|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
125-719 |
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: 1139.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 125 KRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCC 204
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 205 ANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSG 284
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKEKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 285 TTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSLVNTL 364
Cdd:cd05933 161 TTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 365 REVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGSDLKPFTT-RLADYLVLAKVRQALGFA 443
Cdd:cd05933 241 REVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFyRLAKKLVFKKVRKALGLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 444 KCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGR 523
Cdd:cd05933 321 RCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWGR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 524 TIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISNAMLIGDQ 603
Cdd:cd05933 401 HVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGDK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 604 RKFLSMLLTLKCTLDPDTSDQTDNLTEQAMEFCQRVGSRATTVSEIIEKKDEAVYQAIEEGIRRVNMNAAARPYHIQKWA 683
Cdd:cd05933 481 RKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKWV 560
|
570 580 590
....*....|....*....|....*....|....*.
gi 27477105 684 ILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFY 719
Cdd:cd05933 561 ILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
102-722 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 590.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 102 PYTVHRMFYEALDKYGDLIALGFKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAG 181
Cdd:COG1022 10 ADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 182 GIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEV-P 260
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGLRDDPRLLSLDELLALGREVaD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 261 EEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWt 340
Cdd:COG1022 170 PAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGP----GDRTLSFLPLAHVFERTVSYY- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 341 GIQWGAQVCFAE-PDAlkgsLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTC---- 415
Cdd:COG1022 245 ALAAGATVAFAEsPDT----LAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARlagk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 416 -PGSDLKPfTTRLADYLVLAKVRQALG----FAKCqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYN 490
Cdd:COG1022 321 sPSLLLRL-KHALADKLVFSKLREALGgrlrFAVS-----GGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 491 YRLYSSGKLVPGCRVKLvnqdAEgIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELI 570
Cdd:COG1022 395 NRIGTVGPPLPGVEVKI----AE-DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 571 ITAGGENVPPVPIEEAVKmELPIISNAMLIGDQRKFLSMLLtlkcTLDPdtsdqtdnltEQAMEFCQRVGSRATTVSEII 650
Cdd:COG1022 470 VTSGGKNVAPQPIENALK-ASPLIEQAVVVGDGRPFLAALI----VPDF----------EALGEWAEENGLPYTSYAELA 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477105 651 ekKDEAVYQAIEEGIRRVNmNAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQ 722
Cdd:COG1022 535 --QDPEVRALIQEEVDRAN-AGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
130-704 |
6.05e-149 |
|
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: 441.65 E-value: 6.05e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 130 WEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 209
Cdd:cd05907 3 WQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 210 VDTqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtqqPNQCCVLVYTSGTTGNP 289
Cdd:cd05907 83 VED------------------------------------------------------------PDDLATIIYTSGTTGRP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 290 KGVMLSQDNITWTARYGSQAgdIRPAEvqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDAlkgSLVNTLREVEP 369
Cdd:cd05907 103 KGVMLSHRNILSNALALAER--LPATE--GDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAE---TLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 370 TSHMGVPRVWEKIMERIQEVAAQSGfiRRKMLLWAmsvtleqnltcpgsdlkpfttrladylVLAKVRqalgFAKCqknf 449
Cdd:cd05907 176 TVFLAVPRVWEKVYAAIKVKAVPGL--KRKLFDLA---------------------------VGGRLR----FAAS---- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 450 yGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQdaegiGEICLWGRTIFMGY 529
Cdd:cd05907 219 -GGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD-----GEILVRGPNVMLGY 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 530 LNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMElPIISNAMLIGDQRKFLSM 609
Cdd:cd05907 293 YKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PLISQAVVIGDGRPFLVA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 610 LLTLKCtldpdtsdqtdnltEQAMEFCQRVGSRATTVSEIIekKDEAVYQAIEEGIRRVNmNAAARPYHIQKWAILERDF 689
Cdd:cd05907 372 LIVPDP--------------EALEAWAEEHGIAYTDVAELA--ANPAVRAEIEAAVEAAN-ARLSRYEQIKKFLLLPEPF 434
|
570
....*....|....*
gi 27477105 690 SISGGELGPTMKLKR 704
Cdd:cd05907 435 TIENGELTPTLKLKR 449
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
109-573 |
1.93e-105 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 328.12 E-value: 1.93e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 109 FYEALDKYGDLIALGFkrqDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIY 188
Cdd:pfam00501 1 LERQAARTPDKTALEV---GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 189 TTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEAldaii 268
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPP----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 269 dtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 348
Cdd:pfam00501 153 ---DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 349 CFAEPDALK--GSLVNTLREVEPTSHMGVPRVWEKIMEriqevaaqSGFIRRkmllwamsvtleqnltcpgsdlkpfttr 426
Cdd:pfam00501 230 VLPPGFPALdpAALLELIERYKVTVLYGVPTLLNMLLE--------AGAPKR---------------------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 427 ladyLVLAKVRQALgfakcqknfYGAAPMMAETQHFFLGLNIR-LYAGYGLSETSGP---HFMSSPYNYRLYSSGKLVPG 502
Cdd:pfam00501 274 ----ALLSSLRLVL---------SGGAPLPPELARRFRELFGGaLVNGYGLTETTGVvttPLPLDEDLRSLGSVGRPLPG 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477105 503 CRVKLVNQD------AEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITA 573
Cdd:pfam00501 341 TEVKIVDDEtgepvpPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
130-711 |
5.85e-92 |
|
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: 297.80 E-value: 5.85e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 130 WEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 209
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 210 VDTQKQLEKILKIWKQLPHLKAVVIYKeppPNKMAN-----VYTMEEFMELGNEVPE---EALDAIIDTQQPNQCCVLVY 281
Cdd:cd17641 89 AEDEEQVDKLLEIADRIPSVRYVIYCD---PRGMRKyddprLISFEDVVALGRALDRrdpGLYEREVAAGKGEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 282 TSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAevqqEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDAlkgSLV 361
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPG----DEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPE---TMM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 362 NTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSV---TLEQNLTCPGSDLKPFTTR-LADYLVLAKVR 437
Cdd:cd17641 239 EDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLglrALDRGKRGRPVSLWLRLASwLADALLFRPLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 438 QALGFAKCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNqdaegIGE 517
Cdd:cd17641 319 DRLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDE-----VGE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 518 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMElPIISNA 597
Cdd:cd17641 394 ILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFS-PYIAEA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 598 MLIGDQRKFLSMLLtlkcTLDPDTsdqTDNLTEQAmefcqrvGSRATTVSEIIEKkdEAVYQAIEEGIRRVNMNAAArPY 677
Cdd:cd17641 473 VVLGAGRPYLTAFI----CIDYAI---VGKWAEQR-------GIAFTTYTDLASR--PEVYELIRKEVEKVNASLPE-AQ 535
|
570 580 590
....*....|....*....|....*....|....
gi 27477105 678 HIQKWAILERDFSISGGELGPTMKLKRLTVLEKY 711
Cdd:cd17641 536 RIRRFLLLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
129-719 |
1.13e-84 |
|
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: 277.94 E-value: 1.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 129 KWEHISYSQYYLLARRAAKGFLKLGLKQ--AHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCAN 206
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 207 VIMVDtqkqlEKIlkiwkqlphlkavviykepppnkmaNVYTMEEFMELGNEVPEEALDAiidtqQPNQCCVLVYTSGTT 286
Cdd:cd05927 82 IVFCD-----AGV-------------------------KVYSLEEFEKLGKKNKVPPPPP-----KPEDLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 287 GNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYdLWTGIQWGAQVCFAEPDALKgsLVNTLRE 366
Cdd:cd05927 127 GNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFYSGDIRL--LLDDIKA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 367 VEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSvTLEQNLTCPGSdlkpFTTRLADYLVLAKVRQALGfAKCQ 446
Cdd:cd05927 204 LKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALN-YKLAELRSGVV----RASPFWDKLVFNKIKQALG-GNVR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 447 KNFYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLV-----NQDAEGI---GE 517
Cdd:cd05927 278 LMLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVdvpemNYDAKDPnprGE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 518 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIeEAVKMELPIISNA 597
Cdd:cd05927 358 VCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKI-ENIYARSPFVAQI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 598 MLIGDQRKflSMLLTLKCtLDPDTsdqtdnlteqAMEFCQRVGSRATTVSEIIekKDEAVYQAIEEGIRRVNMNAAARPY 677
Cdd:cd05927 437 FVYGDSLK--SFLVAIVV-PDPDV----------LKEWAASKGGGTGSFEELC--KNPEVKKAILEDLVRLGKENGLKGF 501
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 27477105 678 HIQKWAILERD-FSISGGELGPTMKLKRLTVLEKYKGIIDSFY 719
Cdd:cd05927 502 EQVKAIHLEPEpFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
105-601 |
9.81e-75 |
|
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: 248.57 E-value: 9.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 105 VHRMFYEALDKYGDLIALGFKrqdkWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIV 184
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG----GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 185 TGIYTTSSPEacqyiaydccanvimvdtqkQLEKILKiwkqlpHLKAVVIYkepppnkmanvytmeefmelgnevpeeal 264
Cdd:COG0318 77 VPLNPRLTAE--------------------ELAYILE------DSGARALV----------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 265 daiidtqqpnqCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQW 344
Cdd:COG0318 102 -----------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP----GDVVLVALPLFHVFGLTVGLLAPLLA 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 345 GAQ-VCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERiqevaaqsgfirrkmllwamsvtleqnltcpgsdlkpf 423
Cdd:COG0318 167 GATlVLLPRFDP--ERVLELIERERVTVLFGVPTMLARLLRH-------------------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 424 tTRLADYLvLAKVRQAlgfakcqknFYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSgPHFMSSPYNY---RLYSSGKL 499
Cdd:COG0318 207 -PEFARYD-LSSLRLV---------VSGGAPLPPELLERFEErFGVRIVEGYGLTETS-PVVTVNPEDPgerRPGSVGRP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 500 VPGCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIIT 572
Cdd:COG0318 275 LPGVEVRIV--DEDGrelppgeVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
490 500
....*....|....*....|....*....
gi 27477105 573 aGGENVPPVPIEEAVkMELPIISNAMLIG 601
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 ... |
131-704 |
3.01e-69 |
|
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: 234.56 E-value: 3.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGgivtgiyttsspeacqyiaydcCANVIMv 210
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALG----------------------AVDVVR- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 DTQKQLEKILKIwkqLPHLKAVVIYKEPPPNKMAnvytmeefmelgnevpeealdaiidtqqpnqccVLVYTSGTTGNPK 290
Cdd:cd17640 61 GSDSSVEELLYI---LNHSESVALVVENDSDDLA---------------------------------TIIYTSGTTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 291 GVMLSQDNITWTARygsQAGDIRPAEVQQeVVVSYLPLSHIAAQIYDlWTGIQWGAQVCFAEPDALKgslvNTLREVEPT 370
Cdd:cd17640 105 GVMLTHANLLHQIR---SLSDIVPPQPGD-RFLSILPIWHSYERSAE-YFIFACGCSQAYTSIRTLK----DDLKRVKPH 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 371 SHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnltcpgsdlkpfttrladyLVLAKVRQALGFAkcqknfy 450
Cdd:cd17640 176 YIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF--------------------------LSGGIFKFGISGG------- 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 451 GAAPMMAETqhFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI------GEICLWGRT 524
Cdd:cd17640 223 GALPPHVDT--FFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekGIVWVRGPQ 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 525 IFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISNAMLIGDQR 604
Cdd:cd17640 301 VMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEAL-MRSPFIEQIMVVGQDQ 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 605 KFLSMLLTlkctldPDtsdqtdnlTEQAMEFCQRVGSR-ATTVSEIIEKKDE-AVYQaiEEGIRRVNMNAAARPY-HIQK 681
Cdd:cd17640 380 KRLGALIV------PN--------FEELEKWAKESGVKlANDRSQLLASKKVlKLYK--NEIKDEISNRPGFKSFeQIAP 443
|
570 580
....*....|....*....|...
gi 27477105 682 WAILErDFSISGGELGPTMKLKR 704
Cdd:cd17640 444 FALLE-EPFIENGEMTQTMKIKR 465
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
129-710 |
8.86e-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: 223.50 E-value: 8.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 129 KWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVI 208
Cdd:cd05932 3 QVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 209 MVDTqkqlekiLKIWKQLPHLKA--VVIYKEPPPNKMANVYTMEEFMELGNEVPEEAldaiidTQQPNQCCVLVYTSGTT 286
Cdd:cd05932 83 FVGK-------LDDWKAMAPGVPegLISISLPPPSAANCQYQWDDLIAQHPPLEERP------TRFPEQLATLIYTSGTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 287 GNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEpdALKgSLVNTLRE 366
Cdd:cd05932 150 GQPKGVMLTFGSFAWAAQAGIEHIGTEE----NDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE--SLD-TFVEDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 367 VEPTSHMGVPRVWEKIMERIQEVAAQSgfiRRKMLLWAmsvtleqnltcpgsdlkPFTTRLadylVLAKVRQALGFAKCQ 446
Cdd:cd05932 223 ARPTLFFSVPRLWTKFQQGVQDKIPQQ---KLNLLLKI-----------------PVVNSL----VKRKVLKGLGLDQCR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 447 KNFYGAAPMMAETQHFF--LGLNIrlYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQdaegiGEICLWGRT 524
Cdd:cd05932 279 LAGCGSAPVPPALLEWYrsLGLNI--LEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSPA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 525 IFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISNAMLIGDQr 604
Cdd:cd05932 352 LMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKL-AEHDRVEMVCVIGSG- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 605 kfLSMLLTLkCTLDPDTSDQTDNLTEQAMEfcqrvgsraTTVSEIIEKkdeavyqaieegirrvnMNAAARPY-HIQKWA 683
Cdd:cd05932 430 --LPAPLAL-VVLSEEARLRADAFARAELE---------ASLRAHLAR-----------------VNSTLDSHeQLAGIV 480
|
570 580
....*....|....*....|....*..
gi 27477105 684 ILERDFSISGGELGPTMKLKRlTVLEK 710
Cdd:cd05932 481 VVKDPWSIDNGILTPTLKIKR-NVLEK 506
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
133-704 |
4.29e-63 |
|
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: 219.01 E-value: 4.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIaydccanviMVDT 212
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHS---------LNET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 213 QkqlekilkiwkqlphlkAVVIYKEPPPNKManvytmeefmelgnevpeealdaiidtqqpnqcCVLVYTSGTTGNPKGV 292
Cdd:cd17639 77 E-----------------CSAIFTDGKPDDL---------------------------------ACIMYTSGSTGNPKGV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 293 MLSQDNITwtARYGSQAGDIRPAEVQQEVVVSYLPLSHI---AAQIydlwTGIQWGAQVCFAEPDAL-KGSLVNT---LR 365
Cdd:cd17639 107 MLTHGNLV--AGIAGLGDRVPELLGPDDRYLAYLPLAHIfelAAEN----VCLYRGGTIGYGSPRTLtDKSKRGCkgdLT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 366 EVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGsdlkpftTRLADYLVLAKVRQALGfAKC 445
Cdd:cd17639 181 EFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPG-------TPLLDELVFKKVRAALG-GRL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 446 QKNFYGAAPMMAETQHFflgLNI---RLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI------- 515
Cdd:cd17639 253 RYMLSGGAPLSADTQEF---LNIvlcPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYstdkppp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 516 -GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENvppVPIE--EAVKMELP 592
Cdd:cd17639 330 rGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEY---IALEklESIYRSNP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 593 IISNAMLIGDQRKFLSMLLTLkctldPDTSdqtdnlteQAMEFCQRVGSRATTVSEIIEKKD--EAVYQAIEEgirrvnm 670
Cdd:cd17639 407 LVNNICVYADPDKSYPVAIVV-----PNEK--------HLTKLAEKHGVINSEWEELCEDKKlqKAVLKSLAE------- 466
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 27477105 671 naAARPYHIQKWAILERDFSISG------GELGPTMKLKR 704
Cdd:cd17639 467 --TARAAGLEKFEIPQGVVLLDEewtpenGLVTAAQKLKR 504
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
275-588 |
1.41e-62 |
|
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: 212.53 E-value: 1.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 275 QCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAaQIYDLWTGIQWGAQVCFAEPD 354
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTE----GDVFLSTLPLFHIG-GLFGLLGALLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 355 aLKGSLVNTLREVEPTSHMGVPRVWEKIMERIqevaaqsgfirrkmllwamsvtleqnltcpgsdlkpfttRLADYlVLA 434
Cdd:cd04433 76 -DPEAALELIEREKVTILLGVPTLLARLLKAP---------------------------------------ESAGY-DLS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 435 KVRQAlgfakcqknFYGAAPMMAETQHFFLGL-NIRLYAGYGLSETSGPHFMSSPYN--YRLYSSGKLVPGCRVKLVNQD 511
Cdd:cd04433 115 SLRAL---------VSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPDDdaRKPGSVGRPVPGVEVRIVDPD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 512 AE-----GIGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 586
Cdd:cd04433 186 GGelppgEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAV 263
|
..
gi 27477105 587 VK 588
Cdd:cd04433 264 LL 265
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
132-601 |
7.56e-62 |
|
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: 215.15 E-value: 7.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 132 HISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVD 211
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 212 tQKQLEKILKIWKQLPHLKAVVIYKEPPPnKMANVYTMEEFmELGNEVPEEALDAIIDtqqPNQCCVLVYTSGTTGNPKG 291
Cdd:cd05911 90 -PDGLEKVKEAAKELGPKDKIIVLDDKPD-GVLSIEDLLSP-TLGEEDEDLPPPLKDG---KDDTAAILYSSGTTGLPKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 292 VMLSQDNITWTArygSQAGDIRPAEVQ-QEVVVSYLPLSHIAAQIYDLWTgiqwgaqvcfaepdALKGSLVNTLREVEPt 370
Cdd:cd05911 164 VCLSHRNLIANL---SQVQTFLYGNDGsNDVILGFLPLYHIYGLFTTLAS--------------LLNGATVIIMPKFDS- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 371 shmgvprvwEKIMERIQEvaaqsgfiRRKMLLW---AMSVTLeqnLTCPgsDLKPFTtrladylvLAKVRQAlgfakcqk 447
Cdd:cd05911 226 ---------ELFLDLIEK--------YKITFLYlvpPIAAAL---AKSP--LLDKYD--------LSSLRVI-------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 448 nFYGAAPMMAETQHFF--LGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVN---QDAEGI---GEIC 519
Cdd:cd05911 268 -LSGGAPLSKELQELLakRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDddgKDSLGPnepGEIC 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 520 LWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISNAML 599
Cdd:cd05911 347 VRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKEL-IKYKGFQVAPAEL-EAVLLEHPGVADAAV 424
|
..
gi 27477105 600 IG 601
Cdd:cd05911 425 IG 426
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
102-601 |
2.80e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 214.28 E-value: 2.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 102 PYTVHRMFYEALDKYGDLIALgFKRQDKWehiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAG 181
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAV-YFDGRRT---TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 182 GIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ--KQLEKILKiwkQLPHLKAVVIYkEPPPNKMANVYTmEEFMELGNEV 259
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAAILP---QLPTVRTVIVE-GDGPAAPLAPEV-GEYEELLAAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 260 PEEALDAIIDtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAqiydlW 339
Cdd:PRK06187 156 SDTFDFPDID---ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR----DDVYLVIVPMFHVHA-----W 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 340 T----GIQWGA-QVCFAEPDAlkGSLVNTLREVEPT-SHMgVPRVWEkimeriqevaaqsgfirrkMLLwamsvtleQNL 413
Cdd:PRK06187 224 GlpylALMAGAkQVIPRRFDP--ENLLDLIETERVTfFFA-VPTIWQ-------------------MLL--------KAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 414 TCPGSDLkpfttrladylvlAKVRQALgfakcqknfYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSG-------PHFM 485
Cdd:PRK06187 274 RAYFVDF-------------SSLRLVI---------YGGAALPPALLREFKEkFGIDLVQGYGMTETSPvvsvlppEDQL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 486 SSPYNYRlYSSGKLVPGCRVKLVNQ-------DAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEeGWLHTGDAGRLDADG 558
Cdd:PRK06187 332 PGQWTKR-RSAGRPLPGVEARIVDDdgdelppDGGEVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDG 409
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 27477105 559 FLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:PRK06187 410 YLYITDRIKDVIIS-GGENIYPRELEDAL-YGHPAVAEVAVIG 450
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
131-634 |
3.98e-61 |
|
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: 212.30 E-value: 3.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQyylLARRAAK--GFLKL-GLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIaydccanv 207
Cdd:cd05914 6 EPLTYKD---LADNIAKfaLLLKInGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHI-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 208 imvdtqkqlekilkiwkqLPHLKAVVIYkepppnkmanvytmeefmelgnevpeealdaiidTQQPNQCCVLVYTSGTTG 287
Cdd:cd05914 75 ------------------LNHSEAKAIF----------------------------------VSDEDDVALINYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 288 NPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAepDALKGSLVNTLREV 367
Cdd:cd05914 103 NSKGVMLTYRNIVSNVDGVKEVVLLGKGDK----ILSILPLHHIYPLTFTLLLPLLNGAHVVFL--DKIPSAKIIALAFA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 368 EPTSHMGVPRVWE----KIMERIQEVAAqsgfirrKMLLWAMSVtleqnltcpgsdlKPFTTRLADyLVLAKVRQALGfa 443
Cdd:cd05914 177 QVTPTLGVPVPLViekiFKMDIIPKLTL-------KKFKFKLAK-------------KINNRKIRK-LAFKKVHEAFG-- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 444 kcqKNF----YGAAPMMAETQHFFLGLNIRLYAGYGLSETsGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQDAE-GIGE 517
Cdd:cd05914 234 ---GNIkefvIGGAKINPDVEEFLRTIGFPYTIGYGMTET-APIISYSPPNrIRLGSAGKVIDGVEVRIDSPDPAtGEGE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 518 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIE-EAVKMELPIISn 596
Cdd:cd05914 310 IIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEaKINNMPFVLES- 388
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 27477105 597 amLIGDQRKFLSMLLtlkcTLDPDTSD----QTDNLTEQAME 634
Cdd:cd05914 389 --LVVVQEKKLVALA----YIDPDFLDvkalKQRNIIDAIKW 424
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
66-721 |
2.75e-56 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 203.41 E-value: 2.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 66 PEKVNNAQWDAPEEALWTTRADGRVrlridPSCPQLPyTVHRMFYEALDKYGDLIALGFKRQD-------KWehISYSQY 138
Cdd:PLN02736 13 PEKLQTGKWNVYRSARSPLKLVSRF-----PDHPEIG-TLHDNFVYAVETFRDYKYLGTRIRVdgtvgeyKW--MTYGEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 139 YllARRAA--KGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKqL 216
Cdd:PLN02736 85 G--TARTAigSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQT-L 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 217 EKILKIWKQLPHLKAVVIY-------KEPPPNKMANVYTMEEFMELGNEVPEEALdaiidTQQPNQCCVLVYTSGTTGNP 289
Cdd:PLN02736 162 NTLLSCLSEIPSVRLIVVVggadeplPSLPSGTGVEIVTYSKLLAQGRSSPQPFR-----PPKPEDVATICYTSGTTGTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 290 KGVMLSQDNITWTARYGSQAGDIRPAEVQqevvVSYLPLSHIAAQIYDLWTgIQWGAQVCFAEPDALKgsLVNTLREVEP 369
Cdd:PLN02736 237 KGVVLTHGNLIANVAGSSLSTKFYPSDVH----ISYLPLAHIYERVNQIVM-LHYGVAVGFYQGDNLK--LMDDLAALRP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 370 TSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSV---TLEQnltcpGSDLKPfttrLADYLVLAKVRQALGfAKCQ 446
Cdd:PLN02736 310 TIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAkkqALEN-----GKNPSP----MWDRLVFNKIKAKLG-GRVR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 447 KNFYGAAPMMAETQHFflgLNI----RLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLV--------NQDAE- 513
Cdd:PLN02736 380 FMSSGASPLSPDVMEF---LRIcfggRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVdvpemnytSEDQPy 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 514 GIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEaVKMELPI 593
Cdd:PLN02736 457 PRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKF 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 594 ISNAMLIGDQrkFLSMLLTLkCTLDPDT--------SDQTDNLTeqamEFCQRVGSRATTVSEIIEKKDEAVYQAIEEgi 665
Cdd:PLN02736 536 VAQCFVYGDS--LNSSLVAV-VVVDPEVlkawaaseGIKYEDLK----QLCNDPRVRAAVLADMDAVGREAQLRGFEF-- 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 27477105 666 rrvnmnaaARPYHIqkwaILErDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQE 721
Cdd:PLN02736 607 --------AKAVTL----VPE-PFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAE 649
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
133-601 |
8.70e-55 |
|
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: 194.37 E-value: 8.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDT 212
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLFDDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 213 qkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtqqpnqcCVLVYTSGTTGNPKGV 292
Cdd:cd17631 101 ----------------------------------------------------------------ALLMYTSGTTGRPKGA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 293 MLSQDNITWTARYGSQAGDIRPAEVQqeVVVsyLPLSHIAA----QIYDLWTGiqwGAQVCFAEPDAlkGSLVNTLREVE 368
Cdd:cd17631 117 MLTHRNLLWNAVNALAALDLGPDDVL--LVV--APLFHIGGlgvfTLPTLLRG---GTVVILRKFDP--ETVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 369 PTSHMGVPRVWEKImeriqevaaqsgfirrkmllwamsvtleqnLTCPGSDlkpfTTRLADylvLAKVrqalgfakcqkn 448
Cdd:cd17631 188 VTSFFLVPTMIQAL------------------------------LQHPRFA----TTDLSS---LRAV------------ 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 449 FYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYR--LYSSGKLVPGCRVKLVNQDAE-----GIGEICLW 521
Cdd:cd17631 219 IYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVDPDGRevppgEVGEIVVR 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 522 GRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:cd17631 299 GPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVEDVL-YEHPAVAEVAVIG 375
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
108-723 |
5.99e-54 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 197.17 E-value: 5.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 108 MFYEALDKYGDLIALGFK-----RQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGG 182
Cdd:PLN02614 50 VFRMSVEKYPNNPMLGRReivdgKPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 183 IVTGIYTTSSPEACQYIAYDCCANVIMVDTQKqlekILKIWKQLP----HLKAVVIYKEPPPNKMAN-------VYTMEE 251
Cdd:PLN02614 130 YCVPLYDTLGAGAVEFIISHSEVSIVFVEEKK----ISELFKTCPnsteYMKTVVSFGGVSREQKEEaetfglvIYAWDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 252 FMELGnevpeEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNI-TWTARYGSQAGDIRPAEVQQEVVVSYLPLSH 330
Cdd:PLN02614 206 FLKLG-----EGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIvTLIAGVIRLLKSANAALTVKDVYLSYLPLAH 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 331 IAAQIYDLWTgIQWGAQVCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLe 410
Cdd:PLN02614 281 IFDRVIEECF-IQHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKF- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 411 QNLTCPGSDLKpfTTRLADYLVLAKVRQALGfAKCQKNFYGAAPMMAETQHFflglnIRLYA------GYGLSETSGPHF 484
Cdd:PLN02614 357 GNMKKGQSHVE--ASPLCDKLVFNKVKQGLG-GNVRIILSGAAPLASHVESF-----LRVVAcchvlqGYGLTESCAGTF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 485 MSSPYNYRLYSS-GKLVPGCRVKL-----VNQDAEGI---GEICLWGRTIFMGYLNMEDKTCEAIDeEGWLHTGDAGRLD 555
Cdd:PLN02614 429 VSLPDELDMLGTvGPPVPNVDIRLesvpeMEYDALAStprGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQ 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 556 ADGFLYITGRLKELIITAGGENVPPVPIEEaVKMELPIISNAMLIGDQrkFLSMLLTLKctldpDTSDQTdnLTEQAME- 634
Cdd:PLN02614 508 PNGSMKIIDRKKNIFKLSQGEYVAVENIEN-IYGEVQAVDSVWVYGNS--FESFLVAIA-----NPNQQI--LERWAAEn 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 635 --------FCQRVGSRATTVSEIIEKKDEAVYQAIEEgIRRVNMNAAARPyhiqkwaiLERDFsisggeLGPTMKLKRLT 706
Cdd:PLN02614 578 gvsgdynaLCQNEKAKEFILGELVKMAKEKKMKGFEI-IKAIHLDPVPFD--------MERDL------LTPTFKKKRPQ 642
|
650
....*....|....*..
gi 27477105 707 VLEKYKGIIDSFYQEQK 723
Cdd:PLN02614 643 LLKYYQSVIDEMYKTTN 659
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
102-604 |
7.34e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 185.49 E-value: 7.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 102 PYTVHRMFYEALDKYGDLIALGFKRQDkwehISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAG 181
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVFGDQR----LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 182 GIVTGIYTTSSPEACQYIAYDCCANVIMVdTQKQLEKILKIWKQLPHLKAVVIYK-EPPPNKMANVYTMEEFMELGNEVP 260
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYILARGDAKALFV-LGLFLGVDYSATTRLPALEHVVICEtEEDDPHTEKMKTFTDFLAAGDPAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 261 EEAldaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIaaqiydlwt 340
Cdd:PRK07656 159 RAP------EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTE----GDRYLAANPFFHV--------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 341 giqWGAQVCFAEPdALKGSLVNTLREVEPtshmgvprvwEKIMERIQEvaaqsgfirRKMLLWAMSVTLEQNLtcpgsdl 420
Cdd:PRK07656 220 ---FGYKAGVNAP-LMRGATILPLPVFDP----------DEVFRLIET---------ERITVLPGPPTMYNSL------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 421 kpFTTRLADYLVLAKVRQALGfakcqknfyGAAPMMAETQHFF---LGLNIRLyAGYGLSETSGPHFMSSPYNYRL---Y 494
Cdd:PRK07656 270 --LQHPDRSAEDLSSLRLAVT---------GAASMPVALLERFeseLGVDIVL-TGYGLSEASGVTTFNRLDDDRKtvaG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 495 SSGKLVPGCRVKLVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKEL 569
Cdd:PRK07656 338 TIGTAIAGVENKIVNELGEEVpvgevGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDM 417
|
490 500 510
....*....|....*....|....*....|....*..
gi 27477105 570 IITaGGENVPPVPIEEaVKMELPIISNAMLIG--DQR 604
Cdd:PRK07656 418 FIV-GGFNVYPAEVEE-VLYEHPAVAEAAVIGvpDER 452
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
107-601 |
2.87e-49 |
|
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: 179.68 E-value: 2.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 107 RMFYEALDKYGDLIALGFkrQDKWehISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 186
Cdd:cd05936 3 DLLEEAARRFPDKTALIF--MGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 187 IYTTSSPEACQYIAYDCCANVIMVDTQkqLEKILKIWkqlphlkavviykepppnkmanvytmeEFMELGNEVPEEALda 266
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAVS--FTDLLAAG---------------------------APLGERVALTPEDV-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 267 iidtqqpnqcCVLVYTSGTTGNPKGVMLSQDNITWTARygSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGA 346
Cdd:cd05936 128 ----------AVLQYTSGTTGVPKGAMLTHRNLVANAL--QIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 347 QVCFaEPDALKGSLVNTLREVEPTSHMGVPRVWEKIMEriqevaaQSGFIRRkmllwamsvtleqnltcpgsdlkpfttr 426
Cdd:cd05936 196 TIVL-IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLN-------APEFKKR---------------------------- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 427 ladylVLAKVRQALGfakcqknfyGAAPMMAETQHFFLGL-NIRLYAGYGLSETSgP--HFMSSPYNYRLYSSGKLVPGC 503
Cdd:cd05936 240 -----DFSSLRLCIS---------GGAPLPVEVAERFEELtGVPIVEGYGLTETS-PvvAVNPLDGPRKPGSIGIPLPGT 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 504 RVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIDEeGWLHTGDAGRLDADGFLYITGRLKELIItAGGE 576
Cdd:cd05936 305 EVKIV--DDDGeelppgeVGELWVRGPQVMKGYWNRPEETAEAFVD-GWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGF 380
|
490 500
....*....|....*....|....*
gi 27477105 577 NVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:cd05936 381 NVYPREVEEVL-YEHPAVAEAAVVG 404
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
133-723 |
6.83e-47 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 176.96 E-value: 6.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDt 212
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQ- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 213 QKQLEKILKIWKQL-PHLKAVVIY-------KEPPPNKMANVYTMEEFMELGNevpeeaLDAIIDTQQPNQCCVLVYTSG 284
Cdd:PLN02861 157 ESKISSILSCLPKCsSNLKTIVSFgdvsseqKEEAEELGVSCFSWEEFSLMGS------LDCELPPKQKTDICTIMYTSG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 285 TTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQE-VVVSYLPLSHIAAQIYDLWTgIQWGAQVCFAEPDALkgSLVNT 363
Cdd:PLN02861 231 TTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATEEdSYFSYLPLAHVYDQVIETYC-ISKGASIGFWQGDIR--YLMED 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 364 LREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLeQNLT--CPGSDLKPFTtrlaDYLVLAKVRQALG 441
Cdd:PLN02861 308 VQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKL-GNLRkgLKQEEASPRL----DRLVFDKIKEGLG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 442 fAKCQKNFYGAAPMMAETQHFFLGLNIR-LYAGYGLSETSGPHFMSSPYNYRLYSS-GKLVPGCRVKLVNQDAEGI---- 515
Cdd:PLN02861 383 -GRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCGGCFTSIANVFSMVGTvGVPMTTIEARLESVPEMGYdals 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 516 ----GEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVpPVPIEEAVKMEL 591
Cdd:PLN02861 462 dvprGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYV-AVENLENTYSRC 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 592 PIISNAMLIGDQrkFLSMLLTLkctLDPDTSDQTD-----NLTEQAMEFCQRVGSRattvseiiekkdeavyQAIEEGIR 666
Cdd:PLN02861 540 PLIASIWVYGNS--FESFLVAV---VVPDRQALEDwaannNKTGDFKSLCKNLKAR----------------KYILDELN 598
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477105 667 RVNMNAAARPYHIQKWAILERD-FSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQK 723
Cdd:PLN02861 599 STGKKLQLRGFEMLKAIHLEPNpFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAK 656
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
108-720 |
3.27e-46 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 175.00 E-value: 3.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 108 MFYEALDKYGDLIALGFKR-------QDKWEhiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFA 180
Cdd:PLN02430 47 IFSKSVEKYPDNKMLGWRRivdgkvgPYMWK--TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAH 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 181 GGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYK---EPPPNKMANV----YTMEEFM 253
Cdd:PLN02430 125 SLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLKAIVSFTsvtEEESDKASQIgvktYSWIDFL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 254 ELGNEVPEEaldaiIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTAR----YGSQAGDIRPAEvqqEVVVSYLPLS 329
Cdd:PLN02430 205 HMGKENPSE-----TNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRgvdlFMEQFEDKMTHD---DVYLSFLPLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 330 HIAAQIYDLWTgIQWGAQVCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKM--------L 401
Cdd:PLN02430 277 HILDRMIEEYF-FRKGASVGYYHGDL--NALRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIfnalykykL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 402 LWamsvtleQNLTCPGSDLKPfttrLADYLVLAKVRQALGfAKCQKNFYGAAPMMAETQHFflgLNIR----LYAGYGLS 477
Cdd:PLN02430 354 AW-------MNRGYSHKKASP----MADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEF---LRVTscafVVQGYGLT 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 478 ETSGPHFMSSPYNYRLYSSGKLVPGC---RVKLVNQ---DAEG---IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHT 548
Cdd:PLN02430 419 ETLGPTTLGFPDEMCMLGTVGAPAVYnelRLEEVPEmgyDPLGeppRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 549 GDAGRLDADGFLYITGRLKELIITAGGENVpPVPIEEAVKMELPIISNAMLIGDQrkFLSMLLTLkCTLDPDTSDQ---T 625
Cdd:PLN02430 498 GDIGEILPNGVLKIIDRKKNLIKLSQGEYV-ALEYLENVYGQNPIVEDIWVYGDS--FKSMLVAV-VVPNEENTNKwakD 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 626 DNLTEQAMEFCQRVGSRATTVSEIIEKKDEAVYQAIEEgIRRVNMNaaARPYHIqkwailERDFsisggeLGPTMKLKRL 705
Cdd:PLN02430 574 NGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEY-IKGVILE--TKPFDV------ERDL------VTATLKKRRN 638
|
650
....*....|....*
gi 27477105 706 TVLEKYKGIIDSFYQ 720
Cdd:PLN02430 639 NLLKYYQVEIDEMYR 653
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
131-587 |
4.76e-46 |
|
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: 169.78 E-value: 4.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 210
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 DTqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtqqpnqcCVLVYTSGTTGNPK 290
Cdd:cd05934 82 DP----------------------------------------------------------------ASILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 291 GVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVcfaepdalkgslvnTLREVEPT 370
Cdd:cd05934 98 GVVITHANLTFAGYYSARRFGLGE----DDVYLTVLPLFHINAQAVSVLAALSVGATL--------------VLLPRFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 371 ShmgvpRVWEKImeriQEVAAQSGFIRRKMllwaMSVTLEQnltcpgsdlkPFTTRLADylvlAKVRQAlgfakcqknfY 450
Cdd:cd05934 160 S-----RFWSDV----RRYGATVTNYLGAM----LSYLLAQ----------PPSPDDRA----HRLRAA----------Y 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 451 GAAPMMAETQHFFLGLNIRLYAGYGLSETSGPhFMSSPYNYRLYSS-GKLVPGCRVKLVNQD-----AEGIGEICL---W 521
Cdd:cd05934 203 GAPNPPELHEEFEERFGVRLLEGYGMTETIVG-VIGPRDEPRRPGSiGRPAPGYEVRIVDDDgqelpAGEPGELVIrglR 281
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477105 522 GRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIEEAV 587
Cdd:cd05934 282 GWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDM-IRRRGENISSAEVERAI 345
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
147-722 |
6.28e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 168.62 E-value: 6.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 147 KGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQY-IAYDCCANVIMVDtqKQLEKILKIWKQ 225
Cdd:PTZ00216 136 RGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYaLRETECKAIVCNG--KNVPNLLRLMKS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 226 --LPHlkAVVIY-KEPPPNKMA---NVYTMEEFMELGNEvpeEALDAIIDTQQPNQCCVLV-YTSGTTGNPKGVMLSQDN 298
Cdd:PTZ00216 214 ggMPN--TTIIYlDSLPASVDTegcRLVAWTDVVAKGHS---AGSHHPLNIPENNDDLALImYTSGTTGDPKGVMHTHGS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 299 ITwtarYGSQAGDIRPAEV-----QQEVVVSYLPLSHI----AAQIYdlwtgIQWGAQVCFAEPDalkgSLVNT------ 363
Cdd:PTZ00216 289 LT----AGILALEDRLNDLigppeEDETYCSYLPLAHImefgVTNIF-----LARGALIGFGSPR----TLTDTfarphg 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 364 -LREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnltcpgsdlkpFTTRLA-----------DYL 431
Cdd:PTZ00216 356 dLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHA------------------YQSRLRalkegkdtpywNEK 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 432 VLAKVRQALGfAKCQKNFYGAAPMMAETQHFF---LGLNIRlyaGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLV 508
Cdd:PTZ00216 418 VFSAPRAVLG-GRVRAMLSGGGPLSAATQEFVnvvFGMVIQ---GWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLL 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 509 NQD-------AEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENvppV 581
Cdd:PTZ00216 494 DTEeykhtdtPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEY---I 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 582 PIE--EAVKMELPIISN---AMLIGDQRKFLSMLLtlkctldpdtsdqtdnLTEQ--AMEFCQRVGSRAtTVSEIIekKD 654
Cdd:PTZ00216 571 ALEalEALYGQNELVVPngvCVLVHPARSYICALV----------------LTDEakAMAFAKEHGIEG-EYPAIL--KD 631
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477105 655 EAVYQAIEEGIRRVNMNAAARPYHIQKWA-ILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQ 722
Cdd:PTZ00216 632 PEFQKKATESLQETARAAGRKSFEIVRHVrVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFADE 700
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
132-601 |
4.44e-42 |
|
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: 160.09 E-value: 4.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 132 HISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVD 211
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 212 TQkQLEKILkiwkqlPHLKAVVIYKEPPPNKMANVytmeefmELGNEVPEEALDAIIDTQqpNQCCVLVYTSGTTGNPKG 291
Cdd:cd05904 112 AE-LAEKLA------SLALPVVLLDSAEFDSLSFS-------DLLFEADEAEPPVVVIKQ--DDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 292 VMLSQDNITwtARYGSQAGDIRPAEVQQEVVVSYLPLSHIaaqiydlwtgiqWGAQVCFAEPDALKGSLVntlreVepts 371
Cdd:cd05904 176 VMLTHRNLI--AMVAQFVAGEGSNSDSEDVFLCVLPMFHI------------YGLSSFALGLLRLGATVV-----V---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 372 hmgVPR-VWEKIMERIQEVAAQSGFIRRKMLLwAMSvtleqnltcpgsdlkpfTTRLADYLVLAKVRQALGfakcqknfy 450
Cdd:cd05904 233 ---MPRfDLEELLAAIERYKVTHLPVVPPIVL-ALV-----------------KSPIVDKYDLSSLRQIMS--------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 451 GAAPMMAETQHFFLGL--NIRLYAGYGLSETSGP---HFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI------GEIC 519
Cdd:cd05904 283 GAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESlppnqtGELW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 520 LWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISNAML 599
Cdd:cd05904 363 IRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKEL-IKYKGFQVAPAEL-EALLLSHPEILDAAV 440
|
..
gi 27477105 600 IG 601
Cdd:cd05904 441 IP 442
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
100-586 |
1.36e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 158.19 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 100 QLPYTVHRMFYEALDKYGDLIALGF----KRQDKWEHISYSQyyLLAR--RAAKGFLKLGLKQAHSVAILGFNSPEwffs 173
Cdd:PRK07529 22 DLPASTYELLSRAAARHPDAPALSFlldaDPLDRPETWTYAE--LLADvtRTANLLHSLGVGPGDVVAFLLPNLPE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 174 AVGTVFAG---GIVTGIYTTSSPEACQYIAYDCCANVIM-------VDTQKQLEKILKiwkQLPHLKAVVIY----KEPP 239
Cdd:PRK07529 96 THFALWGGeaaGIANPINPLLEPEQIAELLRAAGAKVLVtlgpfpgTDIWQKVAEVLA---ALPELRTVVEVdlarYLPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 240 PNKMAnvytmEEFMELGNEVPEEALDAIIDTQQ-----------PNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQ 308
Cdd:PRK07529 173 PKRLA-----VPLIRRKAHARILDFDAELARQPgdrlfsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGAL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 309 AGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSLVntlreveptshmgVPRVWeKIMERIQe 388
Cdd:PRK07529 248 LLGLGP----GDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGPGV-------------IANFW-KIVERYR- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 389 VAAQSGfirrkmLLWAMSVTLEqnltCP--GSDLkpfttrladylvlakvrQALGFAKCqknfyGAAPMMAET-QHFFLG 465
Cdd:PRK07529 309 INFLSG------VPTVYAALLQ----VPvdGHDI-----------------SSLRYALC-----GAAPLPVEVfRRFEAA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 466 LNIRLYAGYGLSETSGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQDAEG----------IGEICLWGRTIFMGYLNmED 534
Cdd:PRK07529 357 TGVRIVEGYGLTEATCVSSVNPPDGeRRIGSVGLRLPYQRVRVVILDDAGrylrdcavdeVGVLCIAGPNVFSGYLE-AA 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 27477105 535 KTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 586
Cdd:PRK07529 436 HNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIR-GGHNIDPAAIEEA 486
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
129-602 |
8.50e-40 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 156.43 E-value: 8.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 129 KWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYiaydcCANVI 208
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCH-----SLNET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 209 MVDT----QKQLEKILKIWKQLPHLKAVVIYKEPPP------NKMAN--VYTMEEFMELGNEVPEEAldaiiDTQQPNQC 276
Cdd:PLN02387 178 EVTTvicdSKQLKKLIDISSQLETVKRVIYMDDEGVdsdsslSGSSNwtVSSFSEVEKLGKENPVDP-----DLPSPNDI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 277 CVLVYTSGTTGNPKGVMLSQDNITWTArygSQAGDIRPAEVQQEVVVSYLPLSHI---AAQIydlwTGIQWGAQVCFAEP 353
Cdd:PLN02387 253 AVIMYTSGSTGLPKGVMMTHGNIVATV---AGVMTVVPKLGKNDVYLAYLPLAHIlelAAES----VMAAVGAAIGYGSP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 354 DAL--------KGSL--VNTLRevePTSHMGVPRVWEKIMERIQE-VAAQSG---------FIRRKMLL---WAMSVTLE 410
Cdd:PLN02387 326 LTLtdtsnkikKGTKgdASALK---PTLMTAVPAILDRVRDGVRKkVDAKGGlakklfdiaYKRRLAAIegsWFGAWGLE 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 411 QnltcpgsdlkpfttRLADYLVLAKVRQALG----FAKCqknfyGAAPMMAETQHFflgLNIRLYA----GYGLSETSGP 482
Cdd:PLN02387 403 K--------------LLWDALVFKKIRAVLGgrirFMLS-----GGAPLSGDTQRF---INICLGApigqGYGLTETCAG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 483 HFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI---------GEICLWGRTIFMGYLNMEDKTCEA--IDEEG--WLHTG 549
Cdd:PLN02387 461 ATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYlisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTG 540
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 27477105 550 DAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISNAMLIGD 602
Cdd:PLN02387 541 DIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAAL-SVSPYVDNIMVHAD 592
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
99-585 |
1.28e-39 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 154.20 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 99 PQLPYTVHRMFYEALDKYGDLIALGFKRQD-KWehiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWffsaVGT 177
Cdd:PRK08315 12 PLLEQTIGQLLDRTAARYPDREALVYRDQGlRW---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEW----VLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 178 VFAGGIVTGIYTTSSPeacqyiAY------------DCCANVIM--------VDTQKQLEKILKIW-------KQLPHLK 230
Cdd:PRK08315 85 QFATAKIGAILVTINP------AYrlseleyalnqsGCKALIAAdgfkdsdyVAMLYELAPELATCepgqlqsARLPELR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 231 AVVIYKEPPPNKManvYTMEEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAg 310
Cdd:PRK08315 159 RVIFLGDEKHPGM---LNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEA- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 311 dIRPAEvqQEVVVSYLPLSH--------IAAqiydLWTGiqwGAQVCFAEP-DALKgslvnTLREVEP---TSHMGVPrv 378
Cdd:PRK08315 235 -MKLTE--EDRLCIPVPLYHcfgmvlgnLAC----VTHG---ATMVYPGEGfDPLA-----TLAAVEEercTALYGVP-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 379 wekIMeriqevaaqsgFIrrkmllwAMsvtLEQ------NL-----------TCPGSDLKpfttrladylvlakvrqalg 441
Cdd:PRK08315 298 ---TM-----------FI-------AE---LDHpdfarfDLsslrtgimagsPCPIEVMK-------------------- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 442 faKCQKNFYgaapmMAETQhfflglnIrlyaGYGLSETSGPHFMSS---PYNYRLYSSGKLVPGCRVKLVnqDAEG---- 514
Cdd:PRK08315 334 --RVIDKMH-----MSEVT-------I----AYGMTETSPVSTQTRtddPLEKRVTTVGRALPHLEVKIV--DPETgetv 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477105 515 ----IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEE 585
Cdd:PRK08315 394 prgeQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIEE 467
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
133-601 |
3.82e-38 |
|
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: 148.61 E-value: 3.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDT 212
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 213 QKQLEKI-LKIWKQLPHLKAVVIYKEPPPNKMANvytmeefmELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKG 291
Cdd:cd05926 95 GELGPASrAASKLGLAILELALDVGVLIRAPSAE--------SLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 292 VMLSQDNITWTARYGSQAGDIRPAEvqQEVVVsyLPLSHIAAQIYDLWTGIQWGAQVCFaePDALKGSLV-NTLREVEPT 370
Cdd:cd05926 167 VPLTHRNLAASATNITNTYKLTPDD--RTLVV--MPLFHVHGLVASLLSTLAAGGSVVL--PPRFSASTFwPDVRDYNAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 371 SHMGVPRVWEKIMERIQE----VAAQSGFIRrkmllwamsvtleqnlTCpGSDLKPFTtrladylvlakvrqalgFAKCQ 446
Cdd:cd05926 241 WYTAVPTIHQILLNRPEPnpesPPPKLRFIR----------------SC-SASLPPAV-----------------LEALE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 447 KNFygAAPMMaETqhfflglnirlyagYGLSETSgpHFMSS----PYNYRLYSSGKLVpGCRVKLVNQDAE-----GIGE 517
Cdd:cd05926 287 ATF--GAPVL-EA--------------YGMTEAA--HQMTSnplpPGPRKPGSVGKPV-GVEVRILDEDGEilppgVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 518 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISNA 597
Cdd:cd05926 347 ICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINR-GGEKISPLEVDG-VLLSHPAVLEA 424
|
....
gi 27477105 598 MLIG 601
Cdd:cd05926 425 VAFG 428
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-585 |
2.09e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 147.61 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 121 ALGFKRQDKweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQY-I 199
Cdd:PRK12583 36 ALVVRHQAL--RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYaL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 200 AYDCCANVIMVDTQKQ------LEKILK----------IWKQLPHLKAVVIY-KEPPPNKMAnvytMEEFMELGNEVPEE 262
Cdd:PRK12583 114 GQSGVRWVICADAFKTsdyhamLQELLPglaegqpgalACERLPELRGVVSLaPAPPPGFLA----WHELQARGETVSRE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 263 ALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQagdiRPAEVQQEVVVSYLPLSHIAAQIYDLWTGI 342
Cdd:PRK12583 190 ALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAE----SLGLTEHDRLCVPVPLYHCFGMVLANLGCM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 343 QWGAQVCFA----EPDAlkgslvnTLREVEP---TSHMGVPRVWEKIMERIQevaaqsgfiRRKMLLWAMSVTLEQNLTC 415
Cdd:PRK12583 266 TVGACLVYPneafDPLA-------TLQAVEEercTALYGVPTMFIAELDHPQ---------RGNFDLSSLRTGIMAGAPC 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 416 PGSDLKpfttRLADYLvlakvrqalgfakcqknfygaapMMAETQhfflglnirlyAGYGLSETSGPHFMSS---PYNYR 492
Cdd:PRK12583 330 PIEVMR----RVMDEM-----------------------HMAEVQ-----------IAYGMTETSPVSLQTTaadDLERR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 493 LYSSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLK 567
Cdd:PRK12583 372 VETVGRTQPHLEVKVVDPDGAtvprgEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSK 451
|
490
....*....|....*...
gi 27477105 568 ELIITaGGENVPPVPIEE 585
Cdd:PRK12583 452 DMIIR-GGENIYPREIEE 468
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
131-603 |
8.07e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 145.00 E-value: 8.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFL-KLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 209
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 210 VDTQKQlEKILKIWKqlphlkavVIYKEPPpnkmanvytmeefmeLGNEVPEEALDA-IIDTQQPNQ--CCVLVYTSGTT 286
Cdd:PRK06839 106 VEKTFQ-NMALSMQK--------VSYVQRV---------------ISITSLKEIEDRkIDNFVEKNEsaSFIICYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 287 GNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAaqiydlwtGIQwgaqvCFAEPDALKGSLVNTLRE 366
Cdd:PRK06839 162 GKPKGAVLTQENMFWNALNNTFAIDLT----MHDRSIVLLPLFHIG--------GIG-----LFAFPTLFAGGVIIVPRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 367 VEPTSH------------MGVPRVWEKIMERIqevaaqsgfirrkmllwamsvtleqnltcpgsdlKPFTTRLAdylvla 434
Cdd:PRK06839 225 FEPTKAlsmiekhkvtvvMGVPTIHQALINCS----------------------------------KFETTNLQ------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 435 KVRQalgfakcqknFY-GAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYR--LYSSGKLVPGCRVKLVNQD 511
Cdd:PRK06839 265 SVRW----------FYnGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIDEN 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 512 AE-----GIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 586
Cdd:PRK06839 335 KNkvevgEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQV 412
|
490
....*....|....*..
gi 27477105 587 VKmELPIISNAMLIGDQ 603
Cdd:PRK06839 413 IN-KLSDVYEVAVVGRQ 428
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
108-601 |
1.94e-36 |
|
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: 144.21 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 108 MFYeALDKYGDLI-ALGFKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 186
Cdd:cd17642 20 LHK-AMKRYASVPgTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 187 IYTTSSpEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIykepppnkMANVYTMEEFMELGNEVpEEALDA 266
Cdd:cd17642 99 TNDIYN-ERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIII--------LDSKEDYKGYQCLYTFI-TQNLPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 267 IIDTQQ--PN------QCCVLVYTSGTTGNPKGVMLSQDNITwtARYGSQAGDIRPAEVQQEV-VVSYLPLSHiAAQIYD 337
Cdd:cd17642 169 GFNEYDfkPPsfdrdeQVALIMNSSGSTGLPKGVQLTHKNIV--ARFSHARDPIFGNQIIPDTaILTVIPFHH-GFGMFT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 338 LWTGIQWGAQVCFaepdalkgslvntlreveptshmgVPRVWEKI-MERIQEVAAQSGF-IRRKMLLWAMSVTLEQnltc 415
Cdd:cd17642 246 TLGYLICGFRVVL------------------------MYKFEEELfLRSLQDYKVQSALlVPTLFAFFAKSTLVDK---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 416 pgsdlkpftTRLADYLVLAKvrqalgfakcqknfyGAAPMMAETQHFF---LGLN-IRlyAGYGLSETSGPHFMSSPYNY 491
Cdd:cd17642 298 ---------YDLSNLHEIAS---------------GGAPLSKEVGEAVakrFKLPgIR--QGYGLTETTSAILITPEGDD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 492 RLYSSGKLVPGCRVKLVNQDAEGI------GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGR 565
Cdd:cd17642 352 KPGAVGKVVPFFYAKVVDLDTGKTlgpnerGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDR 431
|
490 500 510
....*....|....*....|....*....|....*.
gi 27477105 566 LKELiITAGGENVPPVPIeEAVKMELPIISNAMLIG 601
Cdd:cd17642 432 LKSL-IKYKGYQVPPAEL-ESILLQHPKIFDAGVAG 465
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
281-650 |
8.40e-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: 138.77 E-value: 8.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 281 YTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSL 360
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDP----DDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYRNPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 361 V--NTLREVE---PTSHMGVPRVWEKIMERiqevaaqsgfirrkmllwamsvtleqnltcPGSdlkpfttrlADylvLAK 435
Cdd:cd05944 85 LfdNFWKLVEryrITSLSTVPTVYAALLQV------------------------------PVN---------AD---ISS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 436 VRQALGfakcqknfyGAAPMMAETQHFF---LGLNIrlYAGYGLSETSGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQD 511
Cdd:cd05944 123 LRFAMS---------GAAPLPVELRARFedaTGLPV--VEGYGLTEATCLVAVNPPDGpKRPGSVGLRLPYARVRIKVLD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 512 AEG----------IGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPV 581
Cdd:cd05944 192 GVGrllrdcapdeVGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIR-GGHNIDPA 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477105 582 PIEEAVkMELPIISNAMLIGDQRKFLSMLLTLKCTLDPDTSDQTDNLTEQAMEfcqRVGSRATTVSEII 650
Cdd:cd05944 270 LIEEAL-LRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWARD---HVPERAAVPKHIE 334
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
134-601 |
7.50e-35 |
|
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: 139.30 E-value: 7.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 134 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSP---EWFFSAVGtvfAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 210
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHrhlELYYAVPG---MGAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 DtqKQLEKIL-KIWKQLPHLKAVVIYK---EPPPNKMANVYTMEEFMElgnevpEEALDAIIDTQQPNQCCVLVYTSGTT 286
Cdd:cd12119 104 D--RDFLPLLeAIAPRLPTVEHVVVMTddaAMPEPAGVGVLAYEELLA------AESPEYDWPDFDENTAAAICYTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 287 GNPKGVMLSQDNiTWTARYGSQAGDIRPAEvQQEVVVSYLPLSHIAAqiydlW----TGIQWGAQVCFAEPDALKGSLVN 362
Cdd:cd12119 176 GNPKGVVYSHRS-LVLHAMAALLTDGLGLS-ESDVVLPVVPMFHVNA-----WglpyAAAMVGAKLVLPGPYLDPASLAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 363 TLREVEPTSHMGVPRVWEkimeriqevaaqsgfirrkMLLwamsvtleQNLTCPGSDLKPfttrladylvLAKVrqALGf 442
Cdd:cd12119 249 LIEREGVTFAAGVPTVWQ-------------------GLL--------DHLEANGRDLSS----------LRRV--VIG- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 443 akcqknfyGAA--PMMAETqhfFLGLNIRLYAGYGLSETS--------GPHFMSSPY----NYRLySSGKLVPGCRVKLV 508
Cdd:cd12119 289 --------GSAvpRSLIEA---FEERGVRVIHAWGMTETSplgtvarpPSEHSNLSEdeqlALRA-KQGRPVPGVELRIV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 509 NQ-------DAEGIGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPV 581
Cdd:cd12119 357 DDdgrelpwDGKAVGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKDV-IKSGGEWISSV 434
|
490 500
....*....|....*....|
gi 27477105 582 PIEEAVkMELPIISNAMLIG 601
Cdd:cd12119 435 ELENAI-MAHPAVAEAAVIG 453
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
108-605 |
2.04e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 138.98 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 108 MFYEALDKYGDLIALGF--KRQdkwehiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEwffsAVGTVFA----G 181
Cdd:PRK05605 37 LYDNAVARFGDRPALDFfgATT------TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQ----HIVAFYAvlrlG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 182 GIVT---GIYTTSSPE-------ACQYIAYDCCANVI--MVDTQkQLEKIL--KIWKQLPHLKAVVIyKEPPPNKMAnvy 247
Cdd:PRK05605 107 AVVVehnPLYTAHELEhpfedhgARVAIVWDKVAPTVerLRRTT-PLETIVsvNMIAAMPLLQRLAL-RLPIPALRK--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 248 tMEEFMELG--NEVPEEALDA--------IIDTQQPNQCCV--LVYTSGTTGNPKGVMLSQDNITWTARYGsQA--GDIR 313
Cdd:PRK05605 182 -ARAALTGPapGTVPWETLVDaaiggdgsDVSHPRPTPDDValILYTSGTTGKPKGAQLTHRNLFANAAQG-KAwvPGLG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 314 PaevQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWEKIMEriqevAAQ 392
Cdd:PRK05605 260 D---GPERVLAALPMFHAYGLTLCLTLAVSIGGElVLLPAPDI--DLILDAMKKHPPTWLPGVPPLYEKIAE-----AAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 393 sgfirrkmllwamsvtlEQNLTcpgsdlkpfttrladylvLAKVRQAlgfakcqknFYGAAPMMAETQHFFLGL-NIRLY 471
Cdd:PRK05605 330 -----------------ERGVD------------------LSGVRNA---------FSGAMALPVSTVELWEKLtGGLLV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 472 AGYGLSETSgPHFMSSPYN--YRLYSSGKLVPGCRVKLVNQD------AEG-IGEICLWGRTIFMGYLNMEDKTCEAIdE 542
Cdd:PRK05605 366 EGYGLTETS-PIIVGNPMSddRRPGYVGVPFPDTEVRIVDPEdpdetmPDGeEGELLVRGPQVFKGYWNRPEETAKSF-L 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477105 543 EGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISNAMLIGDQRK 605
Cdd:PRK05605 444 DGWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEEVLR-EHPGVEDAAVVGLPRE 504
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
116-601 |
6.04e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 136.65 E-value: 6.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 116 YGDLIALGFKR-QDK----WEH--ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIY 188
Cdd:PRK06188 14 YGHLLVSALKRyPDRpalvLGDtrLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 189 TTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVViykepppnKMANVYTMEEFMELGNEVPEEALDAII 268
Cdd:PRK06188 94 PLGSLDDHAYVLEDAGISTLIVDPAPFVERALALLARVPSLKHVL--------TLGPVPDGVDLLAAAAKFGPAPLVAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 269 DTQQPNqccVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIrPAEVQqevvvsYL---PLSHIAAqiydlwtgiqwg 345
Cdd:PRK06188 166 LPPDIA---GLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEW-PADPR------FLmctPLSHAGG------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 346 aqvCFAEPDALKGSLVNTLREVEPTShmgVPRVWEKimERIQEVaaqsgfirrkMLLWAMSVTLeqnLTCPGSdlkpftt 425
Cdd:PRK06188 224 ---AFFLPTLLRGGTVIVLAKFDPAE---VLRAIEE--QRITAT----------FLVPTMIYAL---LDHPDL------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 426 RLADYLVLAKVrqalgfakcqknFYGAAPMMAetqhfflglnIRLYAG-----------YGLSE--------TSGPHFMS 486
Cdd:PRK06188 276 RTRDLSSLETV------------YYGASPMSP----------VRLAEAierfgpifaqyYGQTEapmvitylRKRDHDPD 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 487 SPYnyRLYSSGKLVPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLY 561
Cdd:PRK06188 334 DPK--RLTSCGRPTPGLRVALLDEDgrevAQGeVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYY 410
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 27477105 562 ITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:PRK06188 411 IVDRKKDMIVT-GGFNVFPREVEDVL-AEHPAVAQVAVIG 448
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
134-601 |
6.58e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 133.95 E-value: 6.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 134 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG---IYTtsSPEAC-QYIAydccANVIM 209
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTanpFYT--PAEIAkQAKA----SGAKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 210 VDTQKQLEKILKIWKQLPHLKAVVIyKEPPPNKManvytmeEFMELGNEVPEEALDAIIDtqqPNQCCVLVYTSGTTGNP 289
Cdd:PLN02246 126 IITQSCYVDKLKGLAEDDGVTVVTI-DDPPEGCL-------HFSELTQADENELPEVEIS---PDDVVALPYSSGTTGLP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 290 KGVMLSQDN-ITWTArygsqagdirpaevQQ-------------EVVVSYLPLSHIAAQIYDLWTGIQWGAQVCfaepda 355
Cdd:PLN02246 195 KGVMLTHKGlVTSVA--------------QQvdgenpnlyfhsdDVILCVLPMFHIYSLNSVLLCGLRVGAAIL------ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 356 lkgslvntlreveptshmgvprvwekIMERIqEVAAQSGFIRRKMLLWAMSV-----TLEQNltcpgsdlkPFTTRlADy 430
Cdd:PLN02246 255 --------------------------IMPKF-EIGALLELIQRHKVTIAPFVppivlAIAKS---------PVVEK-YD- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 431 lvLAKVRQALGfakcqknfyGAAPMMAETQHFFLGL--NIRLYAGYGLSEtSGP------HFMSSPYNYRLYSSGKLVPG 502
Cdd:PLN02246 297 --LSSIRMVLS---------GAAPLGKELEDAFRAKlpNAVLGQGYGMTE-AGPvlamclAFAKEPFPVKSGSCGTVVRN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 503 CRVKLVNQDAeGI-------GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGG 575
Cdd:PLN02246 365 AELKIVDPET-GAslprnqpGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 443
|
490 500
....*....|....*....|....*.
gi 27477105 576 EnVPPVPIeEAVKMELPIISNAMLIG 601
Cdd:PLN02246 444 Q-VAPAEL-EALLISHPSIADAAVVP 467
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
133-601 |
2.34e-32 |
|
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: 130.49 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFL-KLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSspeacqyiaydccanvimvd 211
Cdd:cd05941 12 ITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSY-------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 212 TQKQLEKILkiwkqlphlkavviykepppnkmanvytmeefmelGNEVPEEALDAiidtqqpnqcCVLVYTSGTTGNPKG 291
Cdd:cd05941 72 PLAELEYVI-----------------------------------TDSEPSLVLDP----------ALILYTSGTTGRPKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 292 VMLSQDNITWTARYGSQAGDIRPAEVQQEVvvsyLPLSHIAAQIYDLWTGIQWGAQVCF-AEPDAlkgSLVNTLREVEP- 369
Cdd:cd05941 107 VVLTHANLAANVRALVDAWRWTEDDVLLHV----LPLHHVHGLVNALLCPLFAGASVEFlPKFDP---KEVAISRLMPSi 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 370 TSHMGVPRVWEKIMERIQEVAAQSGFIRrkmllwamsvtleqnltcpgsdlkpfttrladylvlakvrqALGFAKCQKNF 449
Cdd:cd05941 180 TVFMGVPTIYTRLLQYYEAHFTDPQFAR-----------------------------------------AAAAERLRLMV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 450 YGAAPMMAETQHFFLGLN-IRLYAGYGLSETSgphfM--SSPYN--YRLYSSGKLVPGCRVKLVNQ------DAEGIGEI 518
Cdd:cd05941 219 SGSAALPVPTLEEWEAITgHTLLERYGMTEIG----MalSNPLDgeRRPGTVGMPLPGVQARIVDEetgeplPRGEVGEI 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 519 CLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVkMELPIISNAM 598
Cdd:cd05941 295 QVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVL-LAHPGVSECA 373
|
...
gi 27477105 599 LIG 601
Cdd:cd05941 374 VIG 376
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
115-601 |
3.91e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 131.21 E-value: 3.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 115 KYGDLIALGFkRQDKWehiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPE 194
Cdd:PRK08316 23 RYPDKTALVF-GDRSW---TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 195 ACQYIAYDCCANVIMVDTQ--KQLEKILKIWKQLPHLKAVVIYKEPPPNKMANvytmeeFMELGNEVPEEALDAIIDTQQ 272
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPAlaPTAEAALALLPVDTLILSLVLGGREAPGGWLD------FADWAEAGSVAEPDVELADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 273 PNQccvLVYTSGTTGNPKGVMLSQDNITWtaRYGSQ--AGDIRPAEVQqevvVSYLPLSHiAAQIY-----DLWTGiqwG 345
Cdd:PRK08316 173 LAQ---ILYTSGTESLPKGAMLTHRALIA--EYVSCivAGDMSADDIP----LHALPLYH-CAQLDvflgpYLYVG---A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 346 AQVCFAEPDAlkGSLVNTLREVEPTSHMGVPRVWekimeriqevaaqsgfirrkmllwamsVTLeqnLTCPGSDlkpfTT 425
Cdd:PRK08316 240 TNVILDAPDP--ELILRTIEAERITSFFAPPTVW---------------------------ISL---LRHPDFD----TR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 426 RLadylvlakvrQALgfakcQKNFYGAAPM----MAETQHFFLGLniRLYAGYGLSETSGPHFMSSPYNY--RLYSSGKL 499
Cdd:PRK08316 284 DL----------SSL-----RKGYYGASIMpvevLKELRERLPGL--RFYNCYGQTEIAPLATVLGPEEHlrRPGSAGRP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 500 VPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaG 574
Cdd:PRK08316 347 VLNVETRVVDDDgndvAPGeVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKT-G 424
|
490 500
....*....|....*....|....*..
gi 27477105 575 GENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:PRK08316 425 GENVASREVEEAL-YTHPAVAEVAVIG 450
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
130-721 |
5.23e-32 |
|
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: 131.40 E-value: 5.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 130 WEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAG---GIVTGIYTTSSPE--ACQYIAYDCC 204
Cdd:cd05921 23 WRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGvpaAPVSPAYSLMSQDlaKLKHLFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 205 ANVIMVDTQKQLEKILKIWKqLPHLKAVVIYKEPPPNKMANvytmeeFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSG 284
Cdd:cd05921 103 PGLVFAQDAAPFARALAAIF-PLGTPLVVSRNAVAGRGAIS------FAELAATPPTAAVDAAFAAVGPDTVAKFLFTSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 285 TTGNPKGVMLSQDNITwtaryGSQAGDIRPAEVQQE---VVVSYLPLSHIAAQIYD----LWTG----IQWGAQVcfaeP 353
Cdd:cd05921 176 STGLPKAVINTQRMLC-----ANQAMLEQTYPFFGEeppVLVDWLPWNHTFGGNHNfnlvLYNGgtlyIDDGKPM----P 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 354 DALKGSLVNtLREVEPTSHMGVPRVWEKI---MERiQEVAAQSGFIRRKMLLWAmsvtleqnltcpGSDLKPFT-TRLad 429
Cdd:cd05921 247 GGFEETLRN-LREISPTVYFNVPAGWEMLvaaLEK-DEALRRRFFKRLKLMFYA------------GAGLSQDVwDRL-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 430 ylvlakvrQALGFAKCqknfygaapmmaetqhfflGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVN 509
Cdd:cd05921 311 --------QALAVATV-------------------GERIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 510 QDaeGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRL----DADGFLYITGRLKELIITAGGENVPPVPIE- 584
Cdd:cd05921 364 SG--GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVGPLRa 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 585 EAVKMELPIISNAMLIGDQRKFLSMLLTlkctldPDTSDqtdnlteqamefCQR-VGSRATTVSEIIekKDEAVYQAIEE 663
Cdd:cd05921 442 RAVAACAPLVHDAVVAGEDRAEVGALVF------PDLLA------------CRRlVGLQEASDAEVL--RHAKVRAAFRD 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477105 664 GIRRVNMNAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQE 721
Cdd:cd05921 502 RLAALNGEATGSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYAD 559
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
273-601 |
1.02e-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: 126.62 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 273 PNQCCVLVYTSGTTGNPKGVMLSQDNItwtARYGSQAGDiRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAE 352
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNI---VNNGYFIGE-RLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 353 P--DALKgslvnTLREVEP---TSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAmsvtleqnlTCPGSdlkpfttrl 427
Cdd:cd05917 77 PsfDPLA-----VLEAIEKekcTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGA---------PCPPE--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 428 adylVLAKVRQALGFAKCQknfygaapmmaetqhfflglnirlyAGYGLSETSGPHFMSS---PYNYRLYSSGKLVPGCR 504
Cdd:cd05917 134 ----LMKRVIEVMNMKDVT-------------------------IAYGMTETSPVSTQTRtddSIEKRVNTVGRIMPHTE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 505 VKLVnqDAEG--------IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGE 576
Cdd:cd05917 185 AKIV--DPEGgivppvgvPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGE 261
|
330 340
....*....|....*....|....*
gi 27477105 577 NVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:cd05917 262 NIYPREIEEFL-HTHPKVSDVQVVG 285
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
117-588 |
3.86e-31 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 128.51 E-value: 3.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 117 GDLIALGF--KRQDKWEHISYSQYYLLARRAAKGFLKLGlKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPE 194
Cdd:cd05931 7 PDRPAYTFldDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 195 A---CQYIAYDCCANVIMVDTqkqlekilkiwkqlPHLKAVVIYKEPPPnkmanvytmeEFMELGNEVPEEALDAIIDTQ 271
Cdd:cd05931 86 HaerLAAILADAGPRVVLTTA--------------AALAAVRAFAASRP----------AAGTPRLLVVDLLPDTSAADW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 272 QPNQC-----CVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHiaaqiyDLwtgiqwga 346
Cdd:cd05931 142 PPPSPdpddiAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDP----GDVVVSWLPLYH------DM-------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 347 qvcfaepdALKGSLVNTLreveptsHMGVPRVWekiMeriqevaAQSGFIRRKML-LWAMSvtlEQNLTCPGS-----DL 420
Cdd:cd05931 204 --------GLIGGLLTPL-------YSGGPSVL---M-------SPAAFLRRPLRwLRLIS---RYRATISAApnfayDL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 421 --KPFTTRLADYLVLAKVRQALgfakcqkNfyGAAPMMAET-QHF---FLGLNIR---LYAGYGLSE-----TSGPHF-- 484
Cdd:cd05931 256 cvRRVRDEDLEGLDLSSWRVAL-------N--GAEPVRPATlRRFaeaFAPFGFRpeaFRPSYGLAEatlfvSGGPPGtg 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 485 -------------------MSSPYNYRLYSSGKLVPGCRVKLVNQD-----AEG-IGEICLWGRTIFMGYLNMEDKTCE- 538
Cdd:cd05931 327 pvvlrvdrdalagravavaADDPAARELVSCGRPLPDQEVRIVDPEtgrelPDGeVGEIWVRGPSVASGYWGRPEATAEt 406
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 27477105 539 -----AIDEEGWLHTGDAGRLdADGFLYITGRLKELIITAgGENVPPVPIEEAVK 588
Cdd:cd05931 407 fgalaATDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVR-GRNHYPQDIEATAE 459
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
104-601 |
5.17e-31 |
|
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: 127.98 E-value: 5.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 104 TVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGI 183
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDR----TLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 184 VTGIYTTSSPEACQYIAYDCCANvIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKmanvytmeEFMELGNEVPEEA 263
Cdd:TIGR03098 77 FVPINPLLKAEQVAHILADCNVR-LLVTSSERLDLLHPALPGCHDLRTLIIVGDPAHAS--------EGHPGEEPASWPK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 264 LDAIIDTQQPNQC------CVLvYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAevqqEVVVSYLPLSHIAAQiYD 337
Cdd:TIGR03098 148 LLALGDADPPHPVidsdmaAIL-YTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPD----DRLLAVLPLSFDYGF-NQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 338 LWTGIQWGAQVCFAEPdALKGSLVNTLREVEPTSHMGVPRVWEKIME-RIQEVAAQSgfIRRkmllwamsvtleqnLTCP 416
Cdd:TIGR03098 222 LTTAFYVGATVVLHDY-LLPRDVLKALEKHGITGLAAVPPLWAQLAQlDWPESAAPS--LRY--------------LTNS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 417 GSDLKPFTtrladylvLAKVRQALGfakcqknfygaapmmaetqhfflglNIRLYAGYGLSETsgphFMSS---P--YNY 491
Cdd:TIGR03098 285 GGAMPRAT--------LSRLRSFLP-------------------------NARLFLMYGLTEA----FRSTylpPeeVDR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 492 RLYSSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCE----AIDEEGWLH-------TGDAGRLD 555
Cdd:TIGR03098 328 RPDSIGKAIPNAEVLVLREDGSecapgEEGELVHRGALVAMGYWNDPEKTAErfrpLPPFPGELHlpelavwSGDTVRRD 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 27477105 556 ADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:TIGR03098 408 EEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVA-YATGLVAEAVAFG 451
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
277-586 |
2.59e-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: 122.05 E-value: 2.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 277 CVLVYTSGTTGNPKGVMLSQDNITWTARyGSQAgdiRPAEVQQEVVVSYLPLSHIAAQiYDLWTGIQWGAQVCFAEPDAL 356
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAA-GLHS---RLGFGGGDSWLLSLPLYHVGGL-AILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 357 kgsLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFirRKMLLwamsvtleqnltcpgsdlkpfttrladylvlakv 436
Cdd:cd17630 78 ---LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSL--RAVLL---------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 437 rqalgfakcqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQdaegiG 516
Cdd:cd17630 119 --------------GGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----G 179
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 517 EICLWGRTIFMGYLNMEdkTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 586
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAA 246
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
110-601 |
3.78e-30 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 125.99 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 110 YEALDKY----GDLIALGFKRQDKWE-HISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIV 184
Cdd:COG0365 12 YNCLDRHaegrGDKVALIWEGEDGEErTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 185 TGIYTTSSPEACQYIAYDCCANVIMVD--------TQKQLEKILKIWKQLPHLKAVVIYKEP-PPNKMANVYTMEEFMEL 255
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITAdgglrggkVIDLKEKVDEALEELPSLEHVIVVGRTgADVPMEGDLDWDELLAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 256 -GNEVPEEALDAiidtqqpNQCCVLVYTSGTTGNPKGVMLSQD----NITWTARYGSqagDIRPAEVqqevvvsYLPLSH 330
Cdd:COG0365 172 aSAEFEPEPTDA-------DDPLFILYTSGTTGKPKGVVHTHGgylvHAATTAKYVL---DLKPGDV-------FWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 331 IAaqiydlWTGIQW---------GAQVCFAE-----PDAlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFI 396
Cdd:COG0365 235 IG------WATGHSyivygpllnGATVVLYEgrpdfPDP--GRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 397 RRKMLlwaMSVtleqnltcpGSDLKPfttrladyLVLAKVRQALGfakcqknfygaapmmaetqhfflglnIRLYAGYGL 476
Cdd:COG0365 307 SLRLL---GSA---------GEPLNP--------EVWEWWYEAVG--------------------------VPIVDGWGQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 477 SETSGpHFMSSPYNYRLY--SSGKLVPGCRVKLVnqDAEG-------IGEICL---W-GrtIFMGYLNMEDKTCEAI--D 541
Cdd:COG0365 341 TETGG-IFISNLPGLPVKpgSMGKPVPGYDVAVV--DEDGnpvppgeEGELVIkgpWpG--MFRGYWNDPERYRETYfgR 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 542 EEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:COG0365 416 FPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESAL-VSHPAVAEAAVVG 473
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
128-586 |
4.03e-30 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 125.17 E-value: 4.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 128 DKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANV 207
Cdd:cd05959 25 DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 208 IMVdTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMAnvytmeeFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTG 287
Cdd:cd05959 105 VVV-SGELAPVLAAALTKSEHTLVVLIVSGGAGPEAG-------ALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 288 NPKGVMLSQDNITWTAR-YGSQAGDIRPAevqqEVVVSYLPLSHI----AAQIYDLWTGiqwGAQVCFAE---PDAlkgs 359
Cdd:cd05959 177 RPKGVVHLHADIYWTAElYARNVLGIRED----DVCFSAAKLFFAyglgNSLTFPLSVG---ATTVLMPErptPAA---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 360 LVNTLREVEPTSHMGVPRVWEKIMEriQEVAAQSGFIRRKMLLWAMSVTleqnltcPGSDLKPFTTRladylvlakvrqa 439
Cdd:cd05959 246 VFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEAL-------PAEVGERWKAR------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 440 lgfakcqknfygaapmmaetqhffLGLNIRlyagYGLSETSGPH-FMSS-PYNYRLYSSGKLVPGCRVKLVNQDAE---- 513
Cdd:cd05959 304 ------------------------FGLDIL----DGIGSTEMLHiFLSNrPGRVRYGTTGKPVPGYEVELRDEDGGdvad 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477105 514 -GIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIEEA 586
Cdd:cd05959 356 gEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDM-LKVSGIWVSPFEVESA 427
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
100-668 |
8.67e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 124.76 E-value: 8.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 100 QLPYTV-------HRMFYEALDKYGDLIALGFKRQDkwehISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFF 172
Cdd:PRK06710 14 EIPSTIsydiqplHKYVEQMASRYPEKKALHFLGKD----ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 173 SAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM-----------VDTQKQLEKIL--KIWKQLPHLKAVV--IYKE 237
Cdd:PRK06710 90 GYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnVQSATKIEHVIvtRIADFLPFPKNLLypFVQK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 238 PPPNKMANVyTMEEFMELGNEVPEE---ALDAIIDTQqpNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAgdIRP 314
Cdd:PRK06710 170 KQSNLVVKV-SESETIHLWNSVEKEvntGVEVPCDPE--NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQW--LYN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 315 AEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKgSLVNTLREVEPTSHMGVPRVWEKIMEriqevaaqsg 394
Cdd:PRK06710 245 CKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMK-MVFEAIKKHKVTLFPGAPTIYIALLN---------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 395 firrkmllwamsvtleqnltcpgsdlkpfTTRLADYLVlAKVRQALGfakcqknfyGAAPMMAETQHFFLGLNI-RLYAG 473
Cdd:PRK06710 314 -----------------------------SPLLKEYDI-SSIRACIS---------GSAPLPVEVQEKFETVTGgKLVEG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 474 YGLSEtsgphfmSSPYNYRLYSSGKLVPGC-RVKLVNQDAE-------------GIGEICLWGRTIFMGYLNMEDKTCeA 539
Cdd:PRK06710 355 YGLTE-------SSPVTHSNFLWEKRVPGSiGVPWPDTEAMimsletgealppgEIGEIVVKGPQIMKGYWNKPEETA-A 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 540 IDEEGWLHTGDAGRLDADGFLYITGRLKELIItAGGENVPPVPIEEaVKMELPIISNAMLIGDQRKFLSMLLTLKCTLDP 619
Cdd:PRK06710 427 VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIV-ASGFNVYPREVEE-VLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE 504
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 27477105 620 DTSDQTDNLTEQAMEFCQrvgsrATTVSEIIEKKDEAVYQAIEEGIRRV 668
Cdd:PRK06710 505 GTECSEEELNQFARKYLA-----AYKVPKVYEFRDELPKTTVGKILRRV 548
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
271-604 |
2.83e-29 |
|
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: 121.33 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 271 QQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQqeVVVSylPLSHIAAQIYDLWTGIQWGAQVCF 350
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF--LVAS--PMAHQTGFVYGFTLPLLLGAPVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 351 AEP-DALKGslVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRrKMLlwamsvtleqnltCPGSDLKPFTTRLAD 429
Cdd:cd05903 166 QDIwDPDKA--LALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLR-TFV-------------CGGATVPRSLARRAA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 430 YLVLAKVRQALGfakcqknfygaapmMAETQHFFlglnirlyagyGLSEtsgphfmSSPYNYRLYSSGKLVPGCRVKLVN 509
Cdd:cd05903 230 ELLGAKVCSAYG--------------STECPGAV-----------TSIT-------PAPEDRRLYTDGRPLPGVEIKVVD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 510 QD-----AEGIGEICLWGRTIFMGYLNMEDKTCEAiDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIE 584
Cdd:cd05903 278 DTgatlaPGVEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVE 355
|
330 340
....*....|....*....|..
gi 27477105 585 EAVkMELPIISNAMLIG--DQR 604
Cdd:cd05903 356 DLL-LGHPGVIEAAVVAlpDER 376
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
278-601 |
3.10e-29 |
|
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: 120.91 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 278 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAepDALK 357
Cdd:cd05912 81 TIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT----EDDNWLCALPLFHISG-LSILMRSVIYGMTVYLV--DKFD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 358 GSLVNTLREVEPTSHMG-VPRVWEKIMERIQEVAAQSgfiRRKMLLWAmsvtleqnltcpgsdlkpfttrladylvlakv 436
Cdd:cd05912 154 AEQVLHLINSGKVTIISvVPTMLQRLLEILGEGYPNN---LRCILLGG-------------------------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 437 rqalGFAkcqknfygAAPMMAETQHfflgLNIRLYAGYGLSETSGPHFMSSPYNY--RLYSSGKLVPGCRVKLVN--QDA 512
Cdd:cd05912 199 ----GPA--------PKPLLEQCKE----KGIPVYQSYGMTETCSQIVTLSPEDAlnKIGSAGKPLFPVELKIEDdgQPP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 513 EGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIItAGGENVPPVPIEEAVKmELP 592
Cdd:cd05912 263 YEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEVLL-SHP 339
|
....*....
gi 27477105 593 IISNAMLIG 601
Cdd:cd05912 340 AIKEAGVVG 348
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
275-603 |
5.10e-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: 120.63 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 275 QCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIAAQIYdLWTGIQWGAQVCFAEPD 354
Cdd:TIGR01923 112 QIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGF----TEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDKF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 355 A-LKGSLVNtlrevEPTSHMG-VPrvwekimeriqevaaqsgfirrKMLLWamsvTLEQNLTCpgsdlkpfttrladyLV 432
Cdd:TIGR01923 187 NqLLEMIAN-----ERVTHISlVP----------------------TQLNR----LLDEGGHN---------------EN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 433 LAKVRqaLGFAKCqknfygAAPMMAETQHfflgLNIRLYAGYGLSETSGPHFMSSP--YNYRLySSGKLVPGCRVKLVNQ 510
Cdd:TIGR01923 221 LRKIL--LGGSAI------PAPLIEEAQQ----YGLPIYLSYGMTETCSQVTTATPemLHARP-DVGRPLAGREIKIKVD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 511 DAEGIGEICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKmE 590
Cdd:TIGR01923 288 NKEGHGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIIS-GGENIYPEEIETVLY-Q 364
|
330
....*....|...
gi 27477105 591 LPIISNAMLIGDQ 603
Cdd:TIGR01923 365 HPGIQEAVVVPKP 377
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
131-601 |
7.49e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 121.15 E-value: 7.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 210
Cdd:PRK06145 26 QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 DTQkqlekiLKIWKQLPHLKAVViykepppNKMANVYTmEEFMELGNEVPEEALDAiidtqqPNQCCVLVYTSGTTGNPK 290
Cdd:PRK06145 106 DEE------FDAIVALETPKIVI-------DAAAQADS-RRLAQGGLEIPPQAAVA------PTDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 291 GVMLSQDNITW-----TARYGSQAGDirpaevqQEVVVSylPLSHIAAqiYDLwTGIQWGAQvcfaepdalkGSLVNTLR 365
Cdd:PRK06145 166 GVMHSYGNLHWksidhVIALGLTASE-------RLLVVG--PLYHVGA--FDL-PGIAVLWV----------GGTLRIHR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 366 EVEPtshmgvprvwEKIMERIQEvaaqsgfiRRKMLLWAMSVTLEQNLTCPgsdlkpftTRlaDYLVLAKVRQALGFAKc 445
Cdd:PRK06145 224 EFDP----------EAVLAAIER--------HRLTCAWMAPVMLSRVLTVP--------DR--DRFDLDSLAWCIGGGE- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 446 qknfygAAPMMAETQHFFLGLNIRLYAGYGLSET-SGPHFMSSPYNY-RLYSSGKLVPGCRVKLVNQDAEGI-----GEI 518
Cdd:PRK06145 275 ------KTPESRIRDFTRVFTRARYIDAYGLTETcSGDTLMEAGREIeKIGSTGRALAHVEIRIADGAGRWLppnmkGEI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 519 CLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAM 598
Cdd:PRK06145 349 CMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEVERVI-YELPEVAEAA 425
|
...
gi 27477105 599 LIG 601
Cdd:PRK06145 426 VIG 428
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
278-601 |
1.06e-28 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 117.37 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 278 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQqevvVSYLPLSHIAAQIYDLWTGIQWGAQVC---FAEPD 354
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVY----LNMLPLFHIAGLNLALATFHAGGANVVmekFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 355 ALKgslvntLREVEPTSHMG--VPrvwekIMERIQEVAAQSGfirrkmllwamsvtleqnltcpgsdlkpfttrladyLV 432
Cdd:cd17637 80 ALE------LIEEEKVTLMGsfPP-----ILSNLLDAAEKSG------------------------------------VD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 433 LAKVRQALGFAkcqknfygaAPmmaETQHFFLGL-NIRLYAGYGLSETSGPHFMSsPYNYRLYSSGKLVPGCRVKLVNQD 511
Cdd:cd17637 113 LSSLRHVLGLD---------AP---ETIQRFEETtGATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVDDN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 512 -----AEGIGEICLWGRTIFMGYLNMEDKTCEAIDEeGWLHTGDAGRLDADGFLYITGRL--KELIITaGGENVPPVPIE 584
Cdd:cd17637 180 drpvpAGETGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPAEVE 257
|
330
....*....|....*..
gi 27477105 585 EAVkMELPIISNAMLIG 601
Cdd:cd17637 258 KVI-LEHPAIAEVCVIG 273
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
131-594 |
1.23e-28 |
|
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: 120.85 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVaILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSpeacqyiAYDCCANvimv 210
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEDFIPAFWACVLAGFVPAPLTVPP-------TYDEPNA---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 dtqkQLEKILKIWKQLPhlKAVVIykepppnkmANVYTMEEFMELGNE---------VPEEALDAIIDT----QQPNQCC 277
Cdd:cd05906 106 ----RLRKLRHIWQLLG--SPVVL---------TDAELVAEFAGLETLsglpgirvlSIEELLDTAADHdlpqSRPDDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 278 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAA----QIYDLWTGIQwgaQVcfaep 353
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTP----QDVFLNWVPLDHVGGlvelHLRAVYLGCQ---QV----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 354 dalkgslvNTlrevePTSHM-GVPRVWEKIMERIQevAAQSgfirrkmllWA----MSVTLEQnltcpgsdLKPFTTRLA 428
Cdd:cd05906 239 --------HV-----PTEEIlADPLRWLDLIDRYR--VTIT---------WApnfaFALLNDL--------LEEIEDGTW 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 429 DylvLAKVRQALGfakcqknfyGAAPMMAETQHFFL------GLNIR-LYAGYGLSET-SGPHFMSSPYNY------RLY 494
Cdd:cd05906 287 D---LSSLRYLVN---------AGEAVVAKTIRRLLrllepyGLPPDaIRPAFGMTETcSGVIYSRSFPTYdhsqalEFV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 495 SSGKLVPGCRVKLVNQDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDaDGFLYITGRLKEL 569
Cdd:cd05906 355 SLGRPIPGVSMRIVDDEGQLlpegeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDT 433
|
490 500
....*....|....*....|....*
gi 27477105 570 IITaGGENVPPVPIEEAVKmELPII 594
Cdd:cd05906 434 IIV-NGVNYYSHEIEAAVE-EVPGV 456
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
104-601 |
1.47e-28 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 120.56 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 104 TVHRMFYEALDKYGDLIALGFK-RQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGG 182
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALIFEsSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 183 IVTGIYTTSSPEACQYIAYDCCANVIMVDtqkqlEKILKIWKQLPH-----LKAVVIYKEPPPnKMANVYtmeEFMELGN 257
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTS-----AQFYPMYRQIQQedatpLRHICLTRVALP-ADDGVS---SFTQLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 258 EVPEEALDAII----DTQQpnqccvLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAA 333
Cdd:PRK08008 159 QQPATLCYAPPlstdDTAE------ILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALR----DDDVYLTVMPAFHIDC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 334 QiydlwtgiqwgaqvCFAEPDALkgSLVNTLREVEPTShmgVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNl 413
Cdd:PRK08008 229 Q--------------CTAAMAAF--SAGATFVLLEKYS---ARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQH- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 414 tcpgsdlkpfttRLAD---YLVLAKvrqalgfakcqknfygaapmmAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYN 490
Cdd:PRK08008 289 ------------CLREvmfYLNLSD---------------------QEKDAFEERFGVRLLTSYGMTETIVGIIGDRPGD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 491 YRLYSS-GKLVPGCRVKLVNQD-----AEGIGEICLWG---RTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLY 561
Cdd:PRK08008 336 KRRWPSiGRPGFCYEAEIRDDHnrplpAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFY 415
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 27477105 562 ITGRlKELIITAGGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:PRK08008 416 FVDR-RCNMIKRGGENVSCVELENII-ATHPKIQDIVVVG 453
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
134-604 |
1.66e-27 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 117.54 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 134 SYSQYYLLARRAAKGFLKLGLKQAHSVAilgFNSPEWF-FSAV--GTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 210
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVA---FQLPGWCeFTIIylACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 DTQ-KQ---LEKILKIWKQLPHLKAVVIykepppnkmanvytmeeFMELGNEVPEEALDAIIDTQQPNQ----------C 276
Cdd:PRK06087 128 PTLfKQtrpVDLILPLQNQLPQLQQIVG-----------------VDKLAPATSSLSLSQIIADYEPLTtaitthgdelA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 277 CVLvYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIaaqiydlwTGIQWGAQVCFaepdaL 356
Cdd:PRK06087 191 AVL-FTSGTEGLPKGVMLTHNNILASERAYCARLNL----TWQDVFMMPAPLGHA--------TGFLHGVTAPF-----L 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 357 KGSLVntlreveptshmgvprvwekIMERIQEVAAQSGFIRRKMLLWAMSVTleqnltcpgsdlkPFTtrladYLVLAKV 436
Cdd:PRK06087 253 IGARS--------------------VLLDIFTPDACLALLEQQRCTCMLGAT-------------PFI-----YDLLNLL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 437 RQ------ALGFAKCqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSgPHFM---SSPYNYRLYSSGKLVPGCRVKL 507
Cdd:PRK06087 295 EKqpadlsALRFFLC-----GGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVvnlDDPLSRFMHTDGYAAAGVEIKV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 508 VNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVP 582
Cdd:PRK06087 369 VDEARKTLppgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVR-GGENISSRE 447
|
490 500
....*....|....*....|....
gi 27477105 583 IEEAVkMELPIISNAMLIG--DQR 604
Cdd:PRK06087 448 VEDIL-LQHPKIHDACVVAmpDER 470
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
118-601 |
1.85e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 116.60 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 118 DLIALGFKRQDkwehISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSavgtvfaggivtgIYttsspeACQ 197
Cdd:PRK03640 17 DRTAIEFEEKK----VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILV-------------IH------ALQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 198 YIAydccANVIMVDTQKQLEKILkiWkQLPHLKA-VVIYKEPPPNKMANVY--TMEEFMELGNEVPEealdaIIDTQQPN 274
Cdd:PRK03640 74 QLG----AVAVLLNTRLSREELL--W-QLDDAEVkCLITDDDFEAKLIPGIsvKFAELMNGPKEEAE-----IQEEFDLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 275 QCCVLVYTSGTTGNPKGVMLSQDNITWTAR-----YGSQAGDIRPAEVqqevvvsylPLSHIAAqIYDLWTGIQWGAQVC 349
Cdd:PRK03640 142 EVATIMYTSGTTGKPKGVIQTYGNHWWSAVgsalnLGLTEDDCWLAAV---------PIFHISG-LSILMRSVIYGMRVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 350 FAEP-DALKgslVNTLREVEPTSHMG-VPRVWEKIMERIQEVAAQSGFirRKMLLW---AMSVTLEQnltcpgsdlkpft 424
Cdd:PRK03640 212 LVEKfDAEK---INKLLQTGGVTIISvVSTMLQRLLERLGEGTYPSSF--RCMLLGggpAPKPLLEQ------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 425 trladylvlakvrqalgfakCQknfygaapmmaetQHfflglNIRLYAGYGLSETSG------PHFMSSpynyRLYSSGK 498
Cdd:PRK03640 274 --------------------CK-------------EK-----GIPVYQSYGMTETASqivtlsPEDALT----KLGSAGK 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 499 LVPGCRVKLVNQDAEG----IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaG 574
Cdd:PRK03640 312 PLFPCELKIEKDGVVVppfeEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIIS-G 389
|
490 500
....*....|....*....|....*..
gi 27477105 575 GENVPPVPIeEAVKMELPIISNAMLIG 601
Cdd:PRK03640 390 GENIYPAEI-EEVLLSHPGVAEAGVVG 415
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
134-587 |
5.01e-27 |
|
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: 115.47 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 134 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ 213
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 214 kqlekilkiwkqlphlkavviykepppnkmanvYTMEEFMELGN-----EVPEEALDAIidtqqpnqccVLVYTSGTTGN 288
Cdd:cd12118 111 ---------------------------------FEYEDLLAEGDpdfewIPPADEWDPI----------ALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 289 PKGVMLSQDNItwtarYGSQAGDIRPAEVQQEVVvsYL---PLSHIAAqiydlWTGIqWGaqvcfaePDALKGSLVnTLR 365
Cdd:cd12118 148 PKGVVYHHRGA-----YLNALANILEWEMKQHPV--YLwtlPMFHCNG-----WCFP-WT-------VAAVGGTNV-CLR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 366 EVEPtshmgvPRVWEKI-MERIQEVAAqsgfirrkmllwamSVTLEQNLT-CPGSDLKPFTTRladylvlakVRQALGfa 443
Cdd:cd12118 207 KVDA------KAIYDLIeKHKVTHFCG--------------APTVLNMLAnAPPSDARPLPHR---------VHVMTA-- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 444 kcqknfyGAAP---MMAETQHfflgLNIRLYAGYGLSETSGPHF----------MSSPYNYRLYS----SGKLVPGCRV- 505
Cdd:cd12118 256 -------GAPPpaaVLAKMEE----LGFDVTHVYGLTETYGPATvcawkpewdeLPTEERARLKArqgvRYVGLEEVDVl 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 506 -----KLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPP 580
Cdd:cd12118 325 dpetmKPVPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISS 402
|
....*..
gi 27477105 581 VPIEEAV 587
Cdd:cd12118 403 VEVEGVL 409
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
175-632 |
1.18e-26 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 114.35 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 175 VGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMvdTQKQLEKILKIWKQLPHLK-AVVIYKEpppNKMANVYTMEE-F 252
Cdd:cd05909 49 FALALSGKVPVMLNYTAGLRELRACIKLAGIKTVL--TSKQFIEKLKLHHLFDVEYdARIVYLE---DLRAKISKADKcK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 253 MELGNEVPEEALDAI--IDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSH 330
Cdd:cd05909 124 AFLAGKFPPKWLLRIfgVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNP----EDVVFGALPFFH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 331 IAAQIYDLWTGIQWGAQVCFAePDALKG-SLVNTLREVEPTSHMGVPRVWekimeriqevaaqSGFIRRKMllwamsvtl 409
Cdd:cd05909 200 SFGLTGCLWLPLLSGIKVVFH-PNPLDYkKIPELIYDKKATILLGTPTFL-------------RGYARAAH--------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 410 eqnltcpGSDLkpFTTRLAdylvlakvrqalgfakcqknFYGAAPMMAETQHFFLGL-NIRLYAGYGLSETSGPHFMSSP 488
Cdd:cd05909 257 -------PEDF--SSLRLV--------------------VAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISVNTP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 489 -YNYRLYSSGKLVPGCRVKLVnqDAEG-----IGE---ICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGF 559
Cdd:cd05909 308 qSPNKEGTVGRPLPGMEVKIV--SVETheevpIGEgglLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGF 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477105 560 LYITGRLKELiITAGGENVPPVPIEEAVKMELPIISN--AMLIGDQRKFLSMLLtlkCTLDPDTSdqTDNLTEQA 632
Cdd:cd05909 385 LTITGRLSRF-AKIAGEMVSLEAIEDILSEILPEDNEvaVVSVPDGRKGEKIVL---LTTTTDTD--PSSLNDIL 453
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
133-600 |
1.55e-25 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 111.61 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDt 212
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 213 QKQLEKILKIwkQLPhlkaVVIYKEpppNKMANVYTMEEFMELGNEVPEEALDAIIdtqQPNQCCVLVYTSGTTGNPKGV 292
Cdd:PLN02330 135 DTNYGKVKGL--GLP----VIVLGE---EKIEGAVNWKELLEAADRAGDTSDNEEI---LQTDLCALPFSSGTTGISKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 293 MLSQDNITwtARYGSQAGDIRPAEVQQEVVVSYLPLSHIaaqiYDLwTGIqwgaqvCFAepdalkgslvnTLREVeptsh 372
Cdd:PLN02330 203 MLTHRNLV--ANLCSSLFSVGPEMIGQVVTLGLIPFFHI----YGI-TGI------CCA-----------TLRNK----- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 373 mgvprvwekimeriQEVAAQSGFIRRKML--LWAMSVTLEQnlTCPGSDLKPFTTRLADYLVLAKVrqalgfaKCQKNFY 450
Cdd:PLN02330 254 --------------GKVVVMSRFELRTFLnaLITQEVSFAP--IVPPIILNLVKNPIVEEFDLSKL-------KLQAIMT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 451 GAAPMMAETQHFFLGL--NIRLYAGYGLSETSGPHFMSSPYN-----YRLYSSGKLVPGCRVKLVNQDA------EGIGE 517
Cdd:PLN02330 311 AAAPLAPELLTAFEAKfpGVQVQEAYGLTEHSCITLTHGDPEkghgiAKKNSVGFILPNLEVKFIDPDTgrslpkNTPGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 518 ICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGEnVPPVPIeEAVKMELPIISNA 597
Cdd:PLN02330 391 LCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ-VAPAEL-EAILLTHPSVEDA 468
|
...
gi 27477105 598 MLI 600
Cdd:PLN02330 469 AVV 471
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
76-722 |
7.94e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 109.58 E-value: 7.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 76 APEEALWTTRADGRVRLRidpsCPQLPYTVHRMFYEALDKY----GDLIALGfKRQDK--WEHISYSQYYLLARRAAKGF 149
Cdd:PRK08180 12 APPAVEVERRADGTIYLR----SAEPLGDYPRRLTDRLVHWaqeaPDRVFLA-ERGADggWRRLTYAEALERVRAIAQAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 150 LKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTTSS--PEACQYIAYDCCANVIMVDTQKQLEKILKIwk 224
Cdd:PRK08180 87 LDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSqdFGKLRHVLELLTPGLVFADDGAAFARALAA-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 225 qLPHLKAVVIYKEPPPNKMANVytmeEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTAR 304
Cdd:PRK08180 165 -VVPADVEVVAVRGAVPGRAAT----PFAALLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 305 YGSQAgdIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGaqvcfaepdalkGSL---------------VNTLREVEP 369
Cdd:PRK08180 240 MLAQT--FPFLAEEPPVLVDWLPWNHTFGGNHNLGIVLYNG------------GTLyiddgkptpggfdetLRNLREISP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 370 TSHMGVPRVWEkimeriqevaaqsgfirrkMLLWAmsvtLEQNltcpgsdlkpfttrladylvlAKVRQALgFAKCQKNF 449
Cdd:PRK08180 306 TVYFNVPKGWE-------------------MLVPA----LERD---------------------AALRRRF-FSRLKLLF 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 450 YGAAPM----------MAEtQHffLGLNIRLYAGYGLSETSgPHFMSSpyNYRLYSSGKL---VPGCRVKLVnqDAEGIG 516
Cdd:PRK08180 341 YAGAALsqdvwdrldrVAE-AT--CGERIRMMTGLGMTETA-PSATFT--TGPLSRAGNIglpAPGCEVKLV--PVGGKL 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 517 EICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRL-DAD----GFLYiTGRLKELIITAGGE--NVPPVPIeEAVKM 589
Cdd:PRK08180 413 EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDPAdperGLMF-DGRIAEDFKLSSGTwvSVGPLRA-RAVSA 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 590 ELPIISNAMLIGDQRKFLSMLLTLKctldpdtsdqtdnlteqaMEFCQRVG--SRATTVSEIIEkkDEAVYQAIEEGIRR 667
Cdd:PRK08180 491 GAPLVQDVVITGHDRDEIGLLVFPN------------------LDACRRLAglLADASLAEVLA--HPAVRAAFRERLAR 550
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477105 668 VNMNAAARPYHIQKWAILERDFSISGGELgpTMK--LKRLTVLEKYKGIIDSFYQEQ 722
Cdd:PRK08180 551 LNAQATGSSTRVARALLLDEPPSLDAGEI--TDKgyINQRAVLARRAALVEALYADE 605
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
133-589 |
1.68e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 108.43 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFL-KLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV- 210
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVi 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 ------------DTQ-KQ-----LEKILKIWKQ------LPHLKAVViykepPPNKMANVYTMEEFMELGNEVPEEALDA 266
Cdd:PRK08751 131 dnfgttvqqviaDTPvKQvittgLGDMLGFPKAalvnfvVKYVKKLV-----PEYRINGAIRFREALALGRKHSMPTLQI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 267 iidtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQ----AGDIRPAevqQEVVVSYLPLSHIAAQIYDLWTGI 342
Cdd:PRK08751 206 -----EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagTGKLEEG---CEVVITALPLYHIFALTANGLVFM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 343 QWGAqvC---FAEPDALKGsLVNTLREVEPTSHMGVPRVWEKImeriqevaaqsgfirrkmllwamsvtleqnLTCPGSD 419
Cdd:PRK08751 278 KIGG--CnhlISNPRDMPG-FVKELKKTRFTAFTGVNTLFNGL------------------------------LNTPGFD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 420 LKPFTTrladylvlakVRQALGfakcqknfYGAAPMMAETQHFFLGLNIRLYAGYGLSETSgPHFMSSPYNYRLY--SSG 497
Cdd:PRK08751 325 QIDFSS----------LKMTLG--------GGMAVQRSVAERWKQVTGLTLVEAYGLTETS-PAACINPLTLKEYngSIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 498 KLVPGCRVKLVNQDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIIT 572
Cdd:PRK08751 386 LPIPSTDACIKDDAGTVlaigeIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILV 465
|
490
....*....|....*..
gi 27477105 573 AGGeNVPPVPIEEAVKM 589
Cdd:PRK08751 466 SGF-NVYPNEIEDVIAM 481
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
265-601 |
2.18e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 107.82 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 265 DAIIDTQQPnqcCVLVYTSGTTGNPKGVMLSQDNITWTARygSQAGDIRPAEVQQEVVVSYLPLSHIAaqiydlwtGIQw 344
Cdd:PRK07470 157 NAAVDHDDP---CWFFFTSGTTGRPKAAVLTHGQMAFVIT--NHLADLMPGTTEQDASLVVAPLSHGA--------GIH- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 345 gaqvcfaepdalkgSLVNTLREVE----PTSHMGVPRVWEKIME-RIQEVAAQSGFIrrKMLLWAMSVTleqnlTCPGSD 419
Cdd:PRK07470 223 --------------QLCQVARGAAtvllPSERFDPAEVWALVERhRVTNLFTVPTIL--KMLVEHPAVD-----RYDHSS 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 420 LKpfttrladYLVlakvrqalgfakcqknfYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSG------PHFMSS---Py 489
Cdd:PRK07470 282 LR--------YVI-----------------YAGAPMYRADQKRALAkLGKVLVQYFGLGEVTGnitvlpPALHDAedgP- 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 490 NYRLYSSGKLVPGCRVKLvnQDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYI 562
Cdd:PRK07470 336 DARIGTCGFERTGMEVQI--QDDEGrelppgeTGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYI 412
|
330 340 350
....*....|....*....|....*....|....*....
gi 27477105 563 TGRLKELIITaGGENVPPVPIEEAVKMElPIISNAMLIG 601
Cdd:PRK07470 413 TGRASDMYIS-GGSNVYPREIEEKLLTH-PAVSEVAVLG 449
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
160-696 |
3.52e-24 |
|
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: 107.54 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 160 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQkQLEKILKIWKQLPHLKAVVIY---- 235
Cdd:cd17632 96 VAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAE-HLDLAVEAVLEGGTPPRLVVFdhrp 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 236 ------------KEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQPnqCCVLVYTSGTTGNPKGVMLSQDNIT--W 301
Cdd:cd17632 175 evdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDP--LALLIYTSGSTGTPKGAMYTERLVAtfW 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 302 TARYGSQAGDIRPAevqqeVVVSYLPLSHIAAQIYdLWTGIQWGAQVCF-AEPDAlkGSLVNTLREVEPTSHMGVPRVWE 380
Cdd:cd17632 253 LKVSSIQDIRPPAS-----ITLNFMPMSHIAGRIS-LYGTLARGGTAYFaAASDM--STLFDDLALVRPTELFLVPRVCD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 381 KIMERIQEVaaqsgfIRRKMLLWAMSVTLEQNltcpgsdlkpfttrladylVLAKVRQALGFAKCQKNFYGAAPMMAETQ 460
Cdd:cd17632 325 MLFQRYQAE------LDRRSVAGADAETLAER-------------------VKAELRERVLGGRLLAAVCGSAPLSAEMK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 461 HFFLG-LNIRLYAGYGLSETSGphfmsspynyrLYSSGKLV--PGCRVKLVNQDAEGI---------GEICLWGRTIFMG 528
Cdd:cd17632 380 AFMESlLDLDLHDGYGSTEAGA-----------VILDGVIVrpPVLDYKLVDVPELGYfrtdrphprGELLVKTDTLFPG 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 529 YLNMEDKTCEAIDEEGWLHTGDA-GRLDADGFLYITgRLKELIITAGGENVpPVPIEEAVKMELPIISNAMLIGD-QRKF 606
Cdd:cd17632 449 YYKRPEVTAEVFDEDGFYRTGDVmAELGPDRLVYVD-RRNNVLKLSQGEFV-TVARLEAVFAASPLVRQIFVYGNsERAY 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 607 LSMLLTlkctldPdTSDQTDNLTEQAMefcqrvgsRAttvseiiekkdeavyqAIEEGIRRVNMNAAARPYHIQKWAILE 686
Cdd:cd17632 527 LLAVVV------P-TQDALAGEDTARL--------RA----------------ALAESLQRIAREAGLQSYEIPRDFLIE 575
|
570
....*....|.
gi 27477105 687 RD-FSISGGEL 696
Cdd:cd17632 576 TEpFTIANGLL 586
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
107-586 |
4.81e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 106.96 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 107 RMFYEALDK--------------------YGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFN 166
Cdd:PRK08162 2 NIYEQGLDRnaanyvpltplsfleraaevYPDRPAVIHGDR----RRTWAETYARCRRLASALARRGIGRGDTVAVLLPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 167 SPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQlEKILKIWKQLPHLKAVVIY---KEPPPNKM 243
Cdd:PRK08162 78 IPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFA-EVAREALALLPGPKPLVIDvddPEYPGGRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 244 ANVYTMEEFMELGN-----EVPEEALDAIidtqqpnqccVLVYTSGTTGNPKGV--------MLSQDNI-TWTARygsqa 309
Cdd:PRK08162 157 IGALDYEAFLASGDpdfawTLPADEWDAI----------ALNYTSGTTGNPKGVvyhhrgayLNALSNIlAWGMP----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 310 gdirpaevQQEVVVSYLPLSHIAAQIYDlWT-GIQWGAQVCfaepdalkgslvntLREVEPtshmgvprvwEKIMERIQE 388
Cdd:PRK08162 222 --------KHPVYLWTLPMFHCNGWCFP-WTvAARAGTNVC--------------LRKVDP----------KLIFDLIRE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 389 --VAAQSGF-IRRKMLLWAmsvtleqnltcPGSDLKPFttrlaDYLVLAKVRqalgfakcqknfyGAAP------MMAEt 459
Cdd:PRK08162 269 hgVTHYCGApIVLSALINA-----------PAEWRAGI-----DHPVHAMVA-------------GAAPpaaviaKMEE- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 460 qhfflgLNIRLYAGYGLSETSGP--------HFMSSPYNYRLYSSGK------LVPGCRV------KLVNQDAEGIGEIC 519
Cdd:PRK08162 319 ------IGFDLTHVYGLTETYGPatvcawqpEWDALPLDERAQLKARqgvrypLQEGVTVldpdtmQPVPADGETIGEIM 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477105 520 LWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEA 586
Cdd:PRK08162 393 FRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVEDV 457
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
278-649 |
6.35e-24 |
|
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: 105.60 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 278 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK 357
Cdd:cd05922 121 LLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA----DDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 358 GSLVNTLREVEPTSHMGVPRVWEkIMERIqevaaqsgfIRRKMLLwamsVTLeQNLTCPGSDLKP-FTTRLADYLVLAkv 436
Cdd:cd05922 196 DAFWEDLREHGATGLAGVPSTYA-MLTRL---------GFDPAKL----PSL-RYLTQAGGRLPQeTIARLRELLPGA-- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 437 rqalgfakcqknfygaapmmaetqhfflglniRLYAGYGLSETSG------PHFMSSpynyRLYSSGKLVPGCRVKLVNQ 510
Cdd:cd05922 259 --------------------------------QVYVMYGQTEATRrmtylpPERILE----KPGSIGLAIPGGEFEILDD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 511 D----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEE 585
Cdd:cd05922 303 DgtptPPGePGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEA 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477105 586 AVkMELPIISNAMLIGDQRKF---LSMLLTLKCTLDPDtsDQTDNLTEQAMEFcqRVGSRATTVSEI 649
Cdd:cd05922 382 AA-RSIGLIIEAAAVGLPDPLgekLALFVTAPDKIDPK--DVLRSLAERLPPY--KVPATVRVVDEL 443
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
273-604 |
9.09e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 105.66 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 273 PNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFA- 351
Cdd:PRK09088 134 PERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVD----AHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSn 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 352 --EPDALKGSLVNTLREVepTSHMGVPrvweKIMERIQevaAQSGFirrkmllwamsvtleqnltcPGSDLKPFTtrlad 429
Cdd:PRK09088 210 gfEPKRTLGRLGDPALGI--THYFCVP----QMAQAFR---AQPGF--------------------DAAALRHLT----- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 430 ylvlakvrqALgfakcqknFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMS---SPYNYRLYSSGKLVPGCRVK 506
Cdd:PRK09088 256 ---------AL--------FTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGTVFGMSvdcDVIRAKAGAAGIPTPTVQTR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 507 LVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPV 581
Cdd:PRK09088 319 VVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFIS-GGENVYPA 397
|
330 340
....*....|....*....|....*
gi 27477105 582 PIeEAVKMELPIISNAMLIG--DQR 604
Cdd:PRK09088 398 EI-EAVLADHPGIRECAVVGmaDAQ 421
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
226-604 |
1.39e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 105.52 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 226 LPHLKAVVIYKEPPPNKMANVYTMEEFMElgnevpEEALDAIIDTQQ--PNQCCVLVYTSGTTGNPKGVM-----LSQDN 298
Cdd:PRK13295 153 LPALRHVVVVGGDGADSFEALLITPAWEQ------EPDAPAILARLRpgPDDVTQLIYTSGTTGEPKGVMhtantLMANI 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 299 ITWTARYGSQAGDirpaevqqeVVVSYLPLSHIaaqiydlwTGIQWGAQVcfaePDALKGSLVntLREVeptshmgvprv 378
Cdd:PRK13295 227 VPYAERLGLGADD---------VILMASPMAHQ--------TGFMYGLMM----PVMLGATAV--LQDI----------- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 379 WEkimeriqeVAAQSGFIRRKMLLWAMSVTleqnltcpgsdlkPFTTRLADYLVL-AKVRQALGFAKCQknfyGAA--PM 455
Cdd:PRK13295 273 WD--------PARAAELIRTEGVTFTMAST-------------PFLTDLTRAVKEsGRPVSSLRTFLCA----GAPipGA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 456 MAETQHFFLGLNIrlYAGYGLSETSGP--HFMSSPYNYRLYSSGKLVPGCRVKLVnqDAEG-------IGEICLWGRTIF 526
Cdd:PRK13295 328 LVERARAALGAKI--VSAWGMTENGAVtlTKLDDPDERASTTDGCPLPGVEVRVV--DADGaplpagqIGRLQVRGCSNF 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 527 MGYLNMEDKTceAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISNAMLIG--DQR 604
Cdd:PRK13295 404 GGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEI-EALLYRHPAIAQVAIVAypDER 479
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
134-607 |
2.90e-23 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 104.45 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 134 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ 213
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 214 --KQLEKILKiwkQLPHLKAVVIYKEP---PPNKMANVYTMEEFMElgnevpEEALDAIIDTQQPNQCCVLVYTSGTTGN 288
Cdd:PRK06018 121 fvPILEKIAD---KLPSVERYVVLTDAahmPQTTLKNAVAYEEWIA------EADGDFAWKTFDENTAAGMCYTSGTTGD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 289 PKGVMLSQDNITWTARYGSQAGDIrpAEVQQEVVVSYLPLSHIAAqiydlwtgiqWGaqVCFAEPDA----------LKG 358
Cdd:PRK06018 192 PKGVLYSHRSNVLHALMANNGDAL--GTSAADTMLPVVPLFHANS----------WG--IAFSAPSMgtklvmpgakLDG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 359 SLVNTLREVEPTSH-MGVPRVWEkimeriqevaaqsgfirrkMLLWAMSvtlEQNLTCPgsDLKpfttrladylvlakvR 437
Cdd:PRK06018 258 ASVYELLDTEKVTFtAGVPTVWL-------------------MLLQYME---KEGLKLP--HLK---------------M 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 438 QALGFAKCQKNFYGAapmmaetqhfFLGLNIRLYAGYGLSETS--------GPHFMSSPYNYRL---YSSGKLVPGCRVK 506
Cdd:PRK06018 299 VVCGGSAMPRSMIKA----------FEDMGVEVRHAWGMTEMSplgtlaalKPPFSKLPGDARLdvlQKQGYPPFGVEMK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 507 LVNQDAEGI-------GEICLWGRTIFMGYLNMEDktcEAIDEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVP 579
Cdd:PRK06018 369 ITDDAGKELpwdgktfGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKD-VIKSGGEWIS 444
|
490 500 510
....*....|....*....|....*....|....*
gi 27477105 580 PVPIEE-AVKMelPIISNAMLIG------DQRKFL 607
Cdd:PRK06018 445 SIDLENlAVGH--PKVAEAAVIGvyhpkwDERPLL 477
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
278-604 |
5.19e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 103.75 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 278 VLVYTSGTTGNPKGVMLSQDNITWT-----ARYGSQAGDIRPA-EVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCF 350
Cdd:PRK12492 211 VLQYTGGTTGLAKGAMLTHGNLVANmlqvrACLSQLGPDGQPLmKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHnVLI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 351 AEPDALKGsLVNTLREVEPTSHMGVPRVWEKIMEriqevaaQSGFirRKMLLWAMSVTleqnltcpgsdlkpfttrlady 430
Cdd:PRK12492 291 TNPRDIPG-FIKELGKWRFSALLGLNTLFVALMD-------HPGF--KDLDFSALKLT---------------------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 431 lvlakvrqalgfakcqkNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSgPHFMSSPYN--YRLYSSGKLVPGCRVKLV 508
Cdd:PRK12492 339 -----------------NSGGTALVKATAERWEQLTGCTIVEGYGLTETS-PVASTNPYGelARLGTVGIPVPGTALKVI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 509 NQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGeNVPPVPI 583
Cdd:PRK12492 401 DDDGNELplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF-NVYPNEI 479
|
330 340
....*....|....*....|...
gi 27477105 584 EEAVkMELPIISNAMLIG--DQR 604
Cdd:PRK12492 480 EDVV-MAHPKVANCAAIGvpDER 501
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
134-565 |
2.42e-22 |
|
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: 100.03 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 134 SYSQyylLARRAAK--GFLK--LGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 209
Cdd:TIGR01733 1 TYRE---LDERANRlaRHLRaaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 210 VDTQKQLEkilkiwkqLPHLKAVVIYKEPPPNKMANvytmeefmelgNEVPEEALDAiiDTQQPNQCCVLvYTSGTTGNP 289
Cdd:TIGR01733 78 TDSALASR--------LAGLVLPVILLDPLELAALD-----------DAPAPPPPDA--PSGPDDLAYVI-YTSGSTGRP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 290 KGVMLSQDNI----TWTAR-YGSQAGDirpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVN 362
Cdd:TIGR01733 136 KGVVVTHRSLvnllAWLARrYGLDPDD---------RVLQFASLSFDAS-VEEIFGALLAGATLVVPPEDEERddAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 363 TLREVEPTSHM-GVPRVWEKIMEriqevAAQSGFIRRKMLlwamsvtleqnltCPGSDlkPFTTRLADylvlaKVRQALG 441
Cdd:TIGR01733 206 ALIAEHPVTVLnLTPSLLALLAA-----ALPPALASLRLV-------------ILGGE--ALTPALVD-----RWRARGP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 442 fakcqknfygaapmmaetqhfflglNIRLYAGYGLSETS----------GPHFMSSPYNYrlyssGKLVPGCRVKLVNQD 511
Cdd:TIGR01733 261 -------------------------GARLINLYGPTETTvwstatlvdpDDAPRESPVPI-----GRPLANTRLYVLDDD 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477105 512 -----AEGIGEICLWGRTIFMGYLNMEDKTCEAI--------DEEGWLHTGDAGRLDADGFLYITGR 565
Cdd:TIGR01733 311 lrpvpVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGR 377
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
279-604 |
2.57e-22 |
|
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: 98.73 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 279 LVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEvqqevvvSYL---PLSHIaaqiydlwTGIQWGAQVCFaepda 355
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDD-------RYLiinPFFHT--------FGYKAGIVACL----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 356 LKGSlvntlrEVEPTSHMGVPrvweKIMERIQevaaqsgfiRRKMLLWAMSVTLEQNLtcpgsdLKPFTTRLADylvLAK 435
Cdd:cd17638 65 LTGA------TVVPVAVFDVD----AILEAIE---------RERITVLPGPPTLFQSL------LDHPGRKKFD---LSS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 436 VRQALGfakcqknfyGAA---PMMAETQHFFLGLNIRLYAgYGLSEtSGPHFMSSPYNYRL---YSSGKLVPGCRVKLVN 509
Cdd:cd17638 117 LRAAVT---------GAAtvpVELVRRMRSELGFETVLTA-YGLTE-AGVATMCRPGDDAEtvaTTCGRACPGFEVRIAD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 510 QdaegiGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIItAGGENVPPVPIEEAVkM 589
Cdd:cd17638 186 D-----GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGAL-A 258
|
330
....*....|....*..
gi 27477105 590 ELPIISNAMLIG--DQR 604
Cdd:cd17638 259 EHPGVAQVAVIGvpDER 275
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
131-601 |
1.38e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 99.15 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLK-LGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 209
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 210 VDTQKqLEKilkiwkqLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQpnqCCVLVYTSGTTGNP 289
Cdd:PLN02574 145 TSPEN-VEK-------LSPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKPVIKQDD---VAAIMYSSGTTGAS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 290 KGVMLSQDNITWT---------ARYGSQAGDirpaevqqEVVVSYLPLSHI------AAQIYDLWTGIqwgaqVCFAEPD 354
Cdd:PLN02574 214 KGVVLTHRNLIAMvelfvrfeaSQYEYPGSD--------NVYLAALPMFHIyglslfVVGLLSLGSTI-----VVMRRFD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 355 AlkGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSgfirrkmllwamsvtleqnLTCpgsdLKPFTTrladylvla 434
Cdd:PLN02574 281 A--SDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEV-------------------LKS----LKQVSC--------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 435 kvrqalgfakcqknfyGAAPMMAET-QHFFLGL-NIRLYAGYGLSETS--GPHFMSSPYNYRLYSSGKLVPGCRVKLVNQ 510
Cdd:PLN02574 327 ----------------GAAPLSGKFiQDFVQTLpHVDFIQGYGMTESTavGTRGFNTEKLSKYSSVGLLAPNMQAKVVDW 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 511 DAE------GIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIe 584
Cdd:PLN02574 391 STGcllppgNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKE-IIKYKGFQIAPADL- 468
|
490
....*....|....*..
gi 27477105 585 EAVKMELPIISNAMLIG 601
Cdd:PLN02574 469 EAVLISHPEIIDAAVTA 485
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
131-587 |
2.08e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 98.68 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 210
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 DTQkQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALdaiidtqQPNQCCVLVYTSGTTGNPK 290
Cdd:PRK06155 125 EAA-LLAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAV-------QPGDTAAILYTSGTTGPSK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 291 GVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQiydlwtgiqwgaqvcfaepDALKGSLVNTLREVEpT 370
Cdd:PRK06155 197 GVCCPHAQFYWWGRNSAEDLEIGA----DDVLYTTLPLFHTNAL-------------------NAFFQALLAGATYVL-E 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 371 SHMGVPRVWEkimeRIQEVAAQSGFirrkmLLWAMSVTLeqnltcpgsDLKPFTTRLADYlvlaKVRQALGfakcqknfy 450
Cdd:PRK06155 253 PRFSASGFWP----AVRRHGATVTY-----LLGAMVSIL---------LSQPARESDRAH----RVRVALG--------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 451 GAAPMmAETQHFFLGLNIRLYAGYGLSETSGPhFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI-----GEICLWGRTI 525
Cdd:PRK06155 302 PGVPA-ALHAAFRERFGVDLLDGYGSTETNFV-IAVTHGSQRPGSMGRLAPGFEARVVDEHDQELpdgepGELLLRADEP 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27477105 526 FM---GYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEEAV 587
Cdd:PRK06155 380 FAfatGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKD-AIRRRGENISSFEVEQVL 442
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
160-601 |
8.27e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 96.77 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 160 VAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQkqLEKILKIWKQL-PHLKAVVIYKEP 238
Cdd:PRK07786 70 VLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA--LAPVATAVRDIvPLLSTVVVAGGS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 239 PPnkmANVYTMEEFMELGNEVPeealdAIIDTqqPNQCCVLV-YTSGTTGNPKGVMLSQDNITWTARYGsqagdIRPAEV 317
Cdd:PRK07786 148 SD---DSVLGYEDLLAEAGPAH-----APVDI--PNDSPALImYTSGTTGRPKGAVLTHANLTGQAMTC-----LRTNGA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 318 QQEVVVSYL--PLSHIAAqIYDLWTGIQWGAQVCFAEPDALK-GSLVNTLREVEPTSHMGVPRVWekimeriQEVAAQSG 394
Cdd:PRK07786 213 DINSDVGFVgvPLFHIAG-IGSMLPGLLLGAPTVIYPLGAFDpGQLLDVLEAEKVTGIFLVPAQW-------QAVCAEQQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 395 FIRRKMLLWAMSvtleqnltcpgsdlkpfttrladylvlakvrqalgfakcqknfYGAAPM-------MAETqhfFLGLN 467
Cdd:PRK07786 285 ARPRDLALRVLS-------------------------------------------WGAAPAsdtllrqMAAT---FPEAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 468 IrlYAGYGLSETSGPHFMSSPYN--YRLYSSGKLVPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAI 540
Cdd:PRK07786 319 I--LAAFGQTEMSPVTCMLLGEDaiRKLGSVGKVIPTVAARVVDENmndvPVGeVGEIVYRAPTLMSGYWNNPEATAEAF 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477105 541 DEeGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISNAMLIG 601
Cdd:PRK07786 397 AG-GWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCAEVEN-VLASHPDIVEVAVIG 454
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
142-592 |
1.51e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 95.54 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 142 ARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM--VDTQKQLEKI 219
Cdd:PRK12406 21 AARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIahADLLHGLASA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 220 LKiwkqlPHLKAVVIykePPPNKMANVYTMEEFMElgnEVPEEALD--------AIIDTQQPNQCCVLVYTSGTTGNPKG 291
Cdd:PRK12406 101 LP-----AGVTVLSV---PTPPEIAAAYRISPALL---TPPAGAIDwegwlaqqEPYDGPPVPQPQSMIYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 292 VMLSQDNITWTARYGSQAGDIRPAEvQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFA--EPDALkgsLVNTLREVEP 369
Cdd:PRK12406 170 VRRAAPTPEQAAAAEQMRALIYGLK-PGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPrfDPEEL---LQLIERHRIT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 370 TSHMgVPRVWEKIMERIQEVaaqsgfiRRKMLLWAMSVTLEQNLTCPgsdlkpfttrladylvlAKVRQALgfakcqKNF 449
Cdd:PRK12406 246 HMHM-VPTMFIRLLKLPEEV-------RAKYDVSSLRHVIHAAAPCP-----------------ADVKRAM------IEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 450 YGaaPMMAETqhfflglnirlyagYGLSETSGPHFMSSP-YNYRLYSSGKLVPGCRVKLVNQDAE-----GIGEIC--LW 521
Cdd:PRK12406 295 WG--PVIYEY--------------YGSTESGAVTFATSEdALSHPGTVGKAAPGAELRFVDEDGRplpqgEIGEIYsrIA 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477105 522 GRTIFMgYLNMEDKTCEaIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIeEAVKMELP 592
Cdd:PRK12406 359 GNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEI-EAVLHAVP 425
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
132-584 |
1.83e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 95.80 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 132 HISYSQYYLLARRAAkGFL--KLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 209
Cdd:PRK08314 35 AISYRELLEEAERLA-GYLqqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 210 VdTQKQLEKILKIWKQLPhLKAVVIYK----------EPPPNKMANVYTMEEFMELGNEVPEEALDAIID----TQQPNQ 275
Cdd:PRK08314 114 V-GSELAPKVAPAVGNLR-LRHVIVAQysdylpaepeIAVPAWLRAEPPLQALAPGGVVAWKEALAAGLAppphTAGPDD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 276 CCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFaepda 355
Cdd:PRK08314 192 LAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTP----ESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL----- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 356 lkgslvntlreveptshmgVPRvWEKimeriqEVAAQsgFIRR-KMLLW----AMSVTLeqnLTCPGsdlkpfttrLADY 430
Cdd:PRK08314 263 -------------------MPR-WDR------EAAAR--LIERyRVTHWtnipTMVVDF---LASPG---------LAER 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 431 lVLAKVRQALGfakcqknfyGAAPM---MAETQHFFLGLniRLYAGYGLSETSGPHFMSSPYNYRLYSSGklvpgcrVKL 507
Cdd:PRK08314 303 -DLSSLRYIGG---------GGAAMpeaVAERLKELTGL--DYVEGYGLTETMAQTHSNPPDRPKLQCLG-------IPT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 508 VNQDAEGI-------------GEICLWGRTIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRLKELiI 571
Cdd:PRK08314 364 FGVDARVIdpetleelppgevGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRM-I 442
|
490
....*....|...
gi 27477105 572 TAGGENVPPVPIE 584
Cdd:PRK08314 443 NASGFKVWPAEVE 455
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
133-636 |
2.48e-20 |
|
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: 94.45 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDT 212
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 213 qkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealDAIidtqqpnqcCVLVYTSGTTGNPKGV 292
Cdd:cd05919 91 ----------------------------------------------------DDI---------AYLLYSSGTTGPPKGV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 293 MLSQDNITWTAR-YGSQAGDIRPaevqQEVVVSylplshiAAQIY-------DLWTGIQWGAQVCFAE--PDAlkGSLVN 362
Cdd:cd05919 110 MHAHRDPLLFADaMAREALGLTP----GDRVFS-------SAKMFfgyglgnSLWFPLAVGASAVLNPgwPTA--ERVLA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 363 TLREVEPTSHMGVPRVWEKIMeriqevaAQSGFIRRKMllwamsvtleqnltcpgSDLKPFTTRladylvlakvrqalgf 442
Cdd:cd05919 177 TLARFRPTVLYGVPTFYANLL-------DSCAGSPDAL-----------------RSLRLCVSA---------------- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 443 akcqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETsGPHFMSS-PYNYRLYSSGKLVPGCRVKLVNQDAEGI-----G 516
Cdd:cd05919 217 --------GEALPRGLGERWMEHFGGPILDGIGATEV-GHIFLSNrPGAWRLGSTGRPVPGYEIRLVDEEGHTIppgeeG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 517 EICLWGRTIFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISN 596
Cdd:cd05919 288 DLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLI-IQHPAVAE 364
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 27477105 597 AMLIGDQRKF----LSMLLTLKCTLDPDTSdqtdnLTEQAMEFC 636
Cdd:cd05919 365 AAVVAVPESTglsrLTAFVVLKSPAAPQES-----LARDIHRHL 403
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
132-587 |
2.77e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 95.06 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 132 HISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYT-TSSPEACQYIAydccanvimv 210
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQpTPRTDLAVWAE---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 DTQKQLEKIlkiwkqlpHLKAVVIyKEPppnKMANVYTMEE----FMELGNEVPEEALDaIIDTQQpNQCCVLVYTSGTT 286
Cdd:PRK07768 99 DTLRVIGMI--------GAKAVVV-GEP---FLAAAPVLEEkgirVLTVADLLAADPID-PVETGE-DDLALMQLTSGST 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 287 GNPKGVMLSQDNITWTARYGSQAGDIrpaEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFaepdalkgslvntlre 366
Cdd:PRK07768 165 GSPKAVQITHGNLYANAEAMFVAAEF---DVETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVK---------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 367 VEPTSHMGVPRVWEKIMERiqevaaqsgfiRRKmllwamSVTLEQNLTcpgsdlkpfttrladYLVLAKV--RQA----- 439
Cdd:PRK07768 226 VTPMDFLRDPLLWAELISK-----------YRG------TMTAAPNFA---------------YALLARRlrRQAkpgaf 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 440 ----LGFAKCqknfyGAAPMMAETQHFFL------GLNIR-LYAGYGLSETS----------GPHF-------------- 484
Cdd:PRK07768 274 dlssLRFALN-----GAEPIDPADVEDLLdagarfGLRPEaILPAYGMAEATlavsfspcgaGLVVdevdadllaalrra 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 485 --MSSPYNYRLYSSGKLVPGCRVKLVNQD-----AEGIGEICLWGRTIFMGYLNMeDKTCEAIDEEGWLHTGDAGRLDAD 557
Cdd:PRK07768 349 vpATKGNTRRLATLGPPLPGLEVRVVDEDgqvlpPRGVGVIELRGESVTPGYLTM-DGFIPAQDADGWLDTGDLGYLTEE 427
|
490 500 510
....*....|....*....|....*....|
gi 27477105 558 GFLYITGRLKELIITaGGENVPPVPIEEAV 587
Cdd:PRK07768 428 GEVVVCGRVKDVIIM-AGRNIYPTDIERAA 456
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
279-601 |
5.32e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 93.79 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 279 LVYTSGTTGNPKGVMLSQDNITWTAR-----YGSQAGDirpaevqqeVVVSYLPLSH-----IAAQIYDLWtgiqwGAQV 348
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSNALtlvdyWRFTPDD---------VLIHALPIFHthglfVATNVALLA-----GASM 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 349 CFA---EPDALKGSLVNTlrevepTSHMGVPRVWEKIMeriqevaAQSGFIR---RKMLLwamsvtleqnltcpgsdlkp 422
Cdd:PRK07514 227 IFLpkfDPDAVLALMPRA------TVMMGVPTFYTRLL-------QEPRLTReaaAHMRL-------------------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 423 FTTrladylvlakvrqalgfakcqknfyGAAPMMAETQHFF---LGLNI--RlyagYGLSETSgphfM--SSPYN--YRL 493
Cdd:PRK07514 274 FIS-------------------------GSAPLLAETHREFqerTGHAIleR----YGMTETN----MntSNPYDgeRRA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 494 YSSGKLVPGCRVKLVNQD------AEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLK 567
Cdd:PRK07514 321 GTVGFPLPGVSLRVTDPEtgaelpPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
330 340 350
....*....|....*....|....*....|....
gi 27477105 568 ELIITaGGENVPPVPIEEAVKmELPIISNAMLIG 601
Cdd:PRK07514 401 DLIIS-GGYNVYPKEVEGEID-ELPGVVESAVIG 432
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
76-721 |
6.54e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 94.34 E-value: 6.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 76 APEEALWTTRADGRVRLRIDPSCPQLPYTVHRMFYEALDKYGDLIALGFKRQD--KWEHISYSQYYLLARRAAKGFLKLG 153
Cdd:PRK12582 22 KPPDISVERRADGSIVIKSRHPLGPYPRSIPHLLAKWAAEAPDRPWLAQREPGhgQWRKVTYGEAKRAVDALAQALLDLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 154 LKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTTSSPE--ACQYIAYDCCANVIMVDTQKQLEKILKIwkqLPH 228
Cdd:PRK12582 102 LDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHDhaKLKHLFDLVKPRVVFAQSGAPFARALAA---LDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 229 LKAVVIYKEPPPNKMANVytmeEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITwTARYGSQ 308
Cdd:PRK12582 179 LDVTVVHVTGPGEGIASI----AFADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMC-ANIAMQE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 309 AGDIRPAEVQQEVVVSYLPLSHIAA--QIYD--LWTG----IQWGAQVcfaePdALKGSLVNTLREVEPTSHMGVPRVWE 380
Cdd:PRK12582 254 QLRPREPDPPPPVSLDWMPWNHTMGgnANFNglLWGGgtlyIDDGKPL----P-GMFEETIRNLREISPTVYGNVPAGYA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 381 KIMERIQ--EVAAQSGFIRRKMLLWAmsvtleqnltcpGSdlkpfttRLADYLvLAKVrQALGfakcqknfygaapmMAE 458
Cdd:PRK12582 329 MLAEAMEkdDALRRSFFKNLRLMAYG------------GA-------TLSDDL-YERM-QALA--------------VRT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 459 TQHfflglNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEgiGEICLWGRTIFMGYLNMEDKTCE 538
Cdd:PRK12582 374 TGH-----RIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPVGDK--YEVRVKGPNVTPGYHKDPELTAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 539 AIDEEGWLHTGDAGR-LDAD----GfLYITGRLKELIITAGGE--NVPPVPIeEAVKMELPIISNAMLIGDQRKFLSMLl 611
Cdd:PRK12582 447 AFDEEGFYRLGDAARfVDPDdpekG-LIFDGRVAEDFKLSTGTwvSVGTLRP-DAVAACSPVIHDAVVAGQDRAFIGLL- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 612 tlkCTLDPDTsdqtdnlteqamefCQRVGSRATTVSEIIeKKDEAVYQAIEEGIRRVNMNAAARPYHIQKWAILERDFSI 691
Cdd:PRK12582 524 ---AWPNPAA--------------CRQLAGDPDAAPEDV-VKHPAVLAILREGLSAHNAEAGGSSSRIARALLMTEPPSI 585
|
650 660 670
....*....|....*....|....*....|
gi 27477105 692 SGGELGPTMKLKRLTVLEKYKGIIDSFYQE 721
Cdd:PRK12582 586 DAGEITDKGYINQRAVLERRAALVERLYAE 615
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
279-585 |
1.99e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 90.40 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 279 LVYTSGTTGNPKGVMLSQDN-ITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALK 357
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNW----VVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 358 gSLVNTLREVEPTSHMGVPRVWEKIMeriqevaaqsgfirrkmllwamSVTLEQNLTCPgsdlkpfttrladylvlaKVR 437
Cdd:cd17635 82 -SLFKILTTNAVTTTCLVPTLLSKLV----------------------SELKSANATVP------------------SLR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 438 qALGFAkcqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMssPYNYRLY---SSGKLVPGCRVKLVNQD-AE 513
Cdd:cd17635 121 -LIGYG-------GSRAIAADVRFIEATGLTNTAQVYGLSETGTALCL--PTDDDSIeinAVGRPYPGVDVYLAATDgIA 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27477105 514 GI----GEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEE 585
Cdd:cd17635 191 GPsasfGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSE-SINCGGVKIAPDEVER 264
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
228-587 |
2.23e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 92.52 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 228 HLKAVViykepPPNKMANVYTMEEFMELGNEVPEEALDAiidtqQPNQCCVLVYTSGTTGNPKGVMLSQDNITWT----- 302
Cdd:PRK05677 171 HVKKMV-----PAYHLPQAVKFNDALAKGAGQPVTEANP-----QADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqcr 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 303 ARYGSQAGDIRpaevqqEVVVSYLPLSHIAAQIYDLWTGIQWGAQ-VCFAEPDALKGsLVNTLREVEPTSHMGVPRVWEK 381
Cdd:PRK05677 241 ALMGSNLNEGC------EILIAPLPLYHIYAFTFHCMAMMLIGNHnILISNPRDLPA-MVKELGKWKFSGFVGLNTLFVA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 382 IMERiqevaaqSGFirRKMLLWAMSVTLEQNLTcpgsdlkpfttrladyLVLAKvrqalgfAKCQKNFYGAApmmaetqh 461
Cdd:PRK05677 314 LCNN-------EAF--RKLDFSALKLTLSGGMA----------------LQLAT-------AERWKEVTGCA-------- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 462 fflglnirLYAGYGLSETSgPHFMSSPYNY-RLYSSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDK 535
Cdd:PRK05677 354 --------ICEGYGMTETS-PVVSVNPSQAiQVGTIGIPVPSTLCKVIDDDGNelplgEVGELCVKGPQVMKGYWQRPEA 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 27477105 536 TCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGeNVPPVPIEEAV 587
Cdd:PRK05677 425 TDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGF-NVYPNELEDVL 475
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
146-601 |
5.04e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 91.40 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 146 AKGFLKLGLKQAHSVAILGFNSP---EWFFsAVgtVFAGGIVTGI-YTTSSPEACQyiAYDCCANVIMV-DTQKQLEKIL 220
Cdd:PLN02860 46 AAGLLRLGLRNGDVVAIAALNSDlylEWLL-AV--ACAGGIVAPLnYRWSFEEAKS--AMLLVRPVMLVtDETCSSWYEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 221 KIWKQLPHLKAVVIYKEPPP---NKMANVYTMEEFMELGNEVPEEALdaiidTQQPNQCCVLVYTSGTTGNPKGVMLSQD 297
Cdd:PLN02860 121 LQNDRLPSLMWQVFLESPSSsvfIFLNSFLTTEMLKQRALGTTELDY-----AWAPDDAVLICFTSGTTGRPKGVTISHS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 298 NITW-----TARYGSQAGDIrpaevqqevvvsYL---PLSHI---AAQIYDLWTGiqwGAQVCFAEPDAlkGSLVNTLRE 366
Cdd:PLN02860 196 ALIVqslakIAIVGYGEDDV------------YLhtaPLCHIgglSSALAMLMVG---ACHVLLPKFDA--KAALQAIKQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 367 VEPTSHMGVPrvweKIMERIQEVAaqsgfirRKMLLWAMSVTLEQNLTCPGSdlkpFTTRLADYLVLAKVRQALGFAkcq 446
Cdd:PLN02860 259 HNVTSMITVP----AMMADLISLT-------RKSMTWKVFPSVRKILNGGGS----LSSRLLPDAKKLFPNAKLFSA--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 447 knfYGaapmMAET--QHFFLGLNI-RLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGR 523
Cdd:PLN02860 321 ---YG----MTEAcsSLTFMTLHDpTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIGLDESSRVGRILTRGP 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477105 524 TIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISNAMLIG 601
Cdd:PLN02860 394 HVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKT-GGENVYPEEV-EAVLSQHPGVASVVVVG 469
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
273-601 |
6.21e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 90.43 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 273 PNQCCVLVYTSGTTGNPKGVMLSQDNIT-----------WTARygsqagdirpaevqqEVVVSYLPLSHIAAQIYDLWTG 341
Cdd:PRK07787 127 PDAPALIVYTSGTTGPPKGVVLSRRAIAadldalaeawqWTAD---------------DVLVHGLPLFHVHGLVLGVLGP 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 342 IQWGAQV---------CFAEPDALKGSLVntlreveptshMGVPRVWEkimeRIQEVAAQSGFIRRKMLLWAMSVTLeqn 412
Cdd:PRK07787 192 LRIGNRFvhtgrptpeAYAQALSEGGTLY-----------FGVPTVWS----RIAADPEAARALRGARLLVSGSAAL--- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 413 ltcpgsdlkPFTtrladylVLAKVRQALGFAKCQKnfYGaapmMAETqhfFLGLNIRlyagyglseTSGPHfmsspynyR 492
Cdd:PRK07787 254 ---------PVP-------VFDRLAALTGHRPVER--YG----MTET---LITLSTR---------ADGER--------R 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 493 LYSSGKLVPGCRVKLVNQ-------DAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGR 565
Cdd:PRK07787 292 PGWVGLPLAGVETRLVDEdggpvphDGETVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGR 371
|
330 340 350
....*....|....*....|....*....|....*.
gi 27477105 566 LKELIITAGGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:PRK07787 372 ESTDLIKSGGYRIGAGEIETAL-LGHPGVREAAVVG 406
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
108-601 |
6.71e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 90.72 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 108 MFYEALDKY-----GDLIALGFKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGG 182
Cdd:PRK04319 44 IAYEAIDRHadggrKDKVALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 183 IVTGIYTTSSPEACQYIAYDCCANVImVDTQKQLEKilKIWKQLPHLKAVVIYKEPPPNKmANVYTMEEFMELGNEVPE- 261
Cdd:PRK04319 124 IVGPLFEAFMEEAVRDRLEDSEAKVL-ITTPALLER--KPADDLPSLKHVLLVGEDVEEG-PGTLDFNALMEQASDEFDi 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 262 EALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITW---TARYgsqAGDIRPAEvqqevvvsylplshiaaqIYdl 338
Cdd:PRK04319 200 EWTD-------REDGAILHYTSGSTGKPKGVLHVHNAMLQhyqTGKY---VLDLHEDD------------------VY-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 339 WtgiqwgaqvCFAEPDALKGS-----------LVNTLREVEPTshmgvPRVWEKIMERiQEV----AAQSGFirrKMLLW 403
Cdd:PRK04319 250 W---------CTADPGWVTGTsygifapwlngATNVIDGGRFS-----PERWYRILED-YKVtvwyTAPTAI---RMLMG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 404 AmsvtleqnltcpGSDLkpfttrLADYlVLAKVRQALGFAKcqknfygaaPMMAETQHF---FLGLniRLYAGYGLSETS 480
Cdd:PRK04319 312 A------------GDDL------VKKY-DLSSLRHILSVGE---------PLNPEVVRWgmkVFGL--PIHDNWWMTETG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 481 GpHFMSspyNY-----RLYSSGKLVPGCRVKLV-NQDAEG----IGEICL---WgRTIFMGYLNMEDKTcEAIDEEGWLH 547
Cdd:PRK04319 362 G-IMIA---NYpamdiKPGSMGKPLPGIEAAIVdDQGNELppnrMGNLAIkkgW-PSMMRGIWNNPEKY-ESYFAGDWYV 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 27477105 548 TGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:PRK04319 436 SGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVESKL-MEHPAVAEAGVIG 487
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
279-587 |
2.02e-18 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 90.37 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 279 LVYTSGTTGNPKGVMLSQDNITWTARygsQAGDIRPAEvQQEVVVSYLPLSH----IAAQIYDLWTGIqwgAQVCFAEP- 353
Cdd:PRK08633 787 IIFSSGSEGEPKGVMLSHHNILSNIE---QISDVFNLR-NDDVILSSLPFFHsfglTVTLWLPLLEGI---KVVYHPDPt 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 354 DALKgslvntlreveptshmgvprvwekimerIQEVAAQsgfiRRKMLLWAMSvtleqnltcpgsdlkpftTRLADYLVL 433
Cdd:PRK08633 860 DALG----------------------------IAKLVAK----HRATILLGTP------------------TFLRLYLRN 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 434 AKVrQALGFAKCQKNFYGA---APMMAETqhFFLGLNIRLYAGYGLSETSG------PHFMSSPYNY----RLYSSGKLV 500
Cdd:PRK08633 890 KKL-HPLMFASLRLVVAGAeklKPEVADA--FEEKFGIRILEGYGATETSPvasvnlPDVLAADFKRqtgsKEGSVGMPL 966
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 501 PGCRVKLVNQD-----AEGI-GEICLWGRTIFMGYLNMEDKTCEAI---DEEGWLHTGDAGRLDADGFLYITGRLKEL-- 569
Cdd:PRK08633 967 PGVAVRIVDPEtfeelPPGEdGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFak 1046
|
330
....*....|....*...
gi 27477105 570 IitaGGENVPPVPIEEAV 587
Cdd:PRK08633 1047 I---GGEMVPLGAVEEEL 1061
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
258-566 |
2.11e-18 |
|
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: 88.46 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 258 EVPEEALDAIIDTQQP-------NQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSH 330
Cdd:cd05945 74 SSPAERIREILDAAKPalliadgDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGP----GDVFLNQAPFSF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 331 IAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWEKIMeriqevaaqsgfiRRKMLLWAMSVT 408
Cdd:cd05945 150 DLS-VMDLYPALASGATLVPVPRDATAdpKQLFRFLAEHGITVWVSTPSFAAMCL-------------LSPTFTPESLPS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 409 LEQNLTCpGsdlKPFTTRLADYLVlakvrqalgfakcqknfyGAAPmmaetqhfflglNIRLYAGYGLSET----SGPHF 484
Cdd:cd05945 216 LRHFLFC-G---EVLPHKTARALQ------------------QRFP------------DARIYNTYGPTEAtvavTYIEV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 485 MSSPY--NYRLYSsGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRL 554
Cdd:cd05945 262 TPEVLdgYDRLPI-GYAKPGAKLVILDEDGRpvppgEKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRL 340
|
330
....*....|..
gi 27477105 555 DADGFLYITGRL 566
Cdd:cd05945 341 EADGLLFYRGRL 352
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
79-589 |
3.25e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 88.57 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 79 EALWTTRADGRVRLRIDPScpQLPYTVHrMFYEALDKYGDLIA-------LGFKrqdKWEHISysqyyllarRAAKGFLK 151
Cdd:PRK08974 2 EKVWLNRYPADVPAEINPD--RYQSLVD-MFEQAVARYADQPAfinmgevMTFR---KLEERS---------RAFAAYLQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 152 --LGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV--DTQKQLEKIL------- 220
Cdd:PRK08974 67 ngLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIvsNFAHTLEKVVfktpvkh 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 221 ----KIWKQLPHLKA-----VVIY--KEPPPNKMANVYTMEEFMELGNEV----PEEALDAIidtqqpnqcCVLVYTSGT 285
Cdd:PRK08974 147 viltRMGDQLSTAKGtlvnfVVKYikRLVPKYHLPDAISFRSALHKGRRMqyvkPELVPEDL---------AFLQYTGGT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 286 TGNPKGVMLSQDNITwtARYGSQAGDIRPA-EVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQvcfaepdalkGSLVNTL 364
Cdd:PRK08974 218 TGVAKGAMLTHRNML--ANLEQAKAAYGPLlHPGKELVVTALPLYHIFALTVNCLLFIELGGQ----------NLLITNP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 365 REVEptshmgvprvwekimeriqevaaqsGFIRrkmllwamsvtleqnltcpgsDLK--PFTT-----RLADYLVLAKVR 437
Cdd:PRK08974 286 RDIP-------------------------GFVK---------------------ELKkyPFTAitgvnTLFNALLNNEEF 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 438 QALGFAKCQKNFYGAAPM---MAETQHFFLGLNirLYAGYGLSETSgPHFMSSPYNYRLY--SSGKLVPGCRVKLVNQDA 512
Cdd:PRK08974 320 QELDFSSLKLSVGGGMAVqqaVAERWVKLTGQY--LLEGYGLTECS-PLVSVNPYDLDYYsgSIGLPVPSTEIKLVDDDG 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 513 EGI-----GEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGeNVPPVPIEEAV 587
Cdd:PRK08974 397 NEVppgepGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGF-NVYPNEIEDVV 474
|
..
gi 27477105 588 KM 589
Cdd:PRK08974 475 ML 476
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
467-601 |
3.42e-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: 86.31 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 467 NIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGRTIFMGYLNMEdktceAIDEEGWL 546
Cdd:cd17633 136 KANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGG-----FSNPDGWM 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 27477105 547 HTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKmELPIISNAMLIG 601
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLK-AIPGIEEAIVVG 263
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
134-601 |
6.62e-17 |
|
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: 83.93 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 134 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYiaydccanvimvdtq 213
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEY--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 214 kqlekilkiwkQLPHLKAVVIykepppnkmanvytmeefmelgnevpeealdaIIDTQQPnqcCVLVYTSGTTGNPKGVm 293
Cdd:cd05972 67 -----------RLEAAGAKAI--------------------------------VTDAEDP---ALIYFTSGTTGLPKGV- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 294 lsqdnitwtarygsqagdirpaevqqEVVVSYlPLSHI--AAQIYDL------WTGIQWGAQVC----FAEPdALKGS-- 359
Cdd:cd05972 100 --------------------------LHTHSY-PLGHIptAAYWLGLrpddihWNIADPGWAKGawssFFGP-WLLGAtv 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 360 LVNTLREVEPtshmgvpRVWEKIMERIQevaaqsgfirrkmllwamsVTleqNLTCPGSDLKPFTTRLADYLVLAKVRQA 439
Cdd:cd05972 152 FVYEGPRFDA-------ERILELLERYG-------------------VT---SFCGPPTAYRMLIKQDLSSYKFSHLRLV 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 440 LGfakcqknfyGAAPMMAETQHFF---LGLNIRlyAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI- 515
Cdd:cd05972 203 VS---------AGEPLNPEVIEWWraaTGLPIR--DGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELp 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 516 ----GEICLWGRTI--FMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkM 589
Cdd:cd05972 272 pgeeGDIAIKLPPPglFLGYVGDPEKT-EASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS-GYRIGPFEVESAL-L 348
|
490
....*....|..
gi 27477105 590 ELPIISNAMLIG 601
Cdd:cd05972 349 EHPAVAEAAVVG 360
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
133-605 |
1.13e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 83.94 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIvtgiYTTSSP--------------EACQY 198
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAV----HVPVSPlfrehelsyelndaGAEVL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 199 IAYDCCANVIM-VDTQKQLEKILK--IWKQLPHLKAVviykePPPNKMAN----VYTMEEFMELGNEVPEEALDAIIDTQ 271
Cdd:PRK06178 135 LALDQLAPVVEqVRAETSLRHVIVtsLADVLPAEPTL-----PLPDSLRAprlaAAGAIDLLPALRACTAPVPLPPPALD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 272 QPnqcCVLVYTSGTTGNPKGVMLSQDNITWTArygSQAGDIRPAEVQQEVVVSYLPLSHIAAQ----IYDLWTGI----- 342
Cdd:PRK06178 210 AL---AALNYTGGTTGMPKGCEHTQRDMVYTA---AAAYAVAVVGGEDSVFLSFLPEFWIAGEnfglLFPLFSGAtlvll 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 343 -QWGAQVCFAEPDALK----GSLVNTLREVeptshMGVPRVWEKIMERIQEVAAQSgFIRRkmllwamsvtleqnltcpg 417
Cdd:PRK06178 284 aRWDAVAFMAAVERYRvtrtVMLVDNAVEL-----MDHPRFAEYDLSSLRQVRVVS-FVKK------------------- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 418 sdLKPfttrlaDYlvlakvRQALgfakcqKNFYGAapMMAEtqhfflglnirlyAGYGLSET------------------ 479
Cdd:PRK06178 339 --LNP------DY------RQRW------RALTGS--VLAE-------------AAWGMTEThtcdtftagfqdddfdll 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 480 SGPHFMSSPynyrlyssgklVPGCRVKLVNQDAEGI------GEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGR 553
Cdd:PRK06178 384 SQPVFVGLP-----------VPGTEFKICDFETGELlplgaeGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGK 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 27477105 554 LDADGFLYITGRLKELIITAGGENVPPvpiE-EAVKMELPIISNAMLIG--DQRK 605
Cdd:PRK06178 452 IDEQGFLHYLGRRKEMLKVNGMSVFPS---EvEALLGQHPAVLGSAVVGrpDPDK 503
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
271-590 |
1.51e-16 |
|
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: 83.31 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 271 QQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRpaevQQEVVVSYLPLSH----IAAQIYDLWTGIQwga 346
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWK----TKDRILSWMPLTHdmglIAFHLAPLIAGMN--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 347 qvcfaepdalkgslvntlreveptshmgvprvwekimeriQEVAAQSGFIRRKML-LWAMSVTLEQNLTCP--GSD--LK 421
Cdd:cd05908 176 ----------------------------------------QYLMPTRLFIRRPILwLKKASEHKATIVSSPnfGYKyfLK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 422 PFTTRLADYLVLAKVRQALGfakcqknfyGAAPMMAETQHFFL------GLNIR-LYAGYGLSETS--------GPHFM- 485
Cdd:cd05908 216 TLKPEKANDWDLSSIRMILN---------GAEPIDYELCHEFLdhmskyGLKRNaILPVYGLAEASvgaslpkaQSPFKt 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 486 -------------------SSPYNYRLYSSGKLVPGCRVKLVNQDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAID 541
Cdd:cd05908 287 itlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICDEDNKIlpdgyIGHIQIRGKNVTPGYYNNPEATAKVFT 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 27477105 542 EEGWLHTGDAGrLDADGFLYITGRLKELIITaGGENVPPVPIEE-AVKME 590
Cdd:cd05908 367 DDGWLKTGDLG-FIRNGRLVITGREKDIIFV-NGQNVYPHDIERiAEELE 414
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
131-637 |
1.62e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 83.36 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 210
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 DTQ--KQLEKILKIW--KQLPHLKA---VVIYKE---PPPNKMA---NVYTMEEFMELGNevPEEALdaiidtQQPN--- 274
Cdd:PLN02479 124 DQEffTLAEEALKILaeKKKSSFKPpllIVIGDPtcdPKSLQYAlgkGAIEYEKFLETGD--PEFAW------KPPAdew 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 275 QCCVLVYTSGTTGNPKGVMLSQ---------DNITWTARYGSqagdirpaevqqeVVVSYLPLSHIAAQIYDLWTGIQWG 345
Cdd:PLN02479 196 QSIALGYTSGTTASPKGVVLHHrgaylmalsNALIWGMNEGA-------------VYLWTLPMFHCNGWCFTWTLAALCG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 346 AQVCfaepdalkgslvntLREVEPTShmgvprvwekimerIQEVAAQSGFIRrkmlLWAMSVTLEQNLTCPGSDLKPFTT 425
Cdd:PLN02479 263 TNIC--------------LRQVTAKA--------------IYSAIANYGVTH----FCAAPVVLNTIVNAPKSETILPLP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 426 RLADYLVLakvrqalgfakcqknfyGAAP----MMAETQHFFlglniRLYAGYGLSETSGPHFMSS--PYNYRLYSSGKL 499
Cdd:PLN02479 311 RVVHVMTA-----------------GAAPppsvLFAMSEKGF-----RVTHTYGLSETYGPSTVCAwkPEWDSLPPEEQA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 500 VPGCR------------------VKLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLY 561
Cdd:PLN02479 369 RLNARqgvryiglegldvvdtktMKPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 562 ITGRLKELIITaGGENVPPVPIEEAVKMElPIISNAMLIG--DQRKFLS--MLLTLKCtlDPDTSDQTdNLTEQAMEFCQ 637
Cdd:PLN02479 448 IKDRSKDIIIS-GGENISSLEVENVVYTH-PAVLEASVVArpDERWGESpcAFVTLKP--GVDKSDEA-ALAEDIMKFCR 522
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
252-576 |
1.95e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 83.61 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 252 FMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVvvSYLPLSHI 331
Cdd:PTZ00342 282 IILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKTHL--SYLPISHI 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 332 AAQIY---DLWTGIQ---WGAQVCFAEPDAL--KGSLVntlreveptshMGVPRVWEKIMERIQEVAAQSGFIRRKMLLW 403
Cdd:PTZ00342 360 YERVIaylSFMLGGTiniWSKDINYFSKDIYnsKGNIL-----------AGVPKVFNRIYTNIMTEINNLPPLKRFLVKK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 404 AMSVTLEQNLTCPGSDLKPFTTrladylVLAKVRQALGfAKCQKNFYGAAPMMAE-TQHFFLGLNIRLYAGYGLSETSGP 482
Cdd:PTZ00342 429 ILSLRKSNNNGGFSKFLEGITH------ISSKIKDKVN-PNLEVILNGGGKLSPKiAEELSVLLNVNYYQGYGLTETTGP 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 483 HFMSSPYNYRLYS-SGKLVPGCRVKLVN------QDAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLD 555
Cdd:PTZ00342 502 IFVQHADDNNTESiGGPISPNTKYKVRTwetykaTDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQIN 581
|
330 340
....*....|....*....|.
gi 27477105 556 ADGFLYITGRLKELIITAGGE 576
Cdd:PTZ00342 582 KNGSLTFLDRSKGLVKLSQGE 602
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
133-601 |
2.02e-16 |
|
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: 82.14 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCAnvimvdt 212
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGA------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 213 qkqlekilkiwkqlphlKAVVIYKEpppnkmanvytMEEFMelgnevpeealdaiidtqqpnqccVLVYTSGTTGNPKGV 292
Cdd:cd05935 75 -----------------KVAVVGSE-----------LDDLA------------------------LIPYTSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 293 MLSQDNITWTARYGSQAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCfaepdalkgslvntlreveptsh 372
Cdd:cd05935 103 MHTHFSAAANALQSAVWTGLTPSDV----ILACLPLFHVTGFVGSLNTAVYVGGTYV----------------------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 373 mgvprvwekIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTcpgSDLKPFTTRLADYLVLAKvrqalgfakcqknfyGA 452
Cdd:cd05935 156 ---------LMARWDRETALELIEKYKVTFWTNIPTMLVDLL---ATPEFKTRDLSSLKVLTG---------------GG 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 453 APMMAETQHFFLGL-NIRLYAGYGLSETSGPHFMSSPYNYRLYSSGklVPGCRVKLVNQDAEG--------IGEICLWGR 523
Cdd:cd05935 209 APMPPAVAEKLLKLtGLRFVEGYGLTETMSQTHTNPPLRPKLQCLG--IP*FGVDARVIDIETgrelppneVGEIVVRGP 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 524 TIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGEnVPPVPIeEAVKMELPIISNAMLI 600
Cdd:cd05935 287 QIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK-VWPAEV-EAKLYKHPAI*EVCVI 364
|
.
gi 27477105 601 G 601
Cdd:cd05935 365 S 365
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
278-604 |
2.79e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 80.86 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 278 VLVYTSGTTGNPKGVMLSQDNITWTA-----RYGSQAgdirpaevqQEVVVsyLPLSHIAaqiydlwtgiqwGAQVcfae 352
Cdd:PRK07824 39 LVVATSGTTGTPKGAMLTAAALTASAdathdRLGGPG---------QWLLA--LPAHHIA------------GLQV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 353 pdalkgsLV-NTLREVEPTShMGVPRVWEkIMERIQEVAAQSGFiRRKMLLWAMSvtLEQNLTCPGSdlkpfTTRLADY- 430
Cdd:PRK07824 92 -------LVrSVIAGSEPVE-LDVSAGFD-PTALPRAVAELGGG-RRYTSLVPMQ--LAKALDDPAA-----TAALAELd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 431 LVLAkvrqalgfakcqknfyGAAPMMAETQHFFLGLNIRLYAGYGLSETSGphfmSSPYNyrlyssGKLVPGCRVKLVNq 510
Cdd:PRK07824 155 AVLV----------------GGGPAPAPVLDAAAAAGINVVRTYGMSETSG----GCVYD------GVPLDGVRVRVED- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 511 daegiGEICLWGRTIFMGYLNMEDKtcEAIDEEGWLHTGDAGRLDaDGFLYITGRLKElIITAGGENVPPVPIEEAVkME 590
Cdd:PRK07824 208 -----GRIALGGPTLAKGYRNPVDP--DPFAEPGWFRTDDLGALD-DGVLTVLGRADD-AISTGGLTVLPQVVEAAL-AT 277
|
330
....*....|....*.
gi 27477105 591 LPIISNAMLIG--DQR 604
Cdd:PRK07824 278 HPAVADCAVFGlpDDR 293
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
134-599 |
3.22e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 82.37 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 134 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQ 213
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 214 -----KQLEKILKIWKQLPHLKAVVIYK-EPPPNKMANVYTMEEFMELGNEVPEeALDAIIDTQQPNQCCVLVYTSGTTG 287
Cdd:PLN03102 121 feplaREVLHLLSSEDSNLNLPVIFIHEiDFPKRPSSEELDYECLIQRGEPTPS-LVARMFRIQDEHDPISLNYTSGTTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 288 NPKGVMLSQDNI---TWTARYGSQAGdIRPaevqqeVVVSYLPLSHIAAQIYDLWTGIQWGAQVCF---AEPDALKGSlv 361
Cdd:PLN03102 200 DPKGVVISHRGAylsTLSAIIGWEMG-TCP------VYLWTLPMFHCNGWTFTWGTAARGGTSVCMrhvTAPEIYKNI-- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 362 ntlrEVEPTSHMG-VPRVWEKIME-RIQEVAAQSGFIrrkmllwamsvtleQNLTcpGSDLKPfttrladyLVLAKVRQA 439
Cdd:PLN03102 271 ----EMHNVTHMCcVPTVFNILLKgNSLDLSPRSGPV--------------HVLT--GGSPPP--------AALVKKVQR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 440 LGFakcqknfygaapmmaETQHfflglnirlyaGYGLSETSGPHFMSS--------PYNYRLYSSGKlvPGCRV------ 505
Cdd:PLN03102 323 LGF---------------QVMH-----------AYGLTEATGPVLFCEwqdewnrlPENQQMELKAR--QGVSIlgladv 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 506 --------KLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGEN 577
Cdd:PLN03102 375 dvknketqESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGEN 452
|
490 500
....*....|....*....|..
gi 27477105 578 VPPVPIEEAVKMELPIISNAML 599
Cdd:PLN03102 453 ISSVEVENVLYKYPKVLETAVV 474
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
258-565 |
4.92e-16 |
|
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: 81.03 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 258 EVPEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDirpaevqqeVVVSY 325
Cdd:cd05930 70 SYPAERLAYILeDSGaklvltDPDDLAYVIYTSGSTGKPKGVMVEHRGLVnlllwMQEAYPLTPGD---------RVLQF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 326 LPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWekimeriqevaaqsgfirrkmllw 403
Cdd:cd05930 141 TSFSFDVS-VWEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTPSLL------------------------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 404 amSVTLEQNLTCPGSDLKpfttrladYLVLA--KVRQALgfakcQKNFYGAAPmmaetqhfflglNIRLYAGYGLSETS- 480
Cdd:cd05930 196 --RLLLQELELAALPSLR--------LVLVGgeALPPDL-----VRRWRELLP------------GARLVNLYGPTEATv 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 481 GPHFMSSPYNYRLYSS---GKLVPGCRVKLVNQD-----AEGIGEICLWGRTIFMGYLNMEDKTCEAI-----DEEGWLH 547
Cdd:cd05930 249 DATYYRVPPDDEEDGRvpiGRPIPNTRVYVLDENlrpvpPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfGPGERMY 328
|
330
....*....|....*....
gi 27477105 548 -TGDAGRLDADGFLYITGR 565
Cdd:cd05930 329 rTGDLVRWLPDGNLEFLGR 347
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
131-586 |
6.67e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 81.10 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFfsavgTVFAGGIVTGIYTT------SSPEAcQYIAYDCC 204
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFF-----EVYWAARRSGLYYTpinwhlTAAEI-AYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 205 ANVIMVDtQKQLEKILKIWKQLPHlkavviykepppnkmanvyTMEEFMELGNEVP-----EEALDAIIDTQQPNQC--C 277
Cdd:PRK08276 84 AKVLIVS-AALADTAAELAAELPA-------------------GVPLLLVVAGPVPgfrsyEEALAAQPDTPIADETagA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 278 VLVYTSGTTGNPKGVM--LSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAqiydlwtgIQWGAQVcfaepDA 355
Cdd:PRK08276 144 DMLYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAP--------LRFGMSA-----LA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 356 LKGSLV--------NTLREVE----PTSHMgVPrvwekIMeriqevaaqsgFIRrkMLlwamsvtleqnltcpgsdlkpf 423
Cdd:PRK08276 211 LGGTVVvmekfdaeEALALIEryrvTHSQL-VP-----TM-----------FVR--ML---------------------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 424 ttRLADylvlaKVRQALGFAKCQKNFYGAAP--------MMAetqhfFLGLNIRLYagYGLSETSGPHFMSS------PY 489
Cdd:PRK08276 250 --KLPE-----EVRARYDVSSLRVAIHAAAPcpvevkraMID-----WWGPIIHEY--YASSEGGGVTVITSedwlahPG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 490 nyrlySSGKLVPGcRVKLVNQDAEGI--GEIclwGrTIFM-------GYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFL 560
Cdd:PRK08276 316 -----SVGKAVLG-EVRILDEDGNELppGEI---G-TVYFemdgypfEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYL 385
|
490 500
....*....|....*....|....*.
gi 27477105 561 YITGRLKELIITaGGENVPPVPIEEA 586
Cdd:PRK08276 386 YLTDRKSDMIIS-GGVNIYPQEIENL 410
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
142-601 |
7.43e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 81.29 E-value: 7.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 142 ARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKqLEKILK 221
Cdd:PRK07008 49 AKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTF-LPLVDA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 222 IWKQLPHLKAVVIykepppnkMANVYTMEEfmelgNEVPEEALDAIIDTQQP---------NQCCVLVYTSGTTGNPKGV 292
Cdd:PRK07008 128 LAPQCPNVKGWVA--------MTDAAHLPA-----GSTPLLCYETLVGAQDGdydwprfdeNQASSLCYTSGTTGNPKGA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 293 MLSQDNITWTArYGSQAGDIRPAEVqQEVVVSYLPLSHIAAqiydlWtGIQW-----GAQVCFAEPDaLKGSLVNTLREV 367
Cdd:PRK07008 195 LYSHRSTVLHA-YGAALPDAMGLSA-RDAVLPVVPMFHVNA-----W-GLPYsapltGAKLVLPGPD-LDGKSLYELIEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 368 EP-TSHMGVPRVWEKIMERIQEVAAQSGFIRRkmllwamsvTLEQNLTCPGSDLKPFTtrlADYLVlaKVRQALGfakcq 446
Cdd:PRK07008 266 ERvTFSAGVPTVWLGLLNHMREAGLRFSTLRR---------TVIGGSACPPAMIRTFE---DEYGV--EVIHAWG----- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 447 knfygaapmMAETQHffLGLNIRLYAGY-GLSETSGPHfmsspynyRLYSSGKLVPGCRVKLVNQ-------DAEGIGEI 518
Cdd:PRK07008 327 ---------MTEMSP--LGTLCKLKWKHsQLPLDEQRK--------LLEKQGRVIYGVDMKIVGDdgrelpwDGKAFGDL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 519 CLWGRTIFMGYLNMEDKTCeaIDeeGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEEaVKMELPIISNAM 598
Cdd:PRK07008 388 QVRGPWVIDRYFRGDASPL--VD--GWFPTGDVATIDADGFMQITDRSKD-VIKSGGEWISSIDIEN-VAVAHPAVAEAA 461
|
...
gi 27477105 599 LIG 601
Cdd:PRK07008 462 CIA 464
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
104-636 |
7.85e-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: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 104 TVHRMFYEALDKYGDLIALGFKRQDKweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGI 183
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGL--RLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 184 VTGIYTTSSP-EACQYIAYD-CCANVIMVDTQKQLEKILkiwkqlphlkavviykepppnkmANVYTMEEFMELGNEVPE 261
Cdd:cd05923 80 PALINPRLKAaELAELIERGeMTAAVIAVDAQVMDAIFQ-----------------------SGVRVLALSDLVGLGEPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 262 EALDAIIDTQ-QPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGS-QAGDIRPAevqQEVVVSYLPLSHIAAQIYDLW 339
Cdd:cd05923 137 SAGPLIEDPPrEPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMStQAGLRHGR---HNVVLGLMPLYHVIGFFAVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 340 TGIQWGAQVCFAEPDAlKGSLVNTLREVEPTSHMGVPrvwekimeriqevaaqsgfirrkMLLWAMSVTLEQNltcpGSD 419
Cdd:cd05923 214 AALALDGTYVVVEEFD-PADALKLIEQERVTSLFATP-----------------------THLDALAAAAEFA----GLK 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 420 LKPFTTrladylvlakvrqaLGFAkcqknfyGAA---PMMAETQHFFLGLNIRLYagyGLSETsgphfMSSPYNYRLYSS 496
Cdd:cd05923 266 LSSLRH--------------VTFA-------GATmpdAVLERVNQHLPGEKVNIY---GTTEA-----MNSLYMRDARTG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 497 GKLVPG--CRVKLVN-----QDAEGIGE-----ICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITG 564
Cdd:cd05923 317 TEMRPGffSEVRIVRiggspDEALANGEegeliVAAAADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILG 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477105 565 RLKELIITaGGENVPPVPIEEAVKMElPIISNAMLIG--DQRKFLSMLLTLKCTLDPDTSDQTDnlteqamEFC 636
Cdd:cd05923 396 RVDDMIIS-GGENIHPSEIERVLSRH-PGVTEVVVIGvaDERWGQSVTACVVPREGTLSADELD-------QFC 460
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
278-584 |
4.24e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 78.78 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 278 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSH----IAAQIYDLWTGiqwGAQVCFAEP 353
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSP----RDATVAVMPLYHghglIAALLATLASG---GAVLLPARG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 354 DALKGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSG-----FIRrkmllwamsvtleqnlTCPGsdlkPFTTRLA 428
Cdd:PRK05852 253 RFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKpaalrFIR----------------SCSA----PLTAETA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 429 dylvlakvrQALgfakcQKNFygAAPM-----MAETQHFFLGLNIRlyaGYGLSE----TSGPHFMSSPYNYRLY-SSGK 498
Cdd:PRK05852 313 ---------QAL-----QTEF--AAPVvcafgMTEATHQVTTTQIE---GIGQTEnpvvSTGLVGRSTGAQIRIVgSDGL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 499 LVPgcrvklvnqdAEGIGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENV 578
Cdd:PRK05852 374 PLP----------AGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKEL-INRGGEKI 441
|
....*.
gi 27477105 579 PPVPIE 584
Cdd:PRK05852 442 SPERVE 447
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
134-655 |
4.50e-15 |
|
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: 78.31 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 134 SYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVdTQ 213
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 214 KQLEKilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtQQPNQCCVLVYTSGTTGNPKGVM 293
Cdd:cd05969 81 ELYER----------------------------------------------------TDPEDPTLLHYTSGTTGTPKGVL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 294 LSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDAlkgslvntlreveptshm 373
Cdd:cd05969 109 HVHDAMIFYYFTGKYVLDLHP----DDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF------------------ 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 374 gVPRVWEKIMERIqevaaqsgfirrKMLLWAMSVTLEQNLTcpgsdlkpfttRLADYLVLAKVRQALGFAKCqknfyGAA 453
Cdd:cd05969 167 -DAESWYGIIERV------------KVTVWYTAPTAIRMLM-----------KEGDELARKYDLSSLRFIHS-----VGE 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 454 PMMAETQHFFLG-LNIRLYAGYGLSETSGPHFMSSP-YNYRLYSSGKLVPGCRVKLVNQDAEGI-----GEICL---WgR 523
Cdd:cd05969 218 PLNPEAIRWGMEvFGVPIHDTWWQTETGSIMIANYPcMPIKPGSMGKPLPGVKAAVVDENGNELppgtkGILALkpgW-P 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 524 TIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIGDQ 603
Cdd:cd05969 297 SMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESAL-MEHPAVAEAGVIGKP 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 27477105 604 RKFLSMLLTLKCTLDPDTSdQTDNLTEQAMEFCqRVGSRATTVSEIIEKKDE 655
Cdd:cd05969 374 DPLRGEIIKAFISLKEGFE-PSDELKEEIINFV-RQKLGAHVAPREIEFVDN 423
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
272-605 |
7.65e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 78.85 E-value: 7.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 272 QPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHiaaqiydlwtgiqwgaqvCFA 351
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSP----EDKVFNALPVFH------------------SFG 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 352 epdaLKGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFirrkmllwamsvtleqnltcpGSDlkpftTRLADYl 431
Cdd:PRK06814 849 ----LTGGLVLPLLSGVKVFLYPSPLHYRIIPELIYDTNATILF---------------------GTD-----TFLNGY- 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 432 vlAKVRQALGFAKCQKNFYGAAPMMAETQHFFL-GLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLvnQ 510
Cdd:PRK06814 898 --ARYAHPYDFRSLRYVFAGAEKVKEETRQTWMeKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRL--E 973
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 511 DAEGI---GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIEEAV 587
Cdd:PRK06814 974 PVPGIdegGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRF-AKIAGEMISLAAVEELA 1052
|
330
....*....|....*....
gi 27477105 588 KMELP-IISNAMLIGDQRK 605
Cdd:PRK06814 1053 AELWPdALHAAVSIPDARK 1071
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
277-601 |
1.27e-14 |
|
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: 75.80 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 277 CVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevvvsYL---PLSHIaaqiydlwtgiqwgaqvcfaep 353
Cdd:cd17636 3 VLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTV-------FLnsgPLFHI---------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 354 dalkGSLVNTLrevePTSHMG-----VPRV-WEKIMERIQEVAAQSGFIrrkmllwaMSVTLEQNLtcpgsdlKPFTTRL 427
Cdd:cd17636 54 ----GTLMFTL----ATFHAGgtnvfVRRVdAEEVLELIEAERCTHAFL--------LPPTIDQIV-------ELNADGL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 428 ADYLVLAKVRQALGFAkcqknfygaAPMMAETQHFFLGLnirlyAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKL 507
Cdd:cd17636 111 YDLSSLRSSPAAPEWN---------DMATVDTSPWGRKP-----GGYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 508 VnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRlKELIITAGGENVPP 580
Cdd:cd17636 177 L--DEDGrevpdgeVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYP 252
|
330 340
....*....|....*....|.
gi 27477105 581 VPIEEAVKmELPIISNAMLIG 601
Cdd:cd17636 253 AEVERCLR-QHPAVADAAVIG 272
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
270-589 |
2.84e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 76.21 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 270 TQQPNQCCVLVYTSGTTGNPKGVMLSQDNI--------TWTarygsQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTG 341
Cdd:PRK07059 200 KLGPDDVAFLQYTGGTTGVSKGATLLHRNIvanvlqmeAWL-----QPAFEKKPRPDQLNFVCALPLYHIFALTVCGLLG 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 342 IQWGA-QVCFAEPDALKGsLVNTLREVEPTSHMGVPRVWEKIMEriqevaaQSGFirRKMllwamsvtleqnltcpgsDL 420
Cdd:PRK07059 275 MRTGGrNILIPNPRDIPG-FIKELKKYQVHIFPAVNTLYNALLN-------NPDF--DKL------------------DF 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 421 KPFttrladylvlaKVRQALGFAkCQKNfygaapmMAETQHFFLGLNIrlYAGYGLSETSgPHFMSSPYNYRLYSSGKLV 500
Cdd:PRK07059 327 SKL-----------IVANGGGMA-VQRP-------VAERWLEMTGCPI--TEGYGLSETS-PVATCNPVDATEFSGTIGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 501 PGCRVKLVNQDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITA 573
Cdd:PRK07059 385 PLPSTEVSIRDDDGndlplgePGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
330
....*....|....*.
gi 27477105 574 GGeNVPPVPIEEAVKM 589
Cdd:PRK07059 465 GF-NVYPNEIEEVVAS 479
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
246-590 |
7.55e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 75.04 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 246 VYTMEEFMELgnevpeEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAG-DIRPAEVqqevVVS 324
Cdd:PRK09192 154 VLSHAWFKAL------PEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGlKVRPGDR----CVS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 325 YLPLSHiaaqiyDLwtgiqwGAQVCFAEPDALKGSlVNTLrevePTSHMGV-PRVWEKIMERIQEVAAQS---GF---IR 397
Cdd:PRK09192 224 WLPFYH------DM------GLVGFLLTPVATQLS-VDYL----PTRDFARrPLQWLDLISRNRGTISYSppfGYelcAR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 398 RkmllwAMSVTLEQ-NLTC-----PGSD------LKPFTTRLADylvlakvrqaLGFAkcQKNF---YG------AAPMM 456
Cdd:PRK09192 287 R-----VNSKDLAElDLSCwrvagIGADmirpdvLHQFAEAFAP----------AGFD--DKAFmpsYGlaeatlAVSFS 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 457 AETQHF-FLGLNIRLYAGYGLSETSGphfmSSPYNYRLY-SSGKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGY 529
Cdd:PRK09192 350 PLGSGIvVEEVDRDRLEYQGKAVAPG----AETRRVRTFvNCGKALPGHEIEIRNEAGMplperVVGHICVRGPSLMSGY 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477105 530 LNMEDkTCEAIDEEGWLHTGDAGRLdADGFLYITGRLKELIITaGGENVPPVPIEEAVKME 590
Cdd:PRK09192 426 FRDEE-SQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIII-NGRNIWPQDIEWIAEQE 483
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
131-601 |
1.22e-13 |
|
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: 73.67 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFL-KLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM 209
Cdd:cd05958 9 REWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 210 VDtqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeEALDAIIDTqqpnqcCVLVYTSGTTGNP 289
Cdd:cd05958 89 CA--------------------------------------------------HALTASDDI------CILAFTSGTTGAP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 290 KGVM-LSQDNITWTARYGSQAgdIRPAEvqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQvCFAEPDALKGSLVNTLREVE 368
Cdd:cd05958 113 KATMhFHRDPLASADRYAVNV--LRLRE--DDRFVGSPPLAFTFGLGGVLLFPFGVGAS-GVLLEEATPDLLLSAIARYK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 369 PTSHMGVPRVWEKIMERIQEVAAQSGFIRRkmllwamsvtleqnLTCPGSDLKPFTTRLADYLVLAKVRQALGfakCQKN 448
Cdd:cd05958 188 PTVLFTAPTAYRAMLAHPDAAGPDLSSLRK--------------CVSAGEALPAALHRAWKEATGIPIIDGIG---STEM 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 449 FygaapmmaetqHFFLGlnirlyagyglsetsgphfmSSPYNYRLYSSGKLVPGCRVKLVnqDAEG-------IGEICLW 521
Cdd:cd05958 251 F-----------HIFIS--------------------ARPGDARPGATGKPVPGYEAKVV--DDEGnpvpdgtIGRLAVR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 522 GRTifmGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:cd05958 298 GPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVEDVL-LQHPAVAECAVVG 372
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
497-601 |
1.41e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 73.81 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 497 GKLVPGCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKtcEAIDeeGWLHTGDAGRLDADGFLYITGRLKEL 569
Cdd:PRK07788 379 GRPPKGVTVKIL--DENGnevprgvVGRIFVGNGFPFEGYTDGRDK--QIID--GLLSSGDVGYFDEDGLLFVDGRDDDM 452
|
90 100 110
....*....|....*....|....*....|..
gi 27477105 570 IITaGGENVPPVPIEEAVKmELPIISNAMLIG 601
Cdd:PRK07788 453 IVS-GGENVFPAEVEDLLA-GHPDVVEAAVIG 482
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
131-601 |
1.69e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 73.57 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFfsavgTVFAGGIVTGIYTTS-----SPEACQYIAYDCCA 205
Cdd:PRK13391 23 EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYL-----EVCWAAERSGLYYTCvnshlTPAEAAYIVDDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 206 NViMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPpnkmanvyTMEEFMELgnevpEEALDAIIDTQQPNQC--CVLVYTS 283
Cdd:PRK13391 98 RA-LITSAAKLDVARALLKQCPGVRHRLVLDGDG--------ELEGFVGY-----AEAVAGLPATPIADESlgTDMLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 284 GTTGNPKGVM--LS----QDNITWTA----RYGSQAGDIrpaevqqevvvsYL---PLSHIAAQIYDLwTGIQWGAQVCF 350
Cdd:PRK13391 164 GTTGRPKGIKrpLPeqppDTPLPLTAflqrLWGFRSDMV------------YLspaPLYHSAPQRAVM-LVIRLGGTVIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 351 AEP-DAlkgslvntlreveptshmgvprvwEKIMERIQEVAaqsgfIRRKMLLWAMSVTLeqnLTCPgsdlkpfttrlad 429
Cdd:PRK13391 231 MEHfDA------------------------EQYLALIEEYG-----VTHTQLVPTMFSRM---LKLP------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 430 ylvlAKVRQALGFAKCQKNFYGAAPMMAETQHFFL---GLNIRLYagYGLSETSGPHFMSSP-YNYRLYSSGKLVPGcrv 505
Cdd:PRK13391 266 ----EEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIdwwGPIIHEY--YAATEGLGFTACDSEeWLAHPGTVGRAMFG--- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 506 KLVNQDAEG-------IGEICLWGRTIFMgYLNMEDKTCEAIDEEG-WLHTGDAGRLDADGFLYITGRLKELIITaGGEN 577
Cdd:PRK13391 337 DLHILDDDGaelppgePGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIIS-GGVN 414
|
490 500
....*....|....*....|....
gi 27477105 578 VPPVPIEEAVkMELPIISNAMLIG 601
Cdd:PRK13391 415 IYPQEAENLL-ITHPKVADAAVFG 437
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
107-565 |
2.35e-13 |
|
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: 72.73 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 107 RMFYEALDKYGDLIALgfkrQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGgivtg 186
Cdd:cd17653 1 DAFERIAAAHPDAVAV----ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAG----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 187 iyttsspeaCQYIAydccanvimVDTqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnEVPEEALDA 266
Cdd:cd17653 72 ---------AAYVP---------LDA---------------------------------------------KLPSARIQA 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 267 IIDTQQPNQC---------CVLVYTSGTTGNPKGVMLSQDNIT----WT-ARYGSQAGDiRPAEVqqevvvsylpLShIA 332
Cdd:cd17653 89 ILRTSGATLLlttdspddlAYIIFTSGSTGIPKGVMVPHRGVLnyvsQPpARLDVGPGS-RVAQV----------LS-IA 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 333 --AQIYDLWTGIQWGAQVCFAEPDalkgslvntlrevEPTSHMgvprvwekimeriqevaaqsgfirrkmllwAMSVTLe 410
Cdd:cd17653 157 fdACIGEIFSTLCNGGTLVLADPS-------------DPFAHV------------------------------ARTVDA- 192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 411 qnLTCPGSDLKpfTTRLADYLVLAKVrqALGfakcqknfyGAAPMMAETQHFflGLNIRLYAGYGLSETSGPHFMSSPYN 490
Cdd:cd17653 193 --LMSTPSILS--TLSPQDFPNLKTI--FLG---------GEAVPPSLLDRW--SPGRRLYNAYGPTECTISSTMTELLP 255
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 491 YRLYSSGKLVPGCRVKLVNQD-----AEGIGEICLWGRTIFMGYLNMEDKTCEAI----DEEGWLH--TGDAGRLDADGF 559
Cdd:cd17653 256 GQPVTIGKPIPNSTCYILDADlqpvpEGVVGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGG 335
|
....*.
gi 27477105 560 LYITGR 565
Cdd:cd17653 336 LEFLGR 341
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
466-587 |
4.76e-13 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 71.95 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 466 LNIRLYAGYGLSETSGPHFMSSPYNYRL--YSSGKLVPGCRVKLVNQDaegIGEICLWGRTIFMGYLNmedktcEAIDEE 543
Cdd:PRK07445 253 LQLRLAPTYGMTETASQIATLKPDDFLAgnNSSGQVLPHAQITIPANQ---TGNITIQAQSLALGYYP------QILDSQ 323
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 27477105 544 GWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAV 587
Cdd:PRK07445 324 GIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAI 366
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
133-605 |
1.88e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 70.16 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTT-SSPEACQYIAYDCCANVIMVD 211
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRyRSHEVAHILGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 212 TQKQLE--KILKIWKQ--LPHLKAVVIYKE-----PPPNKMANVYTmeefmeLGNEVPEEALDAIIDTQQPNQCCVLVYT 282
Cdd:PRK06164 116 GFKGIDfaAILAAVPPdaLPPLRAIAVVDDaadatPAPAPGARVQL------FALPDPAPPAAAGERAADPDAGALLFTT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 283 SGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDAlkGSLVN 362
Cdd:PRK06164 190 SGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAV----LLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDA--ARTAR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 363 TLREVEPTSHMGVprvwEKIMERIQEVAAQSG-FIRRKMLLWAmsvtleqnltcpgsdlkPFTTRLADYLVLAKVRQALg 441
Cdd:PRK06164 264 ALRRHRVTHTFGN----DEMLRRILDTAGERAdFPSARLFGFA-----------------SFAPALGELAALARARGVP- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 442 fakcQKNFYGAApmmaETQHFFLGlnirlyagyglsetsgpHFMSSPYNYRLYSSGKLV-PGCRVKLVNQDAEGI----- 515
Cdd:PRK06164 322 ----LTGLYGSS----EVQALVAL-----------------QPATDPVSVRIEGGGRPAsPEARVRARDPQDGALlpdge 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 516 -GEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADG-FLYITgRLKElIITAGGENVPPVPIEEAVKmELPI 593
Cdd:PRK06164 377 sGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGqFVYQT-RMGD-SLRLGGFLVNPAEIEHALE-ALPG 453
|
490
....*....|..
gi 27477105 594 ISNAMLIGDQRK 605
Cdd:PRK06164 454 VAAAQVVGATRD 465
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
270-601 |
3.78e-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: 69.00 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 270 TQQPNQCCVLVYTSGTTGNPKGVMLSQdnitwtarygsqagdirpaevqqEVVVSYLPLSHIAAQIY----DL-WTGIQW 344
Cdd:cd05971 84 TDGSDDPALIIYTSGTTGPPKGALHAH-----------------------RVLLGHLPGVQFPFNLFprdgDLyWTPADW 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 345 gaqvcfaepdALKGSLVNTLRevePTSHMGVPRVWEKiMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGSDLKPFT 424
Cdd:cd05971 141 ----------AWIGGLLDVLL---PSLYFGVPVLAHR-MTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 425 TRL---------ADYLVLAKVRQALGFAKCQknFYGaapmMAETqHFFLGLNirlyagyglsetsgphfmSSPYNYRLYS 495
Cdd:cd05971 207 VKLraiatggesLGEELLGWAREQFGVEVNE--FYG----QTEC-NLVIGNC------------------SALFPIKPGS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 496 SGKLVPGCRVKLVNQDAE-----GIGEICLwgRT----IFMGYLNMEDKTcEAIDEEGWLHTGDAGRLDADGFLYITGRL 566
Cdd:cd05971 262 MGKPIPGHRVAIVDDNGTplppgEVGEIAV--ELpdpvAFLGYWNNPSAT-EKKMAGDWLLTGDLGRKDSDGYFWYVGRD 338
|
330 340 350
....*....|....*....|....*....|....*
gi 27477105 567 KElIITAGGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:cd05971 339 DD-VITSSGYRIGPAEIEECL-LKHPAVLMAAVVG 371
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
467-601 |
4.22e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 69.04 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 467 NIRLYAGYGLSETSGPHFMSSPYNYRLYSS-GKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNmEDKTCEAI 540
Cdd:PRK07638 279 YAKLYEFYGASELSFVTALVDEESERRPNSvGRPFHNVQVRICNEAGEevqkgEIGTVYVKSPQFFMGYII-GGVLAREL 357
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27477105 541 DEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEaVKMELPIISNAMLIG 601
Cdd:PRK07638 358 NADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIES-VLHEHPAVDEIVVIG 416
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
89-565 |
7.05e-12 |
|
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: 69.12 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 89 RVRLRIDPSCPQLPY----TVHRMFYEALDKYGDLIALGFKRQdkweHISYSQyylLARRA---AKGFLKLGLKQAHSVA 161
Cdd:COG1020 458 RQQLLAEWNATAAPYpadaTLHELFEAQAARTPDAVAVVFGDQ----SLTYAE---LNARAnrlAHHLRALGVGPGDLVG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 162 ILGFNSPEWFFSAVGTVFAGGIvtgiYT---TSSPEA-CQYIAYDCCANVIMvdTQKQLEKilkiwkQLPHLKAVVIYKE 237
Cdd:COG1020 531 VCLERSLEMVVALLAVLKAGAA----YVpldPAYPAErLAYMLEDAGARLVL--TQSALAA------RLPELGVPVLALD 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 238 PPpnkmanvytmeefmELGNEvPEEALDAIIDTQQPnqCCVLvYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDi 312
Cdd:COG1020 599 AL--------------ALAAE-PATNPPVPVTPDDL--AYVI-YTSGSTGRPKGVMVEHRALVnllawMQRRYGLGPGD- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 313 rpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDALK--GSLVNTLREVEPTS-HMgVPRVWEKIMEriqev 389
Cdd:COG1020 660 --------RVLQFASLSFDAS-VWEIFGALLSGATLVLAPPEARRdpAALAELLARHRVTVlNL-TPSLLRALLD----- 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 390 AAQSGFIRRKMLLW---AMSVTLeqnltcpgsdlkpfttrladylvLAKVRQALGfakcqknfygaapmmaetqhfflgl 466
Cdd:COG1020 725 AAPEALPSLRLVLVggeALPPEL-----------------------VRRWRARLP------------------------- 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 467 NIRLYAGYGLSETS-----------GPHFMSSPY-----NYRLY---SSGKLVP-GCrvklvnqdaegIGEICLWGRTIF 526
Cdd:COG1020 757 GARLVNLYGPTETTvdstyyevtppDADGGSVPIgrpiaNTRVYvldAHLQPVPvGV-----------PGELYIGGAGLA 825
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 27477105 527 MGYLNMEDKTCEA-----IDEEG--WLHTGDAGRLDADGFLYITGR 565
Cdd:COG1020 826 RGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGR 871
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
495-587 |
1.11e-11 |
|
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: 67.79 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 495 SSGKLVPGcRVKLVNQDAEG-----IGEICLWGRTIFMgYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKEL 569
Cdd:cd05929 298 SVGRAVLG-KVHILDEDGNEvppgeIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDM 375
|
90
....*....|....*...
gi 27477105 570 IITaGGENVPPVPIEEAV 587
Cdd:cd05929 376 IIS-GGVNIYPQEIENAL 392
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
89-333 |
2.58e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 66.82 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 89 RVRLRIDPSCPQLPYTVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSP 168
Cdd:PRK08279 23 RGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQ----SISYAELNARANRYAHWAAARGVGKGDVVALLMENRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 169 EWFFSAVGTVFAGGIVTGIYTTSSPEA---CQYIAYdccANVIMV--DTQKQLEKIlkiwkqLPHLKAVVIYKEPPPNKM 243
Cdd:PRK08279 99 EYLAAWLGLAKLGAVVALLNTQQRGAVlahSLNLVD---AKHLIVgeELVEAFEEA------RADLARPPRLWVAGGDTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 244 ANVYTMEEFMELGNEVPEEALDAiidTQ--QPNQCCVLVYTSGTTGNPKGVMLSQdnITWTARYGSQAGDIRPAEvqQEV 321
Cdd:PRK08279 170 DDPEGYEDLAAAAAGAPTTNPAS---RSgvTAKDTAFYIYTSGTTGLPKAAVMSH--MRWLKAMGGFGGLLRLTP--DDV 242
|
250
....*....|..
gi 27477105 322 VVSYLPLSHIAA 333
Cdd:PRK08279 243 LYCCLPLYHNTG 254
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
133-604 |
3.14e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 66.45 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFLKLGLK-QAHsVAILGFNSPEWFFSAVGTVFAGGIVTGI---YTtssPEACQYIAYDCCANVI 208
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGpGDH-VGIYARNRIEYVEAMLGAFKARAVPVNVnyrYV---EDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 209 MVDTQkQLEKILKIWKQLPHLKAVVIYKEPPPNKmanvytmeefmELGNEVP-EEALDAIIDTQQPNQCC----VLVYTS 283
Cdd:PRK07798 105 VYERE-FAPRVAEVLPRLPKLRTLVVVEDGSGND-----------LLPGAVDyEDALAAGSPERDFGERSpddlYLLYTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 284 GTTGNPKGVMLSQDNItwtarYGSQAGDIRPA---EVQQEVVVSYL-------------PLSHIAAQiydlWTGiqWGAq 347
Cdd:PRK07798 173 GTTGMPKGVMWRQEDI-----FRVLLGGRDFAtgePIEDEEELAKRaaagpgmrrfpapPLMHGAGQ----WAA--FAA- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 348 vcfaepdALKGSLVNTLREVEPTSHmgvpRVWEKI-MERIQEVAaqsgfirrkMLLWAMSVTLEQNLTCPGsdlkpfTTR 426
Cdd:PRK07798 241 -------LFSGQTVVLLPDVRFDAD----EVWRTIeREKVNVIT---------IVGDAMARPLLDALEARG------PYD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 427 LADYLVLAKvrqalgfakcqknfyGAAPMMAETQHFFLGL--NIRLYAGYGLSET-SGPHFMSSPYNYRlySSGKLV-PG 502
Cdd:PRK07798 295 LSSLFAIAS---------------GGALFSPSVKEALLELlpNVVLTDSIGSSETgFGGSGTVAKGAVH--TGGPRFtIG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 503 CRVKLVNQD-------AEGIGEICLWGRtIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRlKELIIT 572
Cdd:PRK07798 358 PRTVVLDEDgnpvepgSGEIGWIARRGH-IPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGR-GSVCIN 435
|
490 500 510
....*....|....*....|....*....|....
gi 27477105 573 AGGENVPPVPIEEAVKMElPIISNAMLIG--DQR 604
Cdd:PRK07798 436 TGGEKVFPEEVEEALKAH-PDVADALVVGvpDER 468
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
271-574 |
4.88e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 66.27 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 271 QQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVcF 350
Cdd:PRK08043 362 QQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTP----NDRFMSALPLFHSFGLTVGLFTPLLTGAEV-F 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 351 AEPDALKGSLVNTLreveptshmgvprVWEkimeriqevaaqsgfiRRKMLLWAMSvtleqnltcpgsdlkpftTRLADY 430
Cdd:PRK08043 437 LYPSPLHYRIVPEL-------------VYD----------------RNCTVLFGTS------------------TFLGNY 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 431 lvlAKVRQALGFAKCQKNFYGAAPMMAET-QHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVN 509
Cdd:PRK08043 470 ---ARFANPYDFARLRYVVAGAEKLQESTkQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLS 546
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477105 510 qdAEGI---GEICLWGRTIFMGYLNMED---------KTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAG 574
Cdd:PRK08043 547 --VPGIeqgGRLQLKGPNIMNGYLRVEKpgvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
470-637 |
7.02e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 65.40 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 470 LYAGYGLSETsGPHFMSSPYNYRLY--SSGKLVPGCRVKLVNQDAEGIGEIcLWGRTIFMGYLNME---DKTCEAIdEEG 544
Cdd:PRK13383 320 LYNGYGSTEV-GIGALATPADLRDApeTVGKPVAGCPVRILDRNNRPVGPR-VTGRIFVGGELAGTrytDGGGKAV-VDG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 545 WLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVKMELPIISNAML-IGDQR--KFLSMLLTLKCTLDPDT 621
Cdd:PRK13383 397 MTSTGDMGYLDNAGRLFIVGREDDMIIS-GGENVYPRAVENALAAHPAVADNAVIgVPDERfgHRLAAFVVLHPGSGVDA 475
|
170
....*....|....*.
gi 27477105 622 SDQTDNLTEQAMEFCQ 637
Cdd:PRK13383 476 AQLRDYLKDRVSRFEQ 491
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
101-601 |
8.81e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 65.03 E-value: 8.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 101 LPYTVHRMFYEALDKYGDLIALgfKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFA 180
Cdd:PRK05857 12 LPSTVLDRVFEQARQQPEAIAL--RRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 181 GGIVtgiyttsspeacqyiaydccanvIMVDTQKQLEKILKiWKQLPHLKAVVIYK------EPPPNKMANVYTMEEFME 254
Cdd:PRK05857 90 GAIA-----------------------VMADGNLPIAAIER-FCQITDPAAALVAPgskmasSAVPEALHSIPVIAVDIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 255 LGNEVPEEALDAIIDTQQPN----QCCVLVYTSGTTGNPKGVMLSqdNITWTArygsqAGDIRPAE-------VQQEVVV 323
Cdd:PRK05857 146 AVTRESEHSLDAASLAGNADqgseDPLAMIFTSGTTGEPKAVLLA--NRTFFA-----VPDILQKEglnwvtwVVGETTY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 324 SYLPLSHIAAqiydLW---TGIQWGAqVCFAepdalKGSLVNTLREVeptshmgvprvwekimeriqevaaqsgfirrkm 400
Cdd:PRK05857 219 SPLPATHIGG----LWwilTCLMHGG-LCVT-----GGENTTSLLEI--------------------------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 401 llwamSVTLEQNLTCpgsdLKP-FTTRLADYLVLAKVR-QALGFAKcqknfYGAAPMMAETQHFFLGLNIRLYAGYGLSE 478
Cdd:PRK05857 256 -----LTTNAVATTC----LVPtLLSKLVSELKSANATvPSLRLVG-----YGGSRAIAADVRFIEATGVRTAQVYGLSE 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 479 TSG-----PHFMSSPYNYRLYSSGKLVPGCRVKLVNQD-----AEGIGEIC----LWGRTI--FMGYLNMEDKTCEAIdE 542
Cdd:PRK05857 322 TGCtalclPTDDGSIVKIEAGAVGRPYPGVDVYLAATDgigptAPGAGPSAsfgtLWIKSPanMLGYWNNPERTAEVL-I 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477105 543 EGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPP---------VP-IEEAVKMELPIISNAMLIG 601
Cdd:PRK05857 401 DGWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPdevdriaegVSgVREAACYEIPDEEFGALVG 468
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
131-601 |
1.08e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 210
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 DTQkqlekilkiwkqLPHLKAVViyKEPPPNKMANVYTMEEFMELgnevpEEALDAIID--TQQPnqC-CVLVYTSGTTG 287
Cdd:PRK13390 103 SAA------------LDGLAAKV--GADLPLRLSFGGEIDGFGSF-----EAALAGAGPrlTEQP--CgAVMLYSSGTTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 288 NPKGvmlsqdnitwtarygsqagdIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQW--GAQVCFAEPdalkgslvntLR 365
Cdd:PRK13390 162 FPKG--------------------IQPDLPGRDVDAPGDPIVAIARAFYDISESDIYysSAPIYHAAP----------LR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 366 EVEPTSHMGVPRVWEKIMEriqeVAAQSGFIRRkmllwaMSVTLEQnltcpgsdLKPftTRLADYLVL-AKVRQALGFAK 444
Cdd:PRK13390 212 WCSMVHALGGTVVLAKRFD----AQATLGHVER------YRITVTQ--------MVP--TMFVRLLKLdADVRTRYDVSS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 445 CQKNFYGAAPMMAETQHFFLG-LNIRLYAGYGLSETSGPHFMSSP-YNYRLYSSGKLVPGcRVKLVNQD-----AEGIGE 517
Cdd:PRK13390 272 LRAVIHAAAPCPVDVKHAMIDwLGPIVYEYYSSTEAHGMTFIDSPdWLAHPGSVGRSVLG-DLHICDDDgnelpAGRIGT 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 518 ICLWGRTIFMGYLNMEDKTCEAIDEEG--WLHTGDAGRLDADGFLYITGRlKELIITAGGENVPPVPIEEAVKMElPIIS 595
Cdd:PRK13390 351 VYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADR-KSFMIISGGVNIYPQETENALTMH-PAVH 428
|
....*.
gi 27477105 596 NAMLIG 601
Cdd:PRK13390 429 DVAVIG 434
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
272-594 |
1.49e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 272 QPNQCCVLVYTSGTTGNPKGVMLSQDNIT---WTARYGSqAGDIRPaevqQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 348
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVaneQLIRHGF-GIDLNP----DDVIVSWLPLYHDMGLIGGLLQPIFSGVPC 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 349 CFAEPDALkgsLVNTLREVEPTSHM-----GVPR-VWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNltcpgsDLKP 422
Cdd:PRK05691 239 VLMSPAYF---LERPLRWLEAISEYggtisGGPDfAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQD------SLER 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 423 FTTRLAdylvlakvrqALGFAkcQKNFYgAAPMMAETQHFFLG-----------LNIRLYAGYGLSETSGPHFMSSpyny 491
Cdd:PRK05691 310 FAEKFA----------ACGFD--PDSFF-ASYGLAEATLFVSGgrrgqgipaleLDAEALARNRAEPGTGSVLMSC---- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 492 rlyssGKLVPGCRVKLVN-QDAEG-----IGEICLWGRTIFMGYLNMEDKTCEAI---DEEGWLHTGDAGRLdADGFLYI 562
Cdd:PRK05691 373 -----GRSQPGHAVLIVDpQSLEVlgdnrVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDLGFL-RDGELFV 446
|
330 340 350
....*....|....*....|....*....|..
gi 27477105 563 TGRLKELIITAgGENVPPVPIEEAVKMELPII 594
Cdd:PRK05691 447 TGRLKDMLIVR-GHNLYPQDIEKTVEREVEVV 477
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
107-565 |
8.72e-10 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 107 RMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 186
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQ----TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 187 IYTTSSPEACQYIAYDCCANVIMvdTQKQLEKilkiwkQLPHLKAVVIYKEpppnkmanvytmeefmELGNEVPEEALDA 266
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILL--TQSHLQP------PIAFIGLIDLLDE----------------DTIYHEESENLEP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 267 IIdtqQPNQCCVLVYTSGTTGNPKGVMLSQDN----ITWTARYGSQAGDIRpaevqqevVVSYLPLShIAAQIYDLWTGI 342
Cdd:cd17655 133 VS---KSDDLAYVIYTSGSTGKPKGVMIEHRGvvnlVEWANKVIYQGEHLR--------VALFASIS-FDASVTEIFASL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 343 QWGAQVCFAEPDALKG--SLVNTLREVEPTSHMGVPRVwekiMERIQEVAAQSGFIRRKMLLwamsvtleqnltcPGSDL 420
Cdd:cd17655 201 LSGNTLYIVRKETVLDgqALTQYIRQNRITIIDLTPAH----LKLLDAADDSEGLSLKHLIV-------------GGEAL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 421 KPfttrladylVLAKVRQALGFAKCQ-KNFYGAapmmAETQhffLGLNIRLYAGYGLSETSGPhfMSSPY-NYRLY---S 495
Cdd:cd17655 264 ST---------ELAKKIIELFGTNPTiTNAYGP----TETT---VDASIYQYEPETDQQVSVP--IGKPLgNTRIYildQ 325
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477105 496 SGKLVPgcrvklvnqdaEGI-GEICLWGRTIFMGYLNMEDKTCEA-IDE-----EGWLHTGDAGRLDADGFLYITGR 565
Cdd:cd17655 326 YGRPQP-----------VGVaGELYIGGEGVARGYLNRPELTAEKfVDDpfvpgERMYRTGDLARWLPDGNIEFLGR 391
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
279-604 |
9.09e-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: 61.24 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 279 LVYTSGTTGNPKGVMLSQDNItwtarYGSQAG-------------DIRPAEVQQEVVVSYL--PLSHIAAQIydLWTGIQ 343
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDI-----FRMLMGgadfgtgeftpseDAHKAAAAAAGTVMFPapPLMHGTGSW--TAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 344 WGAQVCFAEPDALKGslVNTLREVEPTSHMGVPRVWEkimeriqevaaqsgfirrkmllwAMSVTLEQNLTCPGsdlkpf 423
Cdd:cd05924 81 LGGQTVVLPDDRFDP--EEVWRTIEKHKVTSMTIVGD-----------------------AMARPLIDALRDAG------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 424 TTRLADYLVLAKvrqalgfakcqknfyGAAPMMAETQHFFLGL--NIRLYAGYGLSETSgphFMSSPYN-YRLYSSGKLV 500
Cdd:cd05924 130 PYDLSSLFAISS---------------GGALLSPEVKQGLLELvpNITLVDAFGSSETG---FTGSGHSaGSGPETGPFT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 501 ---PGCRV-----KLVNQDAEGIGEICLWGRtIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDADGFLYITGRlKEL 569
Cdd:cd05924 192 ranPDTVVldddgRVVPPGSGGVGWIARRGH-IPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGR-GSV 269
|
330 340 350
....*....|....*....|....*....|....*..
gi 27477105 570 IITAGGENVPPVPIEEAVKMElPIISNAMLIG--DQR 604
Cdd:cd05924 270 CINTGGEKVFPEEVEEALKSH-PAVYDVLVVGrpDER 305
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
468-597 |
1.01e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 61.43 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 468 IRLYAGYGLSEtsgphfMSSPYNYRLYSS----GKLVPGCRVKLVNqdaegiGEICLWGRTIFMGYLnMEDKTCEAIDEE 543
Cdd:PRK09029 265 IRCWCGYGLTE------MASTVCAKRADGlagvGSPLPGREVKLVD------GEIWLRGASLALGYW-RQGQLVPLVNDE 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 27477105 544 GWLHTGDAGRLDaDGFLYITGRLKELIITaGGENVPPVPIeEAVKMELPIISNA 597
Cdd:PRK09029 332 GWFATRDRGEWQ-NGELTILGRLDNLFFS-GGEGIQPEEI-ERVINQHPLVQQV 382
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
505-601 |
1.90e-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: 60.54 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 505 VKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVP 579
Cdd:COG1021 365 VRIVDEDgnpvPPGeVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINR-GGEKIA 443
|
90 100
....*....|....*....|..
gi 27477105 580 PVPIEEAVkMELPIISNAMLIG 601
Cdd:COG1021 444 AEEVENLL-LAHPAVHDAAVVA 464
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
273-606 |
4.67e-09 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 59.39 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 273 PNQCCVLVYTSGTTGNPKGvmlsqdnitwtARYgSQAGDIRPAEVqqevVVSYLPLSH-----IAAQIYDLWtGIqwgAQ 347
Cdd:PRK13382 195 GRKGRVILLTSGTTGTPKG-----------ARR-SGPGGIGTLKA----ILDRTPWRAeeptvIVAPMFHAW-GF---SQ 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 348 VCFAEpdALKGSLVN--------TLREVE---PTSHMGVPRVWEKIMERIQEVAAQsgFIRRKMLLWAMSvtleqnltcp 416
Cdd:PRK13382 255 LVLAA--SLACTIVTrrrfdpeaTLDLIDrhrATGLAVVPVMFDRIMDLPAEVRNR--YSGRSLRFAAAS---------- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 417 GSDLKP-----FTTRLADYLVlakvrqalgfakcqkNFYGA--APMMAetqhfflglnirlyagyglseTSGPHFMSSPY 489
Cdd:PRK13382 321 GSRMRPdvviaFMDQFGDVIY---------------NNYNAteAGMIA---------------------TATPADLRAAP 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 490 NyrlySSGKLVPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEaideEGWLHTGDAGRLDADGFLYITG 564
Cdd:PRK13382 365 D----TAGRPAEGTEIRILDQDfrevPTGeVGTIFVRNDTQFDGYTSGSTKDFH----DGFMASGDVGYLDENGRLFVVG 436
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 27477105 565 RLKELIITaGGENVPPVPIEEAVkMELPIISNAMLIG-DQRKF 606
Cdd:PRK13382 437 RDDEMIVS-GGENVYPIEVEKTL-ATHPDVAEAAVIGvDDEQY 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-317 |
7.81e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.40 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 86 ADGRVRLRIDPSCPQ---LPYTVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAI 162
Cdd:PRK12467 492 AEERARELVRWNAPAteyAPDCVHQLIEAQARQHPERPALVFGEQ----VLSYAELNRQANRLAHVLIAAGVGPDVLVGI 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 163 LGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDccANVIMVDTQKQLEKILKIWKQLPHLkaVVIYKEPPPNK 242
Cdd:PRK12467 568 AVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDD--SGVRLLLTQSHLLAQLPVPAGLRSL--CLDEPADLLCG 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27477105 243 MANVYtmeefmelgnevPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNIT----WTARYGSQAGDIRPAEV 317
Cdd:PRK12467 644 YSGHN------------PEVALD-------PDNLAYVIYTSGSTGQPKGVAISHGALAnyvcVIAERLQLAADDSMLMV 703
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
468-587 |
1.01e-08 |
|
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: 58.28 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 468 IRLYAGYGLSET-----SGPHFMSSPYnyrlySSGKLVPGCRVKLVNQDAEGI-----GEICLwgRT-------IFMGYL 530
Cdd:cd05970 327 IKLMEGFGQTETtltiaTFPWMEPKPG-----SMGKPAPGYEIDLIDREGRSCeageeGEIVI--RTskgkpvgLFGGYY 399
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477105 531 NMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAV 587
Cdd:cd05970 400 KDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS-GYRIGPFEVESAL 454
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
131-620 |
1.51e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 57.77 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSqyyllARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQY-IAY-DCcaNVI 208
Cdd:PRK07867 33 EHIRGS-----AARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARdIAHaDC--QLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 209 MVDTqkqlekilkiwKQLPHLKAVviykePPPNKMANVYTMEEFMELGNEvPEEALDAIIDtqQPNQCCVLVYTSGTTGN 288
Cdd:PRK07867 106 LTES-----------AHAELLDGL-----DPGVRVINVDSPAWADELAAH-RDAEPPFRVA--DPDDLFMLIFTSGTSGD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 289 PKGVMLSQDNITWTARYGSQAGDIRPAEVqqeVVVSyLPLSHIAAQIYDLWTGIQWGAQvcfaepdalkgslvntlreve 368
Cdd:PRK07867 167 PKAVRCTHRKVASAGVMLAQRFGLGPDDV---CYVS-MPLFHSNAVMAGWAVALAAGAS--------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 369 ptshMGVPRVWekimeriqevaAQSGFIrrkmllwamsvtleqnltcpgSDLKPFTTRLADYL------VLAK------- 435
Cdd:PRK07867 222 ----IALRRKF-----------SASGFL---------------------PDVRRYGATYANYVgkplsyVLATperpdda 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 436 ---VRQALGfakcqkNfYGAAPMMAETQHFFlglNIRLYAGYGLSETsGPHFMSSPyNYRLYSSGKLVPGcrVKLVNQD- 511
Cdd:PRK07867 266 dnpLRIVYG------N-EGAPGDIARFARRF---GCVVVDGFGSTEG-GVAITRTP-DTPPGALGPLPPG--VAIVDPDt 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 512 -----------------AEGIGEIC-LWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDAGRLDADGFLYITGRLKELiITA 573
Cdd:PRK07867 332 gtecppaedadgrllnaDEAIGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDW-MRV 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 27477105 574 GGENVPPVPIEEAVkMELPIISNAML-------IGDQrKFLSMLLTLKCTLDPD 620
Cdd:PRK07867 410 DGENLGTAPIERIL-LRYPDATEVAVyavpdpvVGDQ-VMAALVLAPGAKFDPD 461
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
74-601 |
1.57e-08 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 57.97 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 74 WDAPEEAL-WTTRADGRVRLRIDPSCPQ---LPYTVHRMFYEALDKY----GDLIALGFKRQD--KWEHISYSQYYLLAR 143
Cdd:cd17634 16 WGEAGKILdWITPYQKVKNTSFAPGAPSikwFEDATLNLAANALDRHlrenGDRTAIIYEGDDtsQSRTISYRELHREVC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 144 RAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM-----------VDT 212
Cdd:cd17634 96 RFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLItadggvragrsVPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 213 QKQLEKILKIwkQLPHLKAVVIYKepppnKMANVYTMEE-----FMELGNEVPEEALDAIIDTQQPnqcCVLVYTSGTTG 287
Cdd:cd17634 176 KKNVDDALNP--NVTSVEHVIVLK-----RTGSDIDWQEgrdlwWRDLIAKASPEHQPEAMNAEDP---LFILYTSGTTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 288 NPKGVMlsQDN------ITWTARYgsqAGDIRPAEVqqevVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAE--PDALKGS 359
Cdd:cd17634 246 KPKGVL--HTTggylvyAATTMKY---VFDYGPGDI----YWCTADVGWVTGHSYLLYGPLACGATTLLYEgvPNWPTPA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 360 LVNTLREVEPTSHMGV-PRVWEKIMeriqevAAQSGFIRRKmllwamSVTLEQNLTCPGSDLKPFTTRLAdylvlakvRQ 438
Cdd:cd17634 317 RMWQVVDKHGVNILYTaPTAIRALM------AAGDDAIEGT------DRSSLRILGSVGEPINPEAYEWY--------WK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 439 ALGFAKCqknfygaaPMMAEtqhfflglnirlyagYGLSETSGphFMSSP----YNYRLYSSGKLVPGCRVKLVnqDAEG 514
Cdd:cd17634 377 KIGKEKC--------PVVDT---------------WWQTETGG--FMITPlpgaIELKAGSATRPVFGVQPAVV--DNEG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 515 -------IGEICL---W-GRTifMGYLNMEDKTCEAIDE--EGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPV 581
Cdd:cd17634 430 hpqpggtEGNLVItdpWpGQT--RTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDD-VINVAGHRLGTA 506
|
570 580
....*....|....*....|
gi 27477105 582 PIEEAVKMElPIISNAMLIG 601
Cdd:cd17634 507 EIESVLVAH-PKVAEAAVVG 525
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
144-638 |
2.44e-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: 57.06 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 144 RAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQkqlekILKIW 223
Cdd:cd05915 36 RLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN-----LLPLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 224 KQLPHLKAVVIYKeppPNKMANVYTMEEFMELGNevPEEALDAIIDTQQPnqcCVLVYTSGTTGNPKGVMLSQDNITWTA 303
Cdd:cd05915 111 EAIRGELKTVQHF---VVMDEKAPEGYLAYEEAL--GEEADPVRVPERAA---CGMAYTTGTTGLPKGVVYSHRALVLHS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 304 RYGSQAGDIRPAEVqqEVVVSYLPLSHIAAQIYdLWTGIQWGAQ-VCFAEPDALKgSLVNTLREVEPTSHMGVPRVWEKI 382
Cdd:cd05915 183 LAASLVDGTALSEK--DVVLPVVPMFHVNAWCL-PYAATLVGAKqVLPGPRLDPA-SLVELFDGEGVTFTAGVPTVWLAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 383 MERIQEVaaqsgfirRKMLLWAMSVTleqnltcPGSDLKPFTTRLADYLVLAKVRQALGFAKCqknfYG---AAPMMAET 459
Cdd:cd05915 259 ADYLEST--------GHRLKTLRRLV-------VGGSAAPRSLIARFERMGVEVRQGYGLTET----SPvvvQNFVKSHL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 460 QHFFLGLNIRLYAGYGLS------ETSGPHFMSSPYnyrlyssgklvpgcrvklvnqDAEGIGEICLWGRTIFMGYLNME 533
Cdd:cd05915 320 ESLSEEEKLTLKAKTGLPiplvrlRVADEEGRPVPK---------------------DGKALGEVQLKGPWITGGYYGNE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 534 DKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIeEAVKMELPIISNAMLIG--DQRKFLSMLL 611
Cdd:cd05915 379 EATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKD-LIKSGGEWISSVDL-ENALMGHPKVKEAAVVAipHPKWQERPLA 456
|
490 500
....*....|....*....|....*..
gi 27477105 612 TLKCTldpdtsdQTDNLTEQAMEFCQR 638
Cdd:cd05915 457 VVVPR-------GEKPTPEELNEHLLK 476
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
252-565 |
3.34e-08 |
|
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: 56.78 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 252 FMELGNEVPEEALDAIID--------TQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAevqqevvV 323
Cdd:cd05918 76 FVPLDPSHPLQRLQEILQdtgakvvlTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSE-------S 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 324 SYLPLSHIA--AQIYDLWTGIQWGAQVCFAEPDALKGSLVNTLREVEPTSHMGVPRVwekimeriqevaaqsgfirrkml 401
Cdd:cd05918 149 RVLQFASYTfdVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPSV----------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 402 lwAMSVTLEQnltCPgsDLKpfttrladYLVLA--KVRQALGFAKCQK----NFYGAA--PMMAETQHFFLGLNIRLyAG 473
Cdd:cd05918 206 --ARLLDPED---VP--SLR--------TLVLGgeALTQSDVDTWADRvrliNAYGPAecTIAATVSPVVPSTDPRN-IG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 474 YGLSETSgphFMSSPYNYrlyssGKLVP-GCrvklvnqdaegIGEICLWGRTIFMGYLNMEDKTCEA-IDEEGWLH---- 547
Cdd:cd05918 270 RPLGATC---WVVDPDNH-----DRLVPiGA-----------VGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegs 330
|
330 340
....*....|....*....|....*.
gi 27477105 548 --------TGDAGRLDADGFLYITGR 565
Cdd:cd05918 331 grgrrlyrTGDLVRYNPDGSLEYVGR 356
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
492-587 |
4.50e-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: 56.55 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 492 RLYSSGKLVPGCRVKLVNQDAE-----GIGEIC------------LWG---RTIfMGYLNMEDktceaideeGWLHTGDA 551
Cdd:cd05967 409 KAGSPGKPVPGYQVQVLDEDGEpvgpnELGNIViklplppgclltLWKndeRFK-KLYLSKFP---------GYYDTGDA 478
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 27477105 552 GRLDADGFLYITGRLKELIITAG-----GEnvppvpIEEAV 587
Cdd:cd05967 479 GYKDEDGYLFIMGRTDDVINVAGhrlstGE------MEESV 513
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
131-600 |
4.61e-08 |
|
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: 56.33 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMv 210
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 dTQKQLEKILKIWKQLPHLKAVVIYKEPPPNkmanvytmeefmeLGNEVPEEALDAIIdtqqpnqccvlvYTSGTTGNPK 290
Cdd:cd17656 91 -TQRHLKSKLSFNKSTILLEDPSISQEDTSN-------------IDYINNSDDLLYII------------YTSGTTGKPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 291 GVMLSQDNITWTARYG-SQAGDIRPAEVQQEVVVSYlplshiaaqiydlwtgiqwgaQVCFAEPDA--LKGSlvnTLREV 367
Cdd:cd17656 145 GVQLEHKNMVNLLHFErEKTNINFSDKVLQFATCSF---------------------DVCYQEIFStlLSGG---TLYII 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 368 EPTSHMGVPRVWEKI-MERIQEVAAQSGFIRrkmllwamsvtleqnltcpgsdlkpfttrladylVLAKVRQALG-FAKC 445
Cdd:cd17656 201 REETKRDVEQLFDLVkRHNIEVVFLPVAFLK----------------------------------FIFSEREFINrFPTC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 446 QKNFYGAAPMMAETQHF---FLGLNIRLYAGYGLSET---SGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAE-----G 514
Cdd:cd17656 247 VKHIITAGEQLVITNEFkemLHEHNVHLHNHYGPSEThvvTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQlqpqgI 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 515 IGEICLWGRTIFMGYLNMEDKTCEAI------DEEGWLHTGDAGRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVK 588
Cdd:cd17656 327 VGELYISGASVARGYLNRQELTAEKFfpdpfdPNERMYRTGDLARYLPDGNIEFLGRADHQ-VKIRGYRIELGEI-EAQL 404
|
490
....*....|..
gi 27477105 589 MELPIISNAMLI 600
Cdd:cd17656 405 LNHPGVSEAVVL 416
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
272-600 |
4.71e-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: 55.94 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 272 QPNQCCVLVYTSGTTGNPKGVMLSQDNIT-----WTARYGSQAGDIRpaevqqevvvsylpLSHIAAQIYDLWTG----- 341
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAhaahaWRREYELDSFPVR--------------LLQMASFSFDVFAGdfars 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 342 IQWGAQ--VCfaePDALK---GSLVNTLREVEPTSHMGVPRVWEKIMERIQevaaqsgfiRRKMLLWAMSVTLEQNLTCP 416
Cdd:cd17650 157 LLNGGTlvIC---PDEVKldpAALYDLILKSRITLMESTPALIRPVMAYVY---------RNGLDLSAMRLLIVGSDGCK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 417 GSDLKPFTTRLADYLVLAkvrqalgfakcqkNFYGAAPMMAETQHFFLGLnirlyagyGLSETSGPHFMSSPY-NYRLY- 494
Cdd:cd17650 225 AQDFKTLAARFGQGMRII-------------NSYGVTEATIDSTYYEEGR--------DPLGDSANVPIGRPLpNTAMYv 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 495 --SSGKLVPgcrvklvnqdAEGIGEICLWGRTIFMGYLNMEDKTCEAIDE------EGWLHTGDAGRLDADGFLYITGRL 566
Cdd:cd17650 284 ldERLQPQP----------VGVAGELYIGGAGVARGYLNRPELTAERFVEnpfapgERMYRTGDLARWRADGNVELLGRV 353
|
330 340 350
....*....|....*....|....*....|....*...
gi 27477105 567 KELIITAGgenvppVPIE----EAVKMELPIISNAMLI 600
Cdd:cd17650 354 DHQVKIRG------FRIElgeiESQLARHPAIDEAVVA 385
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
493-601 |
5.36e-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: 55.80 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 493 LYSSGK-LVPGCRVKLVNQD----AEG-IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRL 566
Cdd:cd05920 307 IHTQGRpMSPDDEIRVVDEEgnpvPPGeEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRI 386
|
90 100 110
....*....|....*....|....*....|....*
gi 27477105 567 KELiITAGGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:cd05920 387 KDQ-INRGGEKIAAEEVENLL-LRHPAVHDAAVVA 419
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
266-600 |
6.42e-08 |
|
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: 55.45 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 266 AIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAA--QIYDLWTGiq 343
Cdd:cd17649 86 GLLLTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTP----GDRELQFASFNFDGAheQLLPPLIC-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 344 wGAQVCFAePDALKGSLVNTLREVEptsHMGV------PRVWEKIMERIQEVAAqsgfiRRKMLLWAMSVTLEQnltcpg 417
Cdd:cd17649 160 -GACVVLR-PDELWASADELAEMVR---ELGVtvldlpPAYLQQLAEEADRTGD-----GRPPSLRLYIFGGEA------ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 418 sdlkpfttrladyLVLAKVRQALGFAKcqknfygaapmmaetqhfflglniRLYAGYGLSET--SGPHFMSSPYNYRLYS 495
Cdd:cd17649 224 -------------LSPELLRRWLKAPV------------------------RLFNAYGPTEAtvTPLVWKCEAGAARAGA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 496 S---GKLVPGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEAI-----DEEG--WLHTGDAGRLDADGFL 560
Cdd:cd17649 267 SmpiGRPLGGRSAYILDADLNpvpvgVTGELYIGGEGLARGYLGRPELTAERFvpdpfGAPGsrLYRTGDLARWRDDGVI 346
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 27477105 561 YITGRLKELiITAGGENVPPVPIEEAVkMELPIISNAMLI 600
Cdd:cd17649 347 EYLGRVDHQ-VKIRGFRIELGEIEAAL-LEHPGVREAAVV 384
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
107-565 |
6.62e-08 |
|
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: 55.67 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 107 RMFYEALDKYGDLIALgfkrQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTG 186
Cdd:cd12117 1 ELFEEQAARTPDAVAV----VYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 187 IYTTSSPEACQYIAYDccANVIMVDTQKQLEKilkiwkQLPHLKAVVIYKEPPPnkmanvytmeefmelgnEVPEEALDA 266
Cdd:cd12117 77 LDPELPAERLAFMLAD--AGAKVLLTDRSLAG------RAGGLEVAVVIDEALD-----------------AGPAGNPAV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 267 IIDtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARyGSQAGDIRPaevqQEVVVSYLPLSHIAAqIYDLWTGIQWGA 346
Cdd:cd12117 132 PVS---PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK-NTNYVTLGP----DDRVLQTSPLAFDAS-TFEIWGALLNGA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 347 QVCFAEPDALKGslvntlreveptshmgvprvwekiMERIQEVAAQSGFirrkMLLWaMSVTLEQNLTcpgsDLKPFTTR 426
Cdd:cd12117 203 RLVLAPKGTLLD------------------------PDALGALIAEEGV----TVLW-LTAALFNQLA----DEDPECFA 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 427 LADYLV-------LAKVRQALgfAKCQKnfygaapmmaetqhfflglnIRLYAGYGLSET---SGPHFMSSPYNYRlySS 496
Cdd:cd12117 250 GLRELLtggevvsPPHVRRVL--AACPG--------------------LRLVNGYGPTENttfTTSHVVTELDEVA--GS 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 497 ---GKLVPGCRVKLVNQD----AEGI-GEICLWGRTIFMGYLNMEDKTCEAIDEEGWL------HTGDAGRLDADGFLYI 562
Cdd:cd12117 306 ipiGRPIANTRVYVLDEDgrpvPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEF 385
|
...
gi 27477105 563 TGR 565
Cdd:cd12117 386 LGR 388
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
497-586 |
6.90e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 55.54 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 497 GKLVPGCRVKLVNQDA------EGIGEICLWGRTIFMGYLNMEdktceAIDEEGWLHTGDAGRLDADGfLYITGRLKELI 570
Cdd:PRK05851 348 GNPIPGMEVRISPGDGaagvagREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGG-LVVCGRAKELI 421
|
90
....*....|....*.
gi 27477105 571 ITAgGENVPPVPIEEA 586
Cdd:PRK05851 422 TVA-GRNIFPTEIERV 436
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
118-603 |
7.04e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 55.80 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 118 DLIALGFKRQD-KW-EHISYSQyyllARRAAKGFLKLGLKQAHSVAILGfNSPEWFFSAVGTVFAGGIVTGIYTTSSPEA 195
Cdd:PRK13388 16 DTIAVRYGDRTwTWrEVLAEAA----ARAAALIALADPDRPLHVGVLLG-NTPEMLFWLAAAALGGYVLVGLNTTRRGAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 196 -CQYIAY-DCcaNVIMVDTQ--KQLEKIlkiwkQLPHLKAVVIYKEPPPNKMAnvytmeefmELGNEVPEEALDAiiDTQ 271
Cdd:PRK13388 91 lAADIRRaDC--QLLVTDAEhrPLLDGL-----DLPGVRVLDVDTPAYAELVA---------AAGALTPHREVDA--MDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 272 qpnqcCVLVYTSGTTGNPKGVMLSQDNITW-----TARYGSQAGDirpaevqqevvVSYL--PLSHIAAqIYDLWT-GIQ 343
Cdd:PRK13388 153 -----FMLIFTSGTTGAPKAVRCSHGRLAFagralTERFGLTRDD-----------VCYVsmPLFHSNA-VMAGWApAVA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 344 WGAQVCfaepdalkgslvntlreveptshmgVPRVWekimeriqevaAQSGF---IRR----------KMLLWAMSvTLE 410
Cdd:PRK13388 216 SGAAVA-------------------------LPAKF-----------SASGFlddVRRygatyfnyvgKPLAYILA-TPE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 411 QnltcPGSDLKPfttrladylvlakVRQALGFAkcqknfygAAPM-MAETQHFFlglNIRLYAGYGLSETSG-------- 481
Cdd:PRK13388 259 R----PDDADNP-------------LRVAFGNE--------ASPRdIAEFSRRF---GCQVEDGYGSSEGAVivvrepgt 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 482 -PHFMSSPY-NYRLYSSGKLVPgCRV-------KLVNQDaEGIGEIC-LWGRTIFMGYLNMEDKTCEAIdEEGWLHTGDA 551
Cdd:PRK13388 311 pPGSIGRGApGVAIYNPETLTE-CAVarfdahgALLNAD-EAIGELVnTAGAGFFEGYYNNPEATAERM-RHGMYWSGDL 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 27477105 552 GRLDADGFLYITGRLKELiITAGGENVPPVPIeEAVKMELPIISNAML-------IGDQ 603
Cdd:PRK13388 388 AYRDADGWIYFAGRTADW-MRVDGENLSAAPI-ERILLRHPAINRVAVyavpderVGDQ 444
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
254-566 |
8.09e-08 |
|
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: 55.38 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 254 ELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEvqQEVVVS--------- 324
Cdd:cd12116 106 LLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGD--RLLAVTtyafdisll 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 325 --YLPLSHiaaqiydlwtgiqwGAQVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWekimeRIqevAAQSGFIRRKm 400
Cdd:cd12116 184 elLLPLLA--------------GARVVIAPRETQRdpEALARLIEAHSITVMQATPATW-----RM---LLDAGWQGRA- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 401 llwamSVTleqnLTCPGSDLKPfttRLADYLvLAKVRQALgfakcqkNFYG---------AAPMMAETQHFFLGLNIrly 471
Cdd:cd12116 241 -----GLT----ALCGGEALPP---DLAARL-LSRVGSLW-------NLYGptettiwstAARVTAAAGPIPIGRPL--- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 472 agyglsetsgphfmsspYNYRLY---SSGKLVPgcrvklvnqdaEG-IGEICLWGRTIFMGYLNMEDKTCEAI-----DE 542
Cdd:cd12116 298 -----------------ANTQVYvldAALRPVP-----------PGvPGELYIGGDGVAQGYLGRPALTAERFvpdpfAG 349
|
330 340
....*....|....*....|....*.
gi 27477105 543 EG--WLHTGDAGRLDADGFLYITGRL 566
Cdd:cd12116 350 PGsrLYRTGDLVRRRADGRLEYLGRA 375
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
281-601 |
1.02e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 55.42 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 281 YTSGTTGNPKGVMLSQ-DNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGiqwGAQVCFAEPDALKGS 359
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHaDPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATG---GSAVINSAPVTPEAA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 360 LVNTLReVEPTSHMGVPRVWEKIMEriqevaaqsgfirrkmllwAMSVTLEQNLTCPGSDLKPFTTRLADYLVlakvrqa 439
Cdd:PRK06060 229 AILSAR-FGPSVLYGVPNFFARVID-------------------SCSPDSFRSLRCVVSAGEALELGLAERLM------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 440 lgfakcqkNFYGAAPMMAetqhfflglnirlyaGYGLSETsGPHFMSSPYN-YRLYSSGKLVPGCRVKLVNQDAEGIG-- 516
Cdd:PRK06060 282 --------EFFGGIPILD---------------GIGSTEV-GQTFVSNRVDeWRLGTLGRVLPPYEIRVVAPDGTTAGpg 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 517 -EICLW--GRTIFMGYLNMEDKTCEaidEEGWLHTGDAGRLDADGFLYITGRLKELIITaGGENVPPVPIEEAVkMELPI 593
Cdd:PRK06060 338 vEGDLWvrGPAIAKGYWNRPDSPVA---NEGWLDTRDRVCIDSDGWVTYRCRADDTEVI-GGVNVDPREVERLI-IEDEA 412
|
....*...
gi 27477105 594 ISNAMLIG 601
Cdd:PRK06060 413 VAEAAVVA 420
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
279-565 |
1.12e-07 |
|
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: 55.04 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 279 LVYTSGTTGNPKGVMLSQDNIT----WTARYGSQAGDIRpaevqqevVVSYLPLSHIAAQiYDLWTGIQWGAQVCFAEPD 354
Cdd:cd17651 141 VIYTSGSTGRPKGVVMPHRSLAnlvaWQARASSLGPGAR--------TLQFAGLGFDVSV-QEIFSTLCAGATLVLPPEE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 355 ALkgslvntlreveptshMGVPRVWEKIME-RIQEVAAQSGFIRRkmllWAmsvtleqnltcpgSDLKPFTTRLADylvL 433
Cdd:cd17651 212 VR----------------TDPPALAAWLDEqRISRVFLPTVALRA----LA-------------EHGRPLGVRLAA---L 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 434 AKVRQAlgfakcqknfyG-AAPMMAETQHFFLGL-NIRLYAGYGLSETsgpHFMSS------PYNYRLYSS-GKLVPGCR 504
Cdd:cd17651 256 RYLLTG-----------GeQLVLTEDLREFCAGLpGLRLHNHYGPTET---HVVTAlslpgdPAAWPAPPPiGRPIDNTR 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477105 505 VKLVNQDAE----GI-GEICLWGRTIFMGYLNMEDKTCEAIDEEGWL------HTGDAGRLDADGFLYITGR 565
Cdd:cd17651 322 VYVLDAALRpvppGVpGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGR 393
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
278-601 |
1.63e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 54.45 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 278 VLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVqqevvvsylplshiaaqiydLWtgiqwgaqvCFAEPD--- 354
Cdd:cd05973 92 VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS--------------------FW---------NAADPGway 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 355 ----ALKGSLVNTLREVEPTSHMGVPRVWeKIMER--IQEVAAQSGFIRrkmLLWAMSVTLEQNLTcpgsdlkpfttrla 428
Cdd:cd05973 143 glyyAITGPLALGHPTILLEGGFSVESTW-RVIERlgVTNLAGSPTAYR---LLMAAGAEVPARPK-------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 429 dyLVLAKVRQAlgfakcqknfygAAPMMAETQHFF---LGLNIRLYagYGLSETSGP----HFMSSPYnyRLYSSGKLVP 501
Cdd:cd05973 205 --GRLRRVSSA------------GEPLTPEVIRWFdaaLGVPIHDH--YGQTELGMVlanhHALEHPV--HAGSAGRAMP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 502 GCRVKLVNQDAEGIGE-------------ICLWgrtiFMGYLNMEDKTCEAideeGWLHTGDAGRLDADGFLYITGRLKE 568
Cdd:cd05973 267 GWRVAVLDDDGDELGPgepgrlaidiansPLMW----FRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADD 338
|
330 340 350
....*....|....*....|....*....|...
gi 27477105 569 LIITAgGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:cd05973 339 VITMS-GYRIGPFDVESAL-IEHPAVAEAAVIG 369
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
465-600 |
4.54e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 52.96 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 465 GLNIRlyAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI--GEICL-WGRT----IFMGYLNMEDKTC 537
Cdd:cd05974 225 GLTIR--DGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPAteGEVALdLGDTrpvgLMKGYAGDPDKTA 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477105 538 EAIdEEGWLHTGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEEAVkMELPIISNAMLI 600
Cdd:cd05974 303 HAM-RGGYYRTGDIAMRDEDGYLTYVGRADD-VFKSSDYRISPFELESVL-IEHPAVAEAAVV 362
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
131-566 |
9.26e-07 |
|
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: 51.89 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 210
Cdd:cd12114 11 GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 DTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKmanvytmeefmelgnevpeealdaiidtQQPNQCCVLVYTSGTTGNPK 290
Cdd:cd12114 91 DGPDAQLDVAVFDVLILDLDALAAPAPPPPVD----------------------------VAPDDLAYVIFTSGSTGTPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 291 GVMLSQDN-----ITWTARYGSQAGDirpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGAQVCFAEPDalkgslvntlR 365
Cdd:cd12114 143 GVMISHRAalntiLDINRRFAVGPDD---------RVLALSSLSFDLS-VYDIFGALSAGATLVLPDEA----------R 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 366 EVEPTShmgvprvWEKIMERIQ-----EVAAQSgfirrKMLLWAmsvtLEQNLTCPGSdlkpftTRLA----DYLVL--- 433
Cdd:cd12114 203 RRDPAH-------WAELIERHGvtlwnSVPALL-----EMLLDV----LEAAQALLPS------LRLVllsgDWIPLdlp 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 434 AKVRQALgfakcqknfygaapmmAETQHFFLGlnirlyagyGLSETS-----------GPHFMSSPYnyrlyssGKLVPG 502
Cdd:cd12114 261 ARLRALA----------------PDARLISLG---------GATEASiwsiyhpidevPPDWRSIPY-------GRPLAN 308
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477105 503 CRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEA----IDEEGWLHTGDAGRLDADGFLYITGRL 566
Cdd:cd12114 309 QRYRVLDPRGRdcpdwVPGELWIGGRGVALGYLGDPELTAARfvthPDGERLYRTGDLGRYRPDGTLEFLGRR 381
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-311 |
1.04e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.65 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 72 AQWDAPEEALwttradgrvrlridPSCPQlpytVHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLK 151
Cdd:PRK12316 1990 ADWDRTPEAY--------------PRGPG----VHQRIAEQAARAPEAIAVVFGDQ----HLSYAELDSRANRLAHRLRA 2047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 152 LGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMvdTQKQLEKILkiwkqlphlka 231
Cdd:PRK12316 2048 RGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL--TQRHLLERL----------- 2114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 232 vviykePPPNKMAN--VYTMEEFMELGNEVPEEALDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQ----DNITWT-AR 304
Cdd:PRK12316 2115 ------PLPAGVARlpLDRDAEWADYPDTAPAVQLA-------GENLAYVIYTSGSTGLPKGVAVSHgalvAHCQAAgER 2181
|
....*..
gi 27477105 305 YGSQAGD 311
Cdd:PRK12316 2182 YELSPAD 2188
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
515-579 |
1.47e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 51.65 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 515 IGEICLWGRTIFMGYLNMEDKTCEA--------IDE---EG------WLHTGDAGRLdADGFLYITGRLKELIITAGGEN 577
Cdd:PRK07769 418 IGEIWLHGNNIGTGYWGKPEETAATfqnilksrLSEshaEGapddalWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNH 496
|
..
gi 27477105 578 VP 579
Cdd:PRK07769 497 YP 498
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
254-575 |
1.60e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 51.31 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 254 ELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQqevvVSYLPLSHIAA 333
Cdd:cd05910 65 NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVD----LATFPLFALFG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 334 QIYDLWTGIQWGAQVCFAEPDALKgsLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRkmllwamsvtleqnL 413
Cdd:cd05910 141 PALGLTSVIPDMDPTRPARADPQK--LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRR--------------V 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 414 TCPGSDLKPFttrladylVLAKVRQALGFAKCQKNFYGAapmmaeTQhfflGLNIRLYAGYGLSETSGPhfmsSPYNYRL 493
Cdd:cd05910 205 LSAGAPVPIA--------LAARLRKMLSDEAEILTPYGA------TE----ALPVSSIGSRELLATTTA----ATSGGAG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 494 YSSGKLVPGCRVKLVNQDAE--------------GIGEICLWGRTIFMGYLNMEDKTCEA-IDEEG---WLHTGDAGRLD 555
Cdd:cd05910 263 TCVGRPIPGVRVRIIEIDDEpiaewddtlelprgEIGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDLGYLD 342
|
330 340
....*....|....*....|
gi 27477105 556 ADGFLYITGRLKELIITAGG 575
Cdd:cd05910 343 DEGRLWFCGRKAHRVITTGG 362
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-566 |
1.82e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.88 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 105 VHRMFYEALDKYGDLIALGFKRQdkweHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIV 184
Cdd:PRK12316 3059 VHRLFEEQVERTPDAVALAFGEQ----RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAY 3134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 185 TGIYTTSSPEACQYIAYDCCANVIMvdTQKQLekilkiwkQLPHLKAV-VIYKEPPPNkmanvytmeefmELGNEVPEEA 263
Cdd:PRK12316 3135 VPLDPEYPEERLAYMLEDSGAQLLL--SQSHL--------RLPLAQGVqVLDLDRGDE------------NYAEANPAIR 3192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 264 LDaiidtqqPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIrpaeVQQEVVVSYLPLSHIAAqIYDLWTGIQ 343
Cdd:PRK12316 3193 TM-------PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGL----GVGDRVLQFTTFSFDVF-VEELFWPLM 3260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 344 WGAQVCFAEPDalKGSLVNTLREVEPTSHMGVPR-VWEKIMERIQEVAAQSGFIRRKMLlwamsvtleqnltCPGSDLKP 422
Cdd:PRK12316 3261 SGARVVLAGPE--DWRDPALLVELINSEGVDVLHaYPSMLQAFLEEEDAHRCTSLKRIV-------------CGGEALPA 3325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 423 fttrladylvlaKVRQALGFAKCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSetsgphfMSSPYNYRLYSSGKLVPg 502
Cdd:PRK12316 3326 ------------DLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRP-------IANRACYILDGSLEPVP- 3385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 503 crvklvnqdAEGIGEICLWGRTIFMGYLNMEDKTCEAI------DEEGWLHTGDAGRLDADGFLYITGRL 566
Cdd:PRK12316 3386 ---------VGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvPGERLYRTGDLARYRADGVIEYIGRV 3446
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
514-594 |
2.14e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 50.90 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 514 GIGEICLWGRTIFMGYLNMEDKT------------------CEAIDEEGWLHTGDAGrLDADGFLYITGRLKELIITaGG 575
Cdd:PRK12476 428 EVGEIWLHGDNIGRGYWGRPEETertfgaklqsrlaegshaDGAADDGTWLRTGDLG-VYLDGELYITGRIADLIVI-DG 505
|
90
....*....|....*....
gi 27477105 576 ENVPPVPIEEAVKMELPII 594
Cdd:PRK12476 506 RNHYPQDIEATVAEASPMV 524
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
131-348 |
2.64e-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: 50.75 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLK-LGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYiAYDCC-ANVI 208
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLH-CFRCCgAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 209 MVDT--QKQLEKILkiwkqlPHLKA--VVIY---KEPPPNKMANVytMEEFMELGNEVPEEALDAIIDTQQPnqcCVLVY 281
Cdd:cd05938 83 VVAPelQEAVEEVL------PALRAdgVSVWylsHTSNTEGVISL--LDKVDAASDEPVPASLRAHVTIKSP---ALYIY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27477105 282 TSGTTGNPKGVMLSQDNItWTARYGSQAGDIRpaevQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 348
Cdd:cd05938 152 TSGTTGLPKAARISHLRV-LQCSGFLSLCGVT----ADDVIYITLPLYHSSGFLLGIGGCIELGATC 213
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
131-348 |
4.90e-06 |
|
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: 49.66 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 131 EHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMV 210
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 211 DTqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeealdaiidtqqpnqcCVLVYTSGTTGNPK 290
Cdd:cd05940 82 DA----------------------------------------------------------------ALYIYTSGTTGLPK 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27477105 291 GVMLSQDNItWTARYGSQAGDIRpaeVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQV 348
Cdd:cd05940 98 AAIISHRRA-WRGGAFFAGSGGA---LPSDVLYTCLPLYHSTALIVGWSACLASGATL 151
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
470-601 |
8.68e-06 |
|
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: 49.00 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 470 LYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGI-----GEICLWGR-----TIFMGYLNMEDKTCEA 539
Cdd:cd05928 319 IYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLppgteGDIGIRVKpirpfGLFSGYVDNPEKTAAT 398
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27477105 540 IDEEGWLhTGDAGRLDADGFLYITGRLKELIITAgGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:cd05928 399 IRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSS-GYRIGPFEVESAL-IEHPAVVESAVVS 457
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
106-620 |
1.31e-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: 48.32 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 106 HRMFYEALDKYGDLIALGFKRQdKWehiSYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVT 185
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQ-SL---TYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 186 GIYTTSSPEACQYIAYDCCANVIMvdtqkqlekilkiwkqlphlkavviykepppnkmanvytmeefmelgnevpeeald 265
Cdd:cd17645 77 PIDPDYPGERIAYMLADSSAKILL-------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 266 aiidtQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEvQQEVVVSYlplsHIAAQIYDLWTGIQWG 345
Cdd:cd17645 101 -----TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPAD-KSLVYASF----SFDASAWEIFPHLTAG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 346 AQVCFAePDALKGSLVNTLREVEpTSHMGVPRVWEKIMERIQEVAAQSgfirrkmllwamsvtLEQNLTcPGSDLKPFtt 425
Cdd:cd17645 171 AALHVV-PSERRLDLDALNDYFN-QEGITISFLPTGAAEQFMQLDNQS---------------LRVLLT-GGDKLKKI-- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 426 rladylvlakvrqalgfakcQKNFYgaapmmaetqhfflglniRLYAGYGLSE-----TSGPhfMSSPYNYrlYSSGKLV 500
Cdd:cd17645 231 --------------------ERKGY------------------KLVNNYGPTEntvvaTSFE--IDKPYAN--IPIGKPI 268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 501 PGCRVKLVNQD----AEGI-GEICLWGRTIFMGYLNMEDKTCEA------IDEEGWLHTGDAGRLDADGFLYITGRLKEL 569
Cdd:cd17645 269 DNTRVYILDEAlqlqPIGVaGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ 348
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 27477105 570 iITAGGENVPPVPIEEAVkMELPIISNAMLI----GDQRKFLSMLLTLKCTLDPD 620
Cdd:cd17645 349 -VKIRGYRIEPGEIEPFL-MNHPLIELAAVLakedADGRKYLVAYVTAPEEIPHE 401
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
252-566 |
1.53e-05 |
|
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: 48.20 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 252 FMELGNEVPEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQD---NITWTARygSQAGDIRPAEVQQEV 321
Cdd:cd17644 77 YVPLDPNYPQERLTYILeDAQisvlltQPENLAYVIYTSGSTGKPKGVMIEHQslvNLSHGLI--KEYGITSSDRVLQFA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 322 VVSYlplSHIAAQIYDLWtgiqwgaqvcfaepdaLKG-SLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQsgfirrkM 400
Cdd:cd17644 155 SIAF---DVAAEEIYVTL----------------LSGaTLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAY-------W 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 401 LLWAMSVTLEqnlTCPGsdlkPFTTRLAdylvlakvrqALGFAKCQknfygaaPMMAETQHFFLGLNIRLYAGYGLSE-- 478
Cdd:cd17644 209 HLLVLELLLS---TIDL----PSSLRLV----------IVGGEAVQ-------PELVRQWQKNVGNFIQLINVYGPTEat 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 479 -TSGPHFMSSPYNYRLYSS--GKLVPGCRVKLVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCE-------AIDEE 543
Cdd:cd17644 265 iAATVCRLTQLTERNITSVpiGRPIANTQVYILDENLQPVpvgvpGELHIGGVGLARGYLNRPELTAEkfishpfNSSES 344
|
330 340
....*....|....*....|....
gi 27477105 544 GWLH-TGDAGRLDADGFLYITGRL 566
Cdd:cd17644 345 ERLYkTGDLARYLPDGNIEYLGRI 368
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
272-566 |
1.79e-05 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 48.04 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 272 QPNQCCVLVYTSGTTGNPKGVMLSQDNI-----TWTARYGSQAGDirpaevqqeVVVSYLPLSHIAAqIYDLWTGIQWGA 346
Cdd:cd17646 136 RPDNLAYVIYTSGSTGRPKGVMVTHAGIvnrllWMQDEYPLGPGD---------RVLQKTPLSFDVS-VWELFWPLVAGA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 347 QVCFAEPDALK--GSLVNTLREVEPTSHMGVPRVWEkimERIQEVAAQSGfirrkmllwamsVTLEQnLTCPGSDLKPft 424
Cdd:cd17646 206 RLVVARPGGHRdpAYLAALIREHGVTTCHFVPSMLR---VFLAEPAAGSC------------ASLRR-VFCSGEALPP-- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 425 tRLADylvlakvrqalgfakcqknfygaapmmaetqHFFLGLNIRLYAGYGLSETS--GPHFMSSPYNYRLYSS-GKLVP 501
Cdd:cd17646 268 -ELAA-------------------------------RFLALPGAELHNLYGPTEAAidVTHWPVRGPAETPSVPiGRPVP 315
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27477105 502 GCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAI-----DEEGWLH-TGDAGRLDADGFLYITGRL 566
Cdd:cd17646 316 NTRLYVL--DDALrpvpvgvPGELYLGGVQLARGYLGRPALTAERFvpdpfGPGSRMYrTGDLARWRPDGALEFLGRS 391
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
207-601 |
3.13e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 47.08 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 207 VIMVDtQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMA-------NVYTMEEFMElGN-------EVPEEALDAIidtqq 272
Cdd:PRK05620 114 VIVAD-PRLAEQLGEILKECPCVRAVVFIGPSDADSAAahmpegiKVYSYEALLD-GRstvydwpELDETTAAAI----- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 273 pnqcCvlvYTSGTTGNPKGVMLSQDNItWTARYGSQAGD---IRPAEvqqevvvSYL---PLSHIAAqiydlW----TGI 342
Cdd:PRK05620 187 ----C---YSTGTTGAPKGVVYSHRSL-YLQSLSLRTTDslaVTHGE-------SFLccvPIYHVLS-----WgvplAAF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 343 QWGAQVCFAEPDALKGSLVNTLREVEPTSHMGVPRVWEKIMeriqevaaqSGFIR---RKMLLwamsvtleQNLTCPGSD 419
Cdd:PRK05620 247 MSGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLM---------VHYLKnppERMSL--------QEIYVGGSA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 420 LKPfttrladylVLAKVRQALgfakcqknfYGaapmmaetqhfflglnIRLYAGYGLSETSGPHFMSSP---------YN 490
Cdd:PRK05620 310 VPP---------ILIKAWEER---------YG----------------VDVVHVWGMTETSPVGTVARPpsgvsgearWA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 491 YRlYSSGKLVPGCRVKLVNqDAEGI-------GEICLWGRTIFMGYLNME----------------DKTCEAIDEEGWLH 547
Cdd:PRK05620 356 YR-VSQGRFPASLEYRIVN-DGQVMestdrneGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLR 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 27477105 548 TGDAGRLDADGFLYITGRLKElIITAGGENVPPVPIEEAVkMELPIISNAMLIG 601
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARD-VIRSGGEWIYSAQLENYI-MAAPEVVECAVIG 485
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
501-566 |
9.87e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 45.66 E-value: 9.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27477105 501 PGCRVKLVNQDAE-----GIGEICLWGRTIFMGYLNMEDKTCEA---IDEEGWLHTGDAGRLDaDGFLYITGRL 566
Cdd:PRK04813 325 PDSPLLIIDEEGTklpdgEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGYLE-DGLLFYQGRI 397
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
260-628 |
9.95e-05 |
|
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: 45.39 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 260 PEEALDAIIDTQQ-------PNQCCVLVYTSGTTGNPKGVMLSQDN----ITWtarygsqAGDIRPAEVQQEVVVSY--- 325
Cdd:cd12115 84 PPERLRFILEDAQarlvltdPDDLAYVIYTSGSTGRPKGVAIEHRNaaafLQW-------AAAAFSAEELAGVLASTsic 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 326 LPLShiaaqIYDLWTGIQWGAQVCFAE--------PDALKGSLVNTlreveptshmgVPRVwekimerIQEVAAQSGFIR 397
Cdd:cd12115 157 FDLS-----VFELFGPLATGGKVVLADnvlalpdlPAAAEVTLINT-----------VPSA-------AAELLRHDALPA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 398 rkmllwAMSVTleqNLTcpGsdlKPFTTRLADYLvlakvrqalgfakcqknfYGAAPMmaetqhfflglnIRLYAGYGLS 477
Cdd:cd12115 214 ------SVRVV---NLA--G---EPLPRDLVQRL------------------YARLQV------------ERVVNLYGPS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 478 ET---SGPHFMsSPYNYRLYSSGKLVPGCRVKLVnqDAEG-------IGEICLWGRTIFMGYLNMEDKTCEAIDEEGWL- 546
Cdd:cd12115 250 EDttySTVAPV-PPGASGEVSIGRPLANTQAYVL--DRALqpvplgvPGELYIGGAGVARGYLGRPGLTAERFLPDPFGp 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 547 -----HTGDAGRLDADGFLYITGRLKELIITAGgenvppVPIE----EAVKMELPIISNA--MLIGDQ--RKFLSMLLTL 613
Cdd:cd12115 327 garlyRTGDLVRWRPDGLLEFLGRADNQVKVRG------FRIElgeiEAALRSIPGVREAvvVAIGDAagERRLVAYIVA 400
|
410
....*....|....*
gi 27477105 614 KCTLDPDTSDQTDNL 628
Cdd:cd12115 401 EPGAAGLVEDLRRHL 415
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
260-300 |
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 27477105 260 PEEALDAII-DTQ------QPNQCCVLVYTSGTTGNPKGVMLSQDNIT 300
Cdd:cd17643 72 PVERIAFILaDSGpsllltDPDDLAYVIYTSGSTGRPKGVVVSHANVL 119
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
268-578 |
1.38e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 45.19 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 268 IDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDirPAEvqQEVVVSYLPLSHiaaqiydlwtgiQWGAQ 347
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS--PKE--DDVMMSFLPPFH------------AYGFN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 348 VCfaepdalkgSLVNTLreveptshMGVPRVW-------EKIMERIQEVAAqsgfirrkmllwamsvtleqnlTCPGSdl 420
Cdd:PRK06334 241 SC---------TLFPLL--------SGVPVVFaynplypKKIVEMIDEAKV----------------------TFLGS-- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 421 kpfTTRLADYLVLAKVRQ-----ALGFAKCQKNFYGAApMMAETQHFFLglNIRLYAGYGLSETSgP----HFMSSPYNY 491
Cdd:PRK06334 280 ---TPVFFDYILKTAKKQesclpSLRFVVIGGDAFKDS-LYQEALKTFP--HIQLRQGYGTTECS-PvitiNTVNSPKHE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 492 RLYssGKLVPGCRVKLVNQDAEG------IGEICLWGRTIFMGYLNmEDKTCEAI--DEEGWLHTGDAGRLDADGFLYIT 563
Cdd:PRK06334 353 SCV--GMPIRGMDVLIVSEETKVpvssgeTGLVLTRGTSLFSGYLG-EDFGQGFVelGGETWYVTGDLGYVDRHGELFLK 429
|
330
....*....|....*
gi 27477105 564 GRLKELiITAGGENV 578
Cdd:PRK06334 430 GRLSRF-VKIGAEMV 443
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
133-291 |
1.48e-04 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 45.17 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 133 ISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIM--- 209
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALItad 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 210 --------VDTQKQLEKILKiwkQLPHLKAVVIY---KEPPPNKMANVYTMEEFMElgnevpeeALDAIIDTQQPNQCCV 278
Cdd:cd05968 172 gftrrgreVNLKEEADKACA---QCPTVEKVVVVrhlGNDFTPAKGRDLSYDEEKE--------TAGDGAERTESEDPLM 240
|
170
....*....|...
gi 27477105 279 LVYTSGTTGNPKG 291
Cdd:cd05968 241 IIYTSGTTGKPKG 253
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
515-588 |
1.58e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 44.93 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 515 IGEICLWGRTIFMGYLNMEDKT-----------CEAIDEEGWLHTGDAGRLDaDGFLYITGRLKELIITAgGENVPPVPI 583
Cdd:PRK05850 397 VGEIWVHGDNVAAGYWQKPEETertfgatlvdpSPGTPEGPWLRTGDLGFIS-EGELFIVGRIKDLLIVD-GRNHYPDDI 474
|
....*
gi 27477105 584 EEAVK 588
Cdd:PRK05850 475 EATIQ 479
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-566 |
1.94e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.95 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 105 VHRMFYEALDKYGDLIALGFKRQDkwehISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIV 184
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALAFGEET----LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 185 TGIYTTSSPEACQYIAYDCCANVIMvdTQKQLEKILKIWKQLphlkAVVIYKEPPPnkmanvytmeEFMELGNEVPEEAL 264
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGVQLLL--SQSHLGRKLPLAAGV----QVLDLDRPAA----------WLEGYSEENPGTEL 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 265 DaiidtqqPNQCCVLVYTSGTTGNPKGVMLS----QDNITWT-ARYGSQAGDirpaEVQQEVVVSYlplshiAAQIYDLW 339
Cdd:PRK12316 653 N-------PENLAYVIYTSGSTGKPKGAGNRhralSNRLCWMqQAYGLGVGD----TVLQKTPFSF------DVSVWEFF 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 340 TGIQWGAQVCFAEPDALK--GSLVNTL-REVEPTSHMgVPRVWEKImerIQEVAAQsgfirrkmllwamSVTLEQNLTCP 416
Cdd:PRK12316 716 WPLMSGARLVVAAPGDHRdpAKLVELInREGVDTLHF-VPSMLQAF---LQDEDVA-------------SCTSLRRIVCS 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 417 GSDLKpfttrladylvlakvrqalgfAKCQKNFYGAAPmmaetqhfflglNIRLYAGYGLSETS--GPHFMSSPYNYRLY 494
Cdd:PRK12316 779 GEALP---------------------ADAQEQVFAKLP------------QAGLYNLYGPTEAAidVTHWTCVEEGGDSV 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 495 SSGKLVPGCRVKLVNQDAEGI-----GEICLWGRTIFMGYLNMEDKTCEA------IDEEGWLHTGDAGRLDADGFLYIT 563
Cdd:PRK12316 826 PIGRPIANLACYILDANLEPVpvgvlGELYLAGRGLARGYHGRPGLTAERfvpspfVAGERMYRTGDLARYRADGVIEYA 905
|
...
gi 27477105 564 GRL 566
Cdd:PRK12316 906 GRI 908
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
260-356 |
2.29e-04 |
|
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: 44.17 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 260 PEEALDAIIDTQQPnqCCVL---------VYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAevqqEVVVSYLPLSH 330
Cdd:cd17652 72 PAERIAYMLADARP--ALLLttpdnlayvIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPG----SRVLQFASPSF 145
|
90 100
....*....|....*....|....*.
gi 27477105 331 IAAqIYDLWTGIQWGAQVCFAEPDAL 356
Cdd:cd17652 146 DAS-VWELLMALLAGATLVLAPAEEL 170
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
497-575 |
2.82e-04 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 44.12 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 497 GKLVPGCRVKLVNQDAE--------------GIGEICLWGRTIFMGYLNMEDKTCEA--IDEEG--WLHTGDAGRLDADG 558
Cdd:PRK09274 355 GRPVDGVEVRIIAISDApipewddalrlatgEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQG 434
|
90
....*....|....*..
gi 27477105 559 FLYITGRLKELIITAGG 575
Cdd:PRK09274 435 RLWFCGRKAHRVETAGG 451
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
262-348 |
3.49e-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: 43.57 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 262 EALDAIIDTQQPNQCCV-------LVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPaevqQEVVVSYLPLSHIAAQ 334
Cdd:cd05939 85 DPLLTQSSTEPPSQDDVnfrdklfYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRP----EDVVYDCLPLYHSAGG 160
|
90
....*....|....
gi 27477105 335 IYDLWTGIQWGAQV 348
Cdd:cd05939 161 IMGVGQALLHGSTV 174
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
280-298 |
6.35e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 42.96 E-value: 6.35e-04
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
272-355 |
9.76e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 42.72 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 272 QPNQCCVLVYTSGTTGNPKGVMLSQDNIT----WT-ARYGSQAGDI----RPAEVQQEVVVSYLPLshIAaqiydlwtgi 342
Cdd:PRK10252 596 QPHHTAYIIFTSGSTGRPKGVMVGQTAIVnrllWMqNHYPLTADDVvlqkTPCSFDVSVWEFFWPF--IA---------- 663
|
90
....*....|...
gi 27477105 343 qwGAQVCFAEPDA 355
Cdd:PRK10252 664 --GAKLVMAEPEA 674
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
279-330 |
1.50e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 41.85 E-value: 1.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 27477105 279 LVYTSGTTGNPKGVMLSQDNITWT-----ARYGSQAGDIRPAEVqqeVVVSYLPLSH 330
Cdd:PRK05850 165 LQYTSGSTRTPAGVMVSHRNVIANfeqlmSDYFGDTGGVPPPDT---TVVSWLPFYH 218
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
110-317 |
1.50e-03 |
|
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: 41.78 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 110 YEALD----KYGDLIALGFKRQD--KWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEwffsAVGTVFA--- 180
Cdd:cd05966 56 YNCLDrhlkERGDKVAIIWEGDEpdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPE----LVIAMLAcar 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27477105 181 -GGIVTGIYTTSSPEA-CQYIAyDC-CANVIMVDTQKQLEKIL-------KIWKQLPHLKAVVIYKepppnKMANVYTME 250
Cdd:cd05966 132 iGAVHSVVFAGFSAESlADRIN-DAqCKLVITADGGYRGGKVIplkeivdEALEKCPSVEKVLVVK-----RTGGEVPMT 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27477105 251 E-----FMELGNEVPEEALDAIIDTQQPnqcCVLVYTSGTTGNPKGVMLSQ-DNITWTARYGSQAGDIRPAEV 317
Cdd:cd05966 206 EgrdlwWHDLMAKQSPECEPEWMDSEDP---LFILYTSGSTGKPKGVVHTTgGYLLYAATTFKYVFDYHPDDI 275
|
|
| |
