQ----YGLPIYLSYGMTETCSQVTTATPemLHARP-DVGRPLAGREIKIKVD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 508 DADGIGEICLWGRTIFMGYLNMEDKThEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKmE 587
Cdd:TIGR01923 288 NKEGHGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIIS-GGENIYPEEIETVLY-Q 364
|
330
....*....|...
gi 19705503 588 LPIISSAMLIGDQ 600
Cdd:TIGR01923 365 HPGIQEAVVVPKP 377
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
139-601 |
2.85e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 122.93 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 139 ARKVAKGFLKLGLERAHSVAilgFNSPEWF-FSAV--GTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQ-KQ-- 212
Cdd:PRK06087 59 ASRLANWLLAKGIEPGDRVA---FQLPGWCeFTIIylACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLfKQtr 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 213 -LEKILKIWKDLPHLKAVVIYQEPPPKkmANVYTMEELIELGqevpeEALDAIIDTQQPNQCCVLvYTSGTTGNPKGVML 291
Cdd:PRK06087 136 pVDLILPLQNQLPQLQQIVGVDKLAPA--TSSLSLSQIIADY-----EPLTTAITTHGDELAAVL-FTSGTEGLPKGVML 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 292 SQDNITWTARYGSQAGDIqpaeVQQEVVVSYLPLSHIaaqiydlwTGIQWGaqvcFADPDALKGTLVntlreveptshmg 371
Cdd:PRK06087 208 THNNILASERAYCARLNL----TWQDVFMMPAPLGHA--------TGFLHG----VTAPFLIGARSV------------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 372 vprvwekiMERIQEVAAQSGFIRRKMLLWAMSVTleqnltcpsndlkPFTsrladYLVLARVRQ------ALGFAKCqkn 445
Cdd:PRK06087 259 --------LLDIFTPDACLALLEQQRCTCMLGAT-------------PFI-----YDLLNLLEKqpadlsALRFFLC--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 446 fyGAAPMTAETQRFFLGLNIRLYAGYGLSESTgPHFM---SSPYNYRLYSSGRVVPGCRVKLVNQDADGI-----GEICL 517
Cdd:PRK06087 310 --GGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVvnlDDPLSRFMHTDGYAAAGVEIKVVDEARKTLppgceGEEAS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 518 WGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLI 597
Cdd:PRK06087 387 RGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVR-GGENISSREVEDIL-LQHPKIHDACVV 464
|
....*.
gi 19705503 598 G--DQR 601
Cdd:PRK06087 465 AmpDER 470
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
129-584 |
3.32e-29 |
|
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: 122.02 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 208
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 209 TQKQLEKILKIWKDlphlkavviyqEPPPkkmanvytmeelielgqEVPEEALDAIidtqqpnqccVLVYTSGTTGNPKG 288
Cdd:cd12118 109 REFEYEDLLAEGDP-----------DFEW-----------------IPPADEWDPI----------ALNYTSGTTGRPKG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 289 VMLSQDNItwtarYGSQAGDIQPAEVQQEVVvsYL---PLSHIAAqiydlWTGIqWGaqvcfadPDALKGTLVnTLREVE 365
Cdd:cd12118 151 VVYHHRGA-----YLNALANILEWEMKQHPV--YLwtlPMFHCNG-----WCFP-WT-------VAAVGGTNV-CLRKVD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 366 PtshmgvPRVWEKI-MERIQEVAAqsgfirrkmllwamSVTLEQNLT-CPSNDLKPFTsrladylvlARVRQALGfakcq 443
Cdd:cd12118 210 A------KAIYDLIeKHKVTHFCG--------------APTVLNMLAnAPPSDARPLP---------HRVHVMTA----- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 444 knfyGAAP---MTAETQRfflgLNIRLYAGYGLSESTGPHF----------MSSPYNYRLYS-SG---------RVVPGC 500
Cdd:cd12118 256 ----GAPPpaaVLAKMEE----LGFDVTHVYGLTETYGPATvcawkpewdeLPTEERARLKArQGvryvgleevDVLDPE 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 501 RVKLVNQDADGIGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPI 580
Cdd:cd12118 328 TMKPVPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVEV 405
|
....
gi 19705503 581 EEAV 584
Cdd:cd12118 406 EGVL 409
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
275-633 |
5.32e-29 |
|
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: 118.53 E-value: 5.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 275 VLVYTSGTTGNPKGVMLSQDNITwtarygsqAGDIQPAEV----QQEVVVSYLPLSHIAaqiydlwtgiqwGAQVCFAdp 350
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLI--------AANLQLIHAmgltEADVYLNMLPLFHIA------------GLNLALA-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 351 dalkgtlvntlrevepTSHMGVPRVwekIMERIQEVAAQSGFIRRKMLLWAmsvtleqnltcpsnDLKPFTSRLADYLV- 429
Cdd:cd17637 62 ----------------TFHAGGANV---VMEKFDPAEALELIEEEKVTLMG--------------SFPPILSNLLDAAEk 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 430 ----LARVRQALGFAkcqknfygaAPMTAetQRFFLGLNIRLYAGYGLSESTGPHFMSsPYNYRLYSSGRVVPGCRVKLV 505
Cdd:cd17637 109 sgvdLSSLRHVLGLD---------APETI--QRFEETTGATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 506 NQD-----ADGIGEICLWGRTIFMGYLNMEDKTHEAIDsEGWLHTGDMGRLDDDGFLYITGRL--KELIITaGGENVPPV 578
Cdd:cd17637 177 DDNdrpvpAGETGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPA 254
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 19705503 579 PIEEAVkMELPIISSAMLIGDQRKFLSMLLTLKCTLNPETSeptdnLTEQAV-EFC 633
Cdd:cd17637 255 EVEKVI-LEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGAT-----LTADELiEFV 304
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
101-598 |
9.34e-29 |
|
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: 121.04 E-value: 9.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 101 TVHQMFYEALDKYGNLSALgfkrKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGI 180
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATAL----VHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 181 VTGIYTTSSPEACQYIAHDCRANVIVVdTQKQLEKILKIWKDLPHLKAVVIYQEPPPKKM----ANVYTMEELIELGQEV 256
Cdd:TIGR03098 77 FVPINPLLKAEQVAHILADCNVRLLVT-SSERLDLLHPALPGCHDLRTLIIVGDPAHASEghpgEEPASWPKLLALGDAD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 257 PeeALDAIidtqQPNQCCVLvYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAevqqEVVVSYLPLSHIAAQiYDLW 336
Cdd:TIGR03098 156 P--PHPVI----DSDMAAIL-YTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPD----DRLLAVLPLSFDYGF-NQLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 337 TGIQWGAQVCFADPdALKGTLVNTLREVEPTSHMGVPRVWEKIME-RIQEVAAQSgfirrkmllwamsvtleqnltcpsn 415
Cdd:TIGR03098 224 TAFYVGATVVLHDY-LLPRDVLKALEKHGITGLAAVPPLWAQLAQlDWPESAAPS------------------------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 416 dLKPFTsrladylvlarvrqalgfakcqkNFYGAAP--MTAETQRFFlgLNIRLYAGYGLSEStgphFMSS---P--YNY 488
Cdd:TIGR03098 278 -LRYLT-----------------------NSGGAMPraTLSRLRSFL--PNARLFLMYGLTEA----FRSTylpPeeVDR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 489 RLYSSGRVVPGCRVKLVNQDAD-----GIGEICLWGRTIFMGYLNMEDKTHEAI------DSEGWLH-----TGDMGRLD 552
Cdd:TIGR03098 328 RPDSIGKAIPNAEVLVLREDGSecapgEEGELVHRGALVAMGYWNDPEKTAERFrplppfPGELHLPelavwSGDTVRRD 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 19705503 553 DDGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:TIGR03098 408 EEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVA-YATGLVAEAVAFG 451
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
275-598 |
1.89e-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: 118.60 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 275 VLVYTSGTTGNPKGVMLSQDNITWTARyGSQagdIQPAEVQQEVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFADP-DAL 353
Cdd:cd05912 81 TIMYTSGTTGKPKGVQQTFGNHWWSAI-GSA---LNLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKfDAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 354 KgtlVNTLREVEPTSHMGVprvwekimeriqeVAaqsgfirrKMLLWAMSVTLEqnlTCPSNdlkpftsrladylvlarV 433
Cdd:cd05912 156 Q---VLHLINSGKVTIISV-------------VP--------TMLQRLLEILGE---GYPNN-----------------L 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 434 RQAL---GFAkcqknfygAAPMTAETQRfflgLNIRLYAGYGLSEsTGPHFMSSPYNY---RLYSSGRVVPGCRVKLVN- 506
Cdd:cd05912 192 RCILlggGPA--------PKPLLEQCKE----KGIPVYQSYGMTE-TCSQIVTLSPEDalnKIGSAGKPLFPVELKIEDd 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 507 -QDADGIGEICLWGRTIFMGYLNMEDKTHEAIDSeGWLHTGDMGRLDDDGFLYITGRLKELIItAGGENVPPVPIEEAVK 585
Cdd:cd05912 259 gQPPYEVGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEVLL 336
|
330
....*....|...
gi 19705503 586 mELPIISSAMLIG 598
Cdd:cd05912 337 -SHPAIKEAGVVG 348
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
172-602 |
2.50e-27 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 116.28 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 172 VGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVvdTQKQLEKILKIWKDLPHLK-AVVIYQEpppKKMANVYTMEEL- 249
Cdd:cd05909 49 FALALSGKVPVMLNYTAGLRELRACIKLAGIKTVL--TSKQFIEKLKLHHLFDVEYdARIVYLE---DLRAKISKADKCk 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 250 IELGQEVPEEALDAI--IDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSH 327
Cdd:cd05909 124 AFLAGKFPPKWLLRIfgVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNP----EDVVFGALPFFH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 328 IAAQIYDLWTGIQWGAQVCFAdPDALKG-TLVNTLREVEPTSHMGVPRVWekimeriqevaaqSGFIRRKMllwamsvtl 406
Cdd:cd05909 200 SFGLTGCLWLPLLSGIKVVFH-PNPLDYkKIPELIYDKKATILLGTPTFL-------------RGYARAAH--------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 407 eqnltcpSNDLkpFTSRLAdylvlarvrqalgfakcqknFYGAAPMTAETQRFFLGL-NIRLYAGYGLSESTGPHFMSSP 485
Cdd:cd05909 257 -------PEDF--SSLRLV--------------------VAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISVNTP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 486 -YNYRLYSSGRVVPGCRVKLVNQDAD---GIGE---ICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLY 558
Cdd:cd05909 308 qSPNKEGTVGRPLPGMEVKIVSVETHeevPIGEgglLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLT 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 19705503 559 ITGRLKELiITAGGENVPPVPIEEAVKMELPI--ISSAMLIGDQRK 602
Cdd:cd05909 387 ITGRLSRF-AKIAGEMVSLEAIEDILSEILPEdnEVAVVSVPDGRK 431
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
128-601 |
7.63e-27 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 115.54 E-value: 7.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAilgFNSPEWF-FSAVgtVFAG---GIVTG----IYTTSspEACQYIAHd 199
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVS---CQLPNWWeFTVL--YLACsriGAVLNplmpIFRER--ELSFMLKH- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 200 CRANVIVV-------DTQKQLEKILKiwkDLPHLKAVVIYQEPPPKKMANVytmeeLIELGQEVpEEALDAIIDTQQ--P 270
Cdd:PRK13295 126 AESKVLVVpktfrgfDHAAMARRLRP---ELPALRHVVVVGGDGADSFEAL-----LITPAWEQ-EPDAPAILARLRpgP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 271 NQCCVLVYTSGTTGNPKGVM-----LSQDNITWTARYGSQAGDiqpaevqqeVVVSYLPLSHIAAQIYDLWTGIQWGAQV 345
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMhtantLMANIVPYAERLGLGADD---------VILMASPMAHQTGFMYGLMMPVMLGATA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 346 CFADpdalkgtlvntlreveptshmgvprVWEkimeriqeVAAQSGFIRRKMLLWAMSVTleqnltcpsndlkPFtsrLA 425
Cdd:PRK13295 268 VLQD-------------------------IWD--------PARAAELIRTEGVTFTMAST-------------PF---LT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 426 DylvLARVRQALGFAKCQ-KNFY--GAA--PMTAETQRFFLGLNIrlYAGYGLSES---TGpHFMSSPYNYRLYSSGRVV 497
Cdd:PRK13295 299 D---LTRAVKESGRPVSSlRTFLcaGAPipGALVERARAALGAKI--VSAWGMTENgavTL-TKLDDPDERASTTDGCPL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 498 PGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTheAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITa 570
Cdd:PRK13295 373 PGVEVRVV--DADGaplpagqIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR- 447
|
490 500 510
....*....|....*....|....*....|...
gi 19705503 571 GGENVPPVPIeEAVKMELPIISSAMLIG--DQR 601
Cdd:PRK13295 448 GGENIPVVEI-EALLYRHPAIAQVAIVAypDER 479
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
129-598 |
3.09e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 113.60 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQYYLIARKVAKGFLKLglerAHSVailgfNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 208
Cdd:PRK07470 41 RVDALAAALAARGVRKGDRIL----VHSR-----NCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 209 TQKQlEKILKIWKDLPHLKAVVIYQEPPpkkMANVYtmEELI--ELGQEVPeealDAIIDTQQPnqcCVLVYTSGTTGNP 286
Cdd:PRK07470 112 ADFP-EHAAAVRAASPDLTHVVAIGGAR---AGLDY--EALVarHLGARVA----NAAVDHDDP---CWFFFTSGTTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 287 KGVMLSQDNITWTARygSQAGDIQPAEVQQEVVVSYLPLSHIAaqiydlwtGIQWGAQVcfadpdALKGTLVNTlreveP 366
Cdd:PRK07470 179 KAAVLTHGQMAFVIT--NHLADLMPGTTEQDASLVVAPLSHGA--------GIHQLCQV------ARGAATVLL-----P 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 367 TSHMGVPRVWEKIME-RIQEVAAQSGFIrrKMLLWAMSVTleqnlTCPSNDLKpftsrladYLVlarvrqalgfakcqkn 445
Cdd:PRK07470 238 SERFDPAEVWALVERhRVTNLFTVPTIL--KMLVEHPAVD-----RYDHSSLR--------YVI---------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 446 fYGAAPMTAETQRFFLG-LNIRLYAGYGLSESTG------PHFMSS---PyNYRLYSSGRVVPGCRVKLvnQDADG---- 511
Cdd:PRK07470 287 -YAGAPMYRADQKRALAkLGKVLVQYFGLGEVTGnitvlpPALHDAedgP-DARIGTCGFERTGMEVQI--QDDEGrelp 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 512 ---IGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKMEl 588
Cdd:PRK07470 363 pgeTGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYIS-GGSNVYPREIEEKLLTH- 439
|
490
....*....|
gi 19705503 589 PIISSAMLIG 598
Cdd:PRK07470 440 PAVSEVAVLG 449
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
140-597 |
4.30e-26 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 113.15 E-value: 4.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 140 RKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDtQKQLEKILKI 219
Cdd:PLN02330 66 RRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN-DTNYGKVKGL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 220 wkDLPhlkaVVIYQEpppKKMANVYTMEELIELGQEVPEEALDAIIdtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITwt 299
Cdd:PLN02330 145 --GLP----VIVLGE---EKIEGAVNWKELLEAADRAGDTSDNEEI---LQTDLCALPFSSGTTGISKGVMLTHRNLV-- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 300 ARYGSQAGDIQPAEVQQEVVVSYLPLSHIaaqiYDLwTGIqwgaqvCFAdpdalkgTLVNTlreveptshmgvprvweki 379
Cdd:PLN02330 211 ANLCSSLFSVGPEMIGQVVTLGLIPFFHI----YGI-TGI------CCA-------TLRNK------------------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 380 meriQEVAAQSGFIRRKML--LWAMSVTLEQnlTCPSNDLKPFTSRLADYLVLARVrqalgfaKCQKNFYGAAPMTAETQ 457
Cdd:PLN02330 254 ----GKVVVMSRFELRTFLnaLITQEVSFAP--IVPPIILNLVKNPIVEEFDLSKL-------KLQAIMTAAAPLAPELL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 458 RFFLGL--NIRLYAGYGLSES---TGPHfmSSPYN----YRLYSSGRVVPGCRVKLVNQDA------DGIGEICLWGRTI 522
Cdd:PLN02330 321 TAFEAKfpGVQVQEAYGLTEHsciTLTH--GDPEKghgiAKKNSVGFILPNLEVKFIDPDTgrslpkNTPGELCVRSQCV 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19705503 523 FMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGEnVPPVPIeEAVKMELPIISSAMLI 597
Cdd:PLN02330 399 MQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ-VAPAEL-EAILLTHPSVEDAAVV 471
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
275-599 |
2.16e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 110.22 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 275 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFADPDALK 354
Cdd:cd05922 121 LLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA----DDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 355 GTLVNTLREVEPTSHMGVPRVWEkIMERIqevaaqsgfIRRKMLLwamsvtleqnltcPSndLKPFTSrladylVLARVR 434
Cdd:cd05922 196 DAFWEDLREHGATGLAGVPSTYA-MLTRL---------GFDPAKL-------------PS--LRYLTQ------AGGRLP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 435 QALgfakcQKNFYGAAPMTaetqrfflglniRLYAGYGLSESTG------PHFMSSpynyRLYSSGRVVPGCRVKLVNQD 508
Cdd:cd05922 245 QET-----IARLRELLPGA------------QVYVMYGQTEATRrmtylpPERILE----KPGSIGLAIPGGEFEILDDD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 509 ----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEEA 583
Cdd:cd05922 304 gtptPPGePGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAA 382
|
330
....*....|....*.
gi 19705503 584 VkMELPIISSAMLIGD 599
Cdd:cd05922 383 A-RSIGLIIEAAAVGL 397
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
118-598 |
3.19e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 109.67 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 118 ALGFKRKDkwerISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIA 197
Cdd:PRK03640 20 AIEFEEKK----VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 198 HDCRANVIVVD---TQKQLEKILKIWKDLPhlkavviyQEPppkkmanvytmEELIELGQEVPEEALDAIIdtqqpnqcc 274
Cdd:PRK03640 96 DDAEVKCLITDddfEAKLIPGISVKFAELM--------NGP-----------KEEAEIQEEFDLDEVATIM--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 275 vlvYTSGTTGNPKGVMLSQDNITWTAR-----YGSQAGDIQPAEVqqevvvsylPLSHIAA-QIydLWTGIQWGAQVCFA 348
Cdd:PRK03640 148 ---YTSGTTGKPKGVIQTYGNHWWSAVgsalnLGLTEDDCWLAAV---------PIFHISGlSI--LMRSVIYGMRVVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 349 DP-DALKgtlVNTLREVEPTSHMG-VPRVWEKIMERIQEVAAQSGFirRKMLLW---AMSVTLEQnltcpsndlkpftsr 423
Cdd:PRK03640 214 EKfDAEK---INKLLQTGGVTIISvVSTMLQRLLERLGEGTYPSSF--RCMLLGggpAPKPLLEQ--------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 424 ladylvlarvrqalgfakCQknfygaapmtaetQRfflglNIRLYAGYGLSEsTGPHFMSSPYNY---RLYSSGRVVPGC 500
Cdd:PRK03640 274 ------------------CK-------------EK-----GIPVYQSYGMTE-TASQIVTLSPEDaltKLGSAGKPLFPC 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 501 RVKLVNQDADG----IGEICLWGRTIFMGYLNMEDKTHEAIDSeGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVP 576
Cdd:PRK03640 317 ELKIEKDGVVVppfeEGEIVVKGPNVTKGYLNREDATRETFQD-GWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIY 394
|
490 500
....*....|....*....|..
gi 19705503 577 PVPIeEAVKMELPIISSAMLIG 598
Cdd:PRK03640 395 PAEI-EEVLLSHPGVAEAGVVG 415
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
127-719 |
8.51e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 109.58 E-value: 8.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 127 WERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIyttsSPeacQY--IAHD----- 199
Cdd:PRK08180 67 WRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV----SP---AYslVSQDfgklr 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 200 -----CRANVIVVDTQKQLEKILKIwKDLPHLKAVVIYQEPPPKKmanVYTMEELIELGqevPEEALDAIIDTQQPNQCC 274
Cdd:PRK08180 140 hvlelLTPGLVFADDGAAFARALAA-VVPADVEVVAVRGAVPGRA---ATPFAALLATP---PTAAVDAAHAAVGPDTIA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 275 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDiQPAEvQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAD----P 350
Cdd:PRK08180 213 KFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFP-FLAE-EPPVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIDDgkptP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 351 DALKGTLVNtLREVEPTSHMGVPRVWEkimeriqevaaqsgfirrkMLLWAmsvtLEQNltcpsndlkpftSRLADYLvL 430
Cdd:PRK08180 291 GGFDETLRN-LREISPTVYFNVPKGWE-------------------MLVPA----LERD------------AALRRRF-F 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 431 ARVRQAlgfakcqknFYGAAPMTAET----QRF---FLGLNIRLYAGYGLSEsTGPHFMSSpyNYRLYSSGRV---VPGC 500
Cdd:PRK08180 334 SRLKLL---------FYAGAALSQDVwdrlDRVaeaTCGERIRMMTGLGMTE-TAPSATFT--TGPLSRAGNIglpAPGC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 501 RVKLVnqDADGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDD-----GFLYiTGRLKELIITAGGE-- 573
Cdd:PRK08180 402 EVKLV--PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVDPadperGLMF-DGRIAEDFKLSSGTwv 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 574 NVPPVPIeEAVKMELPIISSAMLIGDQRKFLSMLLTLKctlnpetseptdnlteqaVEFCQRVGSKASTVSEIVGQKDEA 653
Cdd:PRK08180 479 SVGPLRA-RAVSAGAPLVQDVVITGHDRDEIGLLVFPN------------------LDACRRLAGLLADASLAEVLAHPA 539
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19705503 654 VYQAIHEGIQRVNANAAARPYHIQKWAILERDFSISGGELgpTMK--LKRLTVLEKYKDIIDSFYQEQ 719
Cdd:PRK08180 540 VRAAFRERLARLNAQATGSSTRVARALLLDEPPSLDAGEI--TDKgyINQRAVLARRAALVEALYADE 605
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
129-581 |
1.68e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 108.12 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQYYLIARKVAkGFL--KLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 206
Cdd:PRK08314 35 AISYRELLEEAERLA-GYLqqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 207 VdTQKQLEKILKIWKDLPhLKAVVIYQ----------EPPPKKMANVYTMEELIELGQEVPEEALDAIID----TQQPNQ 272
Cdd:PRK08314 114 V-GSELAPKVAPAVGNLR-LRHVIVAQysdylpaepeIAVPAWLRAEPPLQALAPGGVVAWKEALAAGLAppphTAGPDD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 273 CCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIaaqiydlwTGIQWGAQVcfadPDA 352
Cdd:PRK08314 192 LAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTP----ESVVLAVLPLFHV--------TGMVHSMNA----PIY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 353 LKGTLVNtlreveptshmgVPRvWEKimeriqEVAAQsgFIRR-KMLLW----AMSVTLeqnLTCPsndlkpftsRLADY 427
Cdd:PRK08314 256 AGATVVL------------MPR-WDR------EAAAR--LIERyRVTHWtnipTMVVDF---LASP---------GLAER 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 428 lVLARVRQALGfakcqknfyGAAPM-TAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSG--------RVV- 497
Cdd:PRK08314 303 -DLSSLRYIGG---------GGAAMpEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGiptfgvdaRVId 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 498 PgcrVKLVNQDADGIGEICLWGRTIFMGYLNMEDKTHEA---IDSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGEN 574
Cdd:PRK08314 373 P---ETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRM-INASGFK 448
|
....*..
gi 19705503 575 VPPVPIE 581
Cdd:PRK08314 449 VWPAEVE 455
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
130-633 |
2.31e-24 |
|
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: 106.78 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 130 ISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDT 209
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 210 qkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealDAIidtqqpnqcCVLVYTSGTTGNPKGV 289
Cdd:cd05919 91 ----------------------------------------------------DDI---------AYLLYSSGTTGPPKGV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 290 MLSQDNITWTAR-YGSQAGDIQPaevqQEVVVSylplshiAAQIY-------DLWTGIQWGAQVCFAD----PDALKGTL 357
Cdd:cd05919 110 MHAHRDPLLFADaMAREALGLTP----GDRVFS-------SAKMFfgyglgnSLWFPLAVGASAVLNPgwptAERVLATL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 358 VntlrEVEPTSHMGVPRVWEKIMeriqevaAQSGFIRRKMllwamsvtleqnltcpsNDLKPFTSRladylvlarvrqal 437
Cdd:cd05919 179 A----RFRPTVLYGVPTFYANLL-------DSCAGSPDAL-----------------RSLRLCVSA-------------- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 438 gfakcqknfyGAAPMTAETQRFFLGLNIRLYAGYGLSEsTGPHFMSS-PYNYRLYSSGRVVPGCRVKLVNQD-----ADG 511
Cdd:cd05919 217 ----------GEALPRGLGERWMEHFGGPILDGIGATE-VGHIFLSNrPGAWRLGSTGRPVPGYEIRLVDEEghtipPGE 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 512 IGEICLWGRTIFMGYLNMEDKThEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPII 591
Cdd:cd05919 286 EGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLI-IQHPAV 362
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 19705503 592 SSAMLIGDQRkfLSMLLTLKCTLNPET-SEPTDNLTEQAVEFC 633
Cdd:cd05919 363 AEAAVVAVPE--STGLSRLTAFVVLKSpAAPQESLARDIHRHL 403
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
140-598 |
5.00e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 106.79 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 140 RKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQkqLEKILKI 219
Cdd:PRK07786 53 AALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA--LAPVATA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 220 WKDL-PHLKAVVIYQEPPPkkmANVYTMEELIELGQEVPeealdAIIDTqqPNQCCVLV-YTSGTTGNPKGVMLSQDNIT 297
Cdd:PRK07786 131 VRDIvPLLSTVVVAGGSSD---DSVLGYEDLLAEAGPAH-----APVDI--PNDSPALImYTSGTTGRPKGAVLTHANLT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 298 WTARYGSQAGDiqpAEVQQEVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFADPDALK-GTLVNTLREVEPTSHMGVPRVW 376
Cdd:PRK07786 201 GQAMTCLRTNG---ADINSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYPLGAFDpGQLLDVLEAEKVTGIFLVPAQW 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 377 EKIMEriqEVAAQSGFIRRKMLLWAMSvtleqnltcPSND--LKPFTSRLADYLVLArvrqalgfakcqknFYGAAPMTA 454
Cdd:PRK07786 277 QAVCA---EQQARPRDLALRVLSWGAA---------PASDtlLRQMAATFPEAQILA--------------AFGQTEMSP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 455 ETQrFFLGLN-IRlyagyglsestgphfmsspynyRLYSSGRVVPGCRVKLVNQDADG-----IGEICLWGRTIFMGYLN 528
Cdd:PRK07786 331 VTC-MLLGEDaIR----------------------KLGSVGKVIPTVAARVVDENMNDvpvgeVGEIVYRAPTLMSGYWN 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 529 MEDKTHEAIDSeGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISSAMLIG 598
Cdd:PRK07786 388 NPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCAEVEN-VLASHPDIVEVAVIG 454
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
238-601 |
5.05e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 106.83 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 238 KKMANVYTMEELIELGQEVPEEALDAIIDTQQP-NQCCVLVYTSGTTGNPKGVMLSQDNITWT-----ARYGSQAGDIQP 311
Cdd:PRK12492 173 KKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGlDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvrACLSQLGPDGQP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 312 A-EVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCFADPDALKGtLVNTLREVEPTSHMGVPRVWEKIMEriqevaaQ 389
Cdd:PRK12492 253 LmKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHnVLITNPRDIPG-FIKELGKWRFSALLGLNTLFVALMD-------H 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 390 SGFirRKMLLWAMSVTleqnltcpsndlkpftsrladylvlarvrqalgfakcqkNFYGAAPMTAETQRFFLGLNIRLYA 469
Cdd:PRK12492 325 PGF--KDLDFSALKLT---------------------------------------NSGGTALVKATAERWEQLTGCTIVE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 470 GYGLSEsTGPHFMSSPYN--YRLYSSGRVVPGCRVKLVNQDADGI-----GEICLWGRTIFMGYLNMEDKTHEAIDSEGW 542
Cdd:PRK12492 364 GYGLTE-TSPVASTNPYGelARLGTVGIPVPGTALKVIDDDGNELplgerGELCIKGPQVMKGYWQQPEATAEALDAEGW 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19705503 543 LHTGDMGRLDDDGFLYITGRLKELIITAGGeNVPPVPIEEAVkMELPIISSAMLIG--DQR 601
Cdd:PRK12492 443 FKTGDIAVIDPDGFVRIVDRKKDLIIVSGF-NVYPNEIEDVV-MAHPKVANCAAIGvpDER 501
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
130-586 |
6.17e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 106.50 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 130 ISYYQYYLIARKVAKGFL-KLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV- 207
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVi 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 ------------DTQ-KQ-----LEKILKIWKD------LPHLKAVViyqepPPKKMANVYTMEELIELGQEVPEEALDA 263
Cdd:PRK08751 131 dnfgttvqqviaDTPvKQvittgLGDMLGFPKAalvnfvVKYVKKLV-----PEYRINGAIRFREALALGRKHSMPTLQI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 264 iidtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQ----AGDIQPAevqQEVVVSYLPLSHIAAQIYDLWTGI 339
Cdd:PRK08751 206 -----EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagTGKLEEG---CEVVITALPLYHIFALTANGLVFM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 340 QWGAqvC---FADPDALKGtLVNTLREVEPTSHMGVPRVWEKImeriqevaaqsgfirrkmllwamsvtleqnLTCPSND 416
Cdd:PRK08751 278 KIGG--CnhlISNPRDMPG-FVKELKKTRFTAFTGVNTLFNGL------------------------------LNTPGFD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 417 LKPFTSrladylvlarVRQALGfakcqknfYGAAPMTAETQRFFLGLNIRLYAGYGLSEsTGPHFMSSPYNYRLYSSGRV 496
Cdd:PRK08751 325 QIDFSS----------LKMTLG--------GGMAVQRSVAERWKQVTGLTLVEAYGLTE-TSPAACINPLTLKEYNGSIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 497 VPGCRVKLVNQDADG-------IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIIT 569
Cdd:PRK08751 386 LPIPSTDACIKDDAGtvlaigeIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILV 465
|
490
....*....|....*..
gi 19705503 570 AGGeNVPPVPIEEAVKM 586
Cdd:PRK08751 466 SGF-NVYPNEIEDVIAM 481
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
246-601 |
1.02e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 105.27 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 246 MEELIELGQEVPEEALD--AIIDTQQPNqccVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQpaevQQEVVVSYL 323
Cdd:PRK09088 111 VEDLAAFIASADALEPAdtPSIPPERVS---LILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVD----AHSSFLCDA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 324 PLSHIAAQIYDLWTGIQWGAQVCFAD---PDALKGTLVNTLREVepTSHMGVPrvweKIMERIQevaAQSGFirrkmllw 400
Cdd:PRK09088 184 PMFHIIGLITSVRPVLAVGGSILVSNgfePKRTLGRLGDPALGI--THYFCVP----QMAQAFR---AQPGF-------- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 401 amsvtleqnltcpsndlkpftsrlaDYLVLARVrQALgfakcqknFYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPH 480
Cdd:PRK09088 247 -------------------------DAAALRHL-TAL--------FTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGTVF 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 481 FMS---SPYNYRLYSSGRVVPGCRVKLVNQDADGI-----GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLD 552
Cdd:PRK09088 293 GMSvdcDVIRAKAGAAGIPTPTVQTRVVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRD 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 19705503 553 DDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISSAMLIG--DQR 601
Cdd:PRK09088 373 ADGFFWVVDRKKDMFIS-GGENVYPAEI-EAVLADHPGIRECAVVGmaDAQ 421
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
276-601 |
2.54e-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: 101.81 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 276 LVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEvqqevvvSYL---PLSHI----AAQIYDLWTGIQWGAQVCFa 348
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDD-------RYLiinPFFHTfgykAGIVACLLTGATVVPVAVF- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 349 DPDALKGTLVNTLREVEPtshmGVPRVWEKIMERIQevaaqsgfiRRKMLLWAMSVTLEQNLTCPSndlkpftsrladyL 428
Cdd:cd17638 77 DVDAILEAIERERITVLP----GPPTLFQSLLDHPG---------RKKFDLSSLRAAVTGAATVPV-------------E 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 429 VLARVRQALGFakcqknfygaapMTAETqrfflglnirlyaGYGLSEStGPHFMSSPYNYRL---YSSGRVVPGCRVKLV 505
Cdd:cd17638 131 LVRRMRSELGF------------ETVLT-------------AYGLTEA-GVATMCRPGDDAEtvaTTCGRACPGFEVRIA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 506 NQdadgiGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIItAGGENVPPVPIEEAVk 585
Cdd:cd17638 185 DD-----GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGAL- 257
|
330
....*....|....*...
gi 19705503 586 MELPIISSAMLIG--DQR 601
Cdd:cd17638 258 AEHPGVAQVAVIGvpDER 275
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
129-584 |
3.65e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 103.92 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYT-TSSPEACQYIAhdcranvivv 207
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQpTPRTDLAVWAE---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DTQKQLEKIlkiwkdlpHLKAVVI---YQEPPP---KKMANVYTMEELIELGQEVPEEALDAIIDTQQpnqccvlvYTSG 281
Cdd:PRK07768 99 DTLRVIGMI--------GAKAVVVgepFLAAAPvleEKGIRVLTVADLLAADPIDPVETGEDDLALMQ--------LTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 282 TTGNPKGVMLSQDNITWTARYGSQAGDIqpaEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAqvcfadpDALKGTlvntl 361
Cdd:PRK07768 163 STGSPKAVQITHGNLYANAEAMFVAAEF---DVETDVMVSWLPLFHDMGMVGFLTVPMYFGA-------ELVKVT----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 362 revePTSHMGVPRVWEKIMERiqevaaqsgfiRRKmllwamSVTLEQNLTcpsndlkpftsrladYLVLARV--RQA--- 436
Cdd:PRK07768 228 ----PMDFLRDPLLWAELISK-----------YRG------TMTAAPNFA---------------YALLARRlrRQAkpg 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 437 ------LGFAKCqknfyGAAPMTAETQRFFL------GLNIR-LYAGYGLSEST----------GPHF------------ 481
Cdd:PRK07768 272 afdlssLRFALN-----GAEPIDPADVEDLLdagarfGLRPEaILPAYGMAEATlavsfspcgaGLVVdevdadllaalr 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 482 ----MSSPYNYRLYSSGRVVPGCRVKLVNQD-----ADGIGEICLWGRTIFMGYLNMeDKTHEAIDSEGWLHTGDMGRLD 552
Cdd:PRK07768 347 ravpATKGNTRRLATLGPPLPGLEVRVVDEDgqvlpPRGVGVIELRGESVTPGYLTM-DGFIPAQDADGWLDTGDLGYLT 425
|
490 500 510
....*....|....*....|....*....|..
gi 19705503 553 DDGFLYITGRLKELIITaGGENVPPVPIEEAV 584
Cdd:PRK07768 426 EEGEVVVCGRVKDVIIM-AGRNIYPTDIERAA 456
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
157-562 |
4.37e-23 |
|
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: 102.34 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 157 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKQLEKIlkiWKDLPHLkavviyqepp 236
Cdd:TIGR01733 28 VAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLA---GLVLPVI---------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 237 pkkmanVYTMEELIELGQEVPEEALDAiiDTQQPNQCCVLvYTSGTTGNPKGVMLSQDNI----TWTAR-YGSQAGDiqp 311
Cdd:TIGR01733 95 ------LLDPLELAALDDAPAPPPPDA--PSGPDDLAYVI-YTSGSTGRPKGVVVTHRSLvnllAWLARrYGLDPDD--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 312 aevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFADPDALKGT--LVNTLREVEPTSHM-GVPRVWEKIMEriqevAA 388
Cdd:TIGR01733 163 ------RVLQFASLSFDAS-VEEIFGALLAGATLVVPPEDEERDDaaLLAALIAEHPVTVLnLTPSLLALLAA-----AL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 389 QSGFIRRKMLLWAmsvtleqnltcpsndlkpftsrlADYLVLARVRQALGfakcqknfygaapmtaetqrffLGLNIRLY 468
Cdd:TIGR01733 231 PPALASLRLVILG-----------------------GEALTPALVDRWRA----------------------RGPGARLI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 469 AGYGLSEST----------GPHFMSSPYNYrlyssGRVVPGCRVKLVNQD-----ADGIGEICLWGRTIFMGYLNMEDKT 533
Cdd:TIGR01733 266 NLYGPTETTvwstatlvdpDDAPRESPVPI-----GRPLANTRLYVLDDDlrpvpVGVVGELYIGGPGVARGYLNRPELT 340
|
410 420 430
....*....|....*....|....*....|....*..
gi 19705503 534 HEAI--------DSEGWLHTGDMGRLDDDGFLYITGR 562
Cdd:TIGR01733 341 AERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGR 377
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
128-584 |
7.43e-23 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 103.30 E-value: 7.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 207
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DTQkQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEVPEEALdaiidtqQPNQCCVLVYTSGTTGNPK 287
Cdd:PRK06155 125 EAA-LLAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAV-------QPGDTAAILYTSGTTGPSK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 288 GVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIaaqiydlwtgiqwGAQVCFAdPDALKG-TLVntlreVEP 366
Cdd:PRK06155 197 GVCCPHAQFYWWGRNSAEDLEIGA----DDVLYTTLPLFHT-------------NALNAFF-QALLAGaTYV-----LEP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 367 tsHMGVPRVWEkimeRIQEVAAQSGFirrkmLLWAM-SVTLEQNLTCPSNDlkpftsrladylvlARVRQALGfakcqkn 445
Cdd:PRK06155 254 --RFSASGFWP----AVRRHGATVTY-----LLGAMvSILLSQPARESDRA--------------HRVRVALG------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 446 fyGAAPmTAETQRFFLGLNIRLYAGYGLSESTGPhFMSSPYNYRLYSSGRVVPGCRVKLVNQD-----ADGIGEICLWGR 520
Cdd:PRK06155 302 --PGVP-AALHAAFRERFGVDLLDGYGSTETNFV-IAVTHGSQRPGSMGRLAPGFEARVVDEHdqelpDGEPGELLLRAD 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19705503 521 TIFM---GYLNMEDKTHEAIDSEgWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEEAV 584
Cdd:PRK06155 378 EPFAfatGYFGMPEKTVEAWRNL-WFHTGDRVVRDADGWFRFVDRIKD-AIRRRGENISSFEVEQVL 442
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
105-598 |
1.33e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 102.67 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 105 MFYEALDKY-----GNLSALGFKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGG 179
Cdd:PRK04319 44 IAYEAIDRHadggrKDKVALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 180 IVTGIYTTSSPEACQYIAHDCRANVIVVdTQKQLEKilKIWKDLPHLKAVVIYQEPppkkmanVYTMEELIELGQEVPEE 259
Cdd:PRK04319 124 IVGPLFEAFMEEAVRDRLEDSEAKVLIT-TPALLER--KPADDLPSLKHVLLVGED-------VEEGPGTLDFNALMEQA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 260 ALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITW---TARYgsqAGDIQPAEvqqevvvsylplshiaaqIYdlW 336
Cdd:PRK04319 194 SDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQhyqTGKY---VLDLHEDD------------------VY--W 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 337 tgiqwgaqvCFADPDALKGT-----------LVNTLREVEPTshmgvPRVWEKIMERiQEV----AAQSGFirrKMLlwa 401
Cdd:PRK04319 251 ---------CTADPGWVTGTsygifapwlngATNVIDGGRFS-----PERWYRILED-YKVtvwyTAPTAI---RML--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 402 MSVTLEqnltcpsndlkpftsrLADYLVLARVRQALGFAKcqknfygaaPMTAETQRFflG---LNIRLYAGYGLSEsTG 478
Cdd:PRK04319 310 MGAGDD----------------LVKKYDLSSLRHILSVGE---------PLNPEVVRW--GmkvFGLPIHDNWWMTE-TG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 479 PHFMSspyNY-----RLYSSGRVVPGCRVKLVNQDADG-----IGEICL---WgRTIFMGYLNMEDKTHEAIdSEGWLHT 545
Cdd:PRK04319 362 GIMIA---NYpamdiKPGSMGKPLPGIEAAIVDDQGNElppnrMGNLAIkkgW-PSMMRGIWNNPEKYESYF-AGDWYVS 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 19705503 546 GDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:PRK04319 437 GDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVESKL-MEHPAVAEAGVIG 487
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
99-604 |
3.48e-22 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 100.98 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 99 PYTVHQMFYEALDKYGNLSALGFKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG 178
Cdd:PRK06018 9 PLLCHRIIDHAARIHGNREVVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 179 GIVTGIYTTSSPEACQYIAHDCRANVIVVDTQ--KQLEKILKiwkDLPHLKAVVIYQEP---PPKKMANVYTMEELIElg 253
Cdd:PRK06018 89 AICHTVNPRLFPEQIAWIINHAEDRVVITDLTfvPILEKIAD---KLPSVERYVVLTDAahmPQTTLKNAVAYEEWIA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 254 qevpEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIqpAEVQQEVVVSYLPLSHIAAqiy 333
Cdd:PRK06018 164 ----EADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDAL--GTSAADTMLPVVPLFHANS--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 334 dlwtgiqWGaqVCFADPDA----------LKGTLVNTLREVEPTSH-MGVPRVWEkimeriqevaaqsgfirrkMLLWAM 402
Cdd:PRK06018 235 -------WG--IAFSAPSMgtklvmpgakLDGASVYELLDTEKVTFtAGVPTVWL-------------------MLLQYM 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 403 SvtlEQNLTCPsnDLKpftsrladylvlarvrqalgfakcqKNFYGAAPMTAETQRFFLGLNIRLYAGYGLSEST----- 477
Cdd:PRK06018 287 E---KEGLKLP--HLK-------------------------MVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSplgtl 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 478 ---GPHFMSSPYNYRL---YSSGRVVPGCRVKLVNQDA-----DG--IGEICLWGRTIFMGYLNMEDkthEAIDSEGWLH 544
Cdd:PRK06018 337 aalKPPFSKLPGDARLdvlQKQGYPPFGVEMKITDDAGkelpwDGktFGRLKVRGPAVAAAYYRVDG---EILDDDGFFD 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19705503 545 TGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEE-AVKMelPIISSAMLIG------DQRKFL 604
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKD-VIKSGGEWISSIDLENlAVGH--PKVAEAAVIGvyhpkwDERPLL 477
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
276-598 |
6.71e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 99.95 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 276 LVYTSGTTGNPKGVMLSQDNITWTAR-----YGSQAGDiqpaevqqeVVVSYLPLSH-----IAAQIYDLWtgiqwGAQV 345
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSNALtlvdyWRFTPDD---------VLIHALPIFHthglfVATNVALLA-----GASM 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 346 CFA---DPDALKGTLVNTlrevepTSHMGVPRVWEKIMeriqevaAQSGFIR---RKMLLwamsvtleqnltcpsndlkp 419
Cdd:PRK07514 227 IFLpkfDPDAVLALMPRA------TVMMGVPTFYTRLL-------QEPRLTReaaAHMRL-------------------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 420 FTSrladylvlarvrqalgfakcqknfyGAAPMTAETQRFF---LGLNI--RlyagYGLSEsTGphfM--SSPYN--YRL 490
Cdd:PRK07514 274 FIS-------------------------GSAPLLAETHREFqerTGHAIleR----YGMTE-TN---MntSNPYDgeRRA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 491 YSSGRVVPGCRVKLVNQD------ADGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLK 564
Cdd:PRK07514 321 GTVGFPLPGVSLRVTDPEtgaelpPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
330 340 350
....*....|....*....|....*....|....*
gi 19705503 565 ELIITaGGENVPPVPIEEAVKmELP-IISSAmLIG 598
Cdd:PRK07514 401 DLIIS-GGYNVYPKEVEGEID-ELPgVVESA-VIG 432
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
129-583 |
1.02e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 99.64 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 208
Cdd:PRK08162 43 RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 209 TQKQlEKILKIWKDLPHLKAVVI-YQEPPPKKMANVYTM--EELIELGQ-----EVPEEALDAIidtqqpnqccVLVYTS 280
Cdd:PRK08162 123 TEFA-EVAREALALLPGPKPLVIdVDDPEYPGGRFIGALdyEAFLASGDpdfawTLPADEWDAI----------ALNYTS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 281 GTTGNPKGV--------MLSQDNITwtarygsqAGDIQPaevqQEVVVSYLPLSHIAAQIYDlWT-GIQWGAQVCfadpd 351
Cdd:PRK08162 192 GTTGNPKGVvyhhrgayLNALSNIL--------AWGMPK----HPVYLWTLPMFHCNGWCFP-WTvAARAGTNVC----- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 352 alkgtlvntLREVEPtshmgvprvwEKIMERIQE--VAAQSGF-IRRKMLLWAmsvtleqnltcPSNDLKPFtsrlaDYL 428
Cdd:PRK08162 254 ---------LRKVDP----------KLIFDLIREhgVTHYCGApIVLSALINA-----------PAEWRAGI-----DHP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 429 VLARVRqalgfakcqknfyGAAP---MTAETQRfflgLNIRLYAGYGLSESTGP--------HFMSSPYNYRLYSSGR-- 495
Cdd:PRK08162 299 VHAMVA-------------GAAPpaaVIAKMEE----IGFDLTHVYGLTETYGPatvcawqpEWDALPLDERAQLKARqg 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 496 ----VVPGCRV------KLVNQDADGIGEICLWGRTIFMGYLNMEDKTHEAIDSeGWLHTGDMGRLDDDGFLYITGRLKE 565
Cdd:PRK08162 362 vrypLQEGVTVldpdtmQPVPADGETIGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKIKDRSKD 440
|
490
....*....|....*...
gi 19705503 566 LIITaGGENVPPVPIEEA 583
Cdd:PRK08162 441 IIIS-GGENISSIEVEDV 457
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
131-598 |
1.04e-21 |
|
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: 98.56 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 131 SYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQ 210
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 211 kqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealdaiiDTqqpnqcCVLVYTSGTTGNPKGVm 290
Cdd:cd05972 82 -------------------------------------------------------DP------ALIYFTSGTTGLPKGV- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 291 lsqdnitwtarygsqagdiqpaevqqEVVVSYlPLSHIAAQIYdlWTGIQWGAQV-CFADPDALKGTLVNTLrevEPTSH 369
Cdd:cd05972 100 --------------------------LHTHSY-PLGHIPTAAY--WLGLRPDDIHwNIADPGWAKGAWSSFF---GPWLL 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 370 mGVPRVwekimeriqeVAAQSGFIRRKML--LWAMSVTleqNLTCPSNDLKPFTSRLADYLVLARVRQALGfakcqknfy 447
Cdd:cd05972 148 -GATVF----------VYEGPRFDAERILelLERYGVT---SFCGPPTAYRMLIKQDLSSYKFSHLRLVVS--------- 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 448 GAAPMTAETQRFF---LGLNIRlyAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGI-----GEICLWG 519
Cdd:cd05972 205 AGEPLNPEVIEWWraaTGLPIR--DGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELppgeeGDIAIKL 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 520 RTI--FMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISSAMLI 597
Cdd:cd05972 283 PPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS-GYRIGPFEVESAL-LEHPAVAEAAVV 359
|
.
gi 19705503 598 G 598
Cdd:cd05972 360 G 360
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
140-598 |
2.99e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 98.33 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 140 RKVAKGFLKLGLERAHSVAILGFNSP---EWFFsAVgtVFAGGIVTGI-YTTSSPEACQYIAHdCRANVIVVDTQKQLEK 215
Cdd:PLN02860 43 LSLAAGLLRLGLRNGDVVAIAALNSDlylEWLL-AV--ACAGGIVAPLnYRWSFEEAKSAMLL-VRPVMLVTDETCSSWY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 216 ILKIWKDLPHLKAVVIYQEPPPKK---MANVYTMEELIELGQEVPEEALdaiidTQQPNQCCVLVYTSGTTGNPKGVMLS 292
Cdd:PLN02860 119 EELQNDRLPSLMWQVFLESPSSSVfifLNSFLTTEMLKQRALGTTELDY-----AWAPDDAVLICFTSGTTGRPKGVTIS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 293 QDNITW-----TARYGSQAGDIqpaevqqevvvsYL---PLSHIAAqIYDLWTGIQWGAQVCFAdPDALKGTLVNTLREV 364
Cdd:PLN02860 194 HSALIVqslakIAIVGYGEDDV------------YLhtaPLCHIGG-LSSALAMLMVGACHVLL-PKFDAKAALQAIKQH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 365 EPTSHMGVPrvweKIMERIQEVAaqsgfirRKMLLWAMSVTLEQNLtcpsNDLKPFTSRLADYLVLARVRQALGFAkcqk 444
Cdd:PLN02860 260 NVTSMITVP----AMMADLISLT-------RKSMTWKVFPSVRKIL----NGGGSLSSRLLPDAKKLFPNAKLFSA---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 445 nfYGaapMT-AETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYN-YRLYSSGRVVPGCRVKLVNQDADGIGEICLWGRTI 522
Cdd:PLN02860 321 --YG---MTeACSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVHqPQGVCVGKPAPHVELKIGLDESSRVGRILTRGPHV 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19705503 523 FMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISSAMLIG 598
Cdd:PLN02860 396 MLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKT-GGENVYPEEV-EAVLSQHPGVASVVVVG 469
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
276-582 |
5.21e-21 |
|
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: 95.02 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 276 LVYTSGTTGNPKGVMLSQDN-ITWTARYGSQAGDIqpaeVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFADPDALK 354
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNW----VVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 355 gTLVNTLREVEPTSHMGVPRVWEKIMeriqevaaqsgfirrkmllwamSVTLEQNLTCPSNDLkpftsrladylvlarvr 434
Cdd:cd17635 82 -SLFKILTTNAVTTTCLVPTLLSKLV----------------------SELKSANATVPSLRL----------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 435 qaLGFAkcqknfyGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMssPYNYRLY---SSGRVVPGCRVKLVNQDA-- 509
Cdd:cd17635 122 --IGYG-------GSRAIAADVRFIEATGLTNTAQVYGLSETGTALCL--PTDDDSIeinAVGRPYPGVDVYLAATDGia 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19705503 510 ---DGIGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEE 582
Cdd:cd17635 191 gpsASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSE-SINCGGVKIAPDEVER 264
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
129-596 |
2.15e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 95.86 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 208
Cdd:PLN03102 39 RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 209 TQ-----KQLEKILKIWKDLPHLKAVVIYQEPPPKK-MANVYTMEELIELGQEVPEeALDAIIDTQQPNQCCVLVYTSGT 282
Cdd:PLN03102 119 RSfeplaREVLHLLSSEDSNLNLPVIFIHEIDFPKRpSSEELDYECLIQRGEPTPS-LVARMFRIQDEHDPISLNYTSGT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 283 TGNPKGVMLSQDNI---TWTARYGSQAGdIQPaevqqeVVVSYLPLSHIAAQIYDLWTGIQWGAQVCF---ADPDALKGT 356
Cdd:PLN03102 198 TADPKGVVISHRGAylsTLSAIIGWEMG-TCP------VYLWTLPMFHCNGWTFTWGTAARGGTSVCMrhvTAPEIYKNI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 357 lvntlrEVEPTSHMG-VPRVWekimeriqevaaqsgfirrKMLLWAMSVtleqNLTCPSNDLKPFTSRLADYLVLARVRQ 435
Cdd:PLN03102 271 ------EMHNVTHMCcVPTVF-------------------NILLKGNSL----DLSPRSGPVHVLTGGSPPPAALVKKVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 436 ALGFakcqknfygaapmtaetqrfflglniRLYAGYGLSESTGPHFMSS--------PYNYRLYSSGRvvPGCRV----- 502
Cdd:PLN03102 322 RLGF--------------------------QVMHAYGLTEATGPVLFCEwqdewnrlPENQQMELKAR--QGVSIlglad 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 503 ---------KLVNQDADGIGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGE 573
Cdd:PLN03102 374 vdvknketqESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGE 451
|
490 500
....*....|....*....|...
gi 19705503 574 NVPPVPIEEAVKMELPIISSAML 596
Cdd:PLN03102 452 NISSVEVENVLYKYPKVLETAVV 474
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
139-589 |
2.50e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 95.15 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 139 ARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV--VDTQKQLEKI 216
Cdd:PRK12406 21 AARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIahADLLHGLASA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 217 LKiwkdlPHLKAVVIyqePPPKKMANVYTMEE--------LIELGQEVPEEALDAIIDTQQPNQccvLVYTSGTTGNPKG 288
Cdd:PRK12406 101 LP-----AGVTVLSV---PTPPEIAAAYRISPalltppagAIDWEGWLAQQEPYDGPPVPQPQS---MIYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 289 VMLSQDNITWTARYGSQAGDIQPAEvQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFA--DPDALkgtLVNTLREVEP 366
Cdd:PRK12406 170 VRRAAPTPEQAAAAEQMRALIYGLK-PGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPrfDPEEL---LQLIERHRIT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 367 TSHMgVPRVWEKIMERIQEVaaqsgfiRRKMLLWAMSVTLEQNLTCPsndlkpftsrladylvlARVRQALgfakcqKNF 446
Cdd:PRK12406 246 HMHM-VPTMFIRLLKLPEEV-------RAKYDVSSLRHVIHAAAPCP-----------------ADVKRAM------IEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 447 YGaaPMTAETqrfflglnirlyagYGLSESTGPHFMSSP-YNYRLYSSGRVVPGCRVKLVnqDADG-------IGEIC-- 516
Cdd:PRK12406 295 WG--PVIYEY--------------YGSTESGAVTFATSEdALSHPGTVGKAAPGAELRFV--DEDGrplpqgeIGEIYsr 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19705503 517 LWGRTIFMgYLNMEDKTHEaIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELP 589
Cdd:PRK12406 357 IAGNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEI-EAVLHAVP 425
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
255-563 |
3.01e-20 |
|
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: 94.24 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 255 EVPEEALDAIIDTQQP-------NQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSH 327
Cdd:cd05945 74 SSPAERIREILDAAKPalliadgDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGP----GDVFLNQAPFSF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 328 IAAqIYDLWTGIQWGAQVCFADPDALK--GTLVNTLREVEPTSHMGVPRVWEKIMeriqevaaqsgfiRRKMLLWAMSVT 405
Cdd:cd05945 150 DLS-VMDLYPALASGATLVPVPRDATAdpKQLFRFLAEHGITVWVSTPSFAAMCL-------------LSPTFTPESLPS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 406 LEQNLTCPsndlKPFTSRLADYLVlarvrqalgfakcqknfyGAAPMTaetqrfflglniRLYAGYGLSESTG------- 478
Cdd:cd05945 216 LRHFLFCG----EVLPHKTARALQ------------------QRFPDA------------RIYNTYGPTEATVavtyiev 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 479 -PHFMSSpyNYRLYSsGRVVPGCRVKLVNQDAD-----GIGEICLWGRTIFMGYLNMEDKTHEA---IDSEGWLHTGDMG 549
Cdd:cd05945 262 tPEVLDG--YDRLPI-GYAKPGAKLVILDEDGRpvppgEKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLV 338
|
330
....*....|....
gi 19705503 550 RLDDDGFLYITGRL 563
Cdd:cd05945 339 RLEADGLLFYRGRL 352
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
276-584 |
6.11e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 95.38 E-value: 6.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 276 LVYTSGTTGNPKGVMLSQDNITWTARygsQAGDIQPAEvQQEVVVSYLPLSH----IAAQIYDLWTGIqwgAQVCFADP- 350
Cdd:PRK08633 787 IIFSSGSEGEPKGVMLSHHNILSNIE---QISDVFNLR-NDDVILSSLPFFHsfglTVTLWLPLLEGI---KVVYHPDPt 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 351 DALKgtlvntlreveptshmgvprvwekimerIQEVAAQsgfiRRKMLLWAMSVTLeqNLTCPSNDLKP--FTS-RLady 427
Cdd:PRK08633 860 DALG----------------------------IAKLVAK----HRATILLGTPTFL--RLYLRNKKLHPlmFASlRL--- 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 428 lVLArvrqalgfakcqknfyGAAPMTAET-QRFFLGLNIRLYAGYGLSESTG------PHFMSSPYNY----RLYSSGRV 496
Cdd:PRK08633 903 -VVA----------------GAEKLKPEVaDAFEEKFGIRILEGYGATETSPvasvnlPDVLAADFKRqtgsKEGSVGMP 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 497 VPGCRVKLVNQD-----ADGI-GEICLWGRTIFMGYLNMEDKTHEAI---DSEGWLHTGDMGRLDDDGFLYITGRLKEL- 566
Cdd:PRK08633 966 LPGVAVRIVDPEtfeelPPGEdGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFa 1045
|
330
....*....|....*....
gi 19705503 567 -IitaGGENVPPVPIEEAV 584
Cdd:PRK08633 1046 kI---GGEMVPLGAVEEEL 1061
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
127-718 |
8.36e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 93.96 E-value: 8.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 127 WERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTTSSPE--ACQYIAHDCR 201
Cdd:PRK12582 78 WRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHDhaKLKHLFDLVK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 202 ANVIVVDTQKQLEKILKIwkdLPHLKAVVIYQEPPPKKMANVytmeELIELGQEVPEEALDAIIDTQQPNQCCVLVYTSG 281
Cdd:PRK12582 158 PRVVFAQSGAPFARALAA---LDLLDVTVVHVTGPGEGIASI----AFADLAATPPTAAVAAAIAAITPDTVAKYLFTSG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 282 TTGNPKGVMLSQDNITwtaryGSQAGDIQ----PAEVQQEVVVSYLPLSHIAA--QIYD--LWTG----IQWGAQVcfad 349
Cdd:PRK12582 231 STGMPKAVINTQRMMC-----ANIAMQEQlrprEPDPPPPVSLDWMPWNHTMGgnANFNglLWGGgtlyIDDGKPL---- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 350 PDALKGTLVNtLREVEPTSHMGVPRVWEKIMERIQ--EVAAQSGFIRRKMLLWAmsvtleqnltcpsndlkpfTSRLADY 427
Cdd:PRK12582 302 PGMFEETIRN-LREISPTVYGNVPAGYAMLAEAMEkdDALRRSFFKNLRLMAYG-------------------GATLSDD 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 428 LvLARVrQALGfakcqknfygaapmTAETqrfflGLNIRLYAGYGLSE----STGPHFMSSpynyRLYSSGRVVPGCRVK 503
Cdd:PRK12582 362 L-YERM-QALA--------------VRTT-----GHRIPFYTGYGATEtaptTTGTHWDTE----RVGLIGLPLPGVELK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 504 LVNqdadgIG---EICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGR-LDDD----GfLYITGRLKELIITAGGE-- 573
Cdd:PRK12582 417 LAP-----VGdkyEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfVDPDdpekG-LIFDGRVAEDFKLSTGTwv 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 574 NVPPVPIeEAVKMELPIISSAMLIGDQRKFLSMLltlkCTLNPETseptdnlteqavefCQR-VGSKASTVSEIVgqKDE 652
Cdd:PRK12582 491 SVGTLRP-DAVAACSPVIHDAVVAGQDRAFIGLL----AWPNPAA--------------CRQlAGDPDAAPEDVV--KHP 549
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19705503 653 AVYQAIHEGIQRVNANAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKDIIDSFYQE 718
Cdd:PRK12582 550 AVLAILREGLSAHNAEAGGSSSRIARALLMTEPPSIDAGEITDKGYINQRAVLERRAALVERLYAE 615
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
151-598 |
1.43e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 92.36 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 151 LERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKQLEKILKIWKDLpHLKAVV 230
Cdd:PRK07787 42 VAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPAPDDPAGLPHVPVRL-HARSWH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 231 IYQEPPPKKMAnvytmeeLIelgqevpeealdaiidtqqpnqccvlVYTSGTTGNPKGVMLSQDNIT-----------WT 299
Cdd:PRK07787 121 RYPEPDPDAPA-------LI--------------------------VYTSGTTGPPKGVVLSRRAIAadldalaeawqWT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 300 ARygsqagdiqpaevqqEVVVSYLPLSHIAAQIYDLWTGIQWGAQV---------CFADPDALKGTLVntlreveptshM 370
Cdd:PRK07787 168 AD---------------DVLVHGLPLFHVHGLVLGVLGPLRIGNRFvhtgrptpeAYAQALSEGGTLY-----------F 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 371 GVPRVWEkimeRIQEVAAQSGFIRRKMLLWAMSVTLeqnltcpsndlkPFTsrladylVLARVRQALGFAKCQKnfYGaa 450
Cdd:PRK07787 222 GVPTVWS----RIAADPEAARALRGARLLVSGSAAL------------PVP-------VFDRLAALTGHRPVER--YG-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 451 pMTaETqrfFLGLNIRlyagyglseSTGPHfmsspynyRLYSSGRVVPGCRVKLVNQD-----ADG--IGEICLWGRTIF 523
Cdd:PRK07787 275 -MT-ET---LITLSTR---------ADGER--------RPGWVGLPLAGVETRLVDEDggpvpHDGetVGELQVRGPTLF 332
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19705503 524 MGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:PRK07787 333 DGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETAL-LGHPGVREAAVVG 406
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
448-598 |
2.62e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 92.21 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 448 GAAPMTAETQRFFLGL--NIRLYAGYGLSEST--GPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDA------DGIGEICL 517
Cdd:PLN02574 327 GAAPLSGKFIQDFVQTlpHVDFIQGYGMTESTavGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTgcllppGNCGELWI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 518 WGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIeEAVKMELPIISSAMLI 597
Cdd:PLN02574 407 QGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKE-IIKYKGFQIAPADL-EAVLISHPEIIDAAVT 484
|
.
gi 19705503 598 G 598
Cdd:PLN02574 485 A 485
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
238-584 |
3.53e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 91.75 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 238 KKMANVYTMEELIEL------GQEVPEEALDAiidtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWT-----ARYGSQA 306
Cdd:PRK05677 173 KKMVPAYHLPQAVKFndalakGAGQPVTEANP-----QADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqcrALMGSNL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 307 GDiqpaevQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCFADPDALKGtLVNTLREVEPTSHMGVPRVWEKIMERiqe 385
Cdd:PRK05677 248 NE------GCEILIAPLPLYHIYAFTFHCMAMMLIGNHnILISNPRDLPA-MVKELGKWKFSGFVGLNTLFVALCNN--- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 386 vaaqSGFirRKMLLWAMSVTLEQNLTcpsndlkpftsrladyLVLARvrqalgfAKCQKNFYGAApmtaetqrfflglni 465
Cdd:PRK05677 318 ----EAF--RKLDFSALKLTLSGGMA----------------LQLAT-------AERWKEVTGCA--------------- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 466 rLYAGYGLSEsTGPHFMSSPYNY-RLYSSGRVVPGCRVKLVNQDAD-----GIGEICLWGRTIFMGYLNMEDKTHEAIDS 539
Cdd:PRK05677 354 -ICEGYGMTE-TSPVVSVNPSQAiQVGTIGIPVPSTLCKVIDDDGNelplgEVGELCVKGPQVMKGYWQRPEATDEILDS 431
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 19705503 540 EGWLHTGDMGRLDDDGFLYITGRLKELIITAGGeNVPPVPIEEAV 584
Cdd:PRK05677 432 DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGF-NVYPNELEDVL 475
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
129-598 |
4.49e-19 |
|
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: 90.62 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVd 208
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 209 tqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielGQEVPEEALdaiidtqqpnqccvLVYTSGTTGNPKG 288
Cdd:cd05935 80 --------------------------------------------GSELDDLAL--------------IPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 289 VMLSQDNITWTARYGSQAGDIQPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGaqvcfadpdalkGTLVntlrevepts 368
Cdd:cd05935 102 CMHTHFSAAANALQSAVWTGLTPSDV----ILACLPLFHVTGFVGSLNTAVYVG------------GTYV---------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 369 hmgvprvwekIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTcpsNDLKPFTSRLADYLVLARvrqalgfakcqknfyG 448
Cdd:cd05935 156 ----------LMARWDRETALELIEKYKVTFWTNIPTMLVDLL---ATPEFKTRDLSSLKVLTG---------------G 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 449 AAPM-TAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGrvVPGCRVKLVNQDA-DGI-------GEICLWG 519
Cdd:cd05935 208 GAPMpPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLG--IP*FGVDARVIDIeTGRelppnevGEIVVRG 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 520 RTIFMGYLNMEDKTHEA---IDSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGEnVPPVPIeEAVKMELPIISSAML 596
Cdd:cd05935 286 PQIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK-VWPAEV-EAKLYKHPAI*EVCV 363
|
..
gi 19705503 597 IG 598
Cdd:cd05935 364 IS 365
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
464-598 |
1.54e-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: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 464 NIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDADGIGEICLWGRTIFMGYLNMEdktheAIDSEGWL 543
Cdd:cd17633 136 KANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGG-----FSNPDGWM 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19705503 544 HTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISSAMLIG 598
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLK-AIPGIEEAIVVG 263
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
276-594 |
1.61e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 89.73 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 276 LVYTSGTTGNPKGVMLSQDNITwtARYGSQAGDIQPA-EVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCFADPDAL 353
Cdd:PRK08974 211 LQYTGGTTGVAKGAMLTHRNML--ANLEQAKAAYGPLlHPGKELVVTALPLYHIFALTVNCLLFIELGGQnLLITNPRDI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 354 KGtLVNTLREVEPTSHMGVPRVWEKIM--ERIQEVaaqsgfirrkmllwamsvtleqnltcpsndlkpftsrlaDYlvlA 431
Cdd:PRK08974 289 PG-FVKELKKYPFTAITGVNTLFNALLnnEEFQEL---------------------------------------DF---S 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 432 RVRQALGfakcqknfYGAAPMTAETQRFFLGLNIRLYAGYGLSESTgPHFMSSPYNYRLY--SSGRVVPGCRVKLVNQDA 509
Cdd:PRK08974 326 SLKLSVG--------GGMAVQQAVAERWVKLTGQYLLEGYGLTECS-PLVSVNPYDLDYYsgSIGLPVPSTEIKLVDDDG 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 510 -----DGIGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITAGGeNVPPVPIEEAV 584
Cdd:PRK08974 397 nevppGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGF-NVYPNEIEDVV 474
|
330
....*....|
gi 19705503 585 KMELPIISSA 594
Cdd:PRK08974 475 MLHPKVLEVA 484
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
265-573 |
2.11e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 89.78 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 265 IDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEVQQEVvvSYLPLSHIAAQIY---DLWTGIQ- 340
Cdd:PTZ00342 298 IQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKTHL--SYLPISHIYERVIaylSFMLGGTi 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 341 --WGAQVCFADPDalkgtLVNTLREVeptsHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPSNDLK 418
Cdd:PTZ00342 376 niWSKDINYFSKD-----IYNSKGNI----LAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILSLRKSNNNGGFSKFLE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 419 PFTSrladylVLARVRQALGfAKCQKNFYGAAPMTAETQR-FFLGLNIRLYAGYGLSESTGPHFMSSPYNYRLYS-SGRV 496
Cdd:PTZ00342 447 GITH------ISSKIKDKVN-PNLEVILNGGGKLSPKIAEeLSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESiGGPI 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 497 VPGCRVKLVN------QDADGIGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITA 570
Cdd:PTZ00342 520 SPNTKYKVRTwetykaTDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
...
gi 19705503 571 GGE 573
Cdd:PTZ00342 600 QGE 602
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
139-583 |
2.22e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 88.81 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 139 ARKVAKGFLKLGLERAHSVAILGFNSPEWFfsavgTVFAGGIVTGIYTT------SSPEAcQYIAHDCRANVIVVDtQKQ 212
Cdd:PRK08276 21 SNRLAHGLRALGLREGDVVAILLENNPEFF-----EVYWAARRSGLYYTpinwhlTAAEI-AYIVDDSGAKVLIVS-AAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 213 LEKILKIWKDLP-HLKAVVIYQEPPPkkmanvytmeelielGQEVPEEALDAIIDTQQPNQC--CVLVYTSGTTGNPKGV 289
Cdd:PRK08276 94 ADTAAELAAELPaGVPLLLVVAGPVP---------------GFRSYEEALAAQPDTPIADETagADMLYSSGTTGRPKGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 290 M--LSQDNITWTARYGSQAGDIQPAEVQQEVVVSYLPLSHIAAqiydlwtgIQWGAQVcfadpDALKGTLV--------N 359
Cdd:PRK08276 159 KrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAP--------LRFGMSA-----LALGGTVVvmekfdaeE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 360 TLREVE----PTSHMgVPrvwekIMeriqevaaqsgFIRrkMLlwamsvtleqnltcpsndlkpftsRLADylvlaRVRQ 435
Cdd:PRK08276 226 ALALIEryrvTHSQL-VP-----TM-----------FVR--ML------------------------KLPE-----EVRA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 436 ALGFAKCQKNFYGAAPMTAETQRFFL---GLNIRLYagYGLSESTGPHFMSS------PYnyrlySSGRVVPGcRVKLVN 506
Cdd:PRK08276 258 RYDVSSLRVAIHAAAPCPVEVKRAMIdwwGPIIHEY--YASSEGGGVTVITSedwlahPG-----SVGKAVLG-EVRILD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 507 QDADGI--GEIclwGrTIFM-------GYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPP 577
Cdd:PRK08276 330 EDGNELppGEI---G-TVYFemdgypfEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIIS-GGVNIYP 404
|
....*.
gi 19705503 578 VPIEEA 583
Cdd:PRK08276 405 QEIENL 410
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
255-562 |
2.26e-18 |
|
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: 88.35 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 255 EVPEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDiqpaevqqeVVVSY 322
Cdd:cd05930 70 SYPAERLAYILeDSGaklvltDPDDLAYVIYTSGSTGKPKGVMVEHRGLVnlllwMQEAYPLTPGD---------RVLQF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 323 LPLSHIAAqIYDLWTGIQWGAQVCFADPDALK--GTLVNTLREVEPTSHMGVPRVWekimeriqevaaqsgfirrkmllw 400
Cdd:cd05930 141 TSFSFDVS-VWEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTPSLL------------------------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 401 amSVTLEQNLTCPSNDLKpftsrladYLVLarvrqalgfakcqknfyGAAPMTAETQRFFLGL--NIRLYAGYGLSEST- 477
Cdd:cd05930 196 --RLLLQELELAALPSLR--------LVLV-----------------GGEALPPDLVRRWRELlpGARLVNLYGPTEATv 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 478 GPHFMSSPYNYRLYSS---GRVVPGCRVKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDKTHEAI-----DSEGWLH 544
Cdd:cd05930 249 DATYYRVPPDDEEDGRvpiGRPIPNTRVYVLDENlrpvPPGvPGELYIGGAGLARGYLNRPELTAERFvpnpfGPGERMY 328
|
330
....*....|....*....
gi 19705503 545 -TGDMGRLDDDGFLYITGR 562
Cdd:cd05930 329 rTGDLVRWLPDGNLEFLGR 347
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
131-632 |
5.05e-18 |
|
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: 87.17 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 131 SYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVvdtq 210
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 211 kqlekilkiwkdlphlkavviyqepppkkmanvyTMEELIElgqevpeealdaiidTQQPNQCCVLVYTSGTTGNPKGVM 290
Cdd:cd05969 78 ----------------------------------TTEELYE---------------RTDPEDPTLLHYTSGTTGTPKGVL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 291 LSQDNITWTARYGSQAGDIQPAEVqqevvvsylplshiaaqiydLWtgiqwgaqvCFADPDALKGTLVNT----LREVEP 366
Cdd:cd05969 109 HVHDAMIFYYFTGKYVLDLHPDDI--------------------YW---------CTADPGWVTGTVYGIwapwLNGVTN 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 367 TSHMGV--PRVWEKIMERIqevaaqsgfirrKMLLWAMSVTLEQNLTcpsndlkpftsRLADYLVLARVRQALGFAKCqk 444
Cdd:cd05969 160 VVYEGRfdAESWYGIIERV------------KVTVWYTAPTAIRMLM-----------KEGDELARKYDLSSLRFIHS-- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 445 nfyGAAPMTAETQRFFLG-LNIRLYAGYGLSEsTGPHFMSspyNY-----RLYSSGRVVPGCRVKLVNQDADGI-----G 513
Cdd:cd05969 215 ---VGEPLNPEAIRWGMEvFGVPIHDTWWQTE-TGSIMIA---NYpcmpiKPGSMGKPLPGVKAAVVDENGNELppgtkG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 514 EICL---WgRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPI 590
Cdd:cd05969 288 ILALkpgW-PSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESAL-MEHPA 363
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 19705503 591 ISSAMLIGDQRKFLSMLLTLKCTLNPETsEPTDNLTEQAVEF 632
Cdd:cd05969 364 VAEAGVIGKPDPLRGEIIKAFISLKEGF-EPSDELKEEIINF 404
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
125-598 |
9.08e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 87.29 E-value: 9.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 125 DKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANV 204
Cdd:PRK07788 70 DERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 205 IVVDtQKQLEKILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEVPEEALdaiidtqqPNQCCVLVYTSGTTG 284
Cdd:PRK07788 150 LVYD-DEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKP--------PKPGGIVILTSGTTG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 285 NPKGVMLSQDNItwtarygsqagdiqPAEVQQevVVSYLPLSH-----IAAQIYDLWTGIQWgaQVCFAdpdaLKGTLVn 359
Cdd:PRK07788 221 TPKGAPRPEPSP--------------LAPLAG--LLSRVPFRAgettlLPAPMFHATGWAHL--TLAMA----LGSTVV- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 360 TLREVEPtshmgvprvwEKIMERIQEvaaqsgfiRRKMLLWAMSVTLEQNLTCPSNDL-KPFTSRLadylvlaRVRqalg 438
Cdd:PRK07788 278 LRRRFDP----------EATLEDIAK--------HKATALVVVPVMLSRILDLGPEVLaKYDTSSL-------KII---- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 439 fakcqknFYGAAPMTAET-QRFFLGLNIRLYAGYGlseSTGPHFMS--SPYNYRLYSS--GRVVPGCRVKLVnqDADG-- 511
Cdd:PRK07788 329 -------FVSGSALSPELaTRALEAFGPVLYNLYG---STEVAFATiaTPEDLAEAPGtvGRPPKGVTVKIL--DENGne 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 512 -----IGEICLWGRTIFMGYLNMEDKthEAIDseGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKm 586
Cdd:PRK07788 397 vprgvVGRIFVGNGFPFEGYTDGRDK--QIID--GLLSSGDVGYFDEDGLLFVDGRDDDMIVS-GGENVFPAEVEDLLA- 470
|
490
....*....|..
gi 19705503 587 ELPIISSAMLIG 598
Cdd:PRK07788 471 GHPDVVEAAVIG 482
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
274-598 |
1.42e-17 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 84.66 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 274 CVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEVqqevvvsYL---PLSHIaaqiydlwtgiqwgaqvcfadp 350
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTV-------FLnsgPLFHI---------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 351 dalkGTLVNTLrevePTSHMG-----VPRV-WEKIMERIQEVAAQSGFIrrkmllwaMSVTLEQNLTCPSNDLKPFTSrl 424
Cdd:cd17636 54 ----GTLMFTL----ATFHAGgtnvfVRRVdAEEVLELIEAERCTHAFL--------LPPTIDQIVELNADGLYDLSS-- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 425 adylvLARVRQALGFAkcqknfygaAPMTAETQRFFLGLnirlyAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKL 504
Cdd:cd17636 116 -----LRSSPAAPEWN---------DMATVDTSPWGRKP-----GGYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 505 VNQD----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDSeGWLHTGDMGRLDDDGFLYITGRlKELIITAGGENVPPVP 579
Cdd:cd17636 177 LDEDgrevPDGeVGEIVARGPTVMAGYWNRPEVNARRTRG-GWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYPAE 254
|
330
....*....|....*....
gi 19705503 580 IEEAVKmELPIISSAMLIG 598
Cdd:cd17636 255 VERCLR-QHPAVADAAVIG 272
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
129-598 |
1.59e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 86.30 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVD 208
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 209 TQKqLEKILKIWKDLPHLKAVVIyqepppkkMANVYTMEElielgQEVPEEALDAIIDTQQP---------NQCCVLVYT 279
Cdd:PRK07008 119 LTF-LPLVDALAPQCPNVKGWVA--------MTDAAHLPA-----GSTPLLCYETLVGAQDGdydwprfdeNQASSLCYT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 280 SGTTGNPKGVMLSQDNITWTArYGSQAGDIQPAEVqQEVVVSYLPLSHIAAqiydlWtGIQW-----GAQVCFADPDaLK 354
Cdd:PRK07008 185 SGTTGNPKGALYSHRSTVLHA-YGAALPDAMGLSA-RDAVLPVVPMFHVNA-----W-GLPYsapltGAKLVLPGPD-LD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 355 GTLVNTLREVEP-TSHMGVPRVWEKIMERIQEVAAQSGFIRRkmllwamsvTLEQNLTCPSNDLKPFTsrlADYLVlaRV 433
Cdd:PRK07008 256 GKSLYELIEAERvTFSAGVPTVWLGLLNHMREAGLRFSTLRR---------TVIGGSACPPAMIRTFE---DEYGV--EV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 434 RQALGfakcqknfygaapMTAETQrffLGLNIRLYAGY-GLSESTGPHfmsspynyRLYSSGRVVPGCRVKLVNQDA--- 509
Cdd:PRK07008 322 IHAWG-------------MTEMSP---LGTLCKLKWKHsQLPLDEQRK--------LLEKQGRVIYGVDMKIVGDDGrel 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 510 --DGI--GEICLWGRTIFMGYLNMEDKTHeaidSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEEaVK 585
Cdd:PRK07008 378 pwDGKafGDLQVRGPWVIDRYFRGDASPL----VDGWFPTGDVATIDADGFMQITDRSKD-VIKSGGEWISSIDIEN-VA 451
|
490
....*....|...
gi 19705503 586 MELPIISSAMLIG 598
Cdd:PRK07008 452 VAHPAVAEAACIA 464
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
257-602 |
5.84e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 84.71 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 257 PEEALDAIidtqqpnqcCVLVYTSGTTGNPKGVMLSQDNITWTArygSQAGDIQPAEVQQEVVVSYLPLSHIAAQ----I 332
Cdd:PRK06178 204 PPPALDAL---------AALNYTGGTTGMPKGCEHTQRDMVYTA---AAAYAVAVVGGEDSVFLSFLPEFWIAGEnfglL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 333 YDLWTGI------QWGAQVCFADPDALKGT----LVNTLREVeptshMGVPRVWEKIMERIQEVAAQSgFIRRkmllwam 402
Cdd:PRK06178 272 FPLFSGAtlvllaRWDAVAFMAAVERYRVTrtvmLVDNAVEL-----MDHPRFAEYDLSSLRQVRVVS-FVKK------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 403 svtleqnltcpsndLKPFTSRladylvlaRVRQALGFAKcqknFYGAAPMTaETQ---RFFLGLNIrlyAGYGLSesTGP 479
Cdd:PRK06178 339 --------------LNPDYRQ--------RWRALTGSVL----AEAAWGMT-ETHtcdTFTAGFQD---DDFDLL--SQP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 480 HFMSSPynyrlyssgrvVPGCRVKLVNQDADGI------GEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDD 553
Cdd:PRK06178 387 VFVGLP-----------VPGTEFKICDFETGELlplgaeGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDE 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 19705503 554 DGFLYITGRLKELIITAGGENVPPvpiE-EAVKMELPIISSAMLIG--DQRK 602
Cdd:PRK06178 455 QGFLHYLGRRKEMLKVNGMSVFPS---EvEALLGQHPAVLGSAVVGrpDPDK 503
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
80-587 |
8.47e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 84.29 E-value: 8.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 80 TTRADGRVRlRLEPFCTqlpytvhqmFYEALDkYGNLSALGFKRKD-KWERISYYQYYLI---ARKVAKGFLKLGLERAH 155
Cdd:PRK09192 7 TPTTSSLPR-RYADFPT---------LVEALD-YAALGEAGMNFYDrRGQLEEALPYQTLrarAEAGARRLLALGLKPGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 156 SVAILGFNSPEW---FFSAVgtvFAGG------IVTGIyttSSPEAcqYIAH------DCRANVIVVDtqkqlekilKIW 220
Cdd:PRK09192 76 RVALIAETDGDFveaFFACQ---YAGLvpvplpLPMGF---GGRES--YIAQlrgmlaSAQPAAIITP---------DEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 221 KDLphLKAVVIYQEPPpkkmaNVYTMEELIELgqevpeEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTA 300
Cdd:PRK09192 139 LPW--VNEATHGNPLL-----HVLSHAWFKAL------PEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 301 RYGSQAG-DIQPAEVqqevVVSYLPLSHiaaqiyDLwtgiqwGAQVCFADPDALKGTlVNTLrevePTSHMGV-PRVWEK 378
Cdd:PRK09192 206 RAISHDGlKVRPGDR----CVSWLPFYH------DM------GLVGFLLTPVATQLS-VDYL----PTRDFARrPLQWLD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 379 IMERiqevaaQSGFIrrkmllwAMSVTLEQNLtCPsndLKPFTSRLADyLVLARVRQAlGFakcqknfyGAAPMTAETQR 458
Cdd:PRK09192 265 LISR------NRGTI-------SYSPPFGYEL-CA---RRVNSKDLAE-LDLSCWRVA-GI--------GADMIRPDVLH 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 459 FF------LGLNIRLY-AGYGLSEST------------------------GPHFMSSPYNYRLYSS----GRVVPGCRVK 503
Cdd:PRK09192 318 QFaeafapAGFDDKAFmPSYGLAEATlavsfsplgsgivveevdrdrleyQGKAVAPGAETRRVRTfvncGKALPGHEIE 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 504 LVNQDAD-----GIGEICLWGRTIFMGYLNMEDkTHEAIDSEGWLHTGDMGRLDDdGFLYITGRLKELIITaGGENVPPV 578
Cdd:PRK09192 398 IRNEAGMplperVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLGYLLD-GYLYITGRAKDLIII-NGRNIWPQ 474
|
....*....
gi 19705503 579 PIEEAVKME 587
Cdd:PRK09192 475 DIEWIAEQE 483
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
128-584 |
2.41e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 82.97 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 207
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DTQ--KQLEKILKIWKD------LPHLKAVVIYQEPPPKKMA-----NVYTMEELIELGQevPEEALdaiidtQQPN--- 271
Cdd:PLN02479 124 DQEffTLAEEALKILAEkkkssfKPPLLIVIGDPTCDPKSLQyalgkGAIEYEKFLETGD--PEFAW------KPPAdew 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 272 QCCVLVYTSGTTGNPKGVMLSQ---------DNITWTARYGSqagdiqpaevqqeVVVSYLPLSHIAAQIYdlwtgiQWG 342
Cdd:PLN02479 196 QSIALGYTSGTTASPKGVVLHHrgaylmalsNALIWGMNEGA-------------VYLWTLPMFHCNGWCF------TWT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 343 AQvcfadpdALKGTLVnTLREVEPTShmgvprvwekimerIQEVAAQSGFIRrkmlLWAMSVTLEQNLTCPSNDlkpfts 422
Cdd:PLN02479 257 LA-------ALCGTNI-CLRQVTAKA--------------IYSAIANYGVTH----FCAAPVVLNTIVNAPKSE------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 423 rlaDYLVLARVRQAlgfakcqkNFYGAAP----MTAETQRFFlglniRLYAGYGLSESTGPHFM--------SSPYNYRL 490
Cdd:PLN02479 305 ---TILPLPRVVHV--------MTAGAAPppsvLFAMSEKGF-----RVTHTYGLSETYGPSTVcawkpewdSLPPEEQA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 491 YSSGR------------VVPGCRVKLVNQDADGIGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLY 558
Cdd:PLN02479 369 RLNARqgvryiglegldVVDTKTMKPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIE 447
|
490 500
....*....|....*....|....*.
gi 19705503 559 ITGRLKELIITaGGENVPPVPIEEAV 584
Cdd:PLN02479 448 IKDRSKDIIIS-GGENISSLEVENVV 472
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
128-633 |
4.92e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 81.66 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFfsavgTVFAGGIVTGIYTTS-----SPEACQYIAHDCRA 202
Cdd:PRK13391 23 EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYL-----EVCWAAERSGLYYTCvnshlTPAEAAYIVDDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 203 NVIVVdTQKQLEKILKIWKDLPHLKAVVIYQEPPpkkmanvyTMEELIELgqevpEEALDAIIDTQQPNQC--CVLVYTS 280
Cdd:PRK13391 98 RALIT-SAAKLDVARALLKQCPGVRHRLVLDGDG--------ELEGFVGY-----AEAVAGLPATPIADESlgTDMLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 281 GTTGNPKGVM--LS----QDNITWTA------RYGSQAGDIQPAevqqevvvsylPLSHIAAQiydLWTGIQwgaqvcfa 348
Cdd:PRK13391 164 GTTGRPKGIKrpLPeqppDTPLPLTAflqrlwGFRSDMVYLSPA-----------PLYHSAPQ---RAVMLV-------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 349 dpDALKGTLVnTLREVEPtshmgvprvwEKIMERIQEVAaqsgfIRRKMLLWAMSVTLeqnLTCPsndlkpftsrladyl 428
Cdd:PRK13391 222 --IRLGGTVI-VMEHFDA----------EQYLALIEEYG-----VTHTQLVPTMFSRM---LKLP--------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 429 vlARVRQALGFAKCQKNFYGAAPMTAETQRFFL---GLNIRLYagYGLSESTGPHFMSSP-YNYRLYSSGRVVPGcrvKL 504
Cdd:PRK13391 266 --EEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIdwwGPIIHEY--YAATEGLGFTACDSEeWLAHPGTVGRAMFG---DL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 505 VNQDADG-------IGEICLWGRTIFMgYLNMEDKTHEAIDSEG-WLHTGDMGRLDDDGFLYITGRLKELIITaGGENVP 576
Cdd:PRK13391 339 HILDDDGaelppgePGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIIS-GGVNIY 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 577 PVPIEEAVkMELPIISSAMLIG--DQrkflSMLLTLKCTLNP-ETSEPTDNLTEQAVEFC 633
Cdd:PRK13391 417 PQEAENLL-ITHPKVADAAVFGvpNE----DLGEEVKAVVQPvDGVDPGPALAAELIAFC 471
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
129-601 |
7.66e-16 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 81.02 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 129 RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSP-EACQYIAHDCRANVIVV 207
Cdd:cd05923 28 RLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAaELAELIERGEMTAAVIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DTQKQLEKILKiwkdlphlkavviyqepppkKMANVYTMEELIELGqeVPEEALDAIIDTQ-QPNQCCVLVYTSGTTGNP 286
Cdd:cd05923 108 VDAQVMDAIFQ--------------------SGVRVLALSDLVGLG--EPESAGPLIEDPPrEPEQPAFVFYTSGTTGLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 287 KGVMLSQDNITWTARYGS-QAGDIQPAevqQEVVVSYLPLSHIAaqiydlwtgiqwGAQVCFADPDALKGTLVnTLREVE 365
Cdd:cd05923 166 KGAVIPQRAAESRVLFMStQAGLRHGR---HNVVLGLMPLYHVI------------GFFAVLVAALALDGTYV-VVEEFD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 366 PTSHMgvprvweKIMERiQEVAAqsgfirrkmlLWAmSVTLEQNLTcpsndlkpfTSRLADYLVLARVRQaLGFAkcqkn 445
Cdd:cd05923 230 PADAL-------KLIEQ-ERVTS----------LFA-TPTHLDALA---------AAAEFAGLKLSSLRH-VTFA----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 446 fyGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPHFMSSPYNYR-----LYSSGRVVP--GCRVKLVNQDADGIGEICLW 518
Cdd:cd05923 276 --GATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDARTGTemrpgFFSEVRIVRigGSPDEALANGEEGELIVAAA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 519 GRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKMElPIISSAMLIG 598
Cdd:cd05923 354 ADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHPSEIERVLSRH-PGVTEVVVIG 430
|
....*
gi 19705503 599 --DQR 601
Cdd:cd05923 431 vaDER 435
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
128-601 |
9.70e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 80.70 E-value: 9.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTtssPEACQYIAHDCRANV 204
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyrYV---EDELRYLLDDSDAVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 205 IVVDTQkQLEKILKIWKDLPHLK-AVVIYQEPPPKKMANVYTMEELIELG---QEVPEEALDAIIdtqqpnqccvLVYTS 280
Cdd:PRK07798 104 LVYERE-FAPRVAEVLPRLPKLRtLVVVEDGSGNDLLPGAVDYEDALAAGspeRDFGERSPDDLY----------LLYTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 281 GTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEVQQEVVVSYL-----------PLSHIAAQiydlWTGIQwgaqvcfad 349
Cdd:PRK07798 173 GTTGMPKGVMWRQEDIFRVLLGGRDFATGEPIEDEEELAKRAAagpgmrrfpapPLMHGAGQ----WAAFA--------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 350 pdAL--KGTLVntlreVEPTSHMGVPRVWEKI-MERIQEVAaqsgfirrkMLLWAMSVTLEQNLTCPSN-DLkpftSRLA 425
Cdd:PRK07798 240 --ALfsGQTVV-----LLPDVRFDADEVWRTIeREKVNVIT---------IVGDAMARPLLDALEARGPyDL----SSLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 426 dylVLARvrqalgfakcqknfyGAAPMTAETQRFFLGL--NIRLYAGYGLSEsTGphFMSSPYNyrlySSG-------RV 496
Cdd:PRK07798 300 ---AIAS---------------GGALFSPSVKEALLELlpNVVLTDSIGSSE-TG--FGGSGTV----AKGavhtggpRF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 497 VPGCRVKLVNQD-------ADGIGEICLWGRtIFMGYLNMEDKTHEA---IDSEGWLHTGDMGRLDDDGFLYITGRlKEL 566
Cdd:PRK07798 355 TIGPRTVVLDEDgnpvepgSGEIGWIARRGH-IPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGR-GSV 432
|
490 500 510
....*....|....*....|....*....|....*..
gi 19705503 567 IITAGGENVPPVPIEEAVKMElPIISSAMLIG--DQR 601
Cdd:PRK07798 433 CINTGGEKVFPEEVEEALKAH-PDVADALVVGvpDER 468
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
275-581 |
1.04e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 80.70 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 275 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSH----IAAQIYDLWTGiqwGAQVCFADP 350
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSP----RDATVAVMPLYHghglIAALLATLASG---GAVLLPARG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 351 DALKGTLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSG-----FIRrkmllwamsvtleqnlTCpSNDLKPFTSRLA 425
Cdd:PRK05852 253 RFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKpaalrFIR----------------SC-SAPLTAETAQAL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 426 DYLVLARVRQALGfakcqknfygaapMTAETQRfflgLNIRLYAGYGLSE----STGPHFMSSPYNYRLY-SSGRVVPgc 500
Cdd:PRK05852 316 QTEFAAPVVCAFG-------------MTEATHQ----VTTTQIEGIGQTEnpvvSTGLVGRSTGAQIRIVgSDGLPLP-- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 501 rvklvnqdADGIGEICLWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPI 580
Cdd:PRK05852 377 --------AGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKEL-INRGGEKISPERV 446
|
.
gi 19705503 581 E 581
Cdd:PRK05852 447 E 447
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
275-601 |
1.13e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 79.32 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 275 VLVYTSGTTGNPKGVMLSQDNITWTA-----RYGSQAgdiqpaevqQEVVVsyLPLSHIAaqiydlwtgiqwGAQVcfad 349
Cdd:PRK07824 39 LVVATSGTTGTPKGAMLTAAALTASAdathdRLGGPG---------QWLLA--LPAHHIA------------GLQV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 350 pdalkgtLV-NTLREVEPTShMGVPRVWEkIMERIQEVAAQSGFiRRKMLLWAMSvtLEQNLTCPSNdlkpfTSRLADY- 427
Cdd:PRK07824 92 -------LVrSVIAGSEPVE-LDVSAGFD-PTALPRAVAELGGG-RRYTSLVPMQ--LAKALDDPAA-----TAALAELd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 428 LVLArvrqalgfakcqknfyGAAPMTAETQRFFLGLNIRLYAGYGLSESTGphfmSSPYNyrlyssGRVVPGCRVKLVNq 507
Cdd:PRK07824 155 AVLV----------------GGGPAPAPVLDAAAAAGINVVRTYGMSETSG----GCVYD------GVPLDGVRVRVED- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 508 dadgiGEICLWGRTIFMGYLNMEDktHEAIDSEGWLHTGDMGRLDDdGFLYITGRLKElIITAGGENVPPVPIEEAVkME 587
Cdd:PRK07824 208 -----GRIALGGPTLAKGYRNPVD--PDPFAEPGWFRTDDLGALDD-GVLTVLGRADD-AISTGGLTVLPQVVEAAL-AT 277
|
330
....*....|....*.
gi 19705503 588 LPIISSAMLIG--DQR 601
Cdd:PRK07824 278 HPAVADCAVFGlpDDR 293
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
130-602 |
1.61e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 80.17 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 130 ISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV-- 207
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVwp 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 -----DTQKQLEKILKiwKDLPHLKAVVIYQE-----PPPKKMANVytmeelIELGQEVPEEALDAIIDTQQPNQCCVLV 277
Cdd:PRK06164 116 gfkgiDFAAILAAVPP--DALPPLRAIAVVDDaadatPAPAPGARV------QLFALPDPAPPAAAGERAADPDAGALLF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 278 YTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCFADPDAlkGTL 357
Cdd:PRK06164 188 TTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAV----LLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDA--ART 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 358 VNTLREVEPTSHMGVprvwEKIMERIQEVAAQSG-FIRRKMLLWAmsvtleqnltcpsndlkPFTSRLADYLVLARVRqa 436
Cdd:PRK06164 262 ARALRRHRVTHTFGN----DEMLRRILDTAGERAdFPSARLFGFA-----------------SFAPALGELAALARAR-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 437 lgfakcqknfygAAPMTaetqrfflGLnirlyagYGLSE-----STGPhfMSSPYNYRLYSSGRVV-PGCRVKLVNQDAD 510
Cdd:PRK06164 319 ------------GVPLT--------GL-------YGSSEvqalvALQP--ATDPVSVRIEGGGRPAsPEARVRARDPQDG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 511 GI------GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDG-FLYITgRLKElIITAGGENVPPVPIEEA 583
Cdd:PRK06164 370 ALlpdgesGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGqFVYQT-RMGD-SLRLGGFLVNPAEIEHA 447
|
490
....*....|....*....
gi 19705503 584 VKmELPIISSAMLIGDQRK 602
Cdd:PRK06164 448 LE-ALPGVAAAQVVGATRD 465
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
104-562 |
4.91e-15 |
|
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: 78.12 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 104 QMFYEALDKYGNLSALgfkrKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 183
Cdd:cd17653 1 DAFERIAAAHPDAVAV----ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 184 IYTTSSPEACQYIAHDCRANVIVVDTQkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealda 263
Cdd:cd17653 77 LDAKLPSARIQAILRTSGATLLLTTDS----------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 264 iidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITwtaRYGSQAGDIQPAEVQQEVvvsyLPLSHIA--AQIYDLWTGIQW 341
Cdd:cd17653 104 ------PDDLAYIIFTSGSTGIPKGVMVPHRGVL---NYVSQPPARLDVGPGSRV----AQVLSIAfdACIGEIFSTLCN 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 342 GAQVCFADPDAlkgTLVNTLREVEPTshMGVPRVWEkimeriqevaaqsgfirrkmllwamsvtleqnlTCPSNDLkpft 421
Cdd:cd17653 171 GGTLVLADPSD---PFAHVARTVDAL--MSTPSILS---------------------------------TLSPQDF---- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 422 SRLaDYLVLArvrqalgfakcqknfyGAAPMTAETQRFflGLNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCR 501
Cdd:cd17653 209 PNL-KTIFLG----------------GEAVPPSLLDRW--SPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNST 269
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19705503 502 VKLVNQD-----ADGIGEICLWGRTIFMGYLNMEDKT----HEAIDSEGWLH--TGDMGRLDDDGFLYITGR 562
Cdd:cd17653 270 CYILDADlqpvpEGVVGEICISGVQVARGYLGNPALTaskfVPDPFWPGSRMyrTGDYGRWTEDGGLEFLGR 341
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
268-587 |
4.92e-15 |
|
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: 78.30 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 268 QQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQpaevQQEVVVSYLPLSH----IAAQIYDLWTGIQwga 343
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWK----TKDRILSWMPLTHdmglIAFHLAPLIAGMN--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 344 qvcfadpdalkgtlvntlreveptshmgvprvwekimeriQEVAAQSGFIRRKML-LWAMSVTLEQNLTCPSNDLKPFTS 422
Cdd:cd05908 176 ----------------------------------------QYLMPTRLFIRRPILwLKKASEHKATIVSSPNFGYKYFLK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 423 RLADYLV----LARVRQALGfakcqknfyGAAPMTAETQRFFL------GLNIR-LYAGYGLSEST--------GPHFM- 482
Cdd:cd05908 216 TLKPEKAndwdLSSIRMILN---------GAEPIDYELCHEFLdhmskyGLKRNaILPVYGLAEASvgaslpkaQSPFKt 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 483 -------------------SSPYNYRLYSSGRVVPGCRVKLVNQDADG-----IGEICLWGRTIFMGYLNMEDKTHEAID 538
Cdd:cd05908 287 itlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICDEDNKIlpdgyIGHIQIRGKNVTPGYYNNPEATAKVFT 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 19705503 539 SEGWLHTGDMGrLDDDGFLYITGRLKELIITaGGENVPPVPIEE-AVKME 587
Cdd:cd05908 367 DDGWLKTGDLG-FIRNGRLVITGREKDIIFV-NGQNVYPHDIERiAEELE 414
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
128-636 |
2.97e-14 |
|
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: 75.59 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFL-KLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 206
Cdd:cd05958 9 REWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 207 VDtqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeEALDAIIDTqqpnqcCVLVYTSGTTGNP 286
Cdd:cd05958 89 CA--------------------------------------------------HALTASDDI------CILAFTSGTTGAP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 287 KGVM-LSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQvCFADPDALKGTLVNTLREVE 365
Cdd:cd05958 113 KATMhFHRDPLASADRYAVNVLRLRE----DDRFVGSPPLAFTFGLGGVLLFPFGVGAS-GVLLEEATPDLLLSAIARYK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 366 PTSHMGVPRVWEKIMERIQEVAAQSGFIRrkmllwaMSVTLEQNLTCPsndlkpftsrladylVLARVRQALGfakcqkn 445
Cdd:cd05958 188 PTVLFTAPTAYRAMLAHPDAAGPDLSSLR-------KCVSAGEALPAA---------------LHRAWKEATG------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 446 fygaapmtaetqrfflglnIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVnqDADG-------IGEICLW 518
Cdd:cd05958 239 -------------------IPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVV--DDEGnpvpdgtIGRLAVR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 519 GRTifmGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:cd05958 298 GPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVEDVL-LQHPAVAECAVVG 372
|
490 500 510
....*....|....*....|....*....|....*...
gi 19705503 599 DQRKFLSMLLTLKCTLNPETSePTDNLTEQAVEFCQRV 636
Cdd:cd05958 373 HPDESRGVVVKAFVVLRPGVI-PGPVLARELQDHAKAH 409
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
267-586 |
4.51e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 75.44 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 267 TQQPNQCCVLVYTSGTTGNPKGVMLSQDNI--------TWTarygsQAGDIQPAEVQQEVVVSYLPLSHIAAQIYDLWTG 338
Cdd:PRK07059 200 KLGPDDVAFLQYTGGTTGVSKGATLLHRNIvanvlqmeAWL-----QPAFEKKPRPDQLNFVCALPLYHIFALTVCGLLG 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 339 IQWGA-QVCFADPDALKGtLVNTLREVEPTSHMGVPRVWEKIMEriqevaaQSGFirRKMllwamsvtleqnltcpsnDL 417
Cdd:PRK07059 275 MRTGGrNILIPNPRDIPG-FIKELKKYQVHIFPAVNTLYNALLN-------NPDF--DKL------------------DF 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 418 KPftsrladyLVLArvrqalgfakcqkNFYGAAPMTAETQRFFLGLNIRLYAGYGLSEsTGPHFMSSPYNYRLYSS--GR 495
Cdd:PRK07059 327 SK--------LIVA-------------NGGGMAVQRPVAERWLEMTGCPITEGYGLSE-TSPVATCNPVDATEFSGtiGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 496 VVPGCRVKLvnQDADG-------IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELII 568
Cdd:PRK07059 385 PLPSTEVSI--RDDDGndlplgePGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMIL 462
|
330
....*....|....*...
gi 19705503 569 TAGGeNVPPVPIEEAVKM 586
Cdd:PRK07059 463 VSGF-NVYPNEIEEVVAS 479
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
492-584 |
7.96e-14 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 74.26 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 492 SSGRVVPGCRVKLVNQDadgIGEICLWGRTIFMGYLNmedkthEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaG 571
Cdd:PRK07445 284 SSGQVLPHAQITIPANQ---TGNITIQAQSLALGYYP------QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-G 353
|
90
....*....|...
gi 19705503 572 GENVPPVPIEEAV 584
Cdd:PRK07445 354 GENVYPAEVEAAI 366
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
96-598 |
3.58e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 72.73 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 96 TQLPYTVHQMFYEALDKygNLSALGFKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTV 175
Cdd:PRK05857 10 PQLPSTVLDRVFEQARQ--QPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 176 FAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQKQLEkilkiwkdlphlkavviyQEPPPKKMANVYTMEELIELGQE 255
Cdd:PRK05857 88 KLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMA------------------SSAVPEALHSIPVIAVDIAAVTR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 256 VPEEALDAIIDTQQPN----QCCVLVYTSGTTGNPKGVMLSqdNITWTArygsqAGDIQPAE-------VQQEVVVSYLP 324
Cdd:PRK05857 150 ESEHSLDAASLAGNADqgseDPLAMIFTSGTTGEPKAVLLA--NRTFFA-----VPDILQKEglnwvtwVVGETTYSPLP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 325 LSHIAAqiydLW---TGIQWGAqVCFADpdalkGTLVNTLREVeptshmgvprvwekimeriqevaaqsgfirrkmllwa 401
Cdd:PRK05857 223 ATHIGG----LWwilTCLMHGG-LCVTG-----GENTTSLLEI------------------------------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 402 mSVTLEQNLTCpsndLKP-FTSRLADYLVLARVR-QALGFAKcqknfYGAAPMTAETQRFFLGLNIRLYAGYGLSEsTGP 479
Cdd:PRK05857 256 -LTTNAVATTC----LVPtLLSKLVSELKSANATvPSLRLVG-----YGGSRAIAADVRFIEATGVRTAQVYGLSE-TGC 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 480 HFMSSPYNYRLYSS------GRVVPGCRVKLvnQDADGIGEIC-----------LWGRTI--FMGYLNMEDKTHEAIdSE 540
Cdd:PRK05857 325 TALCLPTDDGSIVKieagavGRPYPGVDVYL--AATDGIGPTApgagpsasfgtLWIKSPanMLGYWNNPERTAEVL-ID 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19705503 541 GWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPP---------VP-IEEAVKMELPIISSAMLIG 598
Cdd:PRK05857 402 GWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPdevdriaegVSgVREAACYEIPDEEFGALVG 468
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
269-602 |
4.91e-13 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 72.69 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 269 QPNQCCVLVYTSGTTGNPKGVMLSQDNItwtarygsQAGDIQPAEV----QQEVVVSYLPLSHiaaqiydlwtgiqwgaq 344
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNL--------LANRAQVAARidfsPEDKVFNALPVFH----------------- 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 345 vCFAdpdaLKGTLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFirrkmllwamsvtleqnltcpSNDlkpftSRL 424
Cdd:PRK06814 846 -SFG----LTGGLVLPLLSGVKVFLYPSPLHYRIIPELIYDTNATILF---------------------GTD-----TFL 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 425 ADYlvlARVRQALGFAKCQKNFYGAAPMTAETQRFFL-GLNIRLYAGYGLSEsTGPHF-MSSPYNYRLYSSGRVVPGCRV 502
Cdd:PRK06814 895 NGY---ARYAHPYDFRSLRYVFAGAEKVKEETRQTWMeKFGIRILEGYGVTE-TAPVIaLNTPMHNKAGTVGRLLPGIEY 970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 503 KLvnQDADGI---GEICLWGRTIFMGYLNMEDK-THEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPV 578
Cdd:PRK06814 971 RL--EPVPGIdegGRLFVRGPNVMLGYLRAENPgVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRF-AKIAGEMISLA 1046
|
330 340
....*....|....*....|....*
gi 19705503 579 PIEEAVKMELP-IISSAMLIGDQRK 602
Cdd:PRK06814 1047 AVEELAAELWPdALHAAVSIPDARK 1071
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
433-598 |
5.02e-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: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 433 VRQALGFAKCQKNFYGAAPMTAETQRFFLGL-NIRLYAGYGLSESTGPHFMSS------PYnyrlySSGRVVPGcRVKLV 505
Cdd:cd05929 237 VRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWgGPIIWEYYGGTEGQGLTIINGeewlthPG-----SVGRAVLG-KVHIL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 506 nqDADG-------IGEICLWGRTIFMgYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPV 578
Cdd:cd05929 311 --DEDGnevppgeIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIIS-GGVNIYPQ 386
|
170 180
....*....|....*....|
gi 19705503 579 PIEEAVkMELPIISSAMLIG 598
Cdd:cd05929 387 EIENAL-IAHPKVLDAAVVG 405
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
275-583 |
8.28e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 71.34 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 275 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEvqqEVVVSYLPLSHIAAQIYdLWTGIQWGAQVCFAdpdalk 354
Cdd:PRK05851 156 VLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAT---DVGCSWLPLYHDMGLAF-LLTAALAGAPLWLA------ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 355 gtlvntlrevePTSHMGV-PRVWekiMERIQEVAAqsgfirrkmllwamSVTLEQNLTcpSNDLKPFTSRLADyLVLARV 433
Cdd:PRK05851 226 -----------PTTAFSAsPFRW---LSWLSDSRA--------------TLTAAPNFA--YNLIGKYARRVSD-VDLGAL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 434 RQALGFAK---CQknfyGAAPMTAETQRFflGLNIR-LYAGYGLSESTGPHFMSSP---------------YNYRLYSSG 494
Cdd:PRK05851 275 RVALNGGEpvdCD----GFERFATAMAPF--GFDAGaAAPSYGLAESTCAVTVPVPgiglrvdevttddgsGARRHAVLG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 495 RVVPGCRVKLVNQDAD------GIGEICLWGRTIFMGYLNmedktHEAIDSEGWLHTGDMGRLDDDGfLYITGRLKELII 568
Cdd:PRK05851 349 NPIPGMEVRISPGDGAagvagrEIGEIEIRGASMMSGYLG-----QAPIDPDDWFPTGDLGYLVDGG-LVVCGRAKELIT 422
|
330
....*....|....*
gi 19705503 569 TAgGENVPPVPIEEA 583
Cdd:PRK05851 423 VA-GRNIFPTEIERV 436
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
86-562 |
9.82e-13 |
|
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: 71.81 E-value: 9.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 86 RVRLRLEPFCTQLPY----TVHQMFYEALDKYGNLSALGFKRkdkwERISYYQyyLIAR--KVAKGFLKLGLERAHSVAI 159
Cdd:COG1020 458 RQQLLAEWNATAAPYpadaTLHELFEAQAARTPDAVAVVFGD----QSLTYAE--LNARanRLAHHLRALGVGPGDLVGV 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 160 LGFNSPEWFFSAVGTVFAGGIvtgiYT---TSSPEA-CQYIAHDCRANVIVvdTQKQLEKilkiwkDLPHLKAVVIYQEP 235
Cdd:COG1020 532 CLERSLEMVVALLAVLKAGAA----YVpldPAYPAErLAYMLEDAGARLVL--TQSALAA------RLPELGVPVLALDA 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 236 PpkkmanvytmeeliELGQEvPEEALDAIIDTQQPnqCCVLvYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDiq 310
Cdd:COG1020 600 L--------------ALAAE-PATNPPVPVTPDDL--AYVI-YTSGSTGRPKGVMVEHRALVnllawMQRRYGLGPGD-- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 311 paevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFADPDALKGT--LVNTLREVEPTS-HMgVPRVWEKIMEriqevA 387
Cdd:COG1020 660 -------RVLQFASLSFDAS-VWEIFGALLSGATLVLAPPEARRDPaaLAELLARHRVTVlNL-TPSLLRALLD-----A 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 388 AQSGFIRRKMLLW---AMSVTLeqnltcpsndlkpftsrladylvLARVRQALGfakcqknfygaapmtaetqrfflglN 464
Cdd:COG1020 726 APEALPSLRLVLVggeALPPEL-----------------------VRRWRARLP-------------------------G 757
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 465 IRLYAGYGLSEST-----------GPHFMSSPYnyrlyssGRVVPGCRVKLVnqDADG-------IGEICLWGRTIFMGY 526
Cdd:COG1020 758 ARLVNLYGPTETTvdstyyevtppDADGGSVPI-------GRPIANTRVYVL--DAHLqpvpvgvPGELYIGGAGLARGY 828
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 19705503 527 LNMEDKTHEA-------IDSEGWLHTGDMGRLDDDGFLYITGR 562
Cdd:COG1020 829 LNRPELTAERfvadpfgFPGARLYRTGDLARWLPDGNLEFLGR 871
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
186-630 |
1.49e-12 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 70.56 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 186 TTSSPEACQYIAHDCRANVIVVDtQKQLEKILKIWKDLPHLKAVVIYQEPPPKkmanvYTMEELIE--LGQEVPeealda 263
Cdd:PRK13382 125 TSFAGPALAEVVTREGVDTVIYD-EEFSATVDRALADCPQATRIVAWTDEDHD-----LTVEVLIAahAGQRPE------ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 264 iidtQQPNQCCVLVYTSGTTGNPKGvmlsqdnitwtARYgSQAGDIQPAEVqqevVVSYLPLSH-----IAAQIYDLWtG 338
Cdd:PRK13382 193 ----PTGRKGRVILLTSGTTGTPKG-----------ARR-SGPGGIGTLKA----ILDRTPWRAeeptvIVAPMFHAW-G 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 339 IqwgAQVCFADpdALKGTLVN--------TLREVE---PTSHMGVPRVWEKIMERIQEVAAQsgFIRRKMLLWAMSvtle 407
Cdd:PRK13382 252 F---SQLVLAA--SLACTIVTrrrfdpeaTLDLIDrhrATGLAVVPVMFDRIMDLPAEVRNR--YSGRSLRFAAAS---- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 408 qnltcpsndlkpfTSRLADYLVLARVRQalgFAKCQKNFYGA--APMTAetqrfflglnirlyagyglsestgphfMSSP 485
Cdd:PRK13382 321 -------------GSRMRPDVVIAFMDQ---FGDVIYNNYNAteAGMIA---------------------------TATP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 486 YNYRLY--SSGRVVPGCRVKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDK-THEaidseGWLHTGDMGRLDDDGFL 557
Cdd:PRK13382 358 ADLRAApdTAGRPAEGTEIRILDQDfrevPTGeVGTIFVRNDTQFDGYTSGSTKdFHD-----GFMASGDVGYLDENGRL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 558 YITGRLKELIITaGGENVPPVPIEEAVkMELPIISSAMLIG-DQRKFLSML-----LTLKCTLNPET--SEPTDNLTEQA 629
Cdd:PRK13382 433 FVVGRDDEMIVS-GGENVYPIEVEKTL-ATHPDVAEAAVIGvDDEQYGQRLaafvvLKPGASATPETlkQHVRDNLANYK 510
|
.
gi 19705503 630 V 630
Cdd:PRK13382 511 V 511
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
130-591 |
1.55e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.74 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 130 ISYYQYYLIARKVAKGFlklgleRAHSV----AILGFNS-PEWFFSAVGTVFAGGIVTGIYttsSPEACQYiAHDCRANV 204
Cdd:PRK05691 41 LSYRDLDLRARTIAAAL------QARASfgdrAVLLFPSgPDYVAAFFGCLYAGVIAVPAY---PPESARR-HHQERLLS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 205 IVVDTQKQLekILKIWKDLPHLKAVVIYQEPPPKKMANVYTMEELIELGQEVPEEALDAIidtqqpnqcCVLVYTSGTTG 284
Cdd:PRK05691 111 IIADAEPRL--LLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPALQPDDI---------AFLQYTSGSTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 285 NPKGVMLSQDNIT---WTARYGSqAGDIQPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFADPDALkgtLVNTL 361
Cdd:PRK05691 180 LPKGVQVSHGNLVaneQLIRHGF-GIDLNP----DDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPAYF---LERPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 362 REVEPTSHM-----GVPR-VWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNltcpsnDLKPFTSRLAdylvlarvrq 435
Cdd:PRK05691 252 RWLEAISEYggtisGGPDfAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQD------SLERFAEKFA---------- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 436 ALGFAkcQKNF---YGAAPMT---AETQR----FFLGLNIRLYAGYGLSESTGPHFMSSpynyrlyssGRVVPGCRVKLV 505
Cdd:PRK05691 316 ACGFD--PDSFfasYGLAEATlfvSGGRRgqgiPALELDAEALARNRAEPGTGSVLMSC---------GRSQPGHAVLIV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 506 NQD-----ADG-IGEICLWGRTIFMGYL-NMED--KTHEAIDSEGWLHTGDMGRLDDdGFLYITGRLKELIITAgGENVP 576
Cdd:PRK05691 385 DPQslevlGDNrVGEIWASGPSIAHGYWrNPEAsaKTFVEHDGRTWLRTGDLGFLRD-GELFVTGRLKDMLIVR-GHNLY 462
|
490
....*....|....*
gi 19705503 577 PVPIEEAVKMELPII 591
Cdd:PRK05691 463 PQDIEKTVEREVEVV 477
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
128-598 |
1.82e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 207
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DTQkqlekilkiwkdlphLKAVVIYQEPPpkkmanvytMEELIELGQEVP-----EEALDAIID--TQQPnqC-CVLVYT 279
Cdd:PRK13390 103 SAA---------------LDGLAAKVGAD---------LPLRLSFGGEIDgfgsfEAALAGAGPrlTEQP--CgAVMLYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 280 SGTTGNPKGVmlsQDNITwtARYGSQAGDIQPAEV-------QQEVVVSYLPLSHIAAqiydlwtgIQWGAQVcfadpDA 352
Cdd:PRK13390 157 SGTTGFPKGI---QPDLP--GRDVDAPGDPIVAIArafydisESDIYYSSAPIYHAAP--------LRWCSMV-----HA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 353 LKGTLV--------NTLREVEP---TSHMGVPRVWEKIMERIQEVaaqsgfiRRKMLLWAMSVTLEQNLTCPSnDLKpft 421
Cdd:PRK13390 219 LGGTVVlakrfdaqATLGHVERyriTVTQMVPTMFVRLLKLDADV-------RTRYDVSSLRAVIHAAAPCPV-DVK--- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 422 SRLADYLvlarvrqalgfakcqknfygaAPMtaetqrfflglnirLYAGYGLSESTGPHFMSSP-YNYRLYSSGRVVPGc 500
Cdd:PRK13390 288 HAMIDWL---------------------GPI--------------VYEYYSSTEAHGMTFIDSPdWLAHPGSVGRSVLG- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 501 rvKLVNQDADG-------IGEICLWGRTIFMGYLNMEDKTHEAIDSEG--WLHTGDMGRLDDDGFLYITGRlKELIITAG 571
Cdd:PRK13390 332 --DLHICDDDGnelpagrIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADR-KSFMIISG 408
|
490 500
....*....|....*....|....*..
gi 19705503 572 GENVPPVPIEEAVKMElPIISSAMLIG 598
Cdd:PRK13390 409 GVNIYPQETENALTMH-PAVHDVAVIG 434
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
128-598 |
1.89e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 69.77 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 207
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DtqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqEVPEEALdaiidtqqpnqccvLVYTSGTTGNPK 287
Cdd:cd05971 85 D----------------------------------------------GSDDPAL--------------IIYTSGTTGPPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 288 GVMLSQdnitwtarygsqagdiqpaevqqEVVVSYLPLSHIAAQIY----DL-WTGIQWgaqvcfadpdALKGTLVNTLR 362
Cdd:cd05971 105 GALHAH-----------------------RVLLGHLPGVQFPFNLFprdgDLyWTPADW----------AWIGGLLDVLL 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 363 evePTSHMGVPRVWEKiMERIQEVAAQSgfirrkmLLWAMSVTleqNLTCPSNDLKPFtSRLADYLVLARVR-QALGFAk 441
Cdd:cd05971 152 ---PSLYFGVPVLAHR-MTKFDPKAALD-------LMSRYGVT---TAFLPPTALKMM-RQQGEQLKHAQVKlRAIATG- 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 442 cqknfyGAAPMTAETQRFFLGLNIRLYAGYGLSES---TGPHfmSSPYNYRLYSSGRVVPGCRVKLVNQDA-----DGIG 513
Cdd:cd05971 216 ------GESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNC--SALFPIKPGSMGKPIPGHRVAIVDDNGtplppGEVG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 514 EICLwgRT----IFMGYLNMEDKThEAIDSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEEAVkMELP 589
Cdd:cd05971 288 EIAV--ELpdpvAFLGYWNNPSAT-EKKMAGDWLLTGDLGRKDSDGYFWYVGRDDD-VITSSGYRIGPAEIEECL-LKHP 362
|
....*....
gi 19705503 590 IISSAMLIG 598
Cdd:cd05971 363 AVLMAAVVG 371
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
464-598 |
2.14e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 69.81 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 464 NIRLYAGYGLSESTGPHFMSSPYNYRLYSS-GRVVPGCRVKLVNQD-----ADGIGEICLWGRTIFMGYLNmEDKTHEAI 537
Cdd:PRK07638 279 YAKLYEFYGASELSFVTALVDEESERRPNSvGRPFHNVQVRICNEAgeevqKGEIGTVYVKSPQFFMGYII-GGVLAREL 357
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19705503 538 DSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISSAMLIG 598
Cdd:PRK07638 358 NADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIES-VLHEHPAVDEIVVIG 416
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
457-601 |
8.28e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 68.10 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 457 QRFFLGLNIRLYAGYGLSEsTGPHFMSSPYNYRLY--SSGRVVPGCRVKLVNQDADGIGEIcLWGRTIFMGYLNMEDKT- 533
Cdd:PRK13383 310 QRFMDTYGDILYNGYGSTE-VGIGALATPADLRDApeTVGKPVAGCPVRILDRNNRPVGPR-VTGRIFVGGELAGTRYTd 387
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19705503 534 ---HEAIDseGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKMElPIISSAMLIG--DQR 601
Cdd:PRK13383 388 gggKAVVD--GMTSTGDMGYLDNAGRLFIVGREDDMIIS-GGENVYPRAVENALAAH-PAVADNAVIGvpDER 456
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
257-562 |
1.79e-11 |
|
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: 67.18 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 257 PEEALDAIID--------TQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAevqqevvVSYLPLSHI 328
Cdd:cd05918 84 PLQRLQEILQdtgakvvlTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSE-------SRVLQFASY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 329 A--AQIYDLWTGIQWGAQVCfadpdalkgtlvntlreveptshmgVPRvwEKimERIQEVAaqsGFIRRKMLLWAMsvtl 406
Cdd:cd05918 157 TfdVSILEIFTTLAAGGCLC-------------------------IPS--EE--DRLNDLA---GFINRLRVTWAF---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 407 eqnLTcPSndlkpfTSRLAD--------YLVLarvrqalgfakcqknfyGAAPMTAETQRFFLGlNIRLYAGYGLSESTg 478
Cdd:cd05918 201 ---LT-PS------VARLLDpedvpslrTLVL-----------------GGEALTQSDVDTWAD-RVRLINAYGPAECT- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 479 phfMSSPYNYRLYSS-----GRVVpGCRVKLVNQD-------ADGIGEICLWGRTIFMGYLNMEDKTHEA-IDSEGWLH- 544
Cdd:cd05918 252 ---IAATVSPVVPSTdprniGRPL-GATCWVVDPDnhdrlvpIGAVGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKq 327
|
330 340
....*....|....*....|....*....
gi 19705503 545 -----------TGDMGRLDDDGFLYITGR 562
Cdd:cd05918 328 egsgrgrrlyrTGDLVRYNPDGSLEYVGR 356
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
268-571 |
2.39e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 67.04 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 268 QQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVcF 347
Cdd:PRK08043 362 QQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTP----NDRFMSALPLFHSFGLTVGLFTPLLTGAEV-F 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 348 ADPDALKGTLVNTLreveptshmgvprVWEkimeriqevaaqsgfiRRKMLLWAMSvtleqnltcpsndlkpftSRLADY 427
Cdd:PRK08043 437 LYPSPLHYRIVPEL-------------VYD----------------RNCTVLFGTS------------------TFLGNY 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 428 lvlARVRQALGFAKCQKNFYGAAPMTAETQRFFLG-LNIRLYAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVN 506
Cdd:PRK08043 470 ---ARFANPYDFARLRYVVAGAEKLQESTKQLWQDkFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLS 546
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19705503 507 qdADGI---GEICLWGRTIFMGYLNMED----KTHEAIDSEG-----WLHTGDMGRLDDDGFLYITGRLKELIITAG 571
Cdd:PRK08043 547 --VPGIeqgGRLQLKGPNIMNGYLRVEKpgvlEVPTAENARGemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
263-597 |
5.95e-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: 65.08 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 263 AIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAA--QIYDLWTGiq 340
Cdd:cd17649 86 GLLLTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTP----GDRELQFASFNFDGAheQLLPPLIC-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 341 wGAQVCFADPDALKGTlvNTLREVepTSHMGV------PRVWEKIMERIQEVAAqsgfiRRKMLLWAMSVTLEQnltcps 414
Cdd:cd17649 160 -GACVVLRPDELWASA--DELAEM--VRELGVtvldlpPAYLQQLAEEADRTGD-----GRPPSLRLYIFGGEA------ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 415 ndlkpftsrladylvlarvrqalgfakcqknfygaapMTAETQRFFLGLNIRLYAGYGLSES--TGPHFMSSPYNYRLYS 492
Cdd:cd17649 224 -------------------------------------LSPELLRRWLKAPVRLFNAYGPTEAtvTPLVWKCEAGAARAGA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 493 S---GRVVPGCRVKLVNQDA-----DGIGEICLWGRTIFMGYLNMEDKTHEAI-----DSEG--WLHTGDMGRLDDDGFL 557
Cdd:cd17649 267 SmpiGRPLGGRSAYILDADLnpvpvGVTGELYIGGEGLARGYLGRPELTAERFvpdpfGAPGsrLYRTGDLARWRDDGVI 346
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 19705503 558 YITGRLKELiITAGGENVPPVPIEEAVkMELPIISSAMLI 597
Cdd:cd17649 347 EYLGRVDHQ-VKIRGFRIELGEIEAAL-LEHPGVREAAVV 384
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
128-563 |
6.07e-11 |
|
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: 65.37 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 207
Cdd:cd12114 11 GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DtqkqlekilkiwkdlphlkavviyqEPPPKKMANVYTMEELIELGQEVPEEALDAiidTQQPNQCCVLVYTSGTTGNPK 287
Cdd:cd12114 91 D-------------------------GPDAQLDVAVFDVLILDLDALAAPAPPPPV---DVAPDDLAYVIFTSGSTGTPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 288 GVMLSQDN-----ITWTARYGSQAGDiqpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFADPDalkgtlvntlR 362
Cdd:cd12114 143 GVMISHRAalntiLDINRRFAVGPDD---------RVLALSSLSFDLS-VYDIFGALSAGATLVLPDEA----------R 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 363 EVEPTShmgvprvWEKIMERIQ-----EVAAQSgfirrKMLL-WAMSV-TLEQNLTCP--SNDLKPFT--SRLADYLVLA 431
Cdd:cd12114 203 RRDPAH-------WAELIERHGvtlwnSVPALL-----EMLLdVLEAAqALLPSLRLVllSGDWIPLDlpARLRALAPDA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 432 RVRqALGfakcqknfyGAapmtAETQrfflglnirLYAGYGLSESTGPHFMSSPYnyrlyssGRVVPGCRVKLVNQDA-- 509
Cdd:cd12114 271 RLI-SLG---------GA----TEAS---------IWSIYHPIDEVPPDWRSIPY-------GRPLANQRYRVLDPRGrd 320
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19705503 510 --DGI-GEICLWGRTIFMGYLNMEDKTHEA----IDSEGWLHTGDMGRLDDDGFLYITGRL 563
Cdd:cd12114 321 cpDWVpGELWIGGRGVALGYLGDPELTAARfvthPDGERLYRTGDLGRYRPDGTLEFLGRR 381
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
141-584 |
9.13e-11 |
|
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: 64.82 E-value: 9.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 141 KVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTgiyttssPEACQYIAHDcranvIVVDTQK-QLEKILKI 219
Cdd:cd05970 59 KTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAI-------PATHQLTAKD-----IVYRIESaDIKMIVAI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 220 WKDlphlkavvIYQEPPPKKMANVYTMEELIELGQEVPE--EALDAIIDTQQP-------------NQCCVLVYTSGTTG 284
Cdd:cd05970 127 AED--------NIPEEIEKAAPECPSKPKLVWVGDPVPEgwIDFRKLIKNASPdferptansypcgEDILLVYFSSGTTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 285 NPKgvMLSQDNitwtarygsqagdiqpaevqqevvvSYlPLSHIAAQIYdlWTGIqwgaqvcfaDPDALKGTLVNTlrev 364
Cdd:cd05970 199 MPK--MVEHDF-------------------------TY-PLGHIVTAKY--WQNV---------REGGLHLTVADT---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 365 eptshmGVPR-VWEKIMERIQEVAA-----QSGFIRRKML--LWAMSVTleqNLTCPsndlkPFTSRladYLVLARVRQa 436
Cdd:cd05970 236 ------GWGKaVWGKIYGQWIAGAAvfvydYDKFDPKALLekLSKYGVT---TFCAP-----PTIYR---FLIREDLSR- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 437 LGFAKCQKNFYGAAPMTAET-QRFFLGLNIRLYAGYGLSE-----STGPHFMSSPYnyrlySSGRVVPGCRVKLVNQDAD 510
Cdd:cd05970 298 YDLSSLRYCTTAGEALNPEVfNTFKEKTGIKLMEGFGQTEttltiATFPWMEPKPG-----SMGKPAPGYEIDLIDREGR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 511 GI-----GEICLwgRT-------IFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELIITAgGENVPPV 578
Cdd:cd05970 373 SCeageeGEIVI--RTskgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS-GYRIGPF 448
|
....*.
gi 19705503 579 PIEEAV 584
Cdd:cd05970 449 EVESAL 454
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
275-598 |
1.29e-10 |
|
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: 64.08 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 275 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAEVqqevvvsylplshiaaqiydLWtgiqwgaqvCFADPD--- 351
Cdd:cd05973 92 VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS--------------------FW---------NAADPGway 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 352 ----ALKGTLVNTLREVEPTSHMGVPRVWeKIMER--IQEVAAQSGFIRrkmLLWAMSVTLEQNLTcpsndlkpftsrla 425
Cdd:cd05973 143 glyyAITGPLALGHPTILLEGGFSVESTW-RVIERlgVTNLAGSPTAYR---LLMAAGAEVPARPK-------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 426 dyLVLARVRQAlgfakcqknfygAAPMTAETQRFF---LGLNIRLYagYGLSESTGP----HFMSSPYnyRLYSSGRVVP 498
Cdd:cd05973 205 --GRLRRVSSA------------GEPLTPEVIRWFdaaLGVPIHDH--YGQTELGMVlanhHALEHPV--HAGSAGRAMP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 499 GCRVKLVNQDADGIGE-------------ICLWgrtiFMGYLNMEDKtheAIDSeGWLHTGDMGRLDDDGFLYITGRLKE 565
Cdd:cd05973 267 GWRVAVLDDDGDELGPgepgrlaidiansPLMW----FRGYQLPDTP---AIDG-GYYLTGDTVEFDPDGSFSFIGRADD 338
|
330 340 350
....*....|....*....|....*....|...
gi 19705503 566 LIITAgGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:cd05973 339 VITMS-GYRIGPFDVESAL-IEHPAVAEAAVIG 369
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
276-601 |
1.37e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 63.56 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 276 LVYTSGTTGNPKGVMLSQDNItwtarYGSQAG-------------DIQPAEVQQEVVVSYL--PLSHIAAQiydlWT--- 337
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDI-----FRMLMGgadfgtgeftpseDAHKAAAAAAGTVMFPapPLMHGTGS----WTafg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 338 GIQWGAQVCFADP--DAlkgtlVNTLREVEPtshmgvprvwekimERIQEVAAQSGFIRRKMLlwamsVTLEQNLTCPSN 415
Cdd:cd05924 79 GLLGGQTVVLPDDrfDP-----EEVWRTIEK--------------HKVTSMTIVGDAMARPLI-----DALRDAGPYDLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 416 DLKPFTSrladylvlarvrqalgfakcqknfyGAAPMTAETQRFFLGL--NIRLYAGYGLSESTgphFMSSPYN-YRLYS 492
Cdd:cd05924 135 SLFAISS-------------------------GGALLSPEVKQGLLELvpNITLVDAFGSSETG---FTGSGHSaGSGPE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 493 SG-RVVPGCRVKLVNQD-------ADGIGEICLWGRtIFMGYLNMEDKTHEA---IDSEGWLHTGDMGRLDDDGFLYITG 561
Cdd:cd05924 187 TGpFTRANPDTVVLDDDgrvvppgSGGVGWIARRGH-IPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLG 265
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 19705503 562 RlKELIITAGGENVPPVPIEEAVKMElPIISSAMLIG--DQR 601
Cdd:cd05924 266 R-GSVCINTGGEKVFPEEVEEALKSH-PAVYDVLVVGrpDER 305
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
157-600 |
1.70e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 64.28 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 157 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEA-CQYIAH-DCRanVIVVDTQ--KQLEKIlkiwkDLPHLKAVVIY 232
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAAlAADIRRaDCQ--LLVTDAEhrPLLDGL-----DLPGVRVLDVD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 233 QEPPPKKMAnvytmeeliELGQEVPEEALDAiiDTQqpnqcCVLVYTSGTTGNPKGVMLSQDNITW-----TARYGSQAG 307
Cdd:PRK13388 128 TPAYAELVA---------AAGALTPHREVDA--MDP-----FMLIFTSGTTGAPKAVRCSHGRLAFagralTERFGLTRD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 308 DiqpaevqqevvVSYL--PLSHIAAqIYDLWT-GIQWGAQVCfadpdalkgtlvntlreveptshmgVPRVWekimeriq 384
Cdd:PRK13388 192 D-----------VCYVsmPLFHSNA-VMAGWApAVASGAAVA-------------------------LPAKF-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 385 evaAQSGF---IRR----------KMLLWAMSvTLEQnltcPSNDLKPftsrladylvlarVRQALGFAkcqknfygAAP 451
Cdd:PRK13388 227 ---SASGFlddVRRygatyfnyvgKPLAYILA-TPER----PDDADNP-------------LRVAFGNE--------ASP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 452 M-TAETQRFFlglNIRLYAGYGLSESTGphFMSSPYNYRLYSSGRVVPGCRV------------------KLVNQDaDGI 512
Cdd:PRK13388 278 RdIAEFSRRF---GCQVEDGYGSSEGAV--IVVREPGTPPGSIGRGAPGVAIynpetltecavarfdahgALLNAD-EAI 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 513 GEIC-LWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPII 591
Cdd:PRK13388 352 GELVnTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADW-MRVDGENLSAAPI-ERILLRHPAI 428
|
490
....*....|....*.
gi 19705503 592 SSAML-------IGDQ 600
Cdd:PRK13388 429 NRVAVyavpderVGDQ 444
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
99-330 |
1.76e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 64.13 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 99 PYTVHQMFYEALDKYGNLSALGFKRKdkweRISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAG 178
Cdd:PRK08279 36 KRSLGDVFEEAAARHPDRPALLFEDQ----SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 179 GIVTGIYTTSSPEAcqyIAHdC----RANVIVV--DTQKQLEKIlkiwkdLPHLKAVVIYQEPPPKKMANVYTMEELIEL 252
Cdd:PRK08279 112 AVVALLNTQQRGAV---LAH-SlnlvDAKHLIVgeELVEAFEEA------RADLARPPRLWVAGGDTLDDPEGYEDLAAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 253 GQEVPEEALDAiidTQ--QPNQCCVLVYTSGTTGNPKGVMLSQdnITWTARYGSQAG--DIQPaevqQEVVVSYLPLSHI 328
Cdd:PRK08279 182 AAGAPTTNPAS---RSgvTAKDTAFYIYTSGTTGLPKAAVMSH--MRWLKAMGGFGGllRLTP----DDVLYCCLPLYHN 252
|
..
gi 19705503 329 AA 330
Cdd:PRK08279 253 TG 254
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
128-594 |
2.13e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 63.35 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQyylIARKV---AKGFLKLGLERAHSVAILGFNSPEwffsavgTVFAggivtgiyttsspeacqYIA-HDCRAN 203
Cdd:PRK09029 27 EVLTWQQ---LCARIdqlAAGFAQQGVVEGSGVALRGKNSPE-------TLLA-----------------YLAlLQCGAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 204 VIVVDTQKQLEKILKIwkdLPHLKAVVIYQEPPPKKMANvytmeelieLGQEVPEEALDAIIDTQQPNQCCVLVYTSGTT 283
Cdd:PRK09029 80 VLPLNPQLPQPLLEEL---LPSLTLDFALVLEGENTFSA---------LTSLHLQLVEGAHAVAWQPQRLATMTLTSGST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 284 GNPKGVMLsqdniTWTARYGSQAG--DIQPAEVQQEVVVSyLPLSHIAAQiydlwtGIQW-----GAqvcfadpdalkgT 356
Cdd:PRK09029 148 GLPKAAVH-----TAQAHLASAEGvlSLMPFTAQDSWLLS-LPLFHVSGQ------GIVWrwlyaGA------------T 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 357 LVntLREVEPTSHM--GVPRVwekimeriQEVAAQsgfirrkmlLWamsvtleqnltcpsndlkpftsRLADYLVLARVR 434
Cdd:PRK09029 204 LV--VRDKQPLEQAlaGCTHA--------SLVPTQ---------LW----------------------RLLDNRSEPLSL 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 435 QA--LGfakcqknfyGAAPMTAETQRFfLGLNIRLYAGYGLSEstgphfMSSPYNYRLYSS----GRVVPGCRVKLVNqd 508
Cdd:PRK09029 243 KAvlLG---------GAAIPVELTEQA-EQQGIRCWCGYGLTE------MASTVCAKRADGlagvGSPLPGREVKLVD-- 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 509 adgiGEICLWGRTIFMGYLnMEDKTHEAIDSEGWLHTGDMGRLdDDGFLYITGRLKELIITaGGENVPPVPIeEAVKMEL 588
Cdd:PRK09029 305 ----GEIWLRGASLALGYW-RQGQLVPLVNDEGWFATRDRGEW-QNGELTILGRLDNLFFS-GGEGIQPEEI-ERVINQH 376
|
....*.
gi 19705503 589 PIISSA 594
Cdd:PRK09029 377 PLVQQV 382
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
276-562 |
5.23e-10 |
|
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: 62.36 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 276 LVYTSGTTGNPKGVMLSQDNIT----WTARYGSQAgdiQPAEVQQevvvsYLPLSHIAAQiYDLWTGIQWGAQVCFADPD 351
Cdd:cd17651 141 VIYTSGSTGRPKGVVMPHRSLAnlvaWQARASSLG---PGARTLQ-----FAGLGFDVSV-QEIFSTLCAGATLVLPPEE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 352 ALkgtlvntlreveptshMGVPRVWEKIME-RIQEVAAQSGFIRRkmllWAmsvtleqnltcpsNDLKPFTSRLADylvL 430
Cdd:cd17651 212 VR----------------TDPPALAAWLDEqRISRVFLPTVALRA----LA-------------EHGRPLGVRLAA---L 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 431 ARVRQAlgfakcqknfyG-AAPMTAETQRFFLGL-NIRLYAGYGLSEStgpHFMSS------PYNYRLYSS-GRVVPGCR 501
Cdd:cd17651 256 RYLLTG-----------GeQLVLTEDLREFCAGLpGLRLHNHYGPTET---HVVTAlslpgdPAAWPAPPPiGRPIDNTR 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19705503 502 VKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWL------HTGDMGRLDDDGFLYITGR 562
Cdd:cd17651 322 VYVL--DAALrpvppgvPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGR 393
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
139-562 |
8.69e-10 |
|
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: 61.83 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 139 ARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVvdTQKQLEKILk 218
Cdd:cd12117 32 ANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL--TDRSLAGRA- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 219 iwkdLPHLKAVVIYQEPPPKkmanvytmeelielGQEVPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITW 298
Cdd:cd12117 109 ----GGLEVAVVIDEALDAG--------------PAGNPAVPVS-------PDDLAYVMYTSGSTGRPKGVAVTHRGVVR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 299 TARyGSQAGDIQPaevqQEVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFADPDALKGtlvntlreveptshmgvprvwek 378
Cdd:cd12117 164 LVK-NTNYVTLGP----DDRVLQTSPLAFDAS-TFEIWGALLNGARLVLAPKGTLLD----------------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 379 iMERIQEVAAQSGFirrkMLLWaMSVTLEQNLTcpsnDLKPftsrladyLVLARVRQALgfakcqknfYGAAPMTAETQR 458
Cdd:cd12117 215 -PDALGALIAEEGV----TVLW-LTAALFNQLA----DEDP--------ECFAGLRELL---------TGGEVVSPPHVR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 459 FFLGLN--IRLYAGYGLSESTGphFMSSPYNYRLYSSGRVVP------GCRVKLVnqDADGI-------GEICLWGRTIF 523
Cdd:cd12117 268 RVLAACpgLRLVNGYGPTENTT--FTTSHVVTELDEVAGSIPigrpiaNTRVYVL--DEDGRpvppgvpGELYVGGDGLA 343
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 19705503 524 MGYLNMEDKT------HEAIDSEGWLHTGDMGRLDDDGFLYITGR 562
Cdd:cd12117 344 LGYLNRPALTaerfvaDPFGPGERLYRTGDLARWLPDGRLEFLGR 388
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
128-600 |
8.79e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 61.62 E-value: 8.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFL-KLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQY-IAH-DCRanv 204
Cdd:PRK07867 27 SFTSWREHIRGSAARAAALRaRLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARdIAHaDCQ--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 205 IVVDTQKQLEKILKIWKDLPHLkavviyqepppkkmaNVYTME--ELIELGQEVPEEALDAiidtqQPNQCCVLVYTSGT 282
Cdd:PRK07867 104 LVLTESAHAELLDGLDPGVRVI---------------NVDSPAwaDELAAHRDAEPPFRVA-----DPDDLFMLIFTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 283 TGNPKGVMLSQDNI-----TWTARYGSQAGDiqpaevqqevvVSYL--PLSHIAAQIYDLWTGIQWGAQvcfadpdalkg 355
Cdd:PRK07867 164 SGDPKAVRCTHRKVasagvMLAQRFGLGPDD-----------VCYVsmPLFHSNAVMAGWAVALAAGAS----------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 356 tlvntlreveptshMGVPRVWekimeriqevaAQSGFIrrkmllwamsvtleqnltcpsNDLKPFTSRLADYL------V 429
Cdd:PRK07867 222 --------------IALRRKF-----------SASGFL---------------------PDVRRYGATYANYVgkplsyV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 430 LAR----------VRQALGfakcqkNfYGAAPMTAETQRFFlglNIRLYAGYGLSEsTGPHFMSSPyNYRLYSSGRVVPG 499
Cdd:PRK07867 256 LATperpddadnpLRIVYG------N-EGAPGDIARFARRF---GCVVVDGFGSTE-GGVAITRTP-DTPPGALGPLPPG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 500 crVKLVNQD------------------ADGIGEIC-LWGRTIFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYIT 560
Cdd:PRK07867 324 --VAIVDPDtgtecppaedadgrllnaDEAIGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFA 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19705503 561 GRLKELiITAGGENVPPVPIEEAVkMELPIISSAML-------IGDQ 600
Cdd:PRK07867 401 GRLGDW-MRVDGENLGTAPIERIL-LRYPDATEVAVyavpdpvVGDQ 445
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
251-572 |
1.86e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 60.55 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 251 ELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLsqdnitwtaRYGSQAGDIQPAE-----VQQEVVVSYLPL 325
Cdd:cd05910 65 NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVY---------RHGTFAAQIDALRqlygiRPGEVDLATFPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 326 SHIAAQIYDLWTGIQWGAQVCFADPDALKgtLVNTLREVEPTSHMGVPRVWEkimeRIQEVAAQSGfirrkmllwamsvt 405
Cdd:cd05910 136 FALFGPALGLTSVIPDMDPTRPARADPQK--LVGAIRQYGVSIVFGSPALLE----RVARYCAQHG-------------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 406 leqnLTCPSndLKPFTSRLADY--LVLARVRQALGFAKCQKNFYGAapmtaeTQrfflGLNIRLYAGYGLSESTGPhfms 483
Cdd:cd05910 196 ----ITLPS--LRRVLSAGAPVpiALAARLRKMLSDEAEILTPYGA------TE----ALPVSSIGSRELLATTTA---- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 484 SPYNYRLYSSGRVVPGCRVKLVNQDAD--------------GIGEICLWGRTIFMGYLNMEDKTHEA-ID--SEGWLH-T 545
Cdd:cd05910 256 ATSGGAGTCVGRPIPGVRVRIIEIDDEpiaewddtlelprgEIGEITVTGPTVTPTYVNRPVATALAkIDdnSEGFWHrM 335
|
330 340
....*....|....*....|....*..
gi 19705503 546 GDMGRLDDDGFLYITGRLKELIITAGG 572
Cdd:cd05910 336 GDLGYLDDEGRLWFCGRKAHRVITTGG 362
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
128-597 |
1.97e-09 |
|
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: 60.57 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVv 207
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 dTQKQLEKILKIWKDLPHLKAVVIYQEPPPkkmanvytmeeliELGQEVPEEALDAIIdtqqpnqccvlvYTSGTTGNPK 287
Cdd:cd17656 91 -TQRHLKSKLSFNKSTILLEDPSISQEDTS-------------NIDYINNSDDLLYII------------YTSGTTGKPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 288 GVMLSQDNITWTARYG-SQAGDIQPAEVQQEVVVSYLPLSHiaaQIYDLWtgiqwgaqvcfadpdaLKGtlvNTLREVEP 366
Cdd:cd17656 145 GVQLEHKNMVNLLHFErEKTNINFSDKVLQFATCSFDVCYQ---EIFSTL----------------LSG---GTLYIIRE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 367 TSHMGVPRVWEKI-MERIQEVAAQSGFIRrkmllwamsvtleqnltcpsndlkpftsrladylVLARVRQALG-FAKCQK 444
Cdd:cd17656 203 ETKRDVEQLFDLVkRHNIEVVFLPVAFLK----------------------------------FIFSEREFINrFPTCVK 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 445 NFYGAAP---MTAETQRFFLGLNIRLYAGYGLSES---TGPHFMSSPYNYRLYSSGRVVPGCRVKLVNQDAD-----GIG 513
Cdd:cd17656 249 HIITAGEqlvITNEFKEMLHEHNVHLHNHYGPSEThvvTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQlqpqgIVG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 514 EICLWGRTIFMGYLNMEDKTHEAI-----DSEGWLH-TGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIeEAVKME 587
Cdd:cd17656 329 ELYISGASVARGYLNRQELTAEKFfpdpfDPNERMYrTGDLARYLPDGNIEFLGRADHQ-VKIRGYRIELGEI-EAQLLN 406
|
490
....*....|
gi 19705503 588 LPIISSAMLI 597
Cdd:cd17656 407 HPGVSEAVVL 416
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
502-598 |
5.71e-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: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 502 VKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVP 576
Cdd:COG1021 365 VRIVDEDgnpvPPGeVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINR-GGEKIA 443
|
90 100
....*....|....*....|..
gi 19705503 577 PVPIEEAVkMELPIISSAMLIG 598
Cdd:COG1021 444 AEEVENLL-LAHPAVHDAAVVA 464
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
451-597 |
1.39e-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: 57.58 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 451 PMTAETQRFFLGLNIRlyAGYGLSESTGPHFMSSPYNYRLYSSGRVVPGCRVKLVnqDADGI----GEICL-WGRT---- 521
Cdd:cd05974 214 PEVIEQVRRAWGLTIR--DGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALL--DPDGApateGEVALdLGDTrpvg 289
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19705503 522 IFMGYLNMEDKTHEAIdSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEEAVkMELPIISSAMLI 597
Cdd:cd05974 290 LMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADD-VFKSSDYRISPFELESVL-IEHPAVAEAAVV 362
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
128-584 |
2.47e-08 |
|
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: 56.98 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVV 207
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DTqkqlekilkiwkdlphlkavviyqepppkkmanvytmeelielgqevpeealdaiidtqqpnqcCVLVYTSGTTGNPK 287
Cdd:cd05940 82 DA----------------------------------------------------------------ALYIYTSGTTGLPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 288 GVMLSQDNItWTARYGSQAGDIQpaeVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAD--------PDALK--GTL 357
Cdd:cd05940 98 AAIISHRRA-WRGGAFFAGSGGA---LPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKkfsasnfwDDIRKyqATI 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 358 V----NTLREVeptshMGVPrvwEKIMERIQEVAAQSGfirrkmllwamsvtleqnltcpsNDLKP-----FTSRLADyl 428
Cdd:cd05940 174 FqyigELCRYL-----LNQP---PKPTERKHKVRMIFG-----------------------NGLRPdiweeFKERFGV-- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 429 vlARVRQalgfakcqknFYGAapmTAETQRFFLGLNIRLYAGYglsestGPHFMSSPYNYRL----YSSGRVV--PGCRV 502
Cdd:cd05940 221 --PRIAE----------FYAA---TEGNSGFINFFGKPGAIGR------NPSLLRKVAPLALvkydLESGEPIrdAEGRC 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 503 KLVNQDADG--IGEIClwGRTIFMGYLNmEDKTHEAI------DSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGEN 574
Cdd:cd05940 280 IKVPRGEPGllISRIN--PLEPFDGYTD-PAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGD-TFRWKGEN 355
|
490
....*....|
gi 19705503 575 VPPVPIEEAV 584
Cdd:cd05940 356 VSTTEVAAVL 365
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
104-307 |
3.33e-08 |
|
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: 56.57 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 104 QMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 183
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFED----QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 184 IYTTSSPEACQYIAHDCRANVIVvdTQKqlekilkiwkdlpHLKAVVIYQEpppkkmANVYTMEELIelgQEVPEEALDA 263
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILL--TQS-------------HLQPPIAFIG------LIDLLDEDTI---YHEESENLEP 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19705503 264 IIdtqQPNQCCVLVYTSGTTGNPKGVMLSQDN----ITWTARYGSQAG 307
Cdd:cd17655 133 VS---KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlVEWANKVIYQGE 177
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
269-597 |
4.21e-08 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 56.32 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 269 QPNQCCVLVYTSGTTGNPKGVMLSQDNIT-----WTARYGSqagDIQPaevqqevvVSYLPLSHIAAQIY--DLWTGIQW 341
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAhaahaWRREYEL---DSFP--------VRLLQMASFSFDVFagDFARSLLN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 342 GAQ--VCFADPDALKGTLVNTLREVEPTSHMGVPRVWEKIMERIQevaaqsgfiRRKMLLWAMSVTLEQNLTCPSNDLKP 419
Cdd:cd17650 160 GGTlvICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVY---------RNGLDLSAMRLLIVGSDGCKAQDFKT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 420 FTSRLADYLVLArvrqalgfakcqkNFYGAAPMTAETQRFFLGLNirlyagyGLSES-TGPhfMSSPY-NYRLY---SSG 494
Cdd:cd17650 231 LAARFGQGMRII-------------NSYGVTEATIDSTYYEEGRD-------PLGDSaNVP--IGRPLpNTAMYvldERL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 495 RVVPgcrvklvnqdADGIGEICLWGRTIFMGYLNMEDKTHEAI------DSEGWLHTGDMGRLDDDGFLYITGRLKELII 568
Cdd:cd17650 289 QPQP----------VGVAGELYIGGAGVARGYLNRPELTAERFvenpfaPGERMYRTGDLARWRADGNVELLGRVDHQVK 358
|
330 340 350
....*....|....*....|....*....|...
gi 19705503 569 TAGgenvppVPIE----EAVKMELPIISSAMLI 597
Cdd:cd17650 359 IRG------FRIElgeiESQLARHPAIDEAVVA 385
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
490-598 |
7.61e-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: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 490 LYSSGR-VVPGCRVKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRL 563
Cdd:cd05920 307 IHTQGRpMSPDDEIRVVDEEgnpvPPGeEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRI 386
|
90 100 110
....*....|....*....|....*....|....*
gi 19705503 564 KELiITAGGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:cd05920 387 KDQ-INRGGEKIAAEEVENLL-LRHPAVHDAAVVA 419
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
141-635 |
9.43e-08 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 55.13 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 141 KVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTQkqlekILKIW 220
Cdd:cd05915 36 RLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN-----LLPLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 221 KDLPHLKAVVIYQeppPKKMANVYTMEELIELGQevPEEALDAIIDTQQPnqcCVLVYTSGTTGNPKGVMLSQDNITWTA 300
Cdd:cd05915 111 EAIRGELKTVQHF---VVMDEKAPEGYLAYEEAL--GEEADPVRVPERAA---CGMAYTTGTTGLPKGVVYSHRALVLHS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 301 RYGSQAGDIQPAEVqqEVVVSYLPLSHIAAQIYdLWTGIQWGAQVCFADPDALKGTLVNTLREVEPTSHMGVPRVWEKIM 380
Cdd:cd05915 183 LAASLVDGTALSEK--DVVLPVVPMFHVNAWCL-PYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 381 ERIQEVaaqsgfirRKMLLWAMSVtLEQNLTCPSNDLKpfTSRLADYlvlaRVRQALGFAKCqknfYG---AAPMTAETQ 457
Cdd:cd05915 260 DYLEST--------GHRLKTLRRL-VVGGSAAPRSLIA--RFERMGV----EVRQGYGLTET----SPvvvQNFVKSHLE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 458 RFFLGLNIRLYAGYGLS------ESTGPHFMSSPYnyrlyssgrvvpgcrvklvnqDADGIGEICLWGRTIFMGYLNMED 531
Cdd:cd05915 321 SLSEEEKLTLKAKTGLPiplvrlRVADEEGRPVPK---------------------DGKALGEVQLKGPWITGGYYGNEE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 532 KTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIeEAVKMELPIISSAMLIG--DQRKFLSMLLT 609
Cdd:cd05915 380 ATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKD-LIKSGGEWISSVDL-ENALMGHPKVKEAAVVAipHPKWQERPLAV 457
|
490 500
....*....|....*....|....*.
gi 19705503 610 LKCTlNPETSEptdnltEQAVEFCQR 635
Cdd:cd05915 458 VVPR-GEKPTP------EELNEHLLK 476
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
489-584 |
9.54e-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: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 489 RLYSSGRVVPGCRVKLVNQD-----ADGIGEICLwGRTIFMGYLNMEDKTHEAI------DSEGWLHTGDMGRLDDDGFL 557
Cdd:cd05967 409 KAGSPGKPVPGYQVQVLDEDgepvgPNELGNIVI-KLPLPPGCLLTLWKNDERFkklylsKFPGYYDTGDAGYKDEDGYL 487
|
90 100 110
....*....|....*....|....*....|..
gi 19705503 558 YITGRLKELIITAG-----GEnvppvpIEEAV 584
Cdd:cd05967 488 FIMGRTDDVINVAGhrlstGE------MEESV 513
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
278-623 |
9.85e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 55.42 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 278 YTSGTTGNPKGVMLSQ-DNITWTARYGSQAGDIQPAEVQQEVVVSYLPLSHIAAQIYDLWTGiqwGAQVCFADPDALKGT 356
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHaDPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATG---GSAVINSAPVTPEAA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 357 LVNTLReVEPTSHMGVPRVWEKIMEriqevaaqsgfirrkmllwAMSVTLEQNLTCPSNDLKPFTSRLADYLVlarvrqa 436
Cdd:PRK06060 229 AILSAR-FGPSVLYGVPNFFARVID-------------------SCSPDSFRSLRCVVSAGEALELGLAERLM------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 437 lgfakcqkNFYGAAPmtaetqrfflglnirLYAGYGLSEsTGPHFMSSPYN-YRLYSSGRVVPGCRVKLVNQDADGIG-- 513
Cdd:PRK06060 282 --------EFFGGIP---------------ILDGIGSTE-VGQTFVSNRVDeWRLGTLGRVLPPYEIRVVAPDGTTAGpg 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 514 -EICLW--GRTIFMGYLNMEDKTheaIDSEGWLHTGDMGRLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPI 590
Cdd:PRK06060 338 vEGDLWvrGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVI-GGVNVDPREVERLI-IEDEA 412
|
330 340 350
....*....|....*....|....*....|...
gi 19705503 591 ISSAMLIGdQRKFLSMlLTLKCTLNPETSEPTD 623
Cdd:PRK06060 413 VAEAAVVA-VRESTGA-STLQAFLVATSGATID 443
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
492-591 |
1.32e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 54.75 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 492 SSGRVVPGCRVKLVNQDA-----DG-IGEICLWGRTIFMGYLNMEDKTHE------------------AIDSEGWLHTGD 547
Cdd:PRK12476 403 SCGQVARSQWAVIVDPDTgaelpDGeVGEIWLHGDNIGRGYWGRPEETERtfgaklqsrlaegshadgAADDGTWLRTGD 482
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 19705503 548 MGrLDDDGFLYITGRLKELIITaGGENVPPVPIEEAVKMELPII 591
Cdd:PRK12476 483 LG-VYLDGELYITGRIADLIVI-DGRNHYPQDIEATVAEASPMV 524
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
257-625 |
1.77e-07 |
|
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: 54.25 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 257 PEEALDAIIDTQQ-------PNQCCVLVYTSGTTGNPKGVMLSQDN----ITWtarygsqAGDIQPAEVQQEVVVSY--- 322
Cdd:cd12115 84 PPERLRFILEDAQarlvltdPDDLAYVIYTSGSTGRPKGVAIEHRNaaafLQW-------AAAAFSAEELAGVLASTsic 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 323 LPLShiaaqIYDLWTGIQWGAQVCFAD--------PDALKGTLVNTlreveptshmgVPRVwekimerIQEVAAQSGFIR 394
Cdd:cd12115 157 FDLS-----VFELFGPLATGGKVVLADnvlalpdlPAAAEVTLINT-----------VPSA-------AAELLRHDALPA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 395 rkmllwAMSVTleqNLTCpsndlKPFTSRLADYLvlarvrqalgfakcqknfYGAAPMTaetqrfflglniRLYAGYGLS 474
Cdd:cd12115 214 ------SVRVV---NLAG-----EPLPRDLVQRL------------------YARLQVE------------RVVNLYGPS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 475 EST--------GPHFMSSPynyrlySSGRVVPGCRVKLVNQD----ADG-IGEICLWGRTIFMGYLNMEDKTHEAIDSEG 541
Cdd:cd12115 250 EDTtystvapvPPGASGEV------SIGRPLANTQAYVLDRAlqpvPLGvPGELYIGGAGVARGYLGRPGLTAERFLPDP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 542 WL------HTGDMGRLDDDGFLYITGRLKELIITAGgenvppVPIE----EAVKMELPIISSA--MLIGDQ--RKFLSML 607
Cdd:cd12115 324 FGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRG------FRIElgeiEAALRSIPGVREAvvVAIGDAagERRLVAY 397
|
410
....*....|....*...
gi 19705503 608 LTLKCTLNPETSEPTDNL 625
Cdd:cd12115 398 IVAEPGAAGLVEDLRRHL 415
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
71-302 |
5.17e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 53.63 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 71 LDASEealwttRADGRVRLRLEPFcTQLPYTVHQMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLG 150
Cdd:PRK12467 490 LDAEE------RARELVRWNAPAT-EYAPDCVHQLIEAQARQHPERPALVFGE----QVLSYAELNRQANRLAHVLIAAG 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 151 LERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDcrANVIVVDTQKQLEKILKIWKDLPhlkaVV 230
Cdd:PRK12467 559 VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDD--SGVRLLLTQSHLLAQLPVPAGLR----SL 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19705503 231 IYQEPPPkkmanvytmeELIELGQEVPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNIT----WTARY 302
Cdd:PRK12467 633 CLDEPAD----------LLCGYSGHNPEVALD-------PDNLAYVIYTSGSTGQPKGVAISHGALAnyvcVIAER 691
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
509-576 |
5.60e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 52.81 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 509 ADG-IGEICLWGRTIFMGYLNMEDKTHEAID-----------SEG------WLHTGDMGRLDDdGFLYITGRLKELIITA 570
Cdd:PRK07769 414 PDGqIGEIWLHGNNIGTGYWGKPEETAATFQnilksrlseshAEGapddalWVRTGDYGVYFD-GELYITGRVKDLVIID 492
|
....*.
gi 19705503 571 GGENVP 576
Cdd:PRK07769 493 GRNHYP 498
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
126-598 |
7.59e-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: 52.47 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 126 KWeriSYYQYYLIARKVAKGFLKL-GLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTgiyttssPEACQYIAHD----- 199
Cdd:cd05928 41 KW---SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFI-------PGTIQLTAKDilyrl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 200 --CRANVIVVDtQKQLEKILKIWKDLPHLKAVVIYQEPPPKKMANvytmeeLIELGQEVPEEALDAIIDTQQPnqcCVLV 277
Cdd:cd05928 111 qaSKAKCIVTS-DELAPEVDSVASECPSLKTKLLVSEKSRDGWLN------FKELLNEASTEHHCVETGSQEP---MAIY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 278 YTSGTTGNPKGVMLSQDN----ITWTARYGSqagDIQPAEVQQEVVVSYLPLSHIAAqIYDLWTGiqwGAQVcFA----- 348
Cdd:cd05928 181 FTSGTTGSPKMAEHSHSSlglgLKVNGRYWL---DLTASDIMWNTSDTGWIKSAWSS-LFEPWIQ---GACV-FVhhlpr 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 349 -DPDalkgTLVNTLREVEPTSHMGVPRVWekimeriqevaaqsgfirrKMLLwamsvtleqnltcpSNDLKPFTsrlady 427
Cdd:cd05928 253 fDPL----VILKTLSSYPITTFCGAPTVY-------------------RMLV--------------QQDLSSYK------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 428 lvlarvrqalgFAKCQKNFYGAAPMTAETQ---RFFLGLNIrlYAGYGLSEsTG------------PHFM---SSPYNYR 489
Cdd:cd05928 290 -----------FPSLQHCVTGGEPLNPEVLekwKAQTGLDI--YEGYGQTE-TGlicanfkgmkikPGSMgkaSPPYDVQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 490 LYS-SGRVVP-------GCRVKLVNqdadgigEICLwgrtiFMGYLNMEDKTHEAIDSEGWLhTGDMGRLDDDGFLYITG 561
Cdd:cd05928 356 IIDdNGNVLPpgtegdiGIRVKPIR-------PFGL-----FSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMG 422
|
490 500 510
....*....|....*....|....*....|....*..
gi 19705503 562 RLKELIITAgGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:cd05928 423 RADDVINSS-GYRIGPFEVESAL-IEHPAVVESAVVS 457
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
149-598 |
8.33e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 52.48 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 149 LGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDtQKQLEKILKIWKDLPHLKA 228
Cdd:PRK05620 59 LGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKECPCVRA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 229 VVIYQEPPPKKMA-------NVYTMEELIElGQ-------EVPEEALDAIidtqqpnqcCvlvYTSGTTGNPKGVMLSQD 294
Cdd:PRK05620 138 VVFIGPSDADSAAahmpegiKVYSYEALLD-GRstvydwpELDETTAAAI---------C---YSTGTTGAPKGVVYSHR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 295 NItWTARYGSQAGD---IQPAEvqqevvvSYL---PLSHIAAqiydlW----TGIQWGAQVCFADPDALKGTLVNTLREV 364
Cdd:PRK05620 205 SL-YLQSLSLRTTDslaVTHGE-------SFLccvPIYHVLS-----WgvplAAFMSGTPLVFPGPDLSAPTLAKIIATA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 365 EPTSHMGVPRVWEKIMeriqevaaqsgfirrkmllwamsvtleqnltcpsndlkpftsrlADYLVLARVRQALgfakcQK 444
Cdd:PRK05620 272 MPRVAHGVPTLWIQLM--------------------------------------------VHYLKNPPERMSL-----QE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 445 NFYGAAP-----MTAETQRFflGLNIrlYAGYGLSESTGPHFMSSP---------YNYRlYSSGRVVPGCRVKLVNqdaD 510
Cdd:PRK05620 303 IYVGGSAvppilIKAWEERY--GVDV--VHVWGMTETSPVGTVARPpsgvsgearWAYR-VSQGRFPASLEYRIVN---D 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 511 G---------IGEICLWGRTIFMGYLNME----------------DKTHEAIDSEGWLHTGDMGRLDDDGFLYITGRLKE 565
Cdd:PRK05620 375 GqvmestdrnEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARD 454
|
490 500 510
....*....|....*....|....*....|...
gi 19705503 566 lIITAGGENVPPVPIEEAVkMELPIISSAMLIG 598
Cdd:PRK05620 455 -VIRSGGEWIYSAQLENYI-MAAPEVVECAVIG 485
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
250-563 |
1.12e-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: 51.67 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 250 IELGQEVPEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQD---NITWTARygSQAGDIQPAEVQQEVV 319
Cdd:cd17644 78 VPLDPNYPQERLTYILeDAQisvlltQPENLAYVIYTSGSTGKPKGVMIEHQslvNLSHGLI--KEYGITSSDRVLQFAS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 320 VSYlplSHIAAQIYDLWtgiqwgaqvcfadpdaLKG-TLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQsgfirrkML 398
Cdd:cd17644 156 IAF---DVAAEEIYVTL----------------LSGaTLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAY-------WH 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 399 LWAMSVTLEqnlTCPSndlkPFTSRLAdylvlarvrqALGFAKCQknfygaaPMTAETQRFFLGLNIRLYAGYGLSESTG 478
Cdd:cd17644 210 LLVLELLLS---TIDL----PSSLRLV----------IVGGEAVQ-------PELVRQWQKNVGNFIQLINVYGPTEATI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 479 PHFMSSPYNYRLYSS-----GRVVPGCRVKLVNQDADGI-----GEICLWGRTIFMGYLNMEDKTHEAIDSEGWLH---- 544
Cdd:cd17644 266 AATVCRLTQLTERNItsvpiGRPIANTQVYILDENLQPVpvgvpGELHIGGVGLARGYLNRPELTAEKFISHPFNSsese 345
|
330 340
....*....|....*....|...
gi 19705503 545 ----TGDMGRLDDDGFLYITGRL 563
Cdd:cd17644 346 rlykTGDLARYLPDGNIEYLGRI 368
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
128-345 |
1.13e-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: 51.91 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLK-LGLERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIV 206
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 207 VDT--QKQLEKILkiwkdlPHLKA--VVIYQEPPPkkmANVYTMEELIELGQEVPEEALDAIIDTQQ-PNQCCVLVYTSG 281
Cdd:cd05938 84 VAPelQEAVEEVL------PALRAdgVSVWYLSHT---SNTEGVISLLDKVDAASDEPVPASLRAHVtIKSPALYIYTSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19705503 282 TTGNPKGVMLSQDNITWTARYGSQAGdiqpaEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 345
Cdd:cd05938 155 TTGLPKAARISHLRVLQCSGFLSLCG-----VTADDVIYITLPLYHSSGFLLGIGGCIELGATC 213
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
269-563 |
1.34e-06 |
|
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: 51.51 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 269 QPNQCCVLVYTSGTTGNPKGVMLSQDNI-----TWTARYGSQAGDiqpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGA 343
Cdd:cd17646 136 RPDNLAYVIYTSGSTGRPKGVMVTHAGIvnrllWMQDEYPLGPGD---------RVLQKTPLSFDVS-VWELFWPLVAGA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 344 QVCFADPDALK--GTLVNTLREVEPTSHMGVPRVWEkimERIQEVAAQSgfirrkmllwamsvtleqnltCPSndlkpft 421
Cdd:cd17646 206 RLVVARPGGHRdpAYLAALIREHGVTTCHFVPSMLR---VFLAEPAAGS---------------------CAS------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 422 srladylvLARVrqalgfakcqknFYGAAPMTAET-QRFFLGLNIRLYAGYGLSEST--GPHFMSSPYNYRLYSS-GRVV 497
Cdd:cd17646 255 --------LRRV------------FCSGEALPPELaARFLALPGAELHNLYGPTEAAidVTHWPVRGPAETPSVPiGRPV 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19705503 498 PGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTHEAI-----DSEGWLH-TGDMGRLDDDGFLYITGRL 563
Cdd:cd17646 315 PNTRLYVL--DDALrpvpvgvPGELYLGGVQLARGYLGRPALTAERFvpdpfGPGSRMYrTGDLARWRPDGALEFLGRS 391
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
502-585 |
1.99e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.10 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 502 VKLVNQD------ADGIGEICLWGRTIFMGYLNMEDKTHEAID------SEG-----WLHTGDMGRLDDDGfLYITGRLK 564
Cdd:PRK05850 381 VRIVDPDtciecpAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpSPGtpegpWLRTGDLGFISEGE-LFIVGRIK 459
|
90 100
....*....|....*....|.
gi 19705503 565 ELIITAgGENVPPVPIEEAVK 585
Cdd:PRK05850 460 DLLIVD-GRNHYPDDIEATIQ 479
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
71-310 |
2.10e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.50 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 71 LDASEEAlwttRADGRVRLRLEPFCTQLpyTVHQMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLG 150
Cdd:PRK12316 1980 LDAGERQ----RILADWDRTPEAYPRGP--GVHQRIAEQAARAPEAIAVVFGD----QHLSYAELDSRANRLAHRLRARG 2049
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 151 LERAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAHDCRANVIVVDTqkqlekilkiwkdlpHLKAvv 230
Cdd:PRK12316 2050 VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR---------------HLLE-- 2112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 231 iyQEPPPKKMAN--VYTMEELIELGQEVPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQ----DNITWT-ARYG 303
Cdd:PRK12316 2113 --RLPLPAGVARlpLDRDAEWADYPDTAPAVQLA-------GENLAYVIYTSGSTGLPKGVAVSHgalvAHCQAAgERYE 2183
|
....*..
gi 19705503 304 SQAGDIQ 310
Cdd:PRK12316 2184 LSPADCE 2190
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
157-563 |
5.63e-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: 49.60 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 157 VAILGFNSPEWFFSAVGTVFAGGIvtgiYTTSSPEA----CQYIAHDCRANVIVVDTqkqlekilkiwkDLPHLkavviY 232
Cdd:cd12116 40 VAVYLPRSARLVAAMLAVLKAGAA----YVPLDPDYpadrLRYILEDAEPALVLTDD------------ALPDR-----L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 233 QEPPPkkmanvytmeeLIELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARygSQAGDIQPA 312
Cdd:cd12116 99 PAGLP-----------VLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH--SMRERLGLG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 313 EVQQEVVVS-----------YLPLSHiaaqiydlwtgiqwGAQVCFADPDALK--GTLVNTLREVEPTSHMGVPRVWeki 379
Cdd:cd12116 166 PGDRLLAVTtyafdisllelLLPLLA--------------GARVVIAPRETQRdpEALARLIEAHSITVMQATPATW--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 380 meRIqevAAQSGFIRRKmllwamSVTleqnLTCPSNDLKPftsRLADYLvLARVRQALgfakcqkNFYGAAPMT--AETQ 457
Cdd:cd12116 229 --RM---LLDAGWQGRA------GLT----ALCGGEALPP---DLAARL-LSRVGSLW-------NLYGPTETTiwSTAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 458 RfflglnirlyagygLSESTGPHFMSSPY-NYRLY---SSGRVVPgcrvklvnqdADGIGEICLWGRTIFMGYLNMEDKT 533
Cdd:cd12116 283 R--------------VTAAAGPIPIGRPLaNTQVYvldAALRPVP----------PGVPGELYIGGDGVAQGYLGRPALT 338
|
410 420 430
....*....|....*....|....*....|....*..
gi 19705503 534 HEAI-------DSEGWLHTGDMGRLDDDGFLYITGRL 563
Cdd:cd12116 339 AERFvpdpfagPGSRLYRTGDLVRRRADGRLEYLGRA 375
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
191-575 |
7.70e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 49.04 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 191 EACQYIAHdcranVIVVDTQKQL-EKILKIWKDLPHLKAVVIYQEPPPKKManvyTMEELIELG--QEVPEEALDAI--I 265
Cdd:PRK06334 107 TACANLVG-----VTHVLTSKQLmQHLAQTHGEDAEYPFSLIYMEEVRKEL----SFWEKCRIGiyMSIPFEWLMRWfgV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 266 DTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDiqPAEvqQEVVVSYLPLSHiaaqiydlwtgiQWGAQV 345
Cdd:PRK06334 178 SDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS--PKE--DDVMMSFLPPFH------------AYGFNS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 346 CfadpdalkgTLVNTLreveptshMGVPRVW-------EKIMERIQEVAAqsgfirrkMLLWAMSVTLEQNLTCPSndlK 418
Cdd:PRK06334 242 C---------TLFPLL--------SGVPVVFaynplypKKIVEMIDEAKV--------TFLGSTPVFFDYILKTAK---K 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 419 PFTSrladylvLARVRQALGFAKCQKNfygaaPMTAETQRFFLglNIRLYAGYGLSESTgP----HFMSSPYNYRLYssG 494
Cdd:PRK06334 294 QESC-------LPSLRFVVIGGDAFKD-----SLYQEALKTFP--HIQLRQGYGTTECS-PvitiNTVNSPKHESCV--G 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 495 RVVPGCRVKLVNQD------ADGIGEICLWGRTIFMGYLNmEDKTHEAI--DSEGWLHTGDMGRLDDDGFLYITGRLKEL 566
Cdd:PRK06334 357 MPIRGMDVLIVSEEtkvpvsSGETGLVLTRGTSLFSGYLG-EDFGQGFVelGGETWYVTGDLGYVDRHGELFLKGRLSRF 435
|
....*....
gi 19705503 567 iITAGGENV 575
Cdd:PRK06334 436 -VKIGAEMV 443
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
494-572 |
8.30e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 49.13 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 494 GRVVPGCRVKLVN---------QD-----ADGIGEICLWGRTIFMGYLNMEDKTHEA--IDSEG--WLHTGDMGRLDDDG 555
Cdd:PRK09274 355 GRPVDGVEVRIIAisdapipewDDalrlaTGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQG 434
|
90
....*....|....*..
gi 19705503 556 FLYITGRLKELIITAGG 572
Cdd:PRK09274 435 RLWFCGRKAHRVETAGG 451
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
102-563 |
8.87e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.57 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 102 VHQMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIV 181
Cdd:PRK12316 3059 VHRLFEEQVERTPDAVALAFGE----QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAY 3134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 182 TGIYTTSSPEACQYIAHDCRANVIVvdTQKQLEkilkiwkdLPHLKAVVIYqepppkkmanvytmeeLIELGQEVPEEAL 261
Cdd:PRK12316 3135 VPLDPEYPEERLAYMLEDSGAQLLL--SQSHLR--------LPLAQGVQVL----------------DLDRGDENYAEAN 3188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 262 DAIIDTqqPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAAqIYDLWTGIQW 341
Cdd:PRK12316 3189 PAIRTM--PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGV----GDRVLQFTTFSFDVF-VEELFWPLMS 3261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 342 GAQVCFADPDalkgtlvntlreveptshmgvprvwekimeriqevaaqsgfirrkmlLWAMSVTLEQNLTCPSNDLKPFT 421
Cdd:PRK12316 3262 GARVVLAGPE-----------------------------------------------DWRDPALLVELINSEGVDVLHAY 3294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 422 -SRLADYLVLARVRQALGFAKCQKNfyGAAPMTAETQRFFLGLniRLYAGYGLSEST--GPHFMSSPYNYRLYSSGRVVP 498
Cdd:PRK12316 3295 pSMLQAFLEEEDAHRCTSLKRIVCG--GEALPADLQQQVFAGL--PLYNLYGPTEATitVTHWQCVEEGKDAVPIGRPIA 3370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19705503 499 GCRVKLVNQDAD-----GIGEICLWGRTIFMGYLNMEDKTHEAI------DSEGWLHTGDMGRLDDDGFLYITGRL 563
Cdd:PRK12316 3371 NRACYILDGSLEpvpvgALGELYLGGEGLARGYHNRPGLTAERFvpdpfvPGERLYRTGDLARYRADGVIEYIGRV 3446
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
466-617 |
1.62e-05 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 47.93 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 466 RLYAGYGLSESTgphFMSSPY----NYRLYSSGRVVPGCRVKLVNQD----ADGI-GEICLWGRTIFMGYLNMEDKT--- 533
Cdd:cd17645 236 KLVNNYGPTENT---VVATSFeidkPYANIPIGKPIDNTRVYILDEAlqlqPIGVaGELCIAGEGLARGYLNRPELTaek 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 534 ---HEAIDSEGWLHTGDMGRLDDDGFLYITGRLKELiITAGGENVPPVPIEEAVkMELPIISSAMLI----GDQRKFLSM 606
Cdd:cd17645 313 fivHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ-VKIRGYRIEPGEIEPFL-MNHPLIELAAVLakedADGRKYLVA 390
|
170
....*....|.
gi 19705503 607 LLTLKCTLNPE 617
Cdd:cd17645 391 YVTAPEEIPHE 401
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
257-563 |
3.63e-05 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 46.86 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 257 PEEALDAIIDTQQPnqCCVL---------VYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPAevqqEVVVSYLPLSH 327
Cdd:cd17652 72 PAERIAYMLADARP--ALLLttpdnlayvIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPG----SRVLQFASPSF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 328 IAAqIYDLWTGIQWGAQVCFADPDALKG--TLVNTLREvEPTSHMGVPRVwekimeriqevaaqsgfirrkmllwAMSVT 405
Cdd:cd17652 146 DAS-VWELLMALLAGATLVLAPAEELLPgePLADLLRE-HRITHVTLPPA-------------------------ALAAL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 406 leqnltcPSNDLKPFTSrladyLVLArvrqalgfakcqknfyGAAPMTAETQRFFLGLniRLYAGYGLSESTGPHFMSSP 485
Cdd:cd17652 199 -------PPDDLPDLRT-----LVVA----------------GEACPAELVDRWAPGR--RMINAYGPTETTVCATMAGP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 486 Y-------------NYRLY---SSGRVVP-GCrvklvnqdadgIGEICLWGRTIFMGYLNMEDKTHE-------AIDSEG 541
Cdd:cd17652 249 LpgggvppigrpvpGTRVYvldARLRPVPpGV-----------PGELYIAGAGLARGYLNRPGLTAErfvadpfGAPGSR 317
|
330 340
....*....|....*....|..
gi 19705503 542 WLHTGDMGRLDDDGFLYITGRL 563
Cdd:cd17652 318 MYRTGDLARWRADGQLEFLGRA 339
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
102-563 |
4.91e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 47.26 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 102 VHQMFYEALDKYGNLSALGFKRkdkwERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGIV 181
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALAFGE----ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 182 TGIYTTSSPEACQYIAHDCRANVIVvdTQKQLEKILkiwkDLPHLKAVVIYQEPPPkkmanvytmeELIELGQEVPEEAL 261
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGVQLLL--SQSHLGRKL----PLAAGVQVLDLDRPAA----------WLEGYSEENPGTEL 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 262 DaiidtqqPNQCCVLVYTSGTTGNPKGVMLS----QDNITWT-ARYGSQAGDiqpaEVQQEVVVSYlplshiAAQIYDLW 336
Cdd:PRK12316 653 N-------PENLAYVIYTSGSTGKPKGAGNRhralSNRLCWMqQAYGLGVGD----TVLQKTPFSF------DVSVWEFF 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 337 TGIQWGAQVCFA------DPDALKGTL----VNTLreveptsHMgVPRVWEKImerIQEVAAQsgfirrkmllwamSVTL 406
Cdd:PRK12316 716 WPLMSGARLVVAapgdhrDPAKLVELInregVDTL-------HF-VPSMLQAF---LQDEDVA-------------SCTS 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 407 EQNLTCPSNdlkpftsrladylvlarvrqalgfakcqknfygAAPMTAETQRFFLGLNIRLYAGYGLSEST--GPHFMSS 484
Cdd:PRK12316 772 LRRIVCSGE---------------------------------ALPADAQEQVFAKLPQAGLYNLYGPTEAAidVTHWTCV 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 485 PYNYRLYSSGRVVPGCRVKLVnqDADG-------IGEICLWGRTIFMGYLNMEDKTHEA------IDSEGWLHTGDMGRL 551
Cdd:PRK12316 819 EEGGDSVPIGRPIANLACYIL--DANLepvpvgvLGELYLAGRGLARGYHGRPGLTAERfvpspfVAGERMYRTGDLARY 896
|
490
....*....|..
gi 19705503 552 DDDGFLYITGRL 563
Cdd:PRK12316 897 RADGVIEYAGRI 908
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
494-563 |
8.26e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 45.66 E-value: 8.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19705503 494 GRVVPGCRVKLVNQDAD-----GIGEICLWGRTIFMGYLNMEDKTHEA---IDSEGWLHTGDMGRLdDDGFLYITGRL 563
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTklpdgEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGYL-EDGLLFYQGRI 397
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
107-635 |
1.07e-04 |
|
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: 45.65 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 107 YEALDKY----GNLSALGFKRKD--KWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGI 180
Cdd:cd17634 56 ANALDRHlrenGDRTAIIYEGDDtsQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 181 VTGIYTTSSPEACQYIAHDCRANVIV-----------VDTQKQLEKILKIWKDLPHlKAVVIYQEPPPKKM--ANVYTME 247
Cdd:cd17634 136 HSVIFGGFAPEAVAGRIIDSSSRLLItadggvragrsVPLKKNVDDALNPNVTSVE-HVIVLKRTGSDIDWqeGRDLWWR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 248 ELIElgqEVPEEALDAIIDTQQPnqcCVLVYTSGTTGNPKGVMlsQDN------ITWTAR--YGSQAGDI--QPAEVQQE 317
Cdd:cd17634 215 DLIA---KASPEHQPEAMNAEDP---LFILYTSGTTGKPKGVL--HTTggylvyAATTMKyvFDYGPGDIywCTADVGWV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 318 VVVSYL---PLSHIAAQI-YD----------LWTGI-QWGAQVCF-----------ADPDALKGTLVNTLREVEPTSHMG 371
Cdd:cd17634 287 TGHSYLlygPLACGATTLlYEgvpnwptparMWQVVdKHGVNILYtaptairalmaAGDDAIEGTDRSSLRILGSVGEPI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 372 VPRVWEkimeriqevaaqsgfirrkmllWAMSVTLEQNltCPSNDLKPFTsrladylvlarvrQALGFakCQKNFYGAAP 451
Cdd:cd17634 367 NPEAYE----------------------WYWKKIGKEK--CPVVDTWWQT-------------ETGGF--MITPLPGAIE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 452 MTAEtqrfflglnirlyagyglsestgphfmsspynyrlySSGRVVPGCRVKLVN-----QDADGIGEICL---W-GRTi 522
Cdd:cd17634 408 LKAG------------------------------------SATRPVFGVQPAVVDneghpQPGGTEGNLVItdpWpGQT- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 523 fMGYLNMEDKTHEAIDS--EGWLHTGDMGRLDDDGFLYITGRLKElIITAGGENVPPVPIEEAVKMElPIISSAMLIGDQ 600
Cdd:cd17634 451 -RTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDD-VINVAGHRLGTAEIESVLVAH-PKVAEAAVVGIP 527
|
570 580 590
....*....|....*....|....*....|....*
gi 19705503 601 RKFLSMLLTLKCTLNPETsEPTDNLTEQAVEFCQR 635
Cdd:cd17634 528 HAIKGQAPYAYVVLNHGV-EPSPELYAELRNWVRK 561
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
107-290 |
1.35e-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: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 107 YEALDKygNLSALGFKRKDKWE--------RISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEwffsAVGTVFA- 177
Cdd:cd05966 56 YNCLDR--HLKERGDKVAIIWEgdepdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPE----LVIAMLAc 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 178 ---GGIVTGIYTTSSPEACQYIAHDCRANVIV-VDTQKQLEKI--LKIWKD-----LPHLKAVVIYQ----EPPPKKMAN 242
Cdd:cd05966 130 ariGAVHSVVFAGFSAESLADRINDAQCKLVItADGGYRGGKVipLKEIVDealekCPSVEKVLVVKrtggEVPMTEGRD 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19705503 243 VYTMEELIELGQEVPEEALDAiidtQQPnqcCVLVYTSGTTGNPKGVM 290
Cdd:cd05966 210 LWWHDLMAKQSPECEPEWMDS----EDP---LFILYTSGSTGKPKGVV 250
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
257-297 |
1.37e-04 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 44.99 E-value: 1.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 19705503 257 PEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQDNIT 297
Cdd:cd17643 72 PVERIAFILaDSGpsllltDPDDLAYVIYTSGSTGRPKGVVVSHANVL 119
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
259-345 |
4.74e-04 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 43.18 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 259 EALDAIIDTQQPNQCCV-------LVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIQPaevqQEVVVSYLPLSHIAAQ 331
Cdd:cd05939 85 DPLLTQSSTEPPSQDDVnfrdklfYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRP----EDVVYDCLPLYHSAGG 160
|
90
....*....|....
gi 19705503 332 IYDLWTGIQWGAQV 345
Cdd:cd05939 161 IMGVGQALLHGSTV 174
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
128-295 |
5.18e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 43.35 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 128 ERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGgivtgiyttsspeaCQYIAhdcranvivV 207
Cdd:PRK04813 26 EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--------------HAYIP---------V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 208 DTQKQLEKILKIwKDLPHLKAVV-IYQEPPPKKMANVYTMEELIELGQEVPEEALDAIIdtqQPNQCCVLVYTSGTTGNP 286
Cdd:PRK04813 83 DVSSPAERIEMI-IEVAKPSLIIaTEELPLEILGIPVITLDELKDIFATGNPYDFDHAV---KGDDNYYIIFTSGTTGKP 158
|
....*....
gi 19705503 287 KGVMLSQDN 295
Cdd:PRK04813 159 KGVQISHDN 167
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
496-594 |
2.88e-03 |
|
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: 40.94 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 496 VVPGCRVKLVNQDA----DGIGEICLWGRTIFM--GYLNMEDKTHEAIDS--EG-WLHtGDMGRLDDDGFLYITGRLKEL 566
Cdd:cd05968 418 PVPGMKADVLDESGkparPEVGELVLLAPWPGMtrGFWRDEDRYLETYWSrfDNvWVH-GDFAYYDEEGYFYILGRSDDT 496
|
90 100
....*....|....*....|....*...
gi 19705503 567 IITAgGENVPPVPIEEAVKMELPIISSA 594
Cdd:cd05968 497 INVA-GKRVGPAEIESVLNAHPAVLESA 523
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
269-352 |
3.53e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 40.80 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19705503 269 QPNQCCVLVYTSGTTGNPKGVMLSQDNIT----WT-ARYGSQAGDI----QPAEVQQEVVVSYLPLshIAaqiydlwtgi 339
Cdd:PRK10252 596 QPHHTAYIIFTSGSTGRPKGVMVGQTAIVnrllWMqNHYPLTADDVvlqkTPCSFDVSVWEFFWPF--IA---------- 663
|
90
....*....|...
gi 19705503 340 qwGAQVCFADPDA 352
Cdd:PRK10252 664 --GAKLVMAEPEA 674
|
|
| |
