|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
69-665 |
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: 1046.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 69 NGKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSH 148
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 149 AQIVVVDDAKQMDKIHAIRDKLPKLKAAIQIQEPYSPylkKEDGYYRWSEIESMNVSDVEDQYMTRLENVAINECCCLVY 228
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAIIQYKEPLKE---KEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 229 TSGTVGMPKGVMLSHDNITFDVRGIVKAMDRV--VVGAESIVSYLPLSHVAAQTVDIYTCAFVAGCIWFADKDALKGTLV 306
Cdd:cd05933 158 TSGTTGMPKGVMLSHDNITWTAKAASQHMDLRpaTVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 307 KSLQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLASWAKGITLKHYMVSQGKSSGGFR-YKIAKSLIMSKVKQAL 385
Cdd:cd05933 238 KTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLfYRLAKKLVFKKVRKAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 386 GFDRVLTLASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKDANGHGELCI 465
Cdd:cd05933 318 GLDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 466 RGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPPVHIENTIKKELDAISNAFLV 545
Cdd:cd05933 398 WGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 546 GEQRKYLTVLITLKTEVDKDSGEPLDELSHESSVWVKSLGvEHKTVSDILAAGPCPKVWKSIEDAIKRANKQSISNAQKV 625
Cdd:cd05933 478 GDKRKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLG-SQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKI 556
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 17933690 626 QKFTILPHDFSIPTGELGPTLKVKRNVVSKMYADEIEKLY 665
Cdd:cd05933 557 QKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
47-666 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 535.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 47 SVPGLLKRTVNNYGDYPALRTKNGKnGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARG 126
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREKEDG-IWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 127 IIAGIYTTNSADAVQHVLESSHAQIVVVDDAKQMDKIHAIRDKLPKLKAAIQIQEPYspyLKKEDGYYRWSEIESM--NV 204
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRG---LRDDPRLLSLDELLALgrEV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 205 SDvEDQYMTRLENVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHVAAQTVDIY 284
Cdd:COG1022 168 AD-PAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP--LGPGDRTLSFLPLAHVFERTVSYY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 285 tcAFVAGC-IWFADKDAlkgTLVKSLQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLASWAKGITLKHYM-VSQG 362
Cdd:COG1022 245 --ALAAGAtVAFAESPD---TLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARaRLAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 363 KSSGG---FRYKIAKSLIMSKVKQALGfDRVLTLASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLN 439
Cdd:COG1022 320 KSPSLllrLKHALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 440 TIGKTLPGCESKfINKDanghGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAG 519
Cdd:COG1022 399 TVGPPLPGVEVK-IAED----GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 520 GENIPPVHIENTIkKELDAISNAFLVGEQRKYLTVLITLKtevdkdsgepLDELSHessvWVKSLGVEHKTVSDILAAgp 599
Cdd:COG1022 474 GKNVAPQPIENAL-KASPLIEQAVVVGDGRPFLAALIVPD----------FEALGE----WAEENGLPYTSYAELAQD-- 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17933690 600 cPKVWKSIEDAIKRANKQsISNAQKVQKFTILPHDFSIPTGELGPTLKVKRNVVSKMYADEIEKLYA 666
Cdd:COG1022 537 -PEVRALIQEEVDRANAG-LSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
73-653 |
3.39e-131 |
|
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: 393.88 E-value: 3.39e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 73 GYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIV 152
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 153 VVDDAkqmdkihairdklpklkaaiqiqepyspylkkedgyyrwseiesmnvsdvedqymtrlenvaiNECCCLVYTSGT 232
Cdd:cd05907 82 FVEDP---------------------------------------------------------------DDLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 233 VGMPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHVAAQTVDIYTCaFVAG-CIWFADKDAlkgTLVKSLQD 311
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALAERLP--ATEGDRHLSFLPLAHVFERRAGLYVP-LLAGaRIYFASSAE---TLLDDLSE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 312 ARPTRFMGVPRVYEKFQERMVAVASSSgsLKKMLASWAKGitlkhymvsqgkssggfrykiakslimskvkqalgfDRVL 391
Cdd:cd05907 173 VRPTVFLAVPRVWEKVYAAIKVKAVPG--LKRKLFDLAVG------------------------------------GRLR 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 392 TLASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKfINKDanghGELCIRGRHVF 471
Cdd:cd05907 215 FAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVR-IADD----GEILVRGPNVM 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 472 MGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPPVHIENTIKKELdAISNAFLVGEQRKY 551
Cdd:cd05907 290 LGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASP-LISQAVVIGDGRPF 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 552 LTVLITLktevDKDSGEPldelshessvWVKSLGVEHKTVSDILAAgpcPKVWKSIEDAIKRANKQSiSNAQKVQKFTIL 631
Cdd:cd05907 369 LVALIVP----DPEALEA----------WAEEHGIAYTDVAELAAN---PAVRAEIEAAVEAANARL-SRYEQIKKFLLL 430
|
570 580
....*....|....*....|..
gi 17933690 632 PHDFSIPTGELGPTLKVKRNVV 653
Cdd:cd05907 431 PEPFTIENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
78-666 |
1.23e-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: 276.40 E-value: 1.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 78 TYKQYEQKVHQVAKAFIKLGLE--EHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVD 155
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 156 dakqmdkihairdklpklkAAIQIqepyspylkkedgyYRWSEIESMNVSDVEDQYMTRLENVAInecccLVYTSGTVGM 235
Cdd:cd05927 87 -------------------AGVKV--------------YSLEEFEKLGKKNKVPPPPPKPEDLAT-----ICYTSGTTGN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 236 PKGVMLSHDNITFDVRGIVKAMDRVVVGAESIV--SYLPLSHVAAQTVdIYTCAFVAGCIWFADKDALKgtLVKSLQDAR 313
Cdd:cd05927 129 PKGVMLTHGNIVSNVAGVFKILEILNKINPTDVyiSYLPLAHIFERVV-EALFLYHGAKIGFYSGDIRL--LLDDIKALK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 314 PTRFMGVPRVYEKFQERMVAVASSSGSLKKMLASWAKGITLKHYmvsqgKSSGGFRYKIAKSLIMSKVKQALGfDRVLTL 393
Cdd:cd05927 206 PTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAEL-----RSGVVRASPFWDKLVFNKIKQALG-GNVRLM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 394 ASAAAPMSPETKKYFLS-LDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFIN--------KDANGHGELC 464
Cdd:cd05927 280 LTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpemnydaKDPNPRGEVC 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 465 IRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPPVHIENTIKKELdAISNAFL 544
Cdd:cd05927 360 IRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSP-FVAQIFV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 545 VGE-QRKYLTVLITLKTEVDKDsgepldelshessvWVKSLGVEHKTVSDIlaagpC--PKVWKSIEDAIKRANKQS-IS 620
Cdd:cd05927 439 YGDsLKSFLVAIVVPDPDVLKE--------------WAASKGGGTGSFEEL-----CknPEVKKAILEDLVRLGKENgLK 499
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 17933690 621 NAQKVQKFTILPHDFSIPTGELGPTLKVKRNVVSKMYADEIEKLYA 666
Cdd:cd05927 500 GFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
52-518 |
1.81e-82 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 266.49 E-value: 1.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 52 LKRTVNNYGDYPALRTkngkNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGI 131
Cdd:pfam00501 1 LERQAARTPDKTALEV----GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 132 YTTNSADAVQHVLESSHAQIVVVDDAKQMDKIHAIRDKLPKLKAAIQIqepyspylkKEDGYYRWSEIESMNVSDVEDQY 211
Cdd:pfam00501 77 NPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVL---------DRDPVLKEEPLPEEAKPADVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 212 MTrlENVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGI--VKAMDRVVVGAESIVSYLPLSHVAAQTVDIYTCAFV 289
Cdd:pfam00501 148 PP--PPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 290 AGCIWFADKDALK--GTLVKSLQDARPTRFMGVPRVYekfqERMVAvassSGSLKKMLASwakgitlkhymvsqgkssgg 367
Cdd:pfam00501 226 GATVVLPPGFPALdpAALLELIERYKVTVLYGVPTLL----NMLLE----AGAPKRALLS-------------------- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 368 frykiakslimskvkqalgfdRVLTLASAAAPMSPETKKYFLS-LDLKIVDAFGMSETAGCHTICLP---DSVGLNTIGK 443
Cdd:pfam00501 278 ---------------------SLRLVLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTPLPldeDLRSLGSVGR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 444 TLPGCESKFINKD------ANGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIIT 517
Cdd:pfam00501 337 PLPGTEVKIVDDEtgepvpPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKL 416
|
.
gi 17933690 518 A 518
Cdd:pfam00501 417 G 417
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
78-657 |
1.90e-77 |
|
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: 256.24 E-value: 1.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 78 TYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVV--- 154
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgkl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 155 DDAKQMDkiHAIRDKLPKLKAaiqiqepysPYLKKEDGYYRWSEIESMNvSDVEDQYMTRLENVAineccCLVYTSGTVG 234
Cdd:cd05932 88 DDWKAMA--PGVPEGLISISL---------PPPSAANCQYQWDDLIAQH-PPLEERPTRFPEQLA-----TLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 235 MPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHVAaQTVDIYTCAFVAGC-IWFADK-DalkgTLVKSLQDA 312
Cdd:cd05932 151 QPKGVMLTFGSFAWAAQAGIEHIG--TEENDRMLSYLPLAHVT-ERVFVEGGSLYGGVlVAFAESlD----TFVEDVQRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 313 RPTRFMGVPRVYEKFQERMvavasssgslkkmlaswakgitlkHYMVSQGKSSGGFRYKIAKSLIMSKVKQALGFDRVLT 392
Cdd:cd05932 224 RPTLFFSVPRLWTKFQQGV------------------------QDKIPQQKLNLLLKIPVVNSLVKRKVLKGLGLDQCRL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 393 LASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKfINKDanghGELCIRGRHVFM 472
Cdd:cd05932 280 AGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVR-ISED----GEILVRSPALMM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 473 GYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPPVHIENTIkKELDAISNAFLVGEQrkyl 552
Cdd:cd05932 355 GYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKL-AEHDRVEMVCVIGSG---- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 553 tvlitlktevdkdsgepldeLSHESSVWVksLGVEHKTVSDILAAGpcpKVWKSIEDAIKRANKQSISNAQkVQKFTILP 632
Cdd:cd05932 430 --------------------LPAPLALVV--LSEEARLRADAFARA---ELEASLRAHLARVNSTLDSHEQ-LAGIVVVK 483
|
570 580
....*....|....*....|....*
gi 17933690 633 HDFSIPTGELGPTLKVKRNVVSKMY 657
Cdd:cd05932 484 DPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
74-657 |
1.36e-74 |
|
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: 250.42 E-value: 1.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 74 YHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVV 153
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 154 VDDAKQMDKIHAIRDKLPKLKAAIQIQEpySPYLKKEDGYYRWSE--IESMNVSDVED--QYMTRLENVAINECCCLVYT 229
Cdd:cd17641 89 AEDEEQVDKLLEIADRIPSVRYVIYCDP--RGMRKYDDPRLISFEdvVALGRALDRRDpgLYEREVAAGKGEDVAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 230 SGTVGMPKGVMLSHDNItFDVRGIVKAMDRVVVGAEsIVSYLPLSHVAAQtvdIYTC--AFVAG-CIWFADKDAlkgTLV 306
Cdd:cd17641 167 SGTTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDE-YVSVLPLPWIGEQ---MYSVgqALVCGfIVNFPEEPE---TMM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 307 KSLQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLASWAKGITLKhyMVSQGKSSG------GFRYKIAKSLIMSK 380
Cdd:cd17641 239 EDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLR--ALDRGKRGRpvslwlRLASWLADALLFRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 381 VKQALGFDRVLTLASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKdangh 460
Cdd:cd17641 317 LRDRLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV----- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 461 GELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPPVHIENTIKKElDAIS 540
Cdd:cd17641 392 GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFS-PYIA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 541 NAFLVGEQRKYLTVLITLKTE-VDKdsgepldelshessvWVKSLGVEHKTVSDiLAAGpcPKVWKSIEDAIKRANkQSI 619
Cdd:cd17641 471 EAVVLGAGRPYLTAFICIDYAiVGK---------------WAEQRGIAFTTYTD-LASR--PEVYELIRKEVEKVN-ASL 531
|
570 580 590
....*....|....*....|....*....|....*...
gi 17933690 620 SNAQKVQKFTILPHDFSIPTGELGPTLKVKRNVVSKMY 657
Cdd:cd17641 532 PEAQRIRRFLLLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
72-653 |
6.20e-69 |
|
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: 233.26 E-value: 6.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 72 NGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQI 151
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 152 VVVDDakqmdkihairdklpklkaaiqiqepyspylKKEDgyyrwseiesmnvsdvedqymtrlenvaineCCCLVYTSG 231
Cdd:cd17639 81 IFTDG-------------------------------KPDD-------------------------------LACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 232 TVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESIVSYLPLSHVAAQTVDIytCAFVAGC-IWFADKDALKGTLVKS-- 308
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAEN--VCLYRGGtIGYGSPRTLTDKSKRGck 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 309 --LQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLASWAkgITLKHYMVSQGKSSGgfrykIAKSLIMSKVKQALG 386
Cdd:cd17639 177 gdLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTA--YQSKLKALKEGPGTP-----LLDELVFKKVRAALG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 387 fDRVLTLASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKDANGH------ 460
Cdd:cd17639 250 -GRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYstdkpp 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 461 --GELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPPVHIEnTIKKELDA 538
Cdd:cd17639 329 prGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLE-SIYRSNPL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 539 ISNAFLVGEQRKYLTVLITLKTEvdkdsgEPLDELSHEssvwvksLGVEHKTVSDILAAGPCPK-VWKSIEDAIKRANKQ 617
Cdd:cd17639 408 VNNICVYADPDKSYPVAIVVPNE------KHLTKLAEK-------HGVINSEWEELCEDKKLQKaVLKSLAETARAAGLE 474
|
570 580 590
....*....|....*....|....*....|....*.
gi 17933690 618 SIsnaQKVQKFTILPHDFSIPTGELGPTLKVKRNVV 653
Cdd:cd17639 475 KF---EIPQGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
48-546 |
1.70e-68 |
|
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: 230.85 E-value: 1.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 48 VPGLLKRTVNNYGDYPALRTkngknGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGI 127
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF-----GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 128 IAGIYTTNSADAVQHVLESSHAQIVVVddakqmdkihairdklpklkAAIQiqepyspylkkedgyyrwseiesmnvsdv 207
Cdd:COG0318 76 VVPLNPRLTAEELAYILEDSGARALVT--------------------ALIL----------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 208 edqymtrlenvaineccclvYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHVAAQTVDIYTCA 287
Cdd:COG0318 107 --------------------YTSGTTGRPKGVMLTHRNLLANAAAIAAALG--LTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 288 FVAGCIWFADK-DAlkGTLVKSLQDARPTRFMGVPRVYEkfqeRMVAVASssgslkkmlaswakgitlkhymvsqgkssg 366
Cdd:COG0318 165 LAGATLVLLPRfDP--ERVLELIERERVTVLFGVPTMLA----RLLRHPE------------------------------ 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 367 gfrykiakslimskvKQALGFDRVLTLASAAAPMSPETKKYFLS-LDLKIVDAFGMSETAGCHTICLPDSVG--LNTIGK 443
Cdd:COG0318 209 ---------------FARYDLSSLRLVVSGGAPLPPELLERFEErFGVRIVEGYGLTETSPVVTVNPEDPGErrPGSVGR 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 444 TLPGCESKFInkDANGH-------GELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIII 516
Cdd:COG0318 274 PLPGVEVRIV--DEDGRelppgevGEIVVRGPNVMKGYWNDPEATAEAFRDG-WLRTGDLGRLDEDGYLYIVGRKKDMII 350
|
490 500 510
....*....|....*....|....*....|
gi 17933690 517 TaGGENIPPVHIENTIkKELDAISNAFLVG 546
Cdd:COG0318 351 S-GGENVYPAEVEEVL-AAHPGVAEAAVVG 378
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
72-653 |
9.65e-68 |
|
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: 229.17 E-value: 9.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 72 NGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMG--AIHARGIIAGiyTTNSADAVQHVLESSHA 149
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGimALGAVDVVRG--SDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 150 QIVVVDDAkqmdkihairdklPKLKAAIqiqepyspylkkedgyyrwseiesmnvsdvedqymtrlenvaineccclVYT 229
Cdd:cd17640 79 VALVVEND-------------SDDLATI-------------------------------------------------IYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 230 SGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVvgAESIVSYLPLSHVAAQTVDiYTCaFVAGC-IWFADKDALKgtlvKS 308
Cdd:cd17640 97 SGTTGNPKGVMLTHANLLHQIRSLSDIVPPQP--GDRFLSILPIWHSYERSAE-YFI-FACGCsQAYTSIRTLK----DD 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 309 LQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLAswakgitlkHYMVSQGKssggfrykiakslimskVKQALgfd 388
Cdd:cd17640 169 LKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLF---------LFFLSGGI-----------------FKFGI--- 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 389 rvltlaSAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKDAN------GHGE 462
Cdd:cd17640 220 ------SGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNvvlppgEKGI 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 463 LCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPPVHIENTIKKELdAISNA 542
Cdd:cd17640 294 VWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSP-FIEQI 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 543 FLVGEQRKYLTVLITlktevdkdsgeP-LDELSHessvWVKSLGVehKTVSDILAAGPCPKVWKSIEDAIKR--ANKQSI 619
Cdd:cd17640 373 MVVGQDQKRLGALIV-----------PnFEELEK----WAKESGV--KLANDRSQLLASKKVLKLYKNEIKDeiSNRPGF 435
|
570 580 590
....*....|....*....|....*....|....
gi 17933690 620 SNAQKVQKFTILpHDFSIPTGELGPTLKVKRNVV 653
Cdd:cd17640 436 KSFEQIAPFALL-EEPFIENGEMTQTMKIKRNVV 468
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
76-650 |
1.34e-57 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 201.90 E-value: 1.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 76 TVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVd 155
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 156 dakqmdkihairdklpklkaaiqiqepyspylkkedgyyrwseiesmnvSDVEDqymtrlenVAInecccLVYTSGTVGM 235
Cdd:cd05914 86 -------------------------------------------------SDEDD--------VAL-----INYTSGTTGN 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 236 PKGVMLSHDNITFDVRGiVKAMDRVVVGaESIVSYLPLSHVAAQTVDIYTCAFVAGCIWFADKdaLKGTLVKSLQDARPT 315
Cdd:cd05914 104 SKGVMLTYRNIVSNVDG-VKEVVLLGKG-DKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDK--IPSAKIIALAFAQVT 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 316 RFMGVPRVYEKFQERMVAVASSSgSLKKMLASWAKGItlkhymvsqgkssggFRYKIaKSLIMSKVKQALGfDRVLTLAS 395
Cdd:cd05914 180 PTLGVPVPLVIEKIFKMDIIPKL-TLKKFKFKLAKKI---------------NNRKI-RKLAFKKVHEAFG-GNIKEFVI 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 396 AAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKDANGH-GELCIRGRHVFMGY 474
Cdd:cd05914 242 GGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPATGeGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 475 IDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPPVHIENTI-KKELDAISnafLVGEQRKYLT 553
Cdd:cd05914 322 YKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKInNMPFVLES---LVVVQEKKLV 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 554 VLITLKTEVDKDSGEPLDElshessvwvkslgvehktvsdilaagpcpkvwksIEDAIKRANK----QSISNAQKVQKFT 629
Cdd:cd05914 399 ALAYIDPDFLDVKALKQRN----------------------------------IIDAIKWEVRdkvnQKVPNYKKISKVK 444
|
570 580
....*....|....*....|.
gi 17933690 630 ILPHDFsiptgELGPTLKVKR 650
Cdd:cd05914 445 IVKEEF-----EKTPKGKIKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
226-568 |
3.08e-56 |
|
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: 194.43 E-value: 3.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHVAAQTVdIYTCAFVAGCIWFADKDaLKGTL 305
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG--LTEGDVFLSTLPLFHIGGLFG-LLGALLAGGTVVLLPKF-DPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 306 VKSLQDARPTRFMGVPRVYekfqermvavasssgslkkmlaswakgitlkHYMVSQGKSSGgfrykiakslimskvkqaL 385
Cdd:cd04433 81 LELIEREKVTILLGVPTLL-------------------------------ARLLKAPESAG------------------Y 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 386 GFDRVLTLASAAAPMSPETKKYFLSL-DLKIVDAFGMSETAGCHTICLPDSV--GLNTIGKTLPGCESKFINKD-----A 457
Cdd:cd04433 112 DLSSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPDDDarKPGSVGRPVPGVEVRIVDPDggelpP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 458 NGHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTIkKELD 537
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAVDEDG-WYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAVL-LGHP 268
|
330 340 350
....*....|....*....|....*....|....*
gi 17933690 538 AISNAFLVG----EQRKYLTVLITLKTEVDKDSGE 568
Cdd:cd04433 269 GVAEAAVVGvpdpEWGERVVAVVVLRPGADLDAEE 303
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
54-666 |
2.23e-55 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 199.94 E-value: 2.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 54 RTVNNYGDYPALRTKNGKNG----YHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMgAIHARGIIA 129
Cdd:PLN02736 52 YAVETFRDYKYLGTRIRVDGtvgeYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDH-ACSAYSYVS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 130 -GIYTTNSADAVQHVleSSHAQIVVVDDAKQ--------MDKIHAIR---------DKLPKLKAAIQIQepYSPYlkked 191
Cdd:PLN02736 131 vPLYDTLGPDAVKFI--VNHAEVAAIFCVPQtlntllscLSEIPSVRlivvvggadEPLPSLPSGTGVE--IVTY----- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 192 gyyrwSEIESMNVSDVEDQYMTRLENVAInecccLVYTSGTVGMPKGVMLSHDNITFDVRGIvkAMDRVVVGAESIVSYL 271
Cdd:PLN02736 202 -----SKLLAQGRSSPQPFRPPKPEDVAT-----ICYTSGTTGTPKGVVLTHGNLIANVAGS--SLSTKFYPSDVHISYL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 272 PLSHVAaQTVDIYTCAFVAGCIWFADKDALKgtLVKSLQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLasWAKG 351
Cdd:PLN02736 270 PLAHIY-ERVNQIVMLHYGVAVGFYQGDNLK--LMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERL--FNAA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 352 ITLKHYMVSQGKSSGGFRYKiaksLIMSKVKQALGfDRVLTLASAAAPMSPETKKyFLSLDL--KIVDAFGMSETAgcht 429
Cdd:PLN02736 345 YNAKKQALENGKNPSPMWDR----LVFNKIKAKLG-GRVRFMSSGASPLSPDVME-FLRICFggRVLEGYGMTETS---- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 430 iCLPDS--VGLNTIGKT---LPGCESK--------FINKDA-NGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGD 495
Cdd:PLN02736 415 -CVISGmdEGDNLSGHVgspNPACEVKlvdvpemnYTSEDQpYPRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGD 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 496 LGFVDDKGYVSLTGRSKEIIITAGGENIPPVHIENTIKKElDAISNAFLVGEQ-RKYLTVLITLKTEVDKDsgepldels 574
Cdd:PLN02736 494 IGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKC-KFVAQCFVYGDSlNSSLVAVVVVDPEVLKA--------- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 575 hessvWVKSLGVEHKTVSDiLAAGPCPK--VWKSIEDAIKRANKQSISNAQKVqkfTILPHDFSIPTGELGPTLKVKRNV 652
Cdd:PLN02736 564 -----WAASEGIKYEDLKQ-LCNDPRVRaaVLADMDAVGREAQLRGFEFAKAV---TLVPEPFTVENGLLTPTFKVKRPQ 634
|
650
....*....|....
gi 17933690 653 VSKMYADEIEKLYA 666
Cdd:PLN02736 635 AKAYFAKAISDMYA 648
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
75-546 |
2.56e-54 |
|
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: 193.20 E-value: 2.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 75 HTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVV 154
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 155 dDAKQMDKIHAIRDKLPKLKAAIQIQEpyspylkKEDGYYRWSEIESmNVSDVEDQYMTRLENVAINECCCLVYTSGTVG 234
Cdd:cd05911 89 -DPDGLEKVKEAAKELGPKDKIIVLDD-------KPDGVLSIEDLLS-PTLGEEDEDLPPPLKDGKDDTAAILYSSGTTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 235 MPKGVMLSHDNITFD---VRGIVKAMDRVvvgAESIVSYLPLSHVAAQTVDIYTCafVAGC--IWFADKDalkgtlvksl 309
Cdd:cd05911 160 LPKGVCLSHRNLIANlsqVQTFLYGNDGS---NDVILGFLPLYHIYGLFTTLASL--LNGAtvIIMPKFD---------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 310 qdarPTRFMgvpRVYEKFQERMVAVASSsgslkkMLASWAKGITLKHYMVSqgkssggfrykiakSLIMskvkqalgfdr 389
Cdd:cd05911 225 ----SELFL---DLIEKYKITFLYLVPP------IAAALAKSPLLDKYDLS--------------SLRV----------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 390 vltLASAAAPMSPETKKYFLSL--DLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKDA------NGHG 461
Cdd:cd05911 267 ---ILSGGAPLSKELQELLAKRfpNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGkdslgpNEPG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 462 ELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIENTIkKELDAISN 541
Cdd:cd05911 344 EICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE-LIKYKGFQVAPAELEAVL-LEHPGVAD 421
|
....*
gi 17933690 542 AFLVG 546
Cdd:cd05911 422 AAVIG 426
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
67-666 |
7.96e-52 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 190.05 E-value: 7.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 67 TKNGKNG-YHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFySAMGAIHARGI-IAGIYTTNSADAVQHVL 144
Cdd:PLN02861 67 VTDSKVGpYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWI-IAMEACNSQGItYVPLYDTLGANAVEFII 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 145 ESSHAQIVVVddakQMDKIHAIRDKLPK----LKAAIQIQEpYSPYLKKED-----GYYRWSEIESMNVSDVEdqymtrL 215
Cdd:PLN02861 146 NHAEVSIAFV----QESKISSILSCLPKcssnLKTIVSFGD-VSSEQKEEAeelgvSCFSWEEFSLMGSLDCE------L 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 216 ENVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGI---VKAMDRVVVGAESIVSYLPLSHVAAQTVDIYtCAFVAGC 292
Cdd:PLN02861 215 PPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTdhlLKVTDRVATEEDSYFSYLPLAHVYDQVIETY-CISKGAS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 293 IWFADKDALkgTLVKSLQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLASWAkgitlkhYMVSQGKSSGGFRYKI 372
Cdd:PLN02861 294 IGFWQGDIR--YLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFA-------YNYKLGNLRKGLKQEE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 373 AK----SLIMSKVKQALGfDRVLTLASAAAPMSPETKKYFLSLDLK-IVDAFGMSET-AGCHTICLPDSVGLNTIGKTLP 446
Cdd:PLN02861 365 ASprldRLVFDKIKEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTEScGGCFTSIANVFSMVGTVGVPMT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 447 GCESKFINKDANGH--------GELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITA 518
Cdd:PLN02861 444 TIEARLESVPEMGYdalsdvprGEICLRGNTLFSGYHKRQDLTEEVLIDG-WFHTGDIGEWQPNGAMKIIDRKKNIFKLS 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 519 GGENIPPVHIENTIKKeLDAISNAFLVGEQRKYLTVLITLKtevDKDSGEPldelshessvWVKSlgveHKTVSDILAAG 598
Cdd:PLN02861 523 QGEYVAVENLENTYSR-CPLIASIWVYGNSFESFLVAVVVP---DRQALED----------WAAN----NNKTGDFKSLC 584
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17933690 599 PCPKVWKSIEDAIKRANKQ-SISNAQKVQKFTILPHDFSIPTGELGPTLKVKRNVVSKMYADEIEKLYA 666
Cdd:PLN02861 585 KNLKARKYILDELNSTGKKlQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYS 653
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
51-666 |
1.05e-51 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 189.64 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 51 LLKRTVNNYGDYPAL---RTKNGKNG-YHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYsAMGAIHARG 126
Cdd:PLN02430 47 IFSKSVEKYPDNKMLgwrRIVDGKVGpYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIV-AMEACAAHS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 127 II-AGIYTTNSADAVQHVLESSHAQIVVVDDAKQMDKIHAIRDKLPKLKAAIQIQEPYSPYLKKEDGY----YRWSEIES 201
Cdd:PLN02430 126 LIcVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLKAIVSFTSVTEEESDKASQIgvktYSWIDFLH 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 202 MNVSDVEDQYMTRLENVainecCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRV---VVGAESIVSYLPLSHVAA 278
Cdd:PLN02430 206 MGKENPSETNPPKPLDI-----CTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQFedkMTHDDVYLSFLPLAHILD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 279 QTVDIYTcaFVAGC---IWFADKDALKgtlvKSLQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLASwakgiTLK 355
Cdd:PLN02430 281 RMIEEYF--FRKGAsvgYYHGDLNALR----DDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFN-----ALY 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 356 HYMVSQGKSsgGFRYK----IAKSLIMSKVKQALGfDRVLTLASAAAPMSPETKKyFLSLD--LKIVDAFGMSETAGCHT 429
Cdd:PLN02430 350 KYKLAWMNR--GYSHKkaspMADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEE-FLRVTscAFVVQGYGLTETLGPTT 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 430 ICLPD------SVGLNTIGKTLPGCESKFINKDANGH---GELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVD 500
Cdd:PLN02430 426 LGFPDemcmlgTVGAPAVYNELRLEEVPEMGYDPLGEpprGEICVRGKCLFSGYYKNPELTEEVMKDG-WFHTGDIGEIL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 501 DKGYVSLTGRSKEIIITAGGENIPPVHIENtIKKELDAISNAFLVGEQRKYLTVLITLKTEVDKDSgepldelshessvW 580
Cdd:PLN02430 505 PNGVLKIIDRKKNLIKLSQGEYVALEYLEN-VYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNK-------------W 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 581 VKSLGVEhKTVSDILAAgpcPKVWKSIEDAIKR-ANKQSISNAQKVQKFTILPHDFSIPTGELGPTLKVKRNVVSKMYAD 659
Cdd:PLN02430 571 AKDNGFT-GSFEELCSL---PELKEHILSELKStAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQV 646
|
....*..
gi 17933690 660 EIEKLYA 666
Cdd:PLN02430 647 EIDEMYR 653
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
48-551 |
3.14e-48 |
|
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: 176.21 E-value: 3.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 48 VPGLLKRTVNNYGDYPALRtkngkNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGI 127
Cdd:cd05936 1 LADLLEEAARRFPDKTALI-----FMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 128 IAGIYTTNSADAVQHVLESSHAQIVVVDDAKQmdkiHAIRDKLPklkaaiqiqEPYSPYLKKEDgyyrwseiesmnvsdv 207
Cdd:cd05936 76 VVPLNPLYTPRELEHILNDSGAKALIVAVSFT----DLLAAGAP---------LGERVALTPED---------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 208 edqymtrlenvaineCCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESIVSYLPLSHVAAQTVDIYTCA 287
Cdd:cd05936 127 ---------------VAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 288 FVAGCIW----FADKDALKGtlvksLQDARPTRFMGVPRVYEKFqermvavasssgslkkmlaswakgitlkhymvsqgk 363
Cdd:cd05936 192 ALGATIVliprFRPIGVLKE-----IRKHRVTIFPGVPTMYIAL------------------------------------ 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 364 ssggFRYKIAKSLIMSKVKQALgfdrvltlaSAAAPMSPETKKYFLSL-DLKIVDAFGMSET---AGCHTICLPDSVGln 439
Cdd:cd05936 231 ----LNAPEFKKRDFSSLRLCI---------SGGAPLPVEVAERFEELtGVPIVEGYGLTETspvVAVNPLDGPRKPG-- 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 440 TIGKTLPGCESKFINKDAN----G-HGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEI 514
Cdd:cd05936 296 SIGIPLPGTEVKIVDDDGEelppGeVGELWVRGPQVMKGYWNRPEETAEAFVDG-WLRTGDIGYMDEDGYFFIVDRKKDM 374
|
490 500 510
....*....|....*....|....*....|....*..
gi 17933690 515 IItAGGENIPPVHIENTIkKELDAISNAFLVGEQRKY 551
Cdd:cd05936 375 II-VGGFNVYPREVEEVL-YEHPAVAEAAVVGVPDPY 409
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
45-532 |
5.78e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 176.53 E-value: 5.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 45 PISVPGLLKRTVNNYGDYPALRTknGKNGYhtvTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFY-----SAM 119
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYF--DGRRT---TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEayfavPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 120 GAIhargiiagIYTTN---SADAVQHVLESSHAQIVVVDD--AKQMDKIhaiRDKLPKLKAAIQIQEPYSPYLKKEDGYY 194
Cdd:PRK06187 80 GAV--------LHPINirlKPEEIAYILNDAEDRVVLVDSefVPLLAAI---LPQLPTVRTVIVEGDGPAAPLAPEVGEY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 195 R-WSEIESMNVSDVEdqymtrlenVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAM-----DRVVVgaesiv 268
Cdd:PRK06187 149 EeLLAAASDTFDFPD---------IDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLklsrdDVYLV------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 269 sYLPLSHVAAQTVDIYtcAFVAGC-IWFADK-DAlkGTLVKSLQDARPTRFMGVPRVYekfqermvavasssgslkkmla 346
Cdd:PRK06187 214 -IVPMFHVHAWGLPYL--ALMAGAkQVIPRRfDP--ENLLDLIETERVTFFFAVPTIW---------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 347 swakgitlkhYMVSqgkssggfRYKIAKSLIMSKVKQALgfdrvltlaSAAAPMSPETKKYFLS-LDLKIVDAFGMSETA 425
Cdd:PRK06187 267 ----------QMLL--------KAPRAYFVDFSSLRLVI---------YGGAALPPALLREFKEkFGIDLVQGYGMTETS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 426 GCHTICLPDS--VGLNTI----GKTLPGCESKFInkDANGH---------GELCIRGRHVFMGYIDNKEKTEESLDDDcW 490
Cdd:PRK06187 320 PVVSVLPPEDqlPGQWTKrrsaGRPLPGVEARIV--DDDGDelppdggevGEIIVRGPWLMQGYWNRPEATAETIDGG-W 396
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 17933690 491 LHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTI 532
Cdd:PRK06187 397 LHTGDVGYIDEDGYLYITDRIKDVIIS-GGENIYPRELEDAL 437
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
36-665 |
4.78e-47 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 176.75 E-value: 4.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 36 AKDGIgaEEPI----SVPGLLKRTVNNYGDYPALRTK---NGKNG-YHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVL 107
Cdd:PLN02614 33 AKDGF--PNPIegmdSCWDVFRMSVEKYPNNPMLGRReivDGKPGkYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 108 AFNCAEWFYSaMGAIHARGI-IAGIYTTNSADAVQHVLESSHAQIVVVDDAKQMDKIHAIRDKLPKLKAAIQIQEpYSPY 186
Cdd:PLN02614 111 GANSPEWIIS-MEACNAHGLyCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSFGG-VSRE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 187 LKKEDG-----YYRWSEIESMNVSDVEDQYMTRLENVainecCCLVYTSGTVGMPKGVMLSHDNITFDVRGIV---KAMD 258
Cdd:PLN02614 189 QKEEAEtfglvIYAWDEFLKLGEGKQYDLPIKKKSDI-----CTIMYTSGTTGDPKGVMISNESIVTLIAGVIrllKSAN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 259 RVVVGAESIVSYLPLSHVAAQTVDiyTCAF-VAGCIWFADKDAlkGTLVKSLQDARPTRFMGVPRVYEKFQERMVAVASS 337
Cdd:PLN02614 264 AALTVKDVYLSYLPLAHIFDRVIE--ECFIqHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 338 SGSLKKMLASWAkgITLKHYMVSQGKSSGGFRyKIAKSLIMSKVKQALGfDRVLTLASAAAPMSPETKKYFLSLD-LKIV 416
Cdd:PLN02614 340 GGFLKKFVFDSA--FSYKFGNMKKGQSHVEAS-PLCDKLVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVAcCHVL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 417 DAFGMSETAGCHTICLPDSVG-LNTIGKTLPGCESKF-----INKDANG---HGELCIRGRHVFMGYIDNKEKTEESLDD 487
Cdd:PLN02614 416 QGYGLTESCAGTFVSLPDELDmLGTVGPPVPNVDIRLesvpeMEYDALAstpRGEICIRGKTLFSGYYKREDLTKEVLID 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 488 DcWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPPVHIENtIKKELDAISNAFLVGEQRKYLTVLITlktevdKDSG 567
Cdd:PLN02614 496 G-WLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIEN-IYGEVQAVDSVWVYGNSFESFLVAIA------NPNQ 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 568 EPLDELSHESSVW--VKSLGVEHKTVSDILAagpcpkvwksieDAIKRANKQSISNAQKVQKFTILPHDFSIPTGELGPT 645
Cdd:PLN02614 568 QILERWAAENGVSgdYNALCQNEKAKEFILG------------ELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPT 635
|
650 660
....*....|....*....|
gi 17933690 646 LKVKRNVVSKMYADEIEKLY 665
Cdd:PLN02614 636 FKKKRPQLLKYYQSVIDEMY 655
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
48-538 |
8.25e-47 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 174.23 E-value: 8.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 48 VPGLLKRTVNNYGDYPALRtkngkngYHT----VTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEW----FYSA- 118
Cdd:PRK08315 18 IGQLLDRTAARYPDREALV-------YRDqglrWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWvltqFATAk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 119 MGAIhargiiagIYTTNSA---DAVQHVLESSHAQIVVVDDA-KQMDKIHAIRDKLPKLKAAI--QIQEPYSPYLK---- 188
Cdd:PRK08315 91 IGAI--------LVTINPAyrlSELEYALNQSGCKALIAADGfKDSDYVAMLYELAPELATCEpgQLQSARLPELRrvif 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 189 ----KEDGYYRWSEIESMNVSDVEDQYMTRLENVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAM-----DR 259
Cdd:PRK08315 163 lgdeKHPGMLNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMklteeDR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 260 VVvgaesivsyLPlshvaaqtVDIYTCaFvaGCIwfadkdalkgtlvkslqdarptrfMGVprvyekfqermvavasssg 339
Cdd:PRK08315 243 LC---------IP--------VPLYHC-F--GMV------------------------LGN------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 340 slkkmLASWAKGITlkhyMVSQGKssggfrykiakslimskvkqalGFDRVLTLASAAA---------P-M------SPE 403
Cdd:PRK08315 260 -----LACVTHGAT----MVYPGE----------------------GFDPLATLAAVEEerctalygvPtMfiaeldHPD 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 404 TKKYFLSlDL----------------KIVD---------AFGMSETAGCHTICLPDS-----VglNTIGKTLPGCESKFI 453
Cdd:PRK08315 309 FARFDLS-SLrtgimagspcpievmkRVIDkmhmsevtiAYGMTETSPVSTQTRTDDplekrV--TTVGRALPHLEVKIV 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 454 NKDANG------HGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVH 527
Cdd:PRK08315 386 DPETGEtvprgeQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPRE 464
|
570
....*....|....
gi 17933690 528 IEN---TIKKELDA 538
Cdd:PRK08315 465 IEEflyTHPKIQDV 478
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
48-529 |
7.69e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 171.49 E-value: 7.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 48 VPGLLKRTVNNYGDYPALRTKNGKNGYhtvTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGI 127
Cdd:PRK12583 20 IGDAFDATVARFPDREALVVRHQALRY---TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 128 IAGIYTTNSADAVQHVLESSHAQIVVVDDAKQMDKIHAIRDKLPKLKAAIQIQEPYSP---------YLKKED--GYYRW 196
Cdd:PRK12583 97 LVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPGALACErlpelrgvvSLAPAPppGFLAW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 197 SEIESM--NVSDVE----DQYMTRLENVAINeccclvYTSGTVGMPKGVMLSHDNITFDVRGIVKAM-----DRVVVGae 265
Cdd:PRK12583 177 HELQARgeTVSREAlaerQASLDRDDPINIQ------YTSGTTGFPKGATLSHHNILNNGYFVAESLgltehDRLCVP-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 266 sivsyLPLSHVAAQTVDIYTCAFVAGCIWFADK--DALkGTLvKSLQDARPTRFMGVPRVYekfqermvavasssgslkk 343
Cdd:PRK12583 249 -----VPLYHCFGMVLANLGCMTVGACLVYPNEafDPL-ATL-QAVEEERCTALYGVPTMF------------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 344 mLASwakgitLKHymvsqgKSSGGFRYKIAKSLIMskvkqalgfdrvltlasAAAPMSPETKKYFLSlDLKIVD---AFG 420
Cdd:PRK12583 303 -IAE------LDH------PQRGNFDLSSLRTGIM-----------------AGAPCPIEVMRRVMD-EMHMAEvqiAYG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 421 MSETAGC-HTICLPDSVG--LNTIGKTLPGCESKFINKDAN-----GHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLH 492
Cdd:PRK12583 352 MTETSPVsLQTTAADDLErrVETVGRTQPHLEVKVVDPDGAtvprgEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMH 431
|
490 500 510
....*....|....*....|....*....|....*..
gi 17933690 493 SGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIE 529
Cdd:PRK12583 432 TGDLATMDEQGYVRIVGRSKDMIIR-GGENIYPREIE 467
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
17-666 |
1.09e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 173.24 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 17 RQADAYRTTNRqdaVKIRMAKDGIGAEEPISVPGLlkrtvnnygdypalrtkngkNGYHTVTYKQYEQKVHQVAKAFIKL 96
Cdd:PTZ00216 85 RRALAYRPVER---VEKEVVKDADGKERTMEVTHF--------------------NETRYITYAELWERIVNFGRGLAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 97 GLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVDDAKQMDKIHAIRDKlpKLKAA 176
Cdd:PTZ00216 142 GLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLLRLMKSG--GMPNT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 177 IQIQEPYSPYLKKEDGY--YRWSEIESMNVSDVEDQYMTRLENVaiNECCCLVYTSGTVGMPKGVMLSHDNITfdvRGIV 254
Cdd:PTZ00216 220 TIIYLDSLPASVDTEGCrlVAWTDVVAKGHSAGSHHPLNIPENN--DDLALIMYTSGTTGDPKGVMHTHGSLT---AGIL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 255 KAMDRV--VVGA----ESIVSYLPLSHVAAQTVdiyTCAFVA-GC-IWFADKDALKGTLVK---SLQDARPTRFMGVPRV 323
Cdd:PTZ00216 295 ALEDRLndLIGPpeedETYCSYLPLAHIMEFGV---TNIFLArGAlIGFGSPRTLTDTFARphgDLTEFRPVFLIGVPRI 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 324 YEKFQERMVAVASSSGSLKKMLASWAKGITLKHYMvsQGKSSGGFRYKIaksliMSKVKQALGfDRVLTLASAAAPMSPE 403
Cdd:PTZ00216 372 FDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALK--EGKDTPYWNEKV-----FSAPRAVLG-GRVRAMLSGGGPLSAA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 404 TKKyFLSLDL-KIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKDANGH-------GELCIRGRHVFMGYI 475
Cdd:PTZ00216 444 TQE-FVNVVFgMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYKHtdtpeprGEILLRGPFLFKGYY 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 476 DNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPpvhIENtikkeLDAI--SNAF--------LV 545
Cdd:PTZ00216 523 KQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIA---LEA-----LEALygQNELvvpngvcvLV 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 546 GEQRKYLTVLItLKTEVDkdsgepldelshessvwVKSLGVEHK---TVSDILAAgpcP----KVWKSIEDAIKRANKQS 618
Cdd:PTZ00216 595 HPARSYICALV-LTDEAK-----------------AMAFAKEHGiegEYPAILKD---PefqkKATESLQETARAAGRKS 653
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 17933690 619 IsnaQKVQKFTILPHDFSIPTGELGPTLKVKRNVVSKMYADEIEKLYA 666
Cdd:PTZ00216 654 F---EIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
43-546 |
5.91e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 167.77 E-value: 5.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 43 EEPISVPGLLKRTVNNYGDYPALRTkngknGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAI 122
Cdd:PRK07656 2 NEWMTLPELLARAARRFGDKEAYVF-----GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 123 HARGIIAGIYTTNSADAVQHVLESSHAQIVVVDDAkQMDKIHAIRDKLPKLKAAIQIQEPYSPylKKEDGYYRWSE-IES 201
Cdd:PRK07656 77 KAGAVVVPLNTRYTADEAAYILARGDAKALFVLGL-FLGVDYSATTRLPALEHVVICETEEDD--PHTEKMKTFTDfLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 202 MNVSDVEDQYmtRLENVAInecccLVYTSGTVGMPKGVMLSHDNITFDVRGI-----VKAMDRVVVgaesivsYLPLSHV 276
Cdd:PRK07656 154 GDPAERAPEV--DPDDVAD-----ILFTSGTTGRPKGAMLTHRQLLSNAADWaeylgLTEGDRYLA-------ANPFFHV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 277 AAQTVDIYTCAFVAGCIWFADK-DALKgtLVKSLQDARPTRFMGVPRVYEKfqerMVAVASSSgslKKMLASWAKGITlk 355
Cdd:PRK07656 220 FGYKAGVNAPLMRGATILPLPVfDPDE--VFRLIETERITVLPGPPTMYNS----LLQHPDRS---AEDLSSLRLAVT-- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 356 hymvsqGKSSggfrykIAKSLImSKVKQALGFDRVLTlasaaapmspetkkyflsldlkivdAFGMSETAGCHTICLPD- 434
Cdd:PRK07656 289 ------GAAS------MPVALL-ERFESELGVDIVLT-------------------------GYGLSEASGVTTFNRLDd 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 435 --SVGLNTIGKTLPGCESKFINKDANGH-----GELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSL 507
Cdd:PRK07656 331 drKTVAGTIGTAIAGVENKIVNELGEEVpvgevGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYI 410
|
490 500 510
....*....|....*....|....*....|....*....
gi 17933690 508 TGRSKEIIITaGGENIPPVHIENTIkKELDAISNAFLVG 546
Cdd:PRK07656 411 VDRKKDMFIV-GGFNVYPAEVEEVL-YEHPAVAEAAVIG 447
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
52-546 |
9.80e-45 |
|
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: 165.48 E-value: 9.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 52 LKRTVNNYGDYPALRTKNGkngyhTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGI 131
Cdd:cd17631 1 LRRRARRHPDRTALVFGGR-----SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 132 YTTNSADAVQHVLESSHAQiVVVDDAkqmdkihairdklpklkaaiqiqepyspylkkedgyyrwseiesmnvsdvedqy 211
Cdd:cd17631 76 NFRLTPPEVAYILADSGAK-VLFDDL------------------------------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 212 mtrlenvainecCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrVVVGAESIVSyLPLSHVAAQTVDIYTCAFVAG 291
Cdd:cd17631 101 ------------ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALD-LGPDDVLLVV-APLFHIGGLGVFTLPTLLRGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 292 CIWFADK-DAlkGTLVKSLQDARPTRFMGVPRVYekfqermvavasssgslkkmlaswakgitlkhYMVSQgksSGGFRY 370
Cdd:cd17631 167 TVVILRKfDP--ETVLDLIERHRVTSFFLVPTMI--------------------------------QALLQ---HPRFAT 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 371 KIAKSLImskvkqalgfdrvlTLASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSV--GLNTIGKTLPGC 448
Cdd:cd17631 210 TDLSSLR--------------AVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFV 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 449 ESKFINKD-----ANGHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENI 523
Cdd:cd17631 276 EVRIVDPDgrevpPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG-WFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENV 353
|
490 500
....*....|....*....|...
gi 17933690 524 PPVHIENTIkKELDAISNAFLVG 546
Cdd:cd17631 354 YPAEVEDVL-YEHPAVAEVAVIG 375
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
74-666 |
3.53e-43 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 165.68 E-value: 3.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 74 YHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVV 153
Cdd:PLN02387 104 YEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 154 VDDaKQMDKIHAIRDKLPKLKAAIQIQE--PYSPYLKKEDGYY---RWSEIESMNVSDVEDQYMTRLENVAInecccLVY 228
Cdd:PLN02387 184 CDS-KQLKKLIDISSQLETVKRVIYMDDegVDSDSSLSGSSNWtvsSFSEVEKLGKENPVDPDLPSPNDIAV-----IMY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 229 TSGTVGMPKGVMLSHDNITFDVRGIVKamdrVVVGAES---IVSYLPLSHV---AAQTVdiytcAFVAGC-IWFADKDAL 301
Cdd:PLN02387 258 TSGSTGLPKGVMMTHGNIVATVAGVMT----VVPKLGKndvYLAYLPLAHIlelAAESV-----MAAVGAaIGYGSPLTL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 302 KGTLVK----SLQDA---RPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLASWAKGITLkhyMVSQGKSSG--GFRYKI 372
Cdd:PLN02387 329 TDTSNKikkgTKGDAsalKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRL---AAIEGSWFGawGLEKLL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 373 AKSLIMSKVKQALGfDRVLTLASAAAPMSPETKKYF-LSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESK 451
Cdd:PLN02387 406 WDALVFKKIRAVLG-GRIRFMLSGGAPLSGDTQRFInICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVK 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 452 FINKDANGH---------GELCIRGRHVFMGYIDNKEKTEESLDDD----CWLHSGDLGFVDDKGYVSLTGRSKEIIITA 518
Cdd:PLN02387 485 LVSWEEGGYlisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDergmRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQ 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 519 GGENIPPVHIEN--TIKKELDAI---SNAFlvgeqRKYLTVLITLktevdkdSGEPLDElshessvWVKSLGVEHKTVSD 593
Cdd:PLN02387 565 HGEYVSLGKVEAalSVSPYVDNImvhADPF-----HSYCVALVVP-------SQQALEK-------WAKKAGIDYSNFAE 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 594 IlaagpCPKvwksiEDAIKRAnKQSISNAQK---VQKFTI------LPHDFSIPTGELGPTLKVKRNVVSKMYADEIEKL 664
Cdd:PLN02387 626 L-----CEK-----EEAVKEV-QQSLSKAAKaarLEKFEIpakiklLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKL 694
|
..
gi 17933690 665 YA 666
Cdd:PLN02387 695 YE 696
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
58-515 |
8.50e-43 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 161.63 E-value: 8.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 58 NYGDYPALrtKNGKNGyHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSA 137
Cdd:cd05904 17 AHPSRPAL--IDAATG-RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 138 DAVQHVLESSHAQIVVVDdakqmdkihaiRDKLPKLKAA----IQIQEPYSPYLKKEDGyyrwseiesmnvSDVEDQYMT 213
Cdd:cd05904 94 AEIAKQVKDSGAKLAFTT-----------AELAEKLASLalpvVLLDSAEFDSLSFSDL------------LFEADEAEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 214 RLENVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESIVSYLPLSHvaaqtvdIYTCAFVAGCI 293
Cdd:cd05904 151 PVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFH-------IYGLSSFALGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 294 WfadkdALKGTLVkslqdarptrfmgvprVYEKFqermvavasssgSLKKMLASWAKgitlkhYMVSQGKssggfrykIA 373
Cdd:cd05904 224 L-----RLGATVV----------------VMPRF------------DLEELLAAIER------YKVTHLP--------VV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 374 KSLIMSKVKQALGFDRVL----TLASAAAPMSPETKKYFLSL--DLKIVDAFGMSETAGCHTICLP---DSVGLNTIGKT 444
Cdd:cd05904 257 PPIVLALVKSPIVDKYDLsslrQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRL 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17933690 445 LPGCESKFINKDANGH------GELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEII 515
Cdd:cd05904 337 VPNVEAKIVDPETGESlppnqtGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELI 413
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
224-547 |
8.46e-38 |
|
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: 146.28 E-value: 8.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 224 CCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHVAAqTVDIYTCAFVAG--CIWFADKDAL 301
Cdd:cd05941 92 ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWR--WTEDDVLLHVLPLHHVHG-LVNALLCPLFAGasVEFLPKFDPK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 302 KGTLVKSLQDArpTRFMGVPRVYekfqermvavasssgslKKMLASWAKgitlkHYMVSQGKSSGGFRykiakslimskv 381
Cdd:cd05941 169 EVAISRLMPSI--TVFMGVPTIY-----------------TRLLQYYEA-----HFTDPQFARAAAAE------------ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 382 kqalgfdRVLTLASAAAPMSPETKKYFLSLD-LKIVDAFGMSETAgchtICLpdSVGLN------TIGKTLPGCESKFIN 454
Cdd:cd05941 213 -------RLRLMVSGSAALPVPTLEEWEAITgHTLLERYGMTEIG----MAL--SNPLDgerrpgTVGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 455 K------DANGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENIPPVHI 528
Cdd:cd05941 280 EetgeplPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEI 359
|
330
....*....|....*....
gi 17933690 529 ENTIkKELDAISNAFLVGE 547
Cdd:cd05941 360 ERVL-LAHPGVSECAVIGV 377
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
45-529 |
2.30e-36 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 144.71 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 45 PISVPGLLKRTVNNYGDYPALR---TKNGKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGA 121
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPALSfllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 122 iHARGIIAGIYTTNSADAVQHVLESSHAQIVVV----DDAKQMDKIHAIRDKLPKLKAAIQIqePYSPYLKKEDGY-YRW 196
Cdd:PRK07529 104 -EAAGIANPINPLLEPEQIAELLRAAGAKVLVTlgpfPGTDIWQKVAEVLAALPELRTVVEV--DLARYLPGPKRLaVPL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 197 SEIESMNV-----SDVEDQYMTRLE---NVAINECCCLVYTSGTVGMPKGVMLSHDNITFDvrGIVKAMDRVVVGAESIV 268
Cdd:PRK07529 181 IRRKAHARildfdAELARQPGDRLFsgrPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN--AWLGALLLGLGPGDTVF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 269 SYLPLSHVAAQTVDIYTCAFVAGCIWFADKDALKGTLV-----KSLQDARPTRFMGVPRVYEKFQERMVAvASSSGSLKk 343
Cdd:PRK07529 259 CGLPLFHVNALLVTGLAPLARGAHVVLATPQGYRGPGVianfwKIVERYRINFLSGVPTVYAALLQVPVD-GHDISSLR- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 344 mlaswakgitlkhymvsqgkssggfrykiakslimskvkqalgfdrvlTLASAAAPMSPETKKYFLS-LDLKIVDAFGMS 422
Cdd:PRK07529 337 ------------------------------------------------YALCGAAPLPVEVFRRFEAaTGVRIVEGYGLT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 423 ETAGCHTICLPD-SVGLNTIGKTLPGCESKFINKDANGH----------GELCIRGRHVFMGYIdNKEKTEESLDDDCWL 491
Cdd:PRK07529 369 EATCVSSVNPPDgERRIGSVGLRLPYQRVRVVILDDAGRylrdcavdevGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWL 447
|
490 500 510
....*....|....*....|....*....|....*...
gi 17933690 492 HSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIE 529
Cdd:PRK07529 448 NTGDLGRIDADGYFWLTGRAKDLIIR-GGHNIDPAAIE 484
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
75-546 |
3.15e-36 |
|
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: 142.45 E-value: 3.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 75 HTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVV 154
Cdd:cd05926 13 PALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 155 DDAKQMDKIHAirdkLPKLKAAIQiqEPYSPYLKKedgyYRWSEIESMNVSDVEDQYMTRLENVAINECCCLVYTSGTVG 234
Cdd:cd05926 93 PKGELGPASRA----ASKLGLAIL--ELALDVGVL----IRAPSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 235 MPKGVMLSHDNITFDVRGIVKAM-----DRVVVgaesivsYLPLSHVAAQTVDIYTCAFVAGCIWFADK-DALkgTLVKS 308
Cdd:cd05926 163 RPKGVPLTHRNLAASATNITNTYkltpdDRTLV-------VMPLFHVHGLVASLLSTLAAGGSVVLPPRfSAS--TFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 309 LQDARPTRFMGVPRVYEkfqermvavasssgslkkmlaswakgITLKHYMVSQGKSSGGFRykiakslimskvkqalgFD 388
Cdd:cd05926 234 VRDYNATWYTAVPTIHQ--------------------------ILLNRPEPNPESPPPKLR-----------------FI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 389 RvltlaSAAAPMSPET----KKYFlslDLKIVDAFGMSETA----------GCHTiclPDSVG---------LNTIGKTL 445
Cdd:cd05926 271 R-----SCSASLPPAVlealEATF---GAPVLEAYGMTEAAhqmtsnplppGPRK---PGSVGkpvgvevriLDEDGEIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 446 PgceskfinkdANGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPP 525
Cdd:cd05926 340 P----------PGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINR-GGEKISP 408
|
490 500
....*....|....*....|.
gi 17933690 526 VHIENtIKKELDAISNAFLVG 546
Cdd:cd05926 409 LEVDG-VLLSHPAVLEAVAFG 428
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
44-529 |
1.49e-35 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 141.66 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 44 EPISVPGLLKRTVNNYGDYPA-LRTKNGKngyhTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAI 122
Cdd:PLN02330 26 DKLTLPDFVLQDAELYADKVAfVEAVTGK----AVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 123 HARGIIAGIYTTNSADAVQHVLESSHAQIVVVDDAkQMDKIHAIrdKLPklkaAIQIQEpyspylKKEDGYYRWSEIesM 202
Cdd:PLN02330 102 AAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT-NYGKVKGL--GLP----VIVLGE------EKIEGAVNWKEL--L 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 203 NVSDVEDQYMTRlENVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESIVSYLPLSHVAAQTVd 282
Cdd:PLN02330 167 EAADRAGDTSDN-EEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVVTLGLIPFFHIYGITG- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 283 iYTCAFVAGciwfadkdalKGTLVkslqdarptrfmgvprVYEKFQERmvavasssgslkkmlaswakgiTLKHYMVSQG 362
Cdd:PLN02330 245 -ICCATLRN----------KGKVV----------------VMSRFELR----------------------TFLNALITQE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 363 KSSGgfryKIAKSLIMSKVKQAL--GFD----RVLTLASAAAPMSPETKKYFLSL--DLKIVDAFGMSETAgCHTICLPD 434
Cdd:PLN02330 276 VSFA----PIVPPIILNLVKNPIveEFDlsklKLQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHS-CITLTHGD 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 435 S------VGLNTIGKTLPGCESKFINKDA------NGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDK 502
Cdd:PLN02330 351 PekghgiAKKNSVGFILPNLEVKFIDPDTgrslpkNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDD 430
|
490 500
....*....|....*....|....*..
gi 17933690 503 GYVSLTGRSKEIIITAGGEnIPPVHIE 529
Cdd:PLN02330 431 GDIFIVDRIKELIKYKGFQ-VAPAELE 456
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
67-532 |
1.90e-34 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 137.76 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 67 TKNGKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCA---EWFY--SAMGAIhargiiagIYTTN---SAD 138
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHrhlELYYavPGMGAV--------LHTINprlFPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 139 AVQHVLESSHAQIVVVDDAKQmDKIHAIRDKLPKLKAAIQI-------------QEPYSPYLKKEDGYYRWSEIEsmnvs 205
Cdd:cd12119 88 QIAYIINHAEDRVVFVDRDFL-PLLEAIAPRLPTVEHVVVMtddaampepagvgVLAYEELLAAESPEYDWPDFD----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 206 dvedqymtrlENVAinecCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESIVSYLPLSHVAAQTVDiYT 285
Cdd:cd12119 162 ----------ENTA----AAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSESDVVLPVVPMFHVNAWGLP-YA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 286 CAFVAGCIWFADKDALKGTLVKSLQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLaswakgitlkhymvsqgksS 365
Cdd:cd12119 227 AAMVGAKLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVV-------------------I 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 366 GGfrykiakslimskvkqalgfdrvltlasAAAPMSpeTKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLN------ 439
Cdd:cd12119 288 GG----------------------------SAVPRS--LIEAFEERGVRVIHAWGMTETSPLGTVARPPSEHSNlsedeq 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 440 -----TIGKTLPGCESKFIN-------KDANGHGELCIRGRHVFMGYIDNKEKTEEsLDDDCWLHSGDLGFVDDKGYVSL 507
Cdd:cd12119 338 lalraKQGRPVPGVELRIVDddgrelpWDGKAVGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDEDGYLTI 416
|
490 500
....*....|....*....|....*
gi 17933690 508 TGRSKEiIITAGGENIPPVHIENTI 532
Cdd:cd12119 417 TDRSKD-VIKSGGEWISSVELENAI 440
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
228-546 |
3.15e-34 |
|
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: 133.56 E-value: 3.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 228 YTSGTVGMPKGVMLSHDNITFDVRGIVKAM-----DRVVVGaesivsyLPLSH--------VAAQTvdiYTCAFVAGCIW 294
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLglteqDRLCIP-------VPLFHcfgsvlgvLACLT---HGATMVFPSPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 295 FADKDALKgtlvkSLQDARPTRFMGVPRVYekfqermVAVasssgslkkmlaswakgitLKHYMVSQgkssggFRYKIAK 374
Cdd:cd05917 79 FDPLAVLE-----AIEKEKCTALHGVPTMF-------IAE-------------------LEHPDFDK------FDLSSLR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 375 SLIMskvkqalgfdrvltlasAAAPMSPET-KKYFLSLDLK-IVDAFGMSETAGCHTICLPDS---VGLNTIGKTLPGCE 449
Cdd:cd05917 122 TGIM-----------------AGAPCPPELmKRVIEVMNMKdVTIAYGMTETSPVSTQTRTDDsieKRVNTVGRIMPHTE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 450 SKFINKDA------NGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENI 523
Cdd:cd05917 185 AKIVDPEGgivppvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENI 263
|
330 340
....*....|....*....|...
gi 17933690 524 PPVHIENTIKKeLDAISNAFLVG 546
Cdd:cd05917 264 YPREIEEFLHT-HPKVSDVQVVG 285
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
45-532 |
1.13e-31 |
|
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: 128.96 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 45 PISvpgLLKRTVNNYGDYPALRtkngkngYHTV--TYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAI 122
Cdd:cd12118 6 PLS---FLERAAAVYPDRTSIV-------YGDRryTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 123 HARGIIAGIYTTNSADAVQHVLESSHAQIVVVDDAKQMDkihairdklpklkAAIQIQEPYSPYLKKEDgyyRWSEIesm 202
Cdd:cd12118 76 MAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFEYE-------------DLLAEGDPDFEWIPPAD---EWDPI--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 203 nvsdvedqymtrlenvAINeccclvYTSGTVGMPKGVMLSHdnitfdvRGI-VKAMDRVVVGAesivsyLPLSHVAAQTV 281
Cdd:cd12118 137 ----------------ALN------YTSGTTGRPKGVVYHH-------RGAyLNALANILEWE------MKQHPVYLWTL 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 282 DIYTCAfvAGC-IWFADkdALKGTLV-----------KSLQDARPTRFMGVPRVYEkfqerMVAVASSSgslkkmlaswa 349
Cdd:cd12118 182 PMFHCN--GWCfPWTVA--AVGGTNVclrkvdakaiyDLIEKHKVTHFCGAPTVLN-----MLANAPPS----------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 350 kgitlkhymvsqgkssggfrykiakslimskvkQALGFDRVLTLASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHT 429
Cdd:cd12118 242 ---------------------------------DARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYGPAT 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 430 IC--------LPDSV--------GLNTIGKTlpgcESKFINKD------ANGH--GELCIRGRHVFMGYIDNKEKTEESL 485
Cdd:cd12118 289 VCawkpewdeLPTEErarlkarqGVRYVGLE----EVDVLDPEtmkpvpRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF 364
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 17933690 486 DDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTI 532
Cdd:cd12118 365 RGG-WFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEGVL 409
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
78-548 |
1.51e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 128.82 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 78 TYKQYEQKVHQVAKAFI-KLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVDd 156
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 157 akqmdkihairdklPKLKAAIQIqepyspyLKKEDGYYRWSEIESMnvSDVEDQYMTRLENVAINECCCLVYTSGTVGMP 236
Cdd:PRK06839 108 --------------KTFQNMALS-------MQKVSYVQRVISITSL--KEIEDRKIDNFVEKNESASFIICYTSGTTGKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 237 KGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHVAAQTVDIYTCAFVAGCIWFADK-DALKGtlVKSLQDARPT 315
Cdd:PRK06839 165 KGAVLTQENMFWNALNNTFAID--LTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKfEPTKA--LSMIEKHKVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 316 RFMGVPRVYEKfqermvavasssgslkkmlaswakgitlkhymvsqgkssggfrykiaksLIMSKVKQALGFDRVLTLAS 395
Cdd:PRK06839 241 VVMGVPTIHQA-------------------------------------------------LINCSKFETTNLQSVRWFYN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 396 AAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVG--LNTIGKTLPGCESKFINKDAN-----GHGELCIRGR 468
Cdd:PRK06839 272 GGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIDENKNkvevgEVGELLIRGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 469 HVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTIkKELDAISNAFLVGEQ 548
Cdd:PRK06839 352 NVMKEYWNRPDATEETIQDG-WLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQVI-NKLSDVYEVAVVGRQ 428
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
224-546 |
2.14e-31 |
|
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: 127.50 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 224 CCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAM-----DRVVVGAesivsylPLSHvaaQTVDIY--TCAFVAGC---- 292
Cdd:cd05903 96 ALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLglgpgDVFLVAS-------PMAH---QTGFVYgfTLPLLLGApvvl 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 293 --IWFADKdalkgtLVKSLQDARPTRFMGVPrvyeKFQERMVAVASSSG----SLKKMLASWAKgitlkhymvsqgkssg 366
Cdd:cd05903 166 qdIWDPDK------ALALMREHGVTFMMGAT----PFLTDLLNAVEEAGeplsRLRTFVCGGAT---------------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 367 gfrykIAKSLImSKVKQALGfdrvltlasaaapmspetkkyflsldLKIVDAFGMSETAGCHTICLPDSVG--LNTIGKT 444
Cdd:cd05903 220 -----VPRSLA-RRAAELLG--------------------------AKVCSAYGSTECPGAVTSITPAPEDrrLYTDGRP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 445 LPGCESKFINKD-----ANGHGELCIRGRHVFMGYIDNKEKTEESlDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaG 519
Cdd:cd05903 268 LPGVEIKVVDDTgatlaPGVEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIIIR-G 345
|
330 340
....*....|....*....|....*..
gi 17933690 520 GENIPPVHIENTIKKELdAISNAFLVG 546
Cdd:cd05903 346 GENIPVLEVEDLLLGHP-GVIEAAVVA 371
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
77-529 |
2.14e-31 |
|
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: 128.80 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 77 VTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVDD 156
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 157 aKQMDKIHAIRDKLPKLKAAIQIQEPYSPYLKKEDGYYRWSEIE-SMNVSDVEDQYMTRLENVAInecccLVYTSGTVGM 235
Cdd:cd17642 125 -KGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPpGFNEYDFKPPSFDRDEQVAL-----IMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 236 PKGVMLSHDNI--TFDvrgivKAMDRVVVGA----ESIVSYLPLSHVAA--QTVDIYTCAF-VAGCIWFADKdalkgTLV 306
Cdd:cd17642 199 PKGVQLTHKNIvaRFS-----HARDPIFGNQiipdTAILTVIPFHHGFGmfTTLGYLICGFrVVLMYKFEEE-----LFL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 307 KSLQDARPTRFMGVPRVYEKFqermvavasssgslkkmlaswakgitlkhymvsqgkssggfrykiAKSLIMSKVKqalg 386
Cdd:cd17642 269 RSLQDYKVQSALLVPTLFAFF---------------------------------------------AKSTLVDKYD---- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 387 FDRVLTLASAAAPMSPET-----KKYFLSLdlkIVDAFGMSETAGCHTI-----CLPDSVGlntigKTLPGCESKFINKD 456
Cdd:cd17642 300 LSNLHEIASGGAPLSKEVgeavaKRFKLPG---IRQGYGLTETTSAILItpegdDKPGAVG-----KVVPFFYAKVVDLD 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17933690 457 ------ANGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIE 529
Cdd:cd17642 372 tgktlgPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKS-LIKYKGYQVPPAELE 449
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
161-532 |
2.63e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 125.63 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 161 DKIHAIRDKLPKLKAAIQIQEpyspyLKKEdgyyrwseIESMNVSDVEDQY--MTRLENVAINECCCLVYTSGTVGMPKG 238
Cdd:PRK06087 138 DLILPLQNQLPQLQQIVGVDK-----LAPA--------TSSLSLSQIIADYepLTTAITTHGDELAAVLFTSGTEGLPKG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 239 VMLSHDNITFDVRGIVK-----AMDRVVVGAesivsylPLSHVAAqtvdiytcaFVAGCIwfadKDALKGTLVKSLQDAR 313
Cdd:PRK06087 205 VMLTHNNILASERAYCArlnltWQDVFMMPA-------PLGHATG---------FLHGVT----APFLIGARSVLLDIFT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 314 PTRFMGVPRvyekfQERmvavasssgslkkmlASWAKGITlkhymvsqgkssgGFRYKIAKSLIMSKVK-QALGFdrvlt 392
Cdd:PRK06087 265 PDACLALLE-----QQR---------------CTCMLGAT-------------PFIYDLLNLLEKQPADlSALRF----- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 393 LASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGcHTICLPD---SVGLNTIGKTLPGCESKFINKDAN----GH-GELC 464
Cdd:PRK06087 307 FLCGGTTIPKKVARECQQRGIKLLSVYGSTESSP-HAVVNLDdplSRFMHTDGYAAAGVEIKVVDEARKtlppGCeGEEA 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17933690 465 IRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTI 532
Cdd:PRK06087 386 SRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVR-GGENISSREVEDIL 452
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
78-532 |
5.03e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 123.17 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 78 TYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVDDa 157
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDP- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 158 kqmdkihairdklpklkaaiqiqepyspylkkedgyyrwseiesmnvsdvedqymtrlenvainecCCLVYTSGTVGMPK 237
Cdd:cd05934 84 ------------------------------------------------------------------ASILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 238 GVMLSHDNITFdvRGIVKAMDRVVVGAESIVSYLPLSHVAAQTVDIYTcAFVAGciwfadkdalkGTLVksLQDA-RPTR 316
Cdd:cd05934 98 GVVITHANLTF--AGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLA-ALSVG-----------ATLV--LLPRfSASR 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 317 FMGVPRVYekfqermvavasssgslkkmlaswakGITLKHYMVSQGkssggfrykiakSLIMSKVKQALGFDRVLTLASA 396
Cdd:cd05934 162 FWSDVRRY--------------------------GATVTNYLGAML------------SYLLAQPPSPDDRAHRLRAAYG 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 397 AAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFInkDANGH-------GELCIRGRH 469
Cdd:cd05934 204 APNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIV--DDDGQelpagepGELVIRGLR 281
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17933690 470 ---VFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIENTI 532
Cdd:cd05934 282 gwgFFKGYYNMPEATAEAMRNG-WFHTGDLGYRDADGFFYFVDRKKD-MIRRRGENISSAEVERAI 345
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
47-550 |
2.77e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 122.80 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 47 SVPGLLKRTVNNYGDYPALrtkngkngY---HTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEwFYSAMGAIH 123
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPAL--------DffgATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQ-HIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 124 ARGIIA----GIYTtnsADAVQHVLESSHAQIVVVDDaKQMDKIHAIRDK--------------LPKLK-AAIQIqePYS 184
Cdd:PRK05605 104 RLGAVVvehnPLYT---AHELEHPFEDHGARVAIVWD-KVAPTVERLRRTtpletivsvnmiaaMPLLQrLALRL--PIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 185 PYLKKED-------GYYRWSEIES---MNVSDVEDQYMTRLENVAInecccLVYTSGTVGMPKGVMLSHDNITFDVRGIV 254
Cdd:PRK05605 178 ALRKARAaltgpapGTVPWETLVDaaiGGDGSDVSHPRPTPDDVAL-----ILYTSGTTGKPKGAQLTHRNLFANAAQGK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 255 KAMDRVVVGAESIVSYLPLSHVAAQTVdiytcafvagCIWFADkdALKGTLV-----------KSLQDARPTRFMGVPRV 323
Cdd:PRK05605 253 AWVPGLGDGPERVLAALPMFHAYGLTL----------CLTLAV--SIGGELVllpapdidlilDAMKKHPPTWLPGVPPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 324 YEKFQErmvavasssgslkkmlASWAKGITLKhymvsqgkssgGFRYKIakslimskvkqalgfdrvltlaSAAAPMSPE 403
Cdd:PRK05605 321 YEKIAE----------------AAEERGVDLS-----------GVRNAF----------------------SGAMALPVS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 404 TKKYFLSLDL-KIVDAFGMSETAgchTICLPDSVGLN----TIGKTLPGCESKFINKD------ANGH-GELCIRGRHVF 471
Cdd:PRK05605 352 TVELWEKLTGgLLVEGYGLTETS---PIIVGNPMSDDrrpgYVGVPFPDTEVRIVDPEdpdetmPDGEeGELLVRGPQVF 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17933690 472 MGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTIkKELDAISNAFLVGEQRK 550
Cdd:PRK05605 429 KGYWNRPEETAKSFLDG-WFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEEVL-REHPGVEDAAVVGLPRE 504
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
221-546 |
2.15e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 120.16 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 221 NECCCLVYTSGTVGMPKGVMLSHDNItfdVRGIVKAMDRVVVGAESIVsyLPLSHVAAQTVDIYTCAFVAgciwfadkdA 300
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTL---MANIVPYAERLGLGADDVI--LMASPMAHQTGFMYGLMMPV---------M 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 301 LKGTLVksLQDA-RPTRFMGVPRvyekfQERMVAVASSSGSLKKMLAswakgiTLKHymvsQGKSSGGFRykiakslims 379
Cdd:PRK13295 263 LGATAV--LQDIwDPARAAELIR-----TEGVTFTMASTPFLTDLTR------AVKE----SGRPVSSLR---------- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 380 kvkqalgfdrvlTLASAAAPMSP---ETKKYFLSLdlKIVDAFGMSETAGCHTICL--PDSVGLNTIGKTLPGCESKFIN 454
Cdd:PRK13295 316 ------------TFLCAGAPIPGalvERARAALGA--KIVSAWGMTENGAVTLTKLddPDERASTTDGCPLPGVEVRVVD 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 455 KD-----ANGHGELCIRGRHVFMGYIDNKEKTeeSLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIE 529
Cdd:PRK13295 382 ADgaplpAGQIGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEIE 458
|
330
....*....|....*..
gi 17933690 530 NTIKKELdAISNAFLVG 546
Cdd:PRK13295 459 ALLYRHP-AIAQVAIVA 474
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
51-546 |
8.15e-28 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 118.29 E-value: 8.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 51 LLKRTVNNYGDYPALRTKNGKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYsAMGAIHARGIIAG 130
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI-AMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 131 IYTTN-SADAVQHVLESSHAQIVVVDDA--------KQMDKIHAIRDKLPKLKAAIQIQEPYSPYlkKEDGYYRWSEIES 201
Cdd:COG0365 93 PVFPGfGAEALADRIEDAEAKVLITADGglrggkviDLKEKVDEALEELPSLEHVIVVGRTGADV--PMEGDLDWDELLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 202 MNVSDVEDQYMTRlenvaiNECCCLVYTSGTVGMPKGVMLSHDNI----------TFDVR-GivkamDRV--------VV 262
Cdd:COG0365 171 AASAEFEPEPTDA------DDPLFILYTSGTTGKPKGVVHTHGGYlvhaattakyVLDLKpG-----DVFwctadigwAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 263 GAESIVsYLPLSHVAaqTVDIYtcafvAGCIWFADKDAlkgtLVKSLQDARPTRFMGVPRVYekfqeRMvavasssgsLK 342
Cdd:COG0365 240 GHSYIV-YGPLLNGA--TVVLY-----EGRPDFPDPGR----LWELIEKYGVTVFFTAPTAI-----RA---------LM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 343 KMLASWAKGITLkhymvsqgkssggfrykiakslimSKVKqalgfdrvlTLASAAAPMSPET-KKYFLSLDLKIVDAFGM 421
Cdd:COG0365 294 KAGDEPLKKYDL------------------------SSLR---------LLGSAGEPLNPEVwEWWYEAVGVPIVDGWGQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 422 SETAGCHTICLP-DSVGLNTIGKTLPGCESKFInkDANGH-------GELCIRGRH--VFMGYIDNKEKTEESLDDDC-- 489
Cdd:COG0365 341 TETGGIFISNLPgLPVKPGSMGKPVPGYDVAVV--DEDGNpvppgeeGELVIKGPWpgMFRGYWNDPERYRETYFGRFpg 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 17933690 490 WLHSGDLGFVDDKGYVSLTGRSKEIIITAgGENIPPVHIENTIkKELDAISNAFLVG 546
Cdd:COG0365 419 WYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESAL-VSHPAVAEAAVVG 473
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
47-546 |
6.97e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 115.03 E-value: 6.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 47 SVPGLLKRTVNNYGDYPALRtkngkNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNC----AEWFYSAM-GA 121
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALV-----FGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSdayaLLWLACARaGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 122 IHargiIAGIYTTNSADaVQHVLESSHAQIVVVDDAkQMDKIHAIRDKLPKLKAAIQIQEPYSPYLKKEDGYYRWSEIES 201
Cdd:PRK08316 87 VH----VPVNFMLTGEE-LAYILDHSGARAFLVDPA-LAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 202 MNVSDVEdqymtrlenVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvvVGAESI-VSYLPLSHVAAQT 280
Cdd:PRK08316 161 VAEPDVE---------LADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD---MSADDIpLHALPLYHCAQLD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 281 VDIYTCAFVAGCIWFADKDALkGTLVKSLQDARPTRFMGVPRVYekfqermVAVASSSGSLKKMLASWAKGitlkHYmvs 360
Cdd:PRK08316 229 VFLGPYLYVGATNVILDAPDP-ELILRTIEAERITSFFAPPTVW-------ISLLRHPDFDTRDLSSLRKG----YY--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 361 qGKSsggfrykiakslIMSKvkqalgfdRVLTLASAAAPmspetkkyflslDLKIVDAFGMSETAGCHTICLPD------ 434
Cdd:PRK08316 294 -GAS------------IMPV--------EVLKELRERLP------------GLRFYNCYGQTEIAPLATVLGPEehlrrp 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 435 -SVG---LNTigktlpgcESKFINKDAN----GH-GELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYV 505
Cdd:PRK08316 341 gSAGrpvLNV--------ETRVVDDDGNdvapGEvGEIVHRSPQLMLGYWDDPEKTAEAFRGG-WFHSGDLGVMDEEGYI 411
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 17933690 506 SLTGRSKEIIITaGGENIPPVHIENTIkKELDAISNAFLVG 546
Cdd:PRK08316 412 TVVDRKKDMIKT-GGENVASREVEEAL-YTHPAVAEVAVIG 450
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
226-546 |
1.54e-26 |
|
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: 111.05 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNitfDVRGIVKAMDRVVVGAESivSYL---PLSHVAAqtvdiYTCAFVAGCIWFA------ 296
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQ---TLRAAAAWADCADLTEDD--RYLiinPFFHTFG-----YKAGIVACLLTGAtvvpva 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 297 --DKDALkgtlVKSLQDARPTRFMGVPRVYEkfqermvAVASSSGSLKKMLASWAKGITlkhymvsqGKSSggfrykIAK 374
Cdd:cd17638 75 vfDVDAI----LEAIERERITVLPGPPTLFQ-------SLLDHPGRKKFDLSSLRAAVT--------GAAT------VPV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 375 SLImSKVKQALGFDRVLTlasaaapmspetkkyflsldlkivdAFGMSEtAGCHTICLP-DSVGL--NTIGKTLPGCESK 451
Cdd:cd17638 130 ELV-RRMRSELGFETVLT-------------------------AYGLTE-AGVATMCRPgDDAETvaTTCGRACPGFEVR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 452 FInkdanGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIItAGGENIPPVHIENT 531
Cdd:cd17638 183 IA-----DDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGA 256
|
330
....*....|....*
gi 17933690 532 IkKELDAISNAFLVG 546
Cdd:cd17638 257 L-AEHPGVAQVAVIG 270
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
35-532 |
1.97e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 113.93 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 35 MAKDGIGAEEPISVPGLLKRTVNNYGDYPALRTKNGkngyhTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAE- 113
Cdd:PRK06188 1 QATMADLLHSGATYGHLLVSALKRYPDRPALVLGDT-----RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 114 WFysAMGAIHARGI-IAGIYTTNSADAVQHVLESSHAQIVVVDDAKQMDKIHAIRDKLPKLKAAIQIQE-PYSPYLkked 191
Cdd:PRK06188 76 LM--AIGAAQLAGLrRTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVERALALLARVPSLKHVLTLGPvPDGVDL---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 192 gyyrWSEIESMNVsdvedqymTRLENVAI-NECCCLVYTSGTVGMPKGVMLSHDNITfdvrgivkAMDRVVVGAESI--- 267
Cdd:PRK06188 150 ----LAAAAKFGP--------APLVAAALpPDIAGLAYTGGTTGKPKGVMGTHRSIA--------TMAQIQLAEWEWpad 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 268 VSYL---PLSHVAAqtvdiytcAFVAGCIWfadkdalKGTLVKSLQDARPTRFMgvpRVYEKfqERMVAVasssgslkkM 344
Cdd:PRK06188 210 PRFLmctPLSHAGG--------AFFLPTLL-------RGGTVIVLAKFDPAEVL---RAIEE--QRITAT---------F 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 345 LASwakgiTLKHYMVSQGKSSggfrykiakslimskvkqalgfDRVL----TLASAAAPMSP----ETKKYFLSLdlkIV 416
Cdd:PRK06188 261 LVP-----TMIYALLDHPDLR----------------------TRDLssleTVYYGASPMSPvrlaEAIERFGPI---FA 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 417 DAFGMSETAGCHTI------CLPDSVGLNTIGKTLPGCESKFInkDANGH-------GELCIRGRHVFMGYIDNKEKTEE 483
Cdd:PRK06188 311 QYYGQTEAPMVITYlrkrdhDPDDPKRLTSCGRPTPGLRVALL--DEDGRevaqgevGEICVRGPLVMDGYWNRPEETAE 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 17933690 484 SLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTI 532
Cdd:PRK06188 389 AFRDG-WLHTGDVAREDEDGFYYIVDRKKDMIVT-GGFNVFPREVEDVL 435
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
44-545 |
3.54e-26 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 113.15 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 44 EPISVPGLLKRTVNNYGD-YPALRTKNGknGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVgVLAFNCAEWFYSAM-GA 121
Cdd:cd05906 8 APRTLLELLLRAAERGPTkGITYIDADG--SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEDFIPAFwAC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 122 IHArGIIAGIYTTNSADAvqhvlESSHAqivvvddAKQMDKIHAIRDKlPKLKAAIQIQEPYSPyLKKEDGYYRWSEIES 201
Cdd:cd05906 85 VLA-GFVPAPLTVPPTYD-----EPNAR-------LRKLRHIWQLLGS-PVVLTDAELVAEFAG-LETLSGLPGIRVLSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 202 MNVSDVEDQYM---TRLENVAInecccLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVvvGAESIVSYLPLSHVAA 278
Cdd:cd05906 150 EELLDTAADHDlpqSRPDDLAL-----LMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLT--PQDVFLNWVPLDHVGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 279 qTVDIYTCAFVAGC--IWFADKDALkgtlvkslqdARPTRFMGVprvyekFQERMVAVASSSGSLKKMLASWAKGITLKH 356
Cdd:cd05906 223 -LVELHLRAVYLGCqqVHVPTEEIL----------ADPLRWLDL------IDRYRVTITWAPNFAFALLNDLLEEIEDGT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 357 YMVSqgkssgGFRYkiakslimskvkqalgfdrvltLASAAAPMSPETKKYFLSL-------DLKIVDAFGMSET-AGC- 427
Cdd:cd05906 286 WDLS------SLRY----------------------LVNAGEAVVAKTIRRLLRLlepyglpPDAIRPAFGMTETcSGVi 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 428 --HTICLPDSVGLNT---IGKTLPGCESKFINKDANGH-----GELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLG 497
Cdd:cd05906 338 ysRSFPTYDHSQALEfvsLGRPIPGVSMRIVDDEGQLLpegevGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 17933690 498 FVDDkGYVSLTGRSKEIIITaGGENIPPVHIENTIkKELDAISNAFLV 545
Cdd:cd05906 418 FLDN-GNLTITGRTKDTIIV-NGVNYYSHEIEAAV-EEVPGVEPSFTA 462
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
61-546 |
6.51e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 111.90 E-value: 6.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 61 DYPALRTKNgkngyHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAV 140
Cdd:PRK06145 17 DRAALVYRD-----QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 141 QHVLESSHAQIVVVDDakQMDKIHAIRDKLPKLKAAIQIQ--------EPYSP-YLKKEDGYYRwseiesmnvsdvedqy 211
Cdd:PRK06145 92 AYILGDAGAKLLLVDE--EFDAIVALETPKIVIDAAAQADsrrlaqggLEIPPqAAVAPTDLVR---------------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 212 mtrlenvainecccLVYTSGTVGMPKGVMLSHDNI---TFD---VRGIVKAMDRVVVGaesivsylPLSHVAAqtVDIYT 285
Cdd:PRK06145 154 --------------LMYTSGTTDRPKGVMHSYGNLhwkSIDhviALGLTASERLLVVG--------PLYHVGA--FDLPG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 286 CAFVAgciwfadkdaLKGTLvkslqdarptrfmgvpRVYEKFQERMVAVASSSgslKKMLASWAKGITLKHYMVSQGKss 365
Cdd:PRK06145 210 IAVLW----------VGGTL----------------RIHREFDPEAVLAAIER---HRLTCAWMAPVMLSRVLTVPDR-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 366 ggFRYKIAKslimskvkqalgfdrvLTLASAAAPMSPETK-KYFLSL--DLKIVDAFGMSETAGCHTICLP----DSVGl 438
Cdd:PRK06145 259 --DRFDLDS----------------LAWCIGGGEKTPESRiRDFTRVftRARYIDAYGLTETCSGDTLMEAgreiEKIG- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 439 nTIGKTLPGCESKFINKD-----ANGHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKE 513
Cdd:PRK06145 320 -STGRALAHVEIRIADGAgrwlpPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-WFRSGDVGYLDEEGFLYLTDRKKD 397
|
490 500 510
....*....|....*....|....*....|...
gi 17933690 514 IIITaGGENIPPVHIENTIkKELDAISNAFLVG 546
Cdd:PRK06145 398 MIIS-GGENIASSEVERVI-YELPEVAEAAVIG 428
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
226-547 |
7.04e-26 |
|
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: 110.51 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMdrvvvGA---ESIVSYLPLSHVAAQTVdiytcafvagciwfadkdalk 302
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNHWWSAIGSALNL-----GLtedDNWLCALPLFHISGLSI--------------------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 303 gtLVKSLqdarptrFMGVP-RVYEKFQERMVAVASSSGSL------KKMLASWAKgITLKHYmvsqgksSGGFRykiaks 375
Cdd:cd05912 136 --LMRSV-------IYGMTvYLVDKFDAEQVLHLINSGKVtiisvvPTMLQRLLE-ILGEGY-------PNNLR------ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 376 LIMskvkqaLGfdrvltlasaAAPMSPETKKYFLSLDLKIVDAFGMSETagCHTIC------LPDSVGlnTIGKTLPGCE 449
Cdd:cd05912 193 CIL------LG----------GGPAPKPLLEQCKEKGIPVYQSYGMTET--CSQIVtlspedALNKIG--SAGKPLFPVE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 450 SKFINKD--ANGHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIItAGGENIPPVH 527
Cdd:cd05912 253 LKIEDDGqpPYEVGEILLKGPNVTKGYLNRPDATEESFENG-WFKTGDIGYLDEEGFLYVLDRRSDLII-SGGENIYPAE 330
|
330 340
....*....|....*....|
gi 17933690 528 IENTIkKELDAISNAFLVGE 547
Cdd:cd05912 331 IEEVL-LSHPAIKEAGVVGI 349
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
59-529 |
5.71e-25 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 109.30 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 59 YGDYPALrtKNGKNGyHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHaRGII---AGIYTTN 135
Cdd:PLN02246 36 FSDRPCL--IDGATG-RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR-RGAVtttANPFYTP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 136 SADAVQhvLESSHAQIVVVDdAKQMDKI--HAIRDKLPklkaAIQIQEPyspylkkEDGYYRWSEIESMNVSDVEDqymt 213
Cdd:PLN02246 112 AEIAKQ--AKASGAKLIITQ-SCYVDKLkgLAEDDGVT----VVTIDDP-------PEGCLHFSELTQADENELPE---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 214 rlENVAINECCCLVYTSGTVGMPKGVMLSHdnitfdvRGIVKAMDRVVVGA---------ESIVSYLPLSHVAAQTvDIY 284
Cdd:PLN02246 174 --VEISPDDVVALPYSSGTTGLPKGVMLTH-------KGLVTSVAQQVDGEnpnlyfhsdDVILCVLPMFHIYSLN-SVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 285 TCAFVAGC-IWFADKDALkGTLVKSLQDARPTRFMGVPRVyekfqerMVAVASSSGSLKKMLASwakgitlkhymvsqgk 363
Cdd:PLN02246 244 LCGLRVGAaILIMPKFEI-GALLELIQRHKVTIAPFVPPI-------VLAIAKSPVVEKYDLSS---------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 364 ssggfrykiakslimskvkqalgfdrVLTLASAAAPMSPETKKYFLSldlKIVDA-----FGMSETAGCHTICL-----P 433
Cdd:PLN02246 300 --------------------------IRMVLSGAAPLGKELEDAFRA---KLPNAvlgqgYGMTEAGPVLAMCLafakeP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 434 DSVGLNTIGKTLPGCESKFINKDA------NGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSL 507
Cdd:PLN02246 351 FPVKSGSCGTVVRNAELKIVDPETgaslprNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFI 430
|
490 500
....*....|....*....|..
gi 17933690 508 TGRSKEIIITAGGEnIPPVHIE 529
Cdd:PLN02246 431 VDRLKELIKYKGFQ-VAPAELE 451
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
40-532 |
1.13e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 108.81 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 40 IGAEEPISVPGLLKRTVNNYGDYPALrTKNGKngyhTVTYKQYEQKVHQVAKAFI-KLGLEEHHSVGVLAFNCAEWFYSA 118
Cdd:PRK08751 19 IDLEQFRTVAEVFATSVAKFADRPAY-HSFGK----TITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIAT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 119 MGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVDD--AKQMDKIHA-----------IRDKLPKLKAAIQiqEPYSP 185
Cdd:PRK08751 94 FGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDnfGTTVQQVIAdtpvkqvittgLGDMLGFPKAALV--NFVVK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 186 YLKKEDGYYRWS-EIESMNVSDVEDQYMTRLENVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGI---VKAMDRVV 261
Cdd:PRK08751 172 YVKKLVPEYRINgAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAhqwLAGTGKLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 262 VGAESIVSYLPLSHVAAQTVDIYTCAFVAGCIWFADKDALKGTLVKSLQDARPTRFMGVPRVYEKFQermvavasssgsl 341
Cdd:PRK08751 252 EGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLL------------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 342 kkmlaswakgitlkhymvsqgkSSGGFrykiaKSLIMSKVKQALGFDRVLTLASAaapmspETKKYFLSLDLkiVDAFGM 421
Cdd:PRK08751 319 ----------------------NTPGF-----DQIDFSSLKMTLGGGMAVQRSVA------ERWKQVTGLTL--VEAYGL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 422 SET--AGC-HTICLPDSVGlnTIGKTLPGCESKFinKDANGH-------GELCIRGRHVFMGYIDNKEKTEESLDDDCWL 491
Cdd:PRK08751 364 TETspAACiNPLTLKEYNG--SIGLPIPSTDACI--KDDAGTvlaigeiGELCIKGPQVMKGYWKRPEETAKVMDADGWL 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 17933690 492 HSGDLGFVDDKGYVSLTGRSKEIIITAGGeNIPPVHIENTI 532
Cdd:PRK08751 440 HTGDIARMDEQGFVYIVDRKKDMILVSGF-NVYPNEIEDVI 479
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
40-532 |
2.49e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 107.54 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 40 IGAEEPISVPGLLKRTVNNYGDYPALrTKNGKngyhTVTYKQYEQKVHQVAkAFI--KLGLEEHHSVGVLAFNCAEWFYS 117
Cdd:PRK05677 18 INPDEYPNIQAVLKQSCQRFADKPAF-SNLGK----TLTYGELYKLSGAFA-AWLqqHTDLKPGDRIAVQLPNVLQYPVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 118 AMGAIHArGIIagIYTTN---SADAVQHVLESSHAQIVVV--DDAKQMDKI-------HAI----RDKLPKLK-----AA 176
Cdd:PRK05677 92 VFGAMRA-GLI--VVNTNplyTAREMEHQFNDSGAKALVClaNMAHLAEKVlpktgvkHVIvtevADMLPPLKrllinAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 177 IQiqepyspYLKKEDGYYrwSEIESMNVSDVEDQ---YMTRLENVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGi 253
Cdd:PRK05677 169 VK-------HVKKMVPAY--HLPQAVKFNDALAKgagQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 254 VKAM--DRVVVGAESIVSYLPLSHVAAQTVDiytCAF--VAG--CIWFADKDALKGtLVKSLQDARPTRFMGVPRVYekf 327
Cdd:PRK05677 239 CRALmgSNLNEGCEILIAPLPLYHIYAFTFH---CMAmmLIGnhNILISNPRDLPA-MVKELGKWKFSGFVGLNTLF--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 328 qermVAVASSSGslkkmlaswakgitlkhymvsqgkssggFRykiakSLIMSKVKQALGFDRVLTLASAaapmspetKKY 407
Cdd:PRK05677 312 ----VALCNNEA----------------------------FR-----KLDFSALKLTLSGGMALQLATA--------ERW 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 408 FLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKDAN----GH-GELCIRGRHVFMGYIDNKEKTE 482
Cdd:PRK05677 347 KEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNelplGEvGELCVKGPQVMKGYWQRPEATD 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 17933690 483 ESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGeNIPPVHIENTI 532
Cdd:PRK05677 427 EILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGF-NVYPNELEDVL 475
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
77-576 |
3.42e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 107.04 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 77 VTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVV--- 153
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcld 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 154 --------VDDAKQMDKIHAIR--DKLPKLKAAIQiqepysPYLKKEDG--YYRWSEIESMNV-SDVEDQYMTRLENVAI 220
Cdd:PRK06710 130 lvfprvtnVQSATKIEHVIVTRiaDFLPFPKNLLY------PFVQKKQSnlVVKVSESETIHLwNSVEKEVNTGVEVPCD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 221 --NECCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESIVSYLPLSHVAAQTVDIYTCAFVAGCIWFADK 298
Cdd:PRK06710 204 peNDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 299 DALKgTLVKSLQDARPTRFMGVPRVYekfqermVAVASSSgslkkmlaswakgiTLKHYMVSQgkssggfrykiakslim 378
Cdd:PRK06710 284 FDMK-MVFEAIKKHKVTLFPGAPTIY-------IALLNSP--------------LLKEYDISS----------------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 379 skvkqalgfdrVLTLASAAAPMSPETKKYFLSLDL-KIVDAFGMSETAGC-HTICLPDSVGLNTIGKTLPGCESKFINKD 456
Cdd:PRK06710 325 -----------IRACISGSAPLPVEVQEKFETVTGgKLVEGYGLTESSPVtHSNFLWEKRVPGSIGVPWPDTEAMIMSLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 457 ANGH------GELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIItAGGENIPPVHIEN 530
Cdd:PRK06710 394 TGEAlppgeiGEIVVKGPQIMKGYWNKPEETAAVLQDG-WLHTGDVGYMDEDGFFYVKDRKKDMIV-ASGFNVYPREVEE 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 17933690 531 TIkKELDAISNAFLVGEQRKY----LTVLITLKtEVDKDSGEPLDELSHE 576
Cdd:PRK06710 472 VL-YEHEKVQEVVTIGVPDPYrgetVKAFVVLK-EGTECSEEELNQFARK 519
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
226-537 |
7.01e-24 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 103.49 E-value: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGaESIVSYLPLSHVAaQTVDIYTCAFVAG-CIWFADKDALKgT 304
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVG-DVTYLPLPATHIG-GLWWILTCLIHGGlCVTGGENTTYK-S 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 305 LVKSLQDARPTRFMGVPrvyekfqermvavasssgslkkmlaswakgiTLKHYMVSQGKSSggfrYKIAKSLIMSKVkqa 384
Cdd:cd17635 83 LFKILTTNAVTTTCLVP-------------------------------TLLSKLVSELKSA----NATVPSLRLIGY--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 385 lGFDRVLTLASAAAPMSPETKkyflsldlkIVDAFGMSETAGchTICLP---DSVGLNTIGKTLPGCESKFINKDA---- 457
Cdd:cd17635 125 -GGSRAIAADVRFIEATGLTN---------TAQVYGLSETGT--ALCLPtddDSIEINAVGRPYPGVDVYLAATDGiagp 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 458 -NGHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIItAGGENIPPVHIENTIKKEL 536
Cdd:cd17635 193 sASFGTIWIKSPANMLGYWNNPERTAEVLIDG-WVNTGDLGERREDGFLFITGRSSESIN-CGGVKIAPDEVERIAEGVS 270
|
.
gi 17933690 537 D 537
Cdd:cd17635 271 G 271
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
51-532 |
1.10e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 105.51 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 51 LLKRTVNNYGDYPALrtkngKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAg 130
Cdd:PRK07470 12 FLRQAARRFPDRIAL-----VWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 131 iyTTN---SADAVQHVLESSHAQIVVVDDAKQmDKIHAIRDKLPKLKAAIQIQEPyspylKKEDGYyrwseiESMnvsdV 207
Cdd:PRK07470 86 --PTNfrqTPDEVAYLAEASGARAMICHADFP-EHAAAVRAASPDLTHVVAIGGA-----RAGLDY------EAL----V 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 208 EDQYMTRLENVAI--NECCCLVYTSGTVGMPKGVMLSHDNITF-------DVRGIVKAMDRVVVGAesivsylPLSHVA- 277
Cdd:PRK07470 148 ARHLGARVANAAVdhDDPCWFFFTSGTTGRPKAAVLTHGQMAFvitnhlaDLMPGTTEQDASLVVA-------PLSHGAg 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 278 ----------AQTVDIYTCAFVAGCIWfadkdalkgTLVkslQDARPTRFMGVPrvyekfqermvavasssgSLKKMLAs 347
Cdd:PRK07470 221 ihqlcqvargAATVLLPSERFDPAEVW---------ALV---ERHRVTNLFTVP------------------TILKMLV- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 348 wakgitlKHYMVSQGKSSGgFRYKIakslimskvkqalgfdrvltlaSAAAPMSPETKKYFLS-LDLKIVDAFGMSETAG 426
Cdd:PRK07470 270 -------EHPAVDRYDHSS-LRYVI----------------------YAGAPMYRADQKRALAkLGKVLVQYFGLGEVTG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 427 CHTIcLP---------DSVGLNTIGKTLPGCESKFinKDANGH-------GELCIRGRHVFMGYIDNKEKTEESLDDDcW 490
Cdd:PRK07470 320 NITV-LPpalhdaedgPDARIGTCGFERTGMEVQI--QDDEGRelppgetGEICVIGPAVFAGYYNNPEANAKAFRDG-W 395
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 17933690 491 LHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTI 532
Cdd:PRK07470 396 FRTGDLGHLDARGFLYITGRASDMYIS-GGSNVYPREIEEKL 436
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
225-532 |
2.79e-23 |
|
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: 103.29 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 225 CLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHVAAQTVdiYTCAFVAGC-IWFADKDALKG 303
Cdd:cd05922 121 LLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG--ITADDRALTVLPLSYDYGLSV--LNTHLLRGAtLVLTNDGVLDD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 304 TLVKSLQDARPTRFMGVPRVYEkfqermvavasssgslkkMLAS--WAKgITLKHymvsqgkssggFRYkiakslimskv 381
Cdd:cd05922 197 AFWEDLREHGATGLAGVPSTYA------------------MLTRlgFDP-AKLPS-----------LRY----------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 382 kqalgfdrvltLASAAAPMSPETKKYFLSL--DLKIVDAFGMSETAGCHTICLPDSVG--LNTIGKTLPGCESKFINKD- 456
Cdd:cd05922 236 -----------LTQAGGRLPQETIARLRELlpGAQVYVMYGQTEATRRMTYLPPERILekPGSIGLAIPGGEFEILDDDg 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 457 ---ANGH-GELCIRGRHVFMGYI-DNKEKTEESLDDDCwLHSGDLGFVDDKGYVSLTGRSKEIIITAgGENIPPVHIENT 531
Cdd:cd05922 305 tptPPGEpGEIVHRGPNVMKGYWnDPPYRRKEGRGGGV-LHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAA 382
|
.
gi 17933690 532 I 532
Cdd:cd05922 383 A 383
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
51-602 |
3.87e-23 |
|
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: 103.60 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 51 LLKRTVNNYGDYPALRTKNGkngyhTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHArGIIA- 129
Cdd:cd05959 9 VDLNLNEGRGDKTAFIDDAG-----SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRA-GIVPv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 130 GIYTTNSADAVQHVLESSHAQIVVVDDAKqmdkihairdkLPKLKAAIQIQEPYSPYLKKEDGyyRWSEIESMNVSDVED 209
Cdd:cd05959 83 PVNTLLTPDDYAYYLEDSRARVVVVSGEL-----------APVLAAALTKSEHTLVVLIVSGG--AGPEAGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 210 QYMTRLENVAI--NECCCLVYTSGTVGMPKGVMLSHDNITFD----VRGIVK-AMDRVVVGAESIV--------SYLPLS 274
Cdd:cd05959 150 AEAEQLKPAAThaDDPAFWLYSSGSTGRPKGVVHLHADIYWTaelyARNVLGiREDDVCFSAAKLFfayglgnsLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 275 hvaaqtvdiytcaFVAGCIWFADKDALKgTLVKSLQDARPTRFMGVPRVYekfqermvavASssgslkkMLASwakgitl 354
Cdd:cd05959 230 -------------VGATTVLMPERPTPA-AVFKRIRRYRPTVFFGVPTLY----------AA-------MLAA------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 355 khymvsqgkssggfrykiakslimsKVKQALGFDRVLTLASAAAPMSPETKKYFLSL-DLKIVDAFGMSETAgcHTIC-- 431
Cdd:cd05959 272 -------------------------PNLPSRDLSSLRLCVSAGEALPAEVGERWKARfGLDILDGIGSTEML--HIFLsn 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 432 LPDSVGLNTIGKTLPGCESKFINKDAN-----GHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVS 506
Cdd:cd05959 325 RPGRVRYGTTGKPVPGYEVELRDEDGGdvadgEPGELYVRGPSSATMYWNNRDKTRDTFQGE-WTRTGDKYVRDDDGFYT 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 507 LTGRSKEiIITAGGENIPPVHIENTIKKElDAISNAFLVG---EQRkyltvLITLKT-EVDKDSGEPLDELSHESSVWVK 582
Cdd:cd05959 404 YAGRADD-MLKVSGIWVSPFEVESALVQH-PAVLEAAVVGvedEDG-----LTKPKAfVVLRPGYEDSEALEEELKEFVK 476
|
570 580
....*....|....*....|
gi 17933690 583 SLGVEHKTVSDILAAGPCPK 602
Cdd:cd05959 477 DRLAPYKYPRWIVFVDELPK 496
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
224-548 |
4.07e-23 |
|
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: 100.87 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 224 CCLVYTSGTVGMPKGVMLSHDNITFDVRGivkAMDRVVVGAE--SIVSyLPLSHVAAQTVdIYTCAFVAGCIWFADKDAL 301
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAG---LHSRLGFGGGdsWLLS-LPLYHVGGLAI-LVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 302 kgtLVKSLQDARPTRFMGVPRvyekfqermvavasssgSLKKMLASwakgitlkhymvSQGKSSggfrykiakslimskv 381
Cdd:cd17630 78 ---LAEDLAPPGVTHVSLVPT-----------------QLQRLLDS------------GQGPAA---------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 382 kqALGFDRVLtlaSAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKfINKDanghG 461
Cdd:cd17630 110 --LKSLRAVL---LGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELR-IVED----G 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 462 ELCIRGRHVFMGYIDNKEktEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTIKKElDAISN 541
Cdd:cd17630 180 EIWVGGASLAMGYLRGQL--VPEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAALAAH-PAVRD 255
|
....*..
gi 17933690 542 AFLVGEQ 548
Cdd:cd17630 256 AFVVGVP 262
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
225-539 |
4.29e-23 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 103.42 E-value: 4.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 225 CLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAM----DRVVVGAesivsyLPLSHVAAQTVDIYtCAFVAGC--IWFA-- 296
Cdd:PRK07514 160 AILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWrftpDDVLIHA------LPIFHTHGLFVATN-VALLAGAsmIFLPkf 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 297 DKDALKGTLvkslqdARPTRFMGVPRVYEkfqeRMVAVAsssgslkkmlaswakgitlkhymvsqgkssggfrykiaksl 376
Cdd:PRK07514 233 DPDAVLALM------PRATVMMGVPTFYT----RLLQEP----------------------------------------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 377 imskvkqalGFDRVLT-----LASAAAPMSPETKKYFLS-LDLKIVDAFGMSET-------------AGchticlpdsvg 437
Cdd:PRK07514 262 ---------RLTREAAahmrlFISGSAPLLAETHREFQErTGHAILERYGMTETnmntsnpydgerrAG----------- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 438 lnTIGKTLPGCESKFINKDAN---GHGE---LCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRS 511
Cdd:PRK07514 322 --TVGFPLPGVSLRVTDPETGaelPPGEigmIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRG 399
|
330 340
....*....|....*....|....*...
gi 17933690 512 KEIIITaGGENIPPVHIENtikkELDAI 539
Cdd:PRK07514 400 KDLIIS-GGYNVYPKEVEG----EIDEL 422
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
78-546 |
1.55e-22 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 102.18 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 78 TYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNcAEWFYSAMGAI-HARGIIAGIYTTNSADAVQHVLESSHAQIVVVDD 156
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALN-SDLYLEWLLAVaCAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 157 AKQMDKIHAIRDKLPKLKAAIQIQEPYSPYLKKEDGYYRWSEIESMNVSDVEDQYMTRLENVAInecccLVYTSGTVGMP 236
Cdd:PLN02860 113 TCSSWYEELQNDRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLKQRALGTTELDYAWAPDDAVL-----ICFTSGTTGRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 237 KGVMLSHDNItfdvrgIVKAMDRV-VVGAESIVSYL---PLSHVAAQTVDIyTCAFVAGCIWFADK-DAlkGTLVKSLQD 311
Cdd:PLN02860 188 KGVTISHSAL------IVQSLAKIaIVGYGEDDVYLhtaPLCHIGGLSSAL-AMLMVGACHVLLPKfDA--KAALQAIKQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 312 ARPTRFMGVPRvyekfqerMVAVASSSGSLKKmlaSWAKGITLKHYMVSQGKSSGGFRYKIAKSLIMSKVKQALGfdrvl 391
Cdd:PLN02860 259 HNVTSMITVPA--------MMADLISLTRKSM---TWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYG----- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 392 tLASAAAPMSpetkkyFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNT-IGKTLPGCESKfINKDANGH-GELCIRGRH 469
Cdd:PLN02860 323 -MTEACSSLT------FMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAPHVELK-IGLDESSRvGRILTRGPH 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17933690 470 VFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTIKKElDAISNAFLVG 546
Cdd:PLN02860 395 VMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKT-GGENVYPEEVEAVLSQH-PGVASVVVVG 469
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
47-546 |
2.04e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 101.50 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 47 SVPGLLKRTVNNYGDYPALrtkngKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARG 126
Cdd:PRK07798 4 NIADLFEAVADAVPDRVAL-----VCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 127 IIAGI---YTtnsADAVQHVLESSHAQiVVVDDAKQMDKIHAIRDKLPKLKAAIQIQEPYSPYLkkEDGYYRWSEIESMN 203
Cdd:PRK07798 79 VPVNVnyrYV---EDELRYLLDDSDAV-ALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSGNDL--LPGAVDYEDALAAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 204 VSDV-------EDQYMtrlenvaineccclVYTSGTVGMPKGVMLSHDNITF------------DVRGIVKAMDRVVVGA 264
Cdd:PRK07798 153 SPERdfgerspDDLYL--------------LYTGGTTGMPKGVMWRQEDIFRvllggrdfatgePIEDEEELAKRAAAGP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 265 ESIVSYL-PLSHVAAQTVdIYTCAFVAGCIWFADKDALkgtlvkslqDARptrfmgvpRVYEKFQERMVAVASSSGS--L 341
Cdd:PRK07798 219 GMRRFPApPLMHGAGQWA-AFAALFSGQTVVLLPDVRF---------DAD--------EVWRTIEREKVNVITIVGDamA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 342 KKMLASWAKGitlKHYMVSqgkssggfrykiakSLimskvkqalgfdrvLTLASAAAPMSPETKKYFLSL--DLKIVDAF 419
Cdd:PRK07798 281 RPLLDALEAR---GPYDLS--------------SL--------------FAIASGGALFSPSVKEALLELlpNVVLTDSI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 420 GMSETAGCHTIcLPDSVGLNTIGKTL-PGCESKFINKDAN----GHGELCI--RGRHVFMGYIDNKEKTEESL---DDDC 489
Cdd:PRK07798 330 GSSETGFGGSG-TVAKGAVHTGGPRFtIGPRTVVLDEDGNpvepGSGEIGWiaRRGHIPLGYYKDPEKTAETFptiDGVR 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 17933690 490 WLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTIKKElDAISNAFLVG 546
Cdd:PRK07798 409 YAIPGDRARVEADGTITLLGRGSVCINT-GGEKVFPEEVEEALKAH-PDVADALVVG 463
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
51-565 |
2.31e-22 |
|
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: 101.01 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 51 LLKRTVNNYGDYPALRTKNgkngyHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAG 130
Cdd:TIGR03098 5 LLEDAAARLPDATALVHHD-----RTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 131 IYTTNSADAVQHVLESSHAQIVVVDdAKQMDKIHAIRDKLPKLKAAIQIQEPYSPYLKKEDG-YYRWSEIESMNVSDved 209
Cdd:TIGR03098 80 INPLLKAEQVAHILADCNVRLLVTS-SERLDLLHPALPGCHDLRTLIIVGDPAHASEGHPGEePASWPKLLALGDAD--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 210 qymtRLENVAINECCCLVYTSGTVGMPKGVMLSHDNitfdvrgivkamdrVVVGAESIVSY------------LPLSHVA 277
Cdd:TIGR03098 156 ----PPHPVIDSDMAAILYTSGSTGRPKGVVLSHRN--------------LVAGAQSVATYlenrpddrllavLPLSFDY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 278 AQTVdiYTCAFVAGCIWFADKDALKGTLVKSLQDARPTRFMGVPRVyekfqermvavasssgslkkmlasWAKGITLKhy 357
Cdd:TIGR03098 218 GFNQ--LTTAFYVGATVVLHDYLLPRDVLKALEKHGITGLAAVPPL------------------------WAQLAQLD-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 358 mvsqgkssggFRYKIAKSLimskvkqalgfdRVLTLASAAAPMS---------PETKKYFLsldlkivdaFGMSEtAGCH 428
Cdd:TIGR03098 270 ----------WPESAAPSL------------RYLTNSGGAMPRAtlsrlrsflPNARLFLM---------YGLTE-AFRS 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 429 TICLPDSVGL--NTIGKTLPGCESKFINKDA-----NGHGELCIRGRHVFMGYIDNKEKTEESL------DDDCWLH--- 492
Cdd:TIGR03098 318 TYLPPEEVDRrpDSIGKAIPNAEVLVLREDGsecapGEEGELVHRGALVAMGYWNDPEKTAERFrplppfPGELHLPela 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 493 --SGDLGFVDDKGYVSLTGRSKEIIITAgGENIPPVHIENTIkKELDAISNAFLVGE------QRKYLTVLITLKTEVDK 564
Cdd:TIGR03098 398 vwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVA-YATGLVAEAVAFGVpdptlgQAIVLVVTPPGGEELDR 475
|
.
gi 17933690 565 D 565
Cdd:TIGR03098 476 A 476
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
228-529 |
6.65e-22 |
|
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: 97.94 E-value: 6.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 228 YTSGTVGMPKGVMLSHDNITFDvrGIVKAMDRVVVGAESIVSYLPLSHVAAQTVDIYTCAFVAGCIWFAD-----KDALK 302
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyrNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 303 GTLVKSLQDARPTRFMGVPRVYEKFQERMVAVASSSgslkkmlaswakgitlkhymvsqgkssggFRYKIakslimskvk 382
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAALLQVPVNADISS-----------------------------LRFAM---------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 383 qalgfdrvltlaSAAAPMSPETKKYFL-SLDLKIVDAFGMSETAGCHTICLPDS-VGLNTIGKTLPGCESKFINKDANGH 460
Cdd:cd05944 128 ------------SGAAPLPVELRARFEdATGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGLRLPYARVRIKVLDGVGR 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17933690 461 ----------GELCIRGRHVFMGYIDNkEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIE 529
Cdd:cd05944 196 llrdcapdevGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIR-GGHNIDPALIE 272
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
73-547 |
8.92e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 98.88 E-value: 8.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 73 GYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMgAIHARG-IIAGIYTTNSADAVQHVLESSHAQI 151
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIH-ALQQLGaVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 152 VVVDDakqmdkihairDKLPKLKAAIQIqepyspylkkedgyyRWSEIESMNVSDVEDQYMTRLENVAineccCLVYTSG 231
Cdd:PRK03640 103 LITDD-----------DFEAKLIPGISV---------------KFAELMNGPKEEAEIQEEFDLDEVA-----TIMYTSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 232 TVGMPKGVMLSHDNITFDVRGivKAMDRVVVGAESIVSYLPLSHVAAQTVdiytcafvagciwfadkdalkgtLVKSLqd 311
Cdd:PRK03640 152 TTGKPKGVIQTYGNHWWSAVG--SALNLGLTEDDCWLAAVPIFHISGLSI-----------------------LMRSV-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 312 arptrFMGVP-RVYEKFQERMVAVASSSGS----------LKKMLASWAKGitlkHYmvsqgksSGGFRykiakslimsk 380
Cdd:PRK03640 205 -----IYGMRvVLVEKFDAEKINKLLQTGGvtiisvvstmLQRLLERLGEG----TY-------PSSFR----------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 381 vkqalgfdrvlTLASAAAPMSPETKKYFLSLDLKIVDAFGMSETagCHTIC-LPDSVGLNTI---GKTLPGCESKfINKD 456
Cdd:PRK03640 258 -----------CMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTET--ASQIVtLSPEDALTKLgsaGKPLFPCELK-IEKD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 457 -----ANGHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENT 531
Cdd:PRK03640 324 gvvvpPFEEGEIVVKGPNVTKGYLNREDATRETFQDG-WFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEIEEV 401
|
490
....*....|....*.
gi 17933690 532 IKKeLDAISNAFLVGE 547
Cdd:PRK03640 402 LLS-HPGVAEAGVVGV 416
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
390-564 |
7.77e-21 |
|
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: 94.01 E-value: 7.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 390 VLTLASAAAPMSPETKKYF--LSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKDANGHGELCIRG 467
Cdd:cd17633 112 IKSIFSSGQKLFESTKKKLknIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKS 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 468 RHVFMGYIDnkektEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTIKKeLDAISNAFLVGE 547
Cdd:cd17633 192 EMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLKA-IPGIEEAIVVGI 264
|
170 180
....*....|....*....|
gi 17933690 548 QRKY---LTVLITLKTEVDK 564
Cdd:cd17633 265 PDARfgeIAVALYSGDKLTY 284
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
75-530 |
1.41e-20 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 95.97 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 75 HTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCA---EWFYSAMGaihargIIAGIYTTN-SADAVQHVLESSHAQ 150
Cdd:PRK06018 38 VRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWrhlEAWYGIMG------IGAICHTVNpRLFPEQIAWIINHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 151 -IVVVDDAKQMDKIHAIRDKLPKLKAAIQIQE-------------PYSPYLKKEDGYYRWSEIEsmnvsdvedqymtrlE 216
Cdd:PRK06018 112 dRVVITDLTFVPILEKIADKLPSVERYVVLTDaahmpqttlknavAYEEWIAEADGDFAWKTFD---------------E 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 217 NVAinecCCLVYTSGTVGMPKGVMLSHDNitfDVRGIVKAMDRVVVG---AESIVSYLPLSHVAAqtvdiYTCAFVAgci 293
Cdd:PRK06018 177 NTA----AGMCYTSGTTGDPKGVLYSHRS---NVLHALMANNGDALGtsaADTMLPVVPLFHANS-----WGIAFSA--- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 294 wfadkDALKGTLVkslqdaRPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLaswakgitLKHymvsqgkssggfrykia 373
Cdd:PRK06018 242 -----PSMGTKLV------MPGAKLDGASVYELLDTEKVTFTAGVPTVWLML--------LQY----------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 374 ksliMSKVKQALGFDRVLTLASAAAPMSpeTKKYFLSLDLKIVDAFGMSETAGCHTIC--------LPDSVGLN---TIG 442
Cdd:PRK06018 286 ----MEKEGLKLPHLKMVVCGGSAMPRS--MIKAFEDMGVEVRHAWGMTEMSPLGTLAalkppfskLPGDARLDvlqKQG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 443 KTLPGCESKFIN-------KDANGHGELCIRGRHVFMGYIdnkEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEiI 515
Cdd:PRK06018 360 YPPFGVEMKITDdagkelpWDGKTFGRLKVRGPAVAAAYY---RVDGEILDDDGFFDTGDVATIDAYGYMRITDRSKD-V 435
|
490
....*....|....*
gi 17933690 516 ITAGGENIPPVHIEN 530
Cdd:PRK06018 436 IKSGGEWISSIDLEN 450
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
78-576 |
9.50e-20 |
|
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: 92.57 E-value: 9.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 78 TYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVDda 157
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 158 kqmdkihairdklPKLKaaiqiqEPYSPylkkEDGYYrwseiesmnvsdvedqymtrlenvainecccLVYTSGTVGMPK 237
Cdd:cd05969 80 -------------EELY------ERTDP----EDPTL-------------------------------LHYTSGTTGTPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 238 GVMLSHDNITFdvrgivkamdRVVVGAEsivsylplsHVAAQTVDIYTC----AFVAGCIWFADKDALKGTLVKSLQDar 313
Cdd:cd05969 106 GVLHVHDAMIF----------YYFTGKY---------VLDLHPDDIYWCtadpGWVTGTVYGIWAPWLNGVTNVVYEG-- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 314 ptRFmGVPRVYEKFQERMVAVASSSGSLKKMLaswakgITLKHYMVSQGKSSGgFRYkiakslimskvkqalgfdrvltL 393
Cdd:cd05969 165 --RF-DAESWYGIIERVKVTVWYTAPTAIRML------MKEGDELARKYDLSS-LRF----------------------I 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 394 ASAAAPMSPETKKYFLS-LDLKIVDAFGMSETAG---CHTICLPDSVGlnTIGKTLPGCESKFINKDANG-----HGELC 464
Cdd:cd05969 213 HSVGEPLNPEAIRWGMEvFGVPIHDTWWQTETGSimiANYPCMPIKPG--SMGKPLPGVKAAVVDENGNElppgtKGILA 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 465 IRGR--HVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITAgGENIPPVHIENTIkKELDAISNA 542
Cdd:cd05969 291 LKPGwpSMFRGIWNDEERYKNSFIDG-WYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESAL-MEHPAVAEA 367
|
490 500 510
....*....|....*....|....*....|....*...
gi 17933690 543 FLVG----EQRKYLTVLITLKTEVdkdsgEPLDELSHE 576
Cdd:cd05969 368 GVIGkpdpLRGEIIKAFISLKEGF-----EPSDELKEE 400
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
45-530 |
1.21e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 92.85 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 45 PISVPGLLKRTVNNYGDYPAL-RTKNGKngYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNC---AEWFY--SA 118
Cdd:PRK07008 9 PLLISSLIAHAARHAGDTEIVsRRVEGD--IHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGyrhLEAYYgvSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 119 MGAIhargiiagIYTTNS---ADAVQHVLESSHAQIVVVDD--AKQMDKIHAI------------RDKLPKLKAAIQIqe 181
Cdd:PRK07008 87 SGAV--------CHTINPrlfPEQIAYIVNHAEDRYVLFDLtfLPLVDALAPQcpnvkgwvamtdAAHLPAGSTPLLC-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 182 pYSPYLKKEDGYYRWSEIEsmnvsdvedqymtrlENVAINECcclvYTSGTVGMPKGVMLSHDNITF--------DVRGI 253
Cdd:PRK07008 157 -YETLVGAQDGDYDWPRFD---------------ENQASSLC----YTSGTTGNPKGALYSHRSTVLhaygaalpDAMGL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 254 vKAMDrvvvgaeSIVSYLPLSHVAAQTVDiYTCAFVAGCIWFADKDaLKGTLVKSLQDA-RPTRFMGVPRVYEkfqermv 332
Cdd:PRK07008 217 -SARD-------AVLPVVPMFHVNAWGLP-YSAPLTGAKLVLPGPD-LDGKSLYELIEAeRVTFSAGVPTVWL------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 333 avasssGSLKKMLASWAKGITLKHYMVsqgkssGGfrykiakslimskvkqalgfdrvltlaSAAAPMSPETkkYFLSLD 412
Cdd:PRK07008 280 ------GLLNHMREAGLRFSTLRRTVI------GG---------------------------SACPPAMIRT--FEDEYG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 413 LKIVDAFGMSETAGCHTIC--------LPDSVG---LNTIGKTLPGCESKFInkDANGH---------GELCIRGRHVfm 472
Cdd:PRK07008 319 VEVIHAWGMTEMSPLGTLCklkwkhsqLPLDEQrklLEKQGRVIYGVDMKIV--GDDGRelpwdgkafGDLQVRGPWV-- 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 17933690 473 gyIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIEN 530
Cdd:PRK07008 395 --IDRYFRGDASPLVDGWFPTGDVATIDADGFMQITDRSKD-VIKSGGEWISSIDIEN 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
226-510 |
1.65e-19 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 91.92 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvvVGAESIV-SYLPLSHVAAqTVDIYTCAFVAGCIWFADKDALK-- 302
Cdd:cd05945 102 IIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFP---LGPGDVFlNQAPFSFDLS-VMDLYPALASGATLVPVPRDATAdp 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 303 GTLVKSLQDARPTRFMGVPRVyekfqermVAVASSSGSLK-KMLAswakgiTLKHYMVSqGKssggfrykiakslimskv 381
Cdd:cd05945 178 KQLFRFLAEHGITVWVSTPSF--------AAMCLLSPTFTpESLP------SLRHFLFC-GE------------------ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 382 kqalgfdrVLTLASAAAPMS--PETKkyflsldlkIVDAFGMSE-TAGCHTICLPDSV--GLNT--IGKTLPGCESKFIN 454
Cdd:cd05945 225 --------VLPHKTARALQQrfPDAR---------IYNTYGPTEaTVAVTYIEVTPEVldGYDRlpIGYAKPGAKLVILD 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17933690 455 KD-----ANGHGELCIRGRHVFMGYIDNKEKTEESLDDDC---WLHSGDLGFVDDKGYVSLTGR 510
Cdd:cd05945 288 EDgrpvpPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEgqrAYRTGDLVRLEADGLLFYRGR 351
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
215-532 |
1.82e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 92.58 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 215 LENVAInecccLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDR--------VVVGAESIVSYLPLSHVAAQTVDIyTC 286
Cdd:PRK12492 206 LDDIAV-----LQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQlgpdgqplMKEGQEVMIAPLPLYHIYAFTANC-MC 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 287 AFVAGC--IWFADKDALKGtLVKSLQDARPTRFMGVPRVYekfqermVAVasssgslkkmlaswakgitLKHymvsqgks 364
Cdd:PRK12492 280 MMVSGNhnVLITNPRDIPG-FIKELGKWRFSALLGLNTLF-------VAL-------------------MDH-------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 365 sGGFrykiaKSLIMSKVKqalgfdrvLTLASAAAPMSPETKKYFLSLDLKIVDAFGMSETAgchTICLPDSVG----LNT 440
Cdd:PRK12492 325 -PGF-----KDLDFSALK--------LTNSGGTALVKATAERWEQLTGCTIVEGYGLTETS---PVASTNPYGelarLGT 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 441 IGKTLPGCESKFINKDANG-----HGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEII 515
Cdd:PRK12492 388 VGIPVPGTALKVIDDDGNElplgeRGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI 467
|
330
....*....|....*..
gi 17933690 516 ITAGGeNIPPVHIENTI 532
Cdd:PRK12492 468 IVSGF-NVYPNEIEDVV 483
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
61-666 |
4.61e-19 |
|
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: 91.34 E-value: 4.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 61 DYPALRTKNGKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGI---YTTNSA 137
Cdd:cd05921 10 DRTWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 138 DAV--QHVLESSHAQIVVVDDAKQMDKihAIRDKLPKLKAAIQIQEPyspyLKKEDGYYRWSEIESMNVSDVEDQY-MTR 214
Cdd:cd05921 90 DLAklKHLFELLKPGLVFAQDAAPFAR--ALAAIFPLGTPLVVSRNA----VAGRGAISFAELAATPPTAAVDAAFaAVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 215 LENVAInecccLVYTSGTVGMPKGVMLSHDNITFDVRGIvkAMDRVVVGAE--SIVSYLPLSHVAAQTVDIYTCAFVAGC 292
Cdd:cd05921 164 PDTVAK-----FLFTSGSTGLPKAVINTQRMLCANQAML--EQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 293 IWFADKDALKG---TLVKSLQDARPTRFMGVPRVYEKFQERMvavasssgslkkmlaswakgitlkhymvsqgKSSGGFR 369
Cdd:cd05921 237 LYIDDGKPMPGgfeETLRNLREISPTVYFNVPAGWEMLVAAL-------------------------------EKDEALR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 370 YKIakslimskvkqalgFDRVLTLASAAAPMSPETKKYFLSLDLK-------IVDAFGMSETAGCHTIC--LPDSVGLnt 440
Cdd:cd05921 286 RRF--------------FKRLKLMFYAGAGLSQDVWDRLQALAVAtvgeripMMAGLGATETAPTATFThwPTERSGL-- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 441 IGKTLPGCESKFInkDANGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLG-FVDD----KGYVsLTGRSKEII 515
Cdd:cd05921 350 IGLPAPGTELKLV--PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAkLADPddpaKGLV-FDGRVAEDF 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 516 ITAGGENippVHIeNTIKKELDA-----ISNAFLVGEQRKYLTVLITLktevdkdSGEPLDELShessvwvkslGVEHKT 590
Cdd:cd05921 427 KLASGTW---VSV-GPLRARAVAacaplVHDAVVAGEDRAEVGALVFP-------DLLACRRLV----------GLQEAS 485
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17933690 591 VSDILAAgpcPKVWKSIEDAIKRANKQSISNAQKVQKFTILPHDFSIPTGELGPTLKVKRNVVSKMYADEIEKLYA 666
Cdd:cd05921 486 DAEVLRH---AKVRAAFRDRLAALNGEATGSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYA 558
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
226-529 |
5.42e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 90.64 E-value: 5.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDN-----ITFDVRGIVKAMDRVVVGAesivsylPLSHVAAQTVDIYTCAFVAGCIWFADKDA 300
Cdd:PRK09088 140 ILFTSGTSGQPKGVMLSERNlqqtaHNFGVLGRVDAHSSFLCDA-------PMFHIIGLITSVRPVLAVGGSILVSNGFE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 301 LKGTLvkslqdarptrfmgvprvyekfqermvavasssgslkKMLASWAKGITlkHYM-VSQgkssggfrykiakslIMS 379
Cdd:PRK09088 213 PKRTL-------------------------------------GRLGDPALGIT--HYFcVPQ---------------MAQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 380 KVKQALGFD----RVLT-LASAAAPMSPETKKYFLSLDLKIVDAFGMSETA---GCHTICLPDSVGLNTIGKTLPGCESK 451
Cdd:PRK09088 239 AFRAQPGFDaaalRHLTaLFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGtvfGMSVDCDVIRAKAGAAGIPTPTVQTR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 452 FInkDANGH-------GELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIP 524
Cdd:PRK09088 319 VV--DDQGNdcpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFIS-GGENVY 395
|
....*
gi 17933690 525 PVHIE 529
Cdd:PRK09088 396 PAEIE 400
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
221-534 |
8.12e-19 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 89.32 E-value: 8.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 221 NECCCLVYTSGTVGMPKGVMLSHdnitfdvrgivKAMDRVVVGAESIVSYLPlshvaaqtVDIYTCAFV---AGCIWFAd 297
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTH-----------SYPLGHIPTAAYWLGLRP--------DDIHWNIADpgwAKGAWSS- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 298 kdaLKGTLVkslqdarptrfMGVPRV---YEKFQ-ERMVAVASSSGslkkmLASWAKGITLKHYMVSQGKSSGGFRykia 373
Cdd:cd05972 141 ---FFGPWL-----------LGATVFvyeGPRFDaERILELLERYG-----VTSFCGPPTAYRMLIKQDLSSYKFS---- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 374 kslimskvkqalgfdRVLTLASAAAPMSPETKKYFLS-LDLKIVDAFGMSET----AGCHTICL-PDSvglntIGKTLPG 447
Cdd:cd05972 198 ---------------HLRLVVSAGEPLNPEVIEWWRAaTGLPIRDGYGQTETgltvGNFPDMPVkPGS-----MGRPTPG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 448 CESKFINKDANG-----HGELCIR-GRHV-FMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITAgG 520
Cdd:cd05972 258 YDVAIIDDDGRElppgeEGDIAIKlPPPGlFLGYVGDPEKTEASIRGD-YYLTGDRAYRDEDGYFWFVGRADDIIKSS-G 335
|
330
....*....|....
gi 17933690 521 ENIPPVHIENTIKK 534
Cdd:cd05972 336 YRIGPFEVESALLE 349
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
226-523 |
1.14e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 90.55 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESIVSYLPLSHVAAQTVdIYTCAFVAGCIWFADKDAlkGTL 305
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKTHLSYLPISHIYERVI-AYLSFMLGGTINIWSKDI--NYF 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 306 VKSLQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLAswaKGItlkhymVSQGKSS--GGFRYKIAK-----SLIM 378
Cdd:PTZ00342 386 SKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLV---KKI------LSLRKSNnnGGFSKFLEGithisSKIK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 379 SKVKQALGfdrvlTLASAAAPMSPETKKYF-LSLDLKIVDAFGMSETAGC-----HTICLPDSVGlntiGKTLPGCESKF 452
Cdd:PTZ00342 457 DKVNPNLE-----VILNGGGKLSPKIAEELsVLLNVNYYQGYGLTETTGPifvqhADDNNTESIG----GPISPNTKYKV 527
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17933690 453 IN------KDANGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGENI 523
Cdd:PTZ00342 528 RTwetykaTDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYI 604
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
229-529 |
1.68e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 89.28 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 229 TSGTVGMPKGVMLSHDNITFDVRGIVKAMdRVVVGAESIVSYLPLSH----VAAQTVDIYTcafvaGCiwfadkDALKGT 304
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAA-EFDVETDVMVSWLPLFHdmgmVGFLTVPMYF-----GA------ELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 305 lvkslqdarPTRFMGVPrvyekfqermvavasssgslkkmlASWAKGITLKHYMVSQGKssgGFRYKIA----------K 374
Cdd:PRK07768 228 ---------PMDFLRDP------------------------LLWAELISKYRGTMTAAP---NFAYALLarrlrrqakpG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 375 SLIMSKVKQALG------FDRVLTLASAAAP--MSPETkkyflsldlkIVDAFGMSETA--------GC----HTIC--- 431
Cdd:PRK07768 272 AFDLSSLRFALNgaepidPADVEDLLDAGARfgLRPEA----------ILPAYGMAEATlavsfspcGAglvvDEVDadl 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 432 -------LPDSVG----LNTIGKTLPGCESKFINKDAN-----GHGELCIRGRHVFMGYIDnKEKTEESLDDDCWLHSGD 495
Cdd:PRK07768 342 laalrraVPATKGntrrLATLGPPLPGLEVRVVDEDGQvlpprGVGVIELRGESVTPGYLT-MDGFIPAQDADGWLDTGD 420
|
330 340 350
....*....|....*....|....*....|....
gi 17933690 496 LGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIE 529
Cdd:PRK07768 421 LGYLTEEGEVVVCGRVKDVIIM-AGRNIYPTDIE 453
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
61-530 |
4.23e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 87.91 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 61 DYPALRTKNgkngyHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEwFYSAMGAIHARGIIAgiYTTN---SA 137
Cdd:PRK07786 32 DAPALRFLG-----NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTE-FVESVLAANMLGAIA--VPVNfrlTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 138 DAVQHVLESSHAQIVVVDDAKQmDKIHAIRDKLPKLKAAIQIQEPyspylkKEDGyyrwseiesmnVSDVEDQYMTRLEN 217
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALA-PVATAVRDIVPLLSTVVVAGGS------SDDS-----------VLGYEDLLAEAGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 218 VAI----NECCCLV-YTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvvVGAESIVSYL--PLSHVAA-----------Q 279
Cdd:PRK07786 166 HAPvdipNDSPALImYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG---ADINSDVGFVgvPLFHIAGigsmlpglllgA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 280 TVDIY-TCAFVAGCIWfadkDALKGTLVKSLqdarptrFMgVPRVYEkfqermvAVASSSGslkkmlaswAKGITLKHYM 358
Cdd:PRK07786 243 PTVIYpLGAFDPGQLL----DVLEAEKVTGI-------FL-VPAQWQ-------AVCAEQQ---------ARPRDLALRV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 359 VSQGKssggfrykiakslimskvkqALGFDRVLTLASAAAPmspetkkyflslDLKIVDAFGMSETAGCHTICLPDSV-- 436
Cdd:PRK07786 295 LSWGA--------------------APASDTLLRQMAATFP------------EAQILAAFGQTEMSPVTCMLLGEDAir 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 437 GLNTIGKTLPGCESKFINKDAN----GH-GELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRS 511
Cdd:PRK07786 343 KLGSVGKVIPTVAARVVDENMNdvpvGEvGEIVYRAPTLMSGYWNNPEATAEAFAGG-WFHSGDLVRQDEEGYVWVVDRK 421
|
490
....*....|....*....
gi 17933690 512 KEIIITaGGENIPPVHIEN 530
Cdd:PRK07786 422 KDMIIS-GGENIYCAEVEN 439
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
76-628 |
9.83e-18 |
|
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: 86.36 E-value: 9.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 76 TVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVD 155
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 156 DAkqmdkihairdklpklkaaiqiqepyspylkkedgyyrwseiesmnvsdvedqymtrlenvainECCCLVYTSGTVGM 235
Cdd:cd05919 90 AD----------------------------------------------------------------DIAYLLYSSGTTGP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 236 PKGVMLSHDNITFDVRGI------VKAMDRVVVGAESIVSY-------LPLSHVAaqtvdiyTCAFVAGciWfADKDALK 302
Cdd:cd05919 106 PKGVMHAHRDPLLFADAMarealgLTPGDRVFSSAKMFFGYglgnslwFPLAVGA-------SAVLNPG--W-PTAERVL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 303 GTLVKSlqdaRPTRFMGVPRVYEkfqeRMVAVASSSGSLkkmlaswakgitlkhymvsqgkssggfrykiakslimskvk 382
Cdd:cd05919 176 ATLARF----RPTVLYGVPTFYA----NLLDSCAGSPDA----------------------------------------- 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 383 qalgfDRVLTLASAAAPMSPETKKYFLS--LDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFInkDANGH 460
Cdd:cd05919 207 -----LRSLRLCVSAGEALPRGLGERWMehFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLV--DEEGH 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 461 -------GELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTIk 533
Cdd:cd05919 280 tippgeeGDLLVRGPSAAVGYWNNPEKSRATFNGG-WYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLI- 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 534 KELDAISNAFLVGEQRKY----LTVLITLKTEVDkdsgePLDELSHESsvwvkslgveHKTVSDILAAGPCPKVWKSIED 609
Cdd:cd05919 357 IQHPAVAEAAVVAVPESTglsrLTAFVVLKSPAA-----PQESLARDI----------HRHLLERLSAHKVPRRIAFVDE 421
|
570
....*....|....*....
gi 17933690 610 AIKRANKqsisnaqKVQKF 628
Cdd:cd05919 422 LPRTATG-------KLQRF 433
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
60-529 |
1.16e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 86.87 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 60 GDYPALRTKnGKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADA 139
Cdd:PRK04319 58 KDKVALRYL-DASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 140 VQHVLESSHAQIVVVDDAkQMDKIhaIRDKLPKLKAAIQIQEPYSPylkkEDGYYRWSEIesMN-VSDVEDQYMTRLENV 218
Cdd:PRK04319 137 VRDRLEDSEAKVLITTPA-LLERK--PADDLPSLKHVLLVGEDVEE----GPGTLDFNAL--MEqASDEFDIEWTDREDG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 219 AInecccLVYTSGTVGMPKGVMLSHDnitfdvrgivkAMdrvvvgaesivsylpLSH-VAAQTV------DIYTCAfvag 291
Cdd:PRK04319 208 AI-----LHYTSGSTGKPKGVLHVHN-----------AM---------------LQHyQTGKYVldlhedDVYWCT---- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 292 ciwfADKDALKGTlvkslqdarptrfmgvprvyekfqermvavasSSGslkkMLASWAKGITLkhyMVSQGKSSGGFRYK 371
Cdd:PRK04319 253 ----ADPGWVTGT--------------------------------SYG----IFAPWLNGATN---VIDGGRFSPERWYR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 372 I--------------AKSLIMS---KVKQALGFDRVLTLASAAAPMSPETKKYFLS-LDLKIVDAFGMSETaGCHTIC-- 431
Cdd:PRK04319 290 IledykvtvwytaptAIRMLMGagdDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKvFGLPIHDNWWMTET-GGIMIAny 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 432 -----LPDSvglntIGKTLPGCESKFINKDANG-----HGELCIRG--RHVFMGYIDNKEKTEESLDDDcWLHSGDLGFV 499
Cdd:PRK04319 369 pamdiKPGS-----MGKPLPGIEAAIVDDQGNElppnrMGNLAIKKgwPSMMRGIWNNPEKYESYFAGD-WYVSGDSAYM 442
|
490 500 510
....*....|....*....|....*....|
gi 17933690 500 DDKGYVSLTGRSKEIIITAgGENIPPVHIE 529
Cdd:PRK04319 443 DEDGYFWFQGRVDDVIKTS-GERVGPFEVE 471
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
60-533 |
2.03e-17 |
|
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: 85.75 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 60 GDYPALR-TKNGKNGYHTVTYKQYEQKVHQVAKAFIKLGlEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTN--- 135
Cdd:cd05931 7 PDRPAYTfLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTpgr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 136 SADAVQHVLESSHAQiVVVDDAKQMDKIHAIRDKLPKLKAAiqiqepyspylkkedgyyRWSEIESMNVSDVEDqymTRL 215
Cdd:cd05931 86 HAERLAAILADAGPR-VVLTTAAALAAVRAFAASRPAAGTP------------------RLLVVDLLPDTSAAD---WPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 216 ENVAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvvVGAES-IVSYLPLSH----VAAqtvdIYTCAFVA 290
Cdd:cd05931 144 PSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYG---LDPGDvVVSWLPLYHdmglIGG----LLTPLYSG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 291 GCIWFADkdalkgtlvkslqdarPTRFMGVPrvyekfqermvavasssgslkkmlASWAKGITlKHymvsQGKSSGG--F 368
Cdd:cd05931 217 GPSVLMS----------------PAAFLRRP------------------------LRWLRLIS-RY----RATISAApnF 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 369 RYKIAKSLIMSKvkQALGFD--RVLTLASAAAPMSPETKKYFlsldlkiVDAF--------------GMSET-------- 424
Cdd:cd05931 252 AYDLCVRRVRDE--DLEGLDlsSWRVALNGAEPVRPATLRRF-------AEAFapfgfrpeafrpsyGLAEAtlfvsggp 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 425 AGCHTICL------------------PDSVGLNTIGKTLPGCESKFInkDANGH--------GELCIRGRHVFMGYIDNK 478
Cdd:cd05931 323 PGTGPVVLrvdrdalagravavaaddPAARELVSCGRPLPDQEVRIV--DPETGrelpdgevGEIWVRGPSVASGYWGRP 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17933690 479 EKTEE------SLDDDCWLHSGDLGFVDDkGYVSLTGRSKEIIITAgGENIPPVHIENTIK 533
Cdd:cd05931 401 EATAEtfgalaATDEGGWLRTGDLGFLHD-GELYITGRLKDLIIVR-GRNHYPQDIEATAE 459
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
226-532 |
2.29e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 85.88 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNIT---FDVRGIVKAMdrVVVGAESIVSYLPLSHVAAQTVDiytcafvagCIWFADKDA-- 300
Cdd:PRK08974 211 LQYTGGTTGVAKGAMLTHRNMLanlEQAKAAYGPL--LHPGKELVVTALPLYHIFALTVN---------CLLFIELGGqn 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 301 --------LKGtLVKSLQDARPTRFMGVPRVY------EKFQErmvavasssgslkkmlaswakgITLKHYMVSQGkssG 366
Cdd:PRK08974 280 llitnprdIPG-FVKELKKYPFTAITGVNTLFnallnnEEFQE----------------------LDFSSLKLSVG---G 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 367 GfrykiaksliMSkVKQALGfDRVLTLasaaapmspeTKKYFLsldlkivDAFGMSETAGCHTICLPDSVGLN-TIGKTL 445
Cdd:PRK08974 334 G----------MA-VQQAVA-ERWVKL----------TGQYLL-------EGYGLTECSPLVSVNPYDLDYYSgSIGLPV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 446 PGCESKFINKDAN----GH-GELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITAGG 520
Cdd:PRK08974 385 PSTEIKLVDDDGNevppGEpGELWVKGPQVMLGYWQRPEATDEVIKDG-WLATGDIAVMDEEGFLRIVDRKKDMILVSGF 463
|
330
....*....|..
gi 17933690 521 eNIPPVHIENTI 532
Cdd:PRK08974 464 -NVYPNEIEDVV 474
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
228-539 |
2.43e-17 |
|
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: 85.62 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 228 YTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHvaaqtvDIYTCAFVAGCIWFADKDALKGTlvk 307
Cdd:cd05908 113 FSSGSTGDPKGVMLTHENLVHNMFAILNSTE--WKTKDRILSWMPLTH------DMGLIAFHLAPLIAGMNQYLMPT--- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 308 SLQDARPTRFMgvprvyEKFQERMVAVASSSGSLKKMLASWAKGITLKHYMVSQGKSSGGFRYKIAKSLIMSKVKQ--AL 385
Cdd:cd05908 182 RLFIRRPILWL------KKASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHmsKY 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 386 GFDR-----VLTLASAA-APMSPETKKYFLSLdlkIVDAFGMSETAGCHTICLPDSVGLN--TIGKTLPGCESKFINKDA 457
Cdd:cd05908 256 GLKRnailpVYGLAEASvGASLPKAQSPFKTI---TLGRRHVTHGEPEPEVDKKDSECLTfvEVGKPIDETDIRICDEDN 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 458 NG-----HGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDkGYVSLTGRSKEIIITaGGENIPPVHIENTI 532
Cdd:cd05908 333 KIlpdgyIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRN-GRLVITGREKDIIFV-NGQNVYPHDIERIA 410
|
....*..
gi 17933690 533 kKELDAI 539
Cdd:cd05908 411 -EELEGV 416
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
215-555 |
4.61e-17 |
|
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: 84.07 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 215 LENVAInecccLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHVAAQTVDIYTCAFVAGCI- 293
Cdd:cd05935 83 LDDLAL-----IPYTSGTTGLPKGCMHTHFSAAANALQSAVWTG--LTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYv 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 294 ----WfaDKDalkgTLVKSLQDARPTRFMGVPRvyekfqermvavasssgslkkmlaswakgitlkhyMVSQGKSSGGFR 369
Cdd:cd05935 156 lmarW--DRE----TALELIEKYKVTFWTNIPT-----------------------------------MLVDLLATPEFK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 370 YKIAKSLIMskvkqalgfdrvltLASAAAPMSPETKKYFLSL-DLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGC 448
Cdd:cd05935 195 TRDLSSLKV--------------LTGGGAPMPPAVAEKLLKLtGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 449 ESKFINK------DANGHGELCIRGRHVFMGYIDNKEKTEES---LDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAG 519
Cdd:cd05935 261 DARVIDIetgrelPPNEVGEIVVRGPQIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSG 340
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 17933690 520 GEnIPPVHIENTIKKElDAISNAFLV-------GEQRKYLTVL 555
Cdd:cd05935 341 FK-VWPAEVEAKLYKH-PAI*EVCVIsvpdervGEEVKAFIVL 381
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
226-496 |
9.47e-17 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 84.04 E-value: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVgAESIVSYLPLSHVAAQTVDIYTCAfVAGCIWFADKDALKgTL 305
Cdd:cd17632 228 LIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPP-ASITLNFMPMSHIAGRISLYGTLA-RGGTAYFAAASDMS-TL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 306 VKSLQDARPTRFMGVPRVYEKFQERMVAVasssgsLKKMLASWAKGITLKhymvsqgkssggfryKIAKSLIMSKVkqaL 385
Cdd:cd17632 305 FDDLALVRPTELFLVPRVCDMLFQRYQAE------LDRRSVAGADAETLA---------------ERVKAELRERV---L 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 386 GfDRVLTLASAAAPMSPETKKYFLS-LDLKIVDAFGMSETAGchticlpdsVGLNTIGKTLPGCESKFINKDANGH---- 460
Cdd:cd17632 361 G-GRLLAAVCGSAPLSAEMKAFMESlLDLDLHDGYGSTEAGA---------VILDGVIVRPPVLDYKLVDVPELGYfrtd 430
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 17933690 461 -----GELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDL 496
Cdd:cd17632 431 rphprGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV 471
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
45-660 |
1.21e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 83.56 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 45 PISVPGLLKRTVNNYGDYPALRTKNGKNG-YHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIH 123
Cdd:PRK12582 48 PRSIPHLLAKWAAEAPDRPWLAQREPGHGqWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 124 ARGIIAGI---YTTNSAD--AVQHVLESSHAQIVVVDDAKQMDK-IHAIRDKLPKLKAAIQIQEpyspylkkEDGYYRWS 197
Cdd:PRK12582 128 AGVPAAPVspaYSLMSHDhaKLKHLFDLVKPRVVFAQSGAPFARaLAALDLLDVTVVHVTGPGE--------GIASIAFA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 198 EIESMNVSDVEDQYMTRL--ENVAInecccLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESI-VSYLPLS 274
Cdd:PRK12582 200 DLAATPPTAAVAAAIAAItpDTVAK-----YLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVsLDWMPWN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 275 HVAAQTVDIYTCAFVAGCIWFADKDALKG---TLVKSLQDARPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLASWA-K 350
Cdd:PRK12582 275 HTMGGNANFNGLLWGGGTLYIDDGKPLPGmfeETIRNLREISPTVYGNVPAGYAMLAEAMEKDDALRRSFFKNLRLMAyG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 351 GITLKHYMvsqgkssggfrykiakslimskvkqalgFDRVLTLASAaapmspETKKYFLsldlkIVDAFGMSETAG--CH 428
Cdd:PRK12582 355 GATLSDDL----------------------------YERMQALAVR------TTGHRIP-----FYTGYGATETAPttTG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 429 TICLPDSVGLntIGKTLPGCESKFInkdANGHG-ELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLG-FVDD----K 502
Cdd:PRK12582 396 THWDTERVGL--IGLPLPGVELKLA---PVGDKyEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAArFVDPddpeK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 503 GYVsLTGRSKEIIITAGGENippVHIeNTIKKELDA-----ISNAFLVGEQRKYLTVLI-----TLKTEVDKDSGEPLDe 572
Cdd:PRK12582 471 GLI-FDGRVAEDFKLSTGTW---VSV-GTLRPDAVAacspvIHDAVVAGQDRAFIGLLAwpnpaACRQLAGDPDAAPED- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 573 lshessvwvkslGVEHKTVSDILAAGpcpkvwksiedaIKRANKQSISNAQKVQKFTILPHDFSIPTGELG--------P 644
Cdd:PRK12582 545 ------------VVKHPAVLAILREG------------LSAHNAEAGGSSSRIARALLMTEPPSIDAGEITdkgyinqrA 600
|
650
....*....|....*.
gi 17933690 645 TLKVKRNVVSKMYADE 660
Cdd:PRK12582 601 VLERRAALVERLYAEP 616
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
225-546 |
1.62e-16 |
|
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: 81.16 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 225 CLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHVAAqtVDIYTCAFVAGciwfadkdalkgt 304
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMG--LTEADVYLNMLPLFHIAG--LNLALATFHAG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 305 lvkslqdarptrfmGVPRVYEKFQERMVAVASSS------GSLKKMLASwakgITLKHymvsqgkssggfrykIAKSLIM 378
Cdd:cd17637 67 --------------GANVVMEKFDPAEALELIEEekvtlmGSFPPILSN----LLDAA---------------EKSGVDL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 379 SKVKQALGFDrvltlasaaapmSPETKKYFLSL-DLKIVDAFGMSETAGCHTICL----PDSVGlntigKTLPGCESKFI 453
Cdd:cd17637 114 SSLRHVLGLD------------APETIQRFEETtGATFWSLYGQTETSGLVTLSPyrerPGSAG-----RPGPLVRVRIV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 454 NKD-----ANGHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRS--KEIIITaGGENIPPV 526
Cdd:cd17637 177 DDNdrpvpAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-WHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPA 254
|
330 340
....*....|....*....|
gi 17933690 527 HIENTIkKELDAISNAFLVG 546
Cdd:cd17637 255 EVEKVI-LEHPAIAEVCVIG 273
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
45-534 |
3.78e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 81.92 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 45 PISvpgLLKRTVNNYGDYPALrtkngKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHA 124
Cdd:PRK08162 20 PLS---FLERAAEVYPDRPAV-----IHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 125 RGIIAGIYTTNSADAVQHVLESSHAQIVVVD--------DAKQM---DKIHAIRDKLPKLKAAIQIQE-PYSPYLKKEDG 192
Cdd:PRK08162 92 GAVLNTLNTRLDAASIAFMLRHGEAKVLIVDtefaevarEALALlpgPKPLVIDVDDPEYPGGRFIGAlDYEAFLASGDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 193 YYRWSEiesmnvsdVEDQYmtrlENVAINeccclvYTSGTVGMPKGVMLSHdnitfdvRG---------IVKAMDRVVVg 263
Cdd:PRK08162 172 DFAWTL--------PADEW----DAIALN------YTSGTTGNPKGVVYHH-------RGaylnalsniLAWGMPKHPV- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 264 aesivsYL---PLSH---------VAAQT-VDIYTCAFVAGCIWfadkDALKgtlvkslqDARPTRFMGVPRVYekfqer 330
Cdd:PRK08162 226 ------YLwtlPMFHcngwcfpwtVAARAgTNVCLRKVDPKLIF----DLIR--------EHGVTHYCGAPIVL------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 331 mvavasssGSLKKMLASWAKGITLK-HYMVsqgkssggfrykiakslimskvkqalgfdrvltlasAAAPMSPETKKYFL 409
Cdd:PRK08162 282 --------SALINAPAEWRAGIDHPvHAMV------------------------------------AGAAPPAAVIAKME 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 410 SLDLKIVDAFGMSETAGCHTICLPDSvGLNTigktLPGCESKFIN-------------------------KDANGHGELC 464
Cdd:PRK08162 318 EIGFDLTHVYGLTETYGPATVCAWQP-EWDA----LPLDERAQLKarqgvryplqegvtvldpdtmqpvpADGETIGEIM 392
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 465 IRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTIKK 534
Cdd:PRK08162 393 FRGNIVMKGYLKNPKATEEAFAGG-WFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVEDVLYR 460
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
76-566 |
5.66e-16 |
|
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: 81.22 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 76 TVTYKQYEQKVHQVAKAFIKLGLEEHHsVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESshAQIVVVD 155
Cdd:cd05909 7 SLTYRKLLTGAIALARKLAKMTKEGEN-VGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKL--AGIKTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 156 DAKQ---------------------MDKIHAIRDKLPKLKAAIQIQEPYSPYLKKEdgyyrwseiesmNVSDVEdqymtr 214
Cdd:cd05909 84 TSKQfieklklhhlfdveydarivyLEDLRAKISKADKCKAFLAGKFPPKWLLRIF------------GVAPVQ------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 215 LENVAInecccLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMD----RVVVGAesivsyLPLSHvaaqtvdiytcAF-V 289
Cdd:cd05909 146 PDDPAV-----ILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDpnpeDVVFGA------LPFFH-----------SFgL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 290 AGCIWFAdkdALKGtlVKSLQDARPTRFMGVPRVYEkfqERMVAVASSSGSLKKMLASWAKGITLKhymvsqgkssgGFR 369
Cdd:cd05909 204 TGCLWLP---LLSG--IKVVFHPNPLDYKKIPELIY---DKKATILLGTPTFLRGYARAAHPEDFS-----------SLR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 370 YKIAkslimskvkqalgfdrvltlasAAAPMSPETKKYFLSL-DLKIVDAFGMSETAGCHTICLPDS---VGlnTIGKTL 445
Cdd:cd05909 265 LVVA----------------------GAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISVNTPQSpnkEG--TVGRPL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 446 PGCESKFINKD------ANGHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEiIITAG 519
Cdd:cd05909 321 PGMEVKIVSVEtheevpIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDG-WYDTGDIGKIDGEGFLTITGRLSR-FAKIA 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 17933690 520 GENIPPVHIENTIKKEL--DAISNAFLVGEQRK-YLTVLITLKTEVDKDS 566
Cdd:cd05909 399 GEMVSLEAIEDILSEILpeDNEVAVVSVPDGRKgEKIVLLTTTTDTDPSS 448
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
59-546 |
2.09e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 79.34 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 59 YGDYPALRTKNGKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSAD 138
Cdd:PRK08008 20 YGHKTALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 139 AVQHVLESSHAQIVVVDdAKQMDKIHAIRDKLPKLKAAIQIQEPYSPylkKEDGYYRWSEIESMNVSDVEDQYMTRLENV 218
Cdd:PRK08008 100 ESAWILQNSQASLLVTS-AQFYPMYRQIQQEDATPLRHICLTRVALP---ADDGVSSFTQLKAQQPATLCYAPPLSTDDT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 219 AinEcccLVYTSGTVGMPKGVMLSHDNITFdvRGIVKAMDRVVVGAESIVSYLPLSHVAAQtvdiytC-----AFVAGci 293
Cdd:PRK08008 176 A--E---ILFTSGTTSRPKGVVITHYNLRF--AGYYSAWQCALRDDDVYLTVMPAFHIDCQ------CtaamaAFSAG-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 294 wfadkdalkGTLVkslqdarptrfmgvprVYEKFQERmvavasssgslkkmlASWakgitlkhymvsqgKSSGGFRYKIA 373
Cdd:PRK08008 241 ---------ATFV----------------LLEKYSAR---------------AFW--------------GQVCKYRATIT 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 374 KSLIMskvkqalgFDRVLTLASAAA--------------PMSPETKKYFLS-LDLKIVDAFGMSETAgchticlpdsVGL 438
Cdd:PRK08008 267 ECIPM--------MIRTLMVQPPSAndrqhclrevmfylNLSDQEKDAFEErFGVRLLTSYGMTETI----------VGI 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 439 -----------NTIGKTLPGCESKFINKD-----ANGHGELCIRG---RHVFMGYIDNKEKTEESLDDDCWLHSGDLGFV 499
Cdd:PRK08008 329 igdrpgdkrrwPSIGRPGFCYEAEIRDDHnrplpAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYV 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 17933690 500 DDKGYVSLTGRSKEiIITAGGENIPPVHIENTIKKElDAISNAFLVG 546
Cdd:PRK08008 409 DEEGFFYFVDRRCN-MIKRGGENVSCVELENIIATH-PKIQDIVVVG 453
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-546 |
1.65e-14 |
|
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: 75.50 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNI---TFDVRGIVKA-------MDRVVVGAESIVSYL--PLSHVAAQtvdiytcafvagci 293
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmLMGGADFGTGeftpsedAHKAAAAAAGTVMFPapPLMHGTGS-------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 294 WFADKDALKGTLVKSLQDarptRFMGVpRVYEKFQERMVAVASSSGSlkkmlaswakgitlkhymvsqgkssggfryKIA 373
Cdd:cd05924 74 WTAFGGLLGGQTVVLPDD----RFDPE-EVWRTIEKHKVTSMTIVGD------------------------------AMA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 374 KSLImSKVKQALGFD--RVLTLASAAAPMSPETKKYFLSL--DLKIVDAFGMSETAG---CHTICLPDSVGLNTI---GK 443
Cdd:cd05924 119 RPLI-DALRDAGPYDlsSLFAISSGGALLSPEVKQGLLELvpNITLVDAFGSSETGFtgsGHSAGSGPETGPFTRanpDT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 444 TLPGCESKFINKDANGHGELCIRGrHVFMGYIDNKEKTEES---LDDDCWLHSGDLGFVDDKGYVSLTGRSkEIIITAGG 520
Cdd:cd05924 198 VVLDDDGRVVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRG-SVCINTGG 275
|
330 340
....*....|....*....|....*.
gi 17933690 521 ENIPPVHIENTIKKElDAISNAFLVG 546
Cdd:cd05924 276 EKVFPEEVEEALKSH-PAVYDVLVVG 300
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
78-546 |
1.73e-14 |
|
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: 76.70 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 78 TYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVDDa 157
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 158 kqmDKIHAIRDKLPKLKAAIQIQEPYSPYLKKED----GYYRWSEIESMNVSDvedqymtrleNVAINeccclvYTSGTV 233
Cdd:cd05915 105 ---NLLPLVEAIRGELKTVQHFVVMDEKAPEGYLayeeALGEEADPVRVPERA----------ACGMA------YTTGTT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 234 GMPKGVMLSHdnitfdvRGivKAMDRVVVGAESIVSYLPLShVAAQTVDIYTCAfvaGCIWFADKDALKGTLV------- 306
Cdd:cd05915 166 GLPKGVVYSH-------RA--LVLHSLAASLVDGTALSEKD-VVLPVVPMFHVN---AWCLPYAATLVGAKQVlpgprld 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 307 -----KSLQDARPTRFMGVPRVyekfqerMVAVASSSGSLKKMLAsWAKGItlkhymVSQGKSSGGFRYKIaKSLIMSKV 381
Cdd:cd05915 233 paslvELFDGEGVTFTAGVPTV-------WLALADYLESTGHRLK-TLRRL------VVGGSAAPRSLIAR-FERMGVEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 382 KQALGFDRVLTLASAAAPMSP-ETKKYFLSLDLKIVDafGMSETAGCHTICLPDSVGLNTIGKTLPgceskfinkdangh 460
Cdd:cd05915 298 RQGYGLTETSPVVVQNFVKSHlESLSEEEKLTLKAKT--GLPIPLVRLRVADEEGRPVPKDGKALG-------------- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 461 gELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIENTIKKElDAIS 540
Cdd:cd05915 362 -EVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKD-LIKSGGEWISSVDLENALMGH-PKVK 438
|
....*.
gi 17933690 541 NAFLVG 546
Cdd:cd05915 439 EAAVVA 444
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
379-532 |
1.80e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 76.81 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 379 SKVKQALGFDRVLTLASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTIC--------LPDSV--------GLNTIG 442
Cdd:PLN02479 301 PKSETILPLPRVVHVMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETYGPSTVCawkpewdsLPPEEqarlnarqGVRYIG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 443 ktLPGCE------SKFINKDANGHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIII 516
Cdd:PLN02479 381 --LEGLDvvdtktMKPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFANG-WFHSGDLGVKHPDGYIEIKDRSKDIII 457
|
170
....*....|....*.
gi 17933690 517 TaGGENIPPVHIENTI 532
Cdd:PLN02479 458 S-GGENISSLEVENVV 472
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
52-530 |
2.15e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 76.15 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 52 LKRTVNNYGDYPALRTkngkngYHT-VTYKQYEQKVHQVAkAFI--KLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGII 128
Cdd:PRK08314 16 LEVSARRYPDKTAIVF------YGRaISYRELLEEAERLA-GYLqqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 129 AGIYTTNSADAVQHVLESSHAQIVVV--DDAKQMDKI-------HAI----RDKLP-----KLKAAIQIQEPYSPYlkKE 190
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVgsELAPKVAPAvgnlrlrHVIvaqySDYLPaepeiAVPAWLRAEPPLQAL--AP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 191 DGYYRWSEIesmnvsdVEDQYMTRLENVAINECCCLVYTSGTVGMPKGVMLSHDNITFDvrgIVKAMDRVVVGAESIV-S 269
Cdd:PRK08314 167 GGVVAWKEA-------LAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMAN---AVGSVLWSNSTPESVVlA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 270 YLPLSHVAAQTVDIYTCAFVAGCI-----WfaDKDAlkgtlvkslqdarptrfmgVPRVYEKFQermvavasssgslkkm 344
Cdd:PRK08314 237 VLPLFHVTGMVHSMNAPIYAGATVvlmprW--DREA-------------------AARLIERYR---------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 345 LASWAKGITlkhyMVSQGKSSGGFRYKIAKSLIMskvkqalgfdrvltLASAAAPMsPET--KKYFLSLDLKIVDAFGMS 422
Cdd:PRK08314 280 VTHWTNIPT----MVVDFLASPGLAERDLSSLRY--------------IGGGGAAM-PEAvaERLKELTGLDYVEGYGLT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 423 ETAGCHTICLPDSVGLNTIGKTLPGCESKFINKD------ANGHGELCIRGRHVFMGYIDNKEKTEES---LDDDCWLHS 493
Cdd:PRK08314 341 ETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDPEtleelpPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRT 420
|
490 500 510
....*....|....*....|....*....|....*..
gi 17933690 494 GDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIEN 530
Cdd:PRK08314 421 GDLGRMDEEGYFFITDRLKR-MINASGFKVWPAEVEN 456
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
226-529 |
2.47e-14 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 76.08 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHvaaqtvdiyTCAFVAgciwfadkdALKGTL 305
Cdd:PRK05852 181 IMFTGGTTGLPKMVPWTHANIASSVRAIITGYR--LSPRDATVAVMPLYH---------GHGLIA---------ALLATL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 306 V---KSLQDARpTRFMGvprvyEKFQERMVAVAsssgslkkmlASWAKGITLKHYMVSQGKSSGGFRYKIAkslimskvk 382
Cdd:PRK05852 241 AsggAVLLPAR-GRFSA-----HTFWDDIKAVG----------ATWYTAVPTIHQILLERAATEPSGRKPA--------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 383 qALGFDRvltlaSAAAPMSPET----KKYFLSldlKIVDAFGMSETA----------GCHTICLPDSVGLntIGKTlPGC 448
Cdd:PRK05852 296 -ALRFIR-----SCSAPLTAETaqalQTEFAA---PVVCAFGMTEAThqvtttqiegIGQTENPVVSTGL--VGRS-TGA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 449 ESKFINKD-----ANGHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEiIITAGGENI 523
Cdd:PRK05852 364 QIRIVGSDglplpAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG-WLRTGDLGSLSAAGDLSIRGRIKE-LINRGGEKI 441
|
....*.
gi 17933690 524 PPVHIE 529
Cdd:PRK05852 442 SPERVE 447
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
227-547 |
2.79e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 75.80 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 227 VYTSGTVGMPKGVMLSHDNITFDVRGIVKAM----DRVVVGAesivsyLPLSHV----------------AAQTVDIYTC 286
Cdd:PRK07787 134 VYTSGTTGPPKGVVLSRRAIAADLDALAEAWqwtaDDVLVHG------LPLFHVhglvlgvlgplrignrFVHTGRPTPE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 287 AFVAGCiwfadkdALKGTLvkslqdarptrFMGVPRVYEkfqeRMVAVASSSgslkkmlaswakgitlkhymvsqgkssg 366
Cdd:PRK07787 208 AYAQAL-------SEGGTL-----------YFGVPTVWS----RIAADPEAA---------------------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 367 gfrykiakslimskvkQALGFDRVLTLASAAAPMsPETKKYFLSLDLKIVDAFGMSETagchTICL---------PDSVG 437
Cdd:PRK07787 238 ----------------RALRGARLLVSGSAALPV-PVFDRLAALTGHRPVERYGMTET----LITLstradgerrPGWVG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 438 LntigkTLPGCESKFINKDAN--GH-----GELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGR 510
Cdd:PRK07787 297 L-----PLAGVETRLVDEDGGpvPHdgetvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGR 371
|
330 340 350
....*....|....*....|....*....|....*..
gi 17933690 511 SKEIIITAGGENIPPVHIENTIkKELDAISNAFLVGE 547
Cdd:PRK07787 372 ESTDLIKSGGYRIGAGEIETAL-LGHPGVREAAVVGV 407
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
226-532 |
5.66e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 75.06 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMD-----RVVVGAESIVSYLPLSHVAAQTVdiytCAFVA----GC-IWF 295
Cdd:PRK07059 209 LQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpafekKPRPDQLNFVCALPLYHIFALTV----CGLLGmrtgGRnILI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 296 ADKDALKGtLVKSLQDARPTRFMGVPRVYekfqermvavasssgslKKMLaswakgitlkhymvsqgkSSGGFRykiakS 375
Cdd:PRK07059 285 PNPRDIPG-FIKELKKYQVHIFPAVNTLY-----------------NALL------------------NNPDFD-----K 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 376 LIMSKVKqalgfdrvLTLASAAAPMSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLN-TIGKTLPGCESKFIN 454
Cdd:PRK07059 324 LDFSKLI--------VANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSgTIGLPLPSTEVSIRD 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 455 KDAN----GH-GELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAGGeNIPPVHIE 529
Cdd:PRK07059 396 DDGNdlplGEpGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGF-NVYPNEIE 474
|
...
gi 17933690 530 NTI 532
Cdd:PRK07059 475 EVV 477
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
226-553 |
7.43e-14 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 74.49 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIVK--AMDRVVVGAESI-VSYLPLSHvaaqtvdIYTCA-FVAGCIWFADK--- 298
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIAMVELFVRfeASQYEYPGSDNVyLAALPMFH-------IYGLSlFVVGLLSLGSTivv 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 299 ----DAlkGTLVKSLQDARPTRFMGVPRVyekfqerMVAVASSsgslkkmlaswAKGITlkhymvsqgkssggfrykiak 374
Cdd:PLN02574 276 mrrfDA--SDMVKVIDRFKVTHFPVVPPI-------LMALTKK-----------AKGVC--------------------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 375 slimskvkqALGFDRVLTLASAAAPMSPETKKYFLSL--DLKIVDAFGMSETAGCHTiclpdsVGLNT--------IGKT 444
Cdd:PLN02574 315 ---------GEVLKSLKQVSCGAAPLSGKFIQDFVQTlpHVDFIQGYGMTESTAVGT------RGFNTeklskyssVGLL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 445 LPGCESKFINKDA------NGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITA 518
Cdd:PLN02574 380 APNMQAKVVDWSTgcllppGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYK 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17933690 519 GGEnIPPVHIE---------------NTIKKELDAISNAFLVGEQRKYLT 553
Cdd:PLN02574 460 GFQ-IAPADLEavlishpeiidaavtAVPDKECGEIPVAFVVRRQGSTLS 508
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
60-666 |
1.11e-13 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 74.14 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 60 GDYPALRTKNGKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHArGI----IAGIYTTN 135
Cdd:PRK08180 53 PDRVFLAERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYA-GVpyapVSPAYSLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 136 SAD--AVQHVLESSHAQIVVVDDAKQMDKihAIrDKLPKLKAAIQIQEPYSPylkkEDGYYRWSE-IESMNVSDVEDQYM 212
Cdd:PRK08180 132 SQDfgKLRHVLELLTPGLVFADDGAAFAR--AL-AAVVPADVEVVAVRGAVP----GRAATPFAAlLATPPTAAVDAAHA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 213 -TRLENVAInecccLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESIVSYLPLSHVAAQTVDIYTCAFVAG 291
Cdd:PRK08180 205 aVGPDTIAK-----FLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVDWLPWNHTFGGNHNLGIVLYNGG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 292 CIWFADKD---ALKGTLVKSLQDARPTRFMGVPRVYEkfqerMVAVAsssgsLKKMLAswakgitlkhymvsqgkssggf 368
Cdd:PRK08180 280 TLYIDDGKptpGGFDETLRNLREISPTVYFNVPKGWE-----MLVPA-----LERDAA---------------------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 369 rykIAKSLimskvkqalgFDRVLTLASAAAPMSPETkkyFLSLD----------LKIVDAFGMSETAGCHTICLPDSVGL 438
Cdd:PRK08180 328 ---LRRRF----------FSRLKLLFYAGAALSQDV---WDRLDrvaeatcgerIRMMTGLGMTETAPSATFTTGPLSRA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 439 NTIGKTLPGCESKFInkDANGHGELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLG-FVD----DKG---------- 503
Cdd:PRK08180 392 GNIGLPAPGCEVKLV--PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVrFVDpadpERGlmfdgriaed 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 504 -------YVSlTG--RSKeiIITAGGenippvhientikkelDAISNAFLVGEQRKYLTVLITLKT-EVDKDSGEPLDEl 573
Cdd:PRK08180 470 fklssgtWVS-VGplRAR--AVSAGA----------------PLVQDVVITGHDRDEIGLLVFPNLdACRRLAGLLADA- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 574 shessvwvkslgvehkTVSDILAAgpcPKVWKSIEDAIKRANKQSISNAQKVQKFTILPHDFSIPTGELgpTLK--VKRN 651
Cdd:PRK08180 530 ----------------SLAEVLAH---PAVRAAFRERLARLNAQATGSSTRVARALLLDEPPSLDAGEI--TDKgyINQR 588
|
650
....*....|....*
gi 17933690 652 VVSKMYADEIEKLYA 666
Cdd:PRK08180 589 AVLARRAALVEALYA 603
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
78-534 |
1.46e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 73.90 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 78 TYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVDD- 156
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRs 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 157 ----AKQMDKIHAIRDKLPKLKAAI--QIQEPYSPYLKKED--GYYRWSEIESMNVSDvedqyMTRLENVaiNECCCLVY 228
Cdd:PLN03102 121 feplAREVLHLLSSEDSNLNLPVIFihEIDFPKRPSSEELDyeCLIQRGEPTPSLVAR-----MFRIQDE--HDPISLNY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 229 TSGTVGMPKGVMLSHdnitfdvRGIVKAMDRVVVGAEsivsyLPLSHVAAQTVDIYTCAfvaGCIWFADKDALKGTLVks 308
Cdd:PLN03102 194 TSGTTADPKGVVISH-------RGAYLSTLSAIIGWE-----MGTCPVYLWTLPMFHCN---GWTFTWGTAARGGTSV-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 309 lqdarPTRFMGVPRVYEKFQERMVAVASSSGSLKKMLaswakgitLKHYMVSQGKSSGgfrykiakslimskvkqalgfd 388
Cdd:PLN03102 257 -----CMRHVTAPEIYKNIEMHNVTHMCCVPTVFNIL--------LKGNSLDLSPRSG---------------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 389 RVLTLASAAAPMSPETKKyFLSLDLKIVDAFGMSETAGCHTIC--------LPDSV--------GLNTIG------KTLP 446
Cdd:PLN03102 302 PVHVLTGGSPPPAALVKK-VQRLGFQVMHAYGLTEATGPVLFCewqdewnrLPENQqmelkarqGVSILGladvdvKNKE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 447 GCESkfINKDANGHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPV 526
Cdd:PLN03102 381 TQES--VPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFKHG-WLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSV 456
|
....*...
gi 17933690 527 HIENTIKK 534
Cdd:PLN03102 457 EVENVLYK 464
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
77-582 |
1.72e-13 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 72.85 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 77 VTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVDD 156
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 157 AkqmdkihairdklpklkaaiqiqepyspylkkedgyyrwseiesmnvsdvedqymtrlenvaiNECCCLVYTSGTVGMP 236
Cdd:cd05971 87 S---------------------------------------------------------------DDPALIIYTSGTTGPP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 237 KGVMLSHdnitfdvrgivkamdRVVVGAESIVsYLPLShVAAQTVDIY-TCAFVAgciWFAdkdALKGTLVKSLqdarpt 315
Cdd:cd05971 104 KGALHAH---------------RVLLGHLPGV-QFPFN-LFPRDGDLYwTPADWA---WIG---GLLDVLLPSL------ 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 316 rFMGVPRVYEKFQ----ERMVAVASSSG--------SLKKMLAswAKGITLKHYMVS-QGKSSGGfrykiakslimskvk 382
Cdd:cd05971 155 -YFGVPVLAHRMTkfdpKAALDLMSRYGvttaflppTALKMMR--QQGEQLKHAQVKlRAIATGG--------------- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 383 QALGfdRVLTLASAAApmspetkkyflsLDLKIVDAFGMSET---AGCHTICLPDSVGlnTIGKTLPGCESKFInkDANG 459
Cdd:cd05971 217 ESLG--EELLGWAREQ------------FGVEVNEFYGQTECnlvIGNCSALFPIKPG--SMGKPIPGHRVAIV--DDNG 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 460 H-------GELCIR--GRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIEN 530
Cdd:cd05971 279 TplppgevGEIAVElpDPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDD-VITSSGYRIGPAEIEE 356
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 17933690 531 TIKKElDAISNAFLVG-------EQRKYLTVLitlktevdKDSGEPLDELSHESSVWVK 582
Cdd:cd05971 357 CLLKH-PAVLMAAVVGipdpirgEIVKAFVVL--------NPGETPSDALAREIQELVK 406
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
75-525 |
2.12e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 73.15 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 75 HTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEwFYSAMGAIHARGII-AGIYTTNSADAVQHVLESSHAQIVV 153
Cdd:PRK06178 57 HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQ-FHIVFFGILKLGAVhVPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 154 VDDAkQMDKIHAIRDKLP-----------KLKAAIQIQEPYS---PYLKKEDgyyrWSEI-ESMNVSDVEdqymTRLENV 218
Cdd:PRK06178 136 ALDQ-LAPVVEQVRAETSlrhvivtsladVLPAEPTLPLPDSlraPRLAAAG----AIDLlPALRACTAP----VPLPPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 219 AINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAmdrVVVGAESIV--SYLPLshvaaqtvdiytcafvagcIWFA 296
Cdd:PRK06178 207 ALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAV---AVVGGEDSVflSFLPE-------------------FWIA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 297 DKDAlkGTLVkslqdarPTrFMGVPRVyekfqermvavasssgslkkMLASW-AKGI--TLKHYMVSqgkSSGGFRYKIA 373
Cdd:PRK06178 265 GENF--GLLF-------PL-FSGATLV--------------------LLARWdAVAFmaAVERYRVT---RTVMLVDNAV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 374 KSLIMSKVKQalgFD-RVLTLASAAA---PMSPETKKYFLSLDLKIV--DAFGMSETAGCHTICL---PDSVGLNT---- 440
Cdd:PRK06178 312 ELMDHPRFAE---YDlSSLRQVRVVSfvkKLNPDYRQRWRALTGSVLaeAAWGMTETHTCDTFTAgfqDDDFDLLSqpvf 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 441 IGKTLPGCESKFINKDAN------GHGELCIRGRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEI 514
Cdd:PRK06178 389 VGLPVPGTEFKICDFETGellplgAEGEIVVRTPSLLKGYWNKPEATAEALRDG-WLHTGDIGKIDEQGFLHYLGRRKEM 467
|
490
....*....|.
gi 17933690 515 IITAGGENIPP 525
Cdd:PRK06178 468 LKVNGMSVFPS 478
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
63-510 |
4.05e-13 |
|
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: 71.79 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 63 PALRTKNGkngyhTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQH 142
Cdd:cd05930 4 VAVVDGDQ-----SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 143 VLESSHAQIVVVDDakqmdkihairdklpklkaaiqiqepyspylkkedgyyrwseiesmnvsdvedqymtrlenvaiNE 222
Cdd:cd05930 79 ILEDSGAKLVLTDP----------------------------------------------------------------DD 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 223 CCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvVVGAESIVSYLPLSHVAAQTvDIYTCAFVAGCIWFADKDALK 302
Cdd:cd05930 95 LAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP--LTPGDRVLQFTSFSFDVSVW-EIFGALLAGATLVVLPEEVRK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 303 --GTLVKSLQDARPTRFMGVPrvyekfqermvavasssgSLKKMLASWAKGITLkhymvsqgkssggfrykiaKSLimsk 380
Cdd:cd05930 172 dpEALADLLAEEGITVLHLTP------------------SLLRLLLQELELAAL-------------------PSL---- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 381 vkqalgfdRVLTLASAAAPmsPETKKYFLSL--DLKIVDAFGMSETAGCHTI--CLPDSVGLN--TIGKTLPGCESKFIn 454
Cdd:cd05930 211 --------RLVLVGGEALP--PDLVRRWRELlpGARLVNLYGPTEATVDATYyrVPPDDEEDGrvPIGRPIPNTRVYVL- 279
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17933690 455 kDANGH-------GELCIRGRHVFMGYIDNKEKTEESLDDDCWLH------SGDLGFVDDKGYVSLTGR 510
Cdd:cd05930 280 -DENLRpvppgvpGELYIGGAGLARGYLNRPELTAERFVPNPFGPgermyrTGDLVRWLPDGNLEFLGR 347
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
78-510 |
7.84e-13 |
|
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: 70.76 E-value: 7.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 78 TYKQYEQKVHQVAKAFIKL-GLEEHHSVGVLAFNCAeWFYSAMGAIHARGiiaGIY----TTNSADAVQHVLESSHAQIV 152
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSA-ELVVAILAVLKAG---AAYvpldPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 153 VVDdakqmdkiHAIRDKLPKLKAAIQIQEPyspylkkedgyyRWSEIESMNVSDVEDQYMTRLENVAineccCLVYTSGT 232
Cdd:TIGR01733 77 LTD--------SALASRLAGLVLPVILLDP------------LELAALDDAPAPPPPDAPSGPDDLA-----YVIYTSGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 233 VGMPKGVMLSHDNItfdVRGIVKAMDRVVVGAESIV-SYLPLSHVAAQTvDIYTCAFVAGCIWFADKDALKGTLvKSLQD 311
Cdd:TIGR01733 132 TGRPKGVVVTHRSL---VNLLAWLARRYGLDPDDRVlQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDDA-ALLAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 312 ARptrfmgvprvyekfQERMVAVASSSGSLKKML--ASWAKGITLKHYMVsqgkssGGfrykiakslimskvkQALGFDR 389
Cdd:TIGR01733 207 LI--------------AEHPVTVLNLTPSLLALLaaALPPALASLRLVIL------GG---------------EALTPAL 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 390 VLTLASAAApmspetkkyflslDLKIVDAFGMSET---AGCHTICLPD--SVGLNTIGKTLPGCESKFINKD-----ANG 459
Cdd:TIGR01733 252 VDRWRARGP-------------GARLINLYGPTETtvwSTATLVDPDDapRESPVPIGRPLANTRLYVLDDDlrpvpVGV 318
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 17933690 460 HGELCIRGRHVFMGYIDNKEKTEE--------SLDDDCWLHSGDLGFVDDKGYVSLTGR 510
Cdd:TIGR01733 319 VGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGR 377
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
76-576 |
7.86e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 71.26 E-value: 7.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 76 TVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFySAMGAiharGIIAGIYTT--NS---ADAVQHVLESSHAQ 150
Cdd:PRK13391 24 VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYL-EVCWA----AERSGLYYTcvNShltPAEAAYIVDDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 151 IVVVDDAKqMDKIHAIRDKLPKLKAAIQIQEPyspylKKEDGYYRWSEIesmnvsdVEDQYMTRLENVAINECccLVYTS 230
Cdd:PRK13391 99 ALITSAAK-LDVARALLKQCPGVRHRLVLDGD-----GELEGFVGYAEA-------VAGLPATPIADESLGTD--MLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 231 GTVGMPKGVM--LSHDNITfDVRGIVKAMDRVV-VGAESIvsYL---PLSHVAAQtvdiytcAFVAGCIwfadkdALKGT 304
Cdd:PRK13391 164 GTTGRPKGIKrpLPEQPPD-TPLPLTAFLQRLWgFRSDMV--YLspaPLYHSAPQ-------RAVMLVI------RLGGT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 305 LVkslqdarptrfmgvprVYEKFQ-ERMVAVASssgslkkmlaswakgitlkhymvsqgkssggfRYKIAKSLIMSKVkq 383
Cdd:PRK13391 228 VI----------------VMEHFDaEQYLALIE--------------------------------EYGVTHTQLVPTM-- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 384 algFDRVLTLAS----------------AAAPMSPETKKYFLSLDLKIVDAF-GMSETAGChTIC-------LPDSVGLN 439
Cdd:PRK13391 258 ---FSRMLKLPEevrdkydlsslevaihAAAPCPPQVKEQMIDWWGPIIHEYyAATEGLGF-TACdseewlaHPGTVGRA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 440 TIGKtLPGCeskfinkDANGH-------GELCIRGRHVFMgYIDNKEKTEESLDDDC-WLHSGDLGFVDDKGYVSLTGRS 511
Cdd:PRK13391 334 MFGD-LHIL-------DDDGAelppgepGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRA 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17933690 512 KEIIITaGGENIPPVHIEN---TIKKELDA----ISNAFLvGEQRKYLTVLItlktevdkDSGEPLDELSHE 576
Cdd:PRK13391 405 AFMIIS-GGVNIYPQEAENlliTHPKVADAavfgVPNEDL-GEEVKAVVQPV--------DGVDPGPALAAE 466
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
419-546 |
1.10e-12 |
|
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: 70.94 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 419 FGMSEtaGchTICL-----PDSVGLNTIGKTL-PGCESKFInkDANGH-------GELCIRGRHVFMGYIDNKEKTEESL 485
Cdd:COG1021 332 FGMAE--G--LVNYtrlddPEEVILTTQGRPIsPDDEVRIV--DEDGNpvppgevGELLTRGPYTIRGYYRAPEHNARAF 405
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17933690 486 DDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTIkKELDAISNAFLVG 546
Cdd:COG1021 406 TPDGFYRTGDLVRRTPDGYLVVEGRAKDQINR-GGEKIAAEEVENLL-LAHPAVHDAAVVA 464
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
78-532 |
3.01e-12 |
|
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: 69.45 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 78 TYKQYEQKVHQVAKAFIKLGLEEHHSVgVLAFNCAEWFYSAMGAIHARGIIA--GIYTTNSADAVQHVLESSHAQIVVVD 155
Cdd:cd05970 49 TFAELADYSDKTANFFKAMGIGKGDTV-MLTLKRRYEFWYSLLALHKLGAIAipATHQLTAKDIVYRIESADIKMIVAIA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 156 DAKQMDKIHAIRDKLPKLKAAIQIQEPyspylkKEDGYYRWSEiESMNVSdvEDQYMTRLENVAINECCCLVY-TSGTVG 234
Cdd:cd05970 128 EDNIPEEIEKAAPECPSKPKLVWVGDP------VPEGWIDFRK-LIKNAS--PDFERPTANSYPCGEDILLVYfSSGTTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 235 MPKgvMLSHDNiTFDVRGIVKAMDRVVVGAESivsylpLSHVAAQTV-------DIYTcAFVAGCIWFA-DKDALK-GTL 305
Cdd:cd05970 199 MPK--MVEHDF-TYPLGHIVTAKYWQNVREGG------LHLTVADTGwgkavwgKIYG-QWIAGAAVFVyDYDKFDpKAL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 306 VKSLQDARPTRFMGVPRVYEkfqermvavasssgslkkmlaswakgitlkhYMVSQGKSsggfRYKiaksliMSKVKQAl 385
Cdd:cd05970 269 LEKLSKYGVTTFCAPPTIYR-------------------------------FLIREDLS----RYD------LSSLRYC- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 386 gfdrvltlASAAAPMSPETKKYFLSLD-LKIVDAFGMSETagchTICLPDSVGLN----TIGKTLPGCESKFINKD---- 456
Cdd:cd05970 307 --------TTAGEALNPEVFNTFKEKTgIKLMEGFGQTET----TLTIATFPWMEpkpgSMGKPAPGYEIDLIDREgrsc 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 457 -ANGHGELCIR---GRHV--FMGYIDNKEKTEESLDDDCWlHSGDLGFVDDKGYVSLTGRSKEIIITAgGENIPPVHIEN 530
Cdd:cd05970 375 eAGEEGEIVIRtskGKPVglFGGYYKDAEKTAEVWHDGYY-HTGDAAWMDEDGYLWFVGRTDDLIKSS-GYRIGPFEVES 452
|
..
gi 17933690 531 TI 532
Cdd:cd05970 453 AL 454
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
226-561 |
5.59e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 69.18 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIvkamdRVVVGAES---IVSYLPLSHVAAQTVdiyTCAFVA----GCIWFADK 298
Cdd:PRK08633 787 IIFSSGSEGEPKGVMLSHHNILSNIEQI-----SDVFNLRNddvILSSLPFFHSFGLTV---TLWLPLlegiKVVYHPDP 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 299 -DALK-GTLVK----SLQDARPTRFmgvpRVYEKfqermvavassSGSLKK-MLASwakgitlkhymvsqgkssggFRYK 371
Cdd:PRK08633 859 tDALGiAKLVAkhraTILLGTPTFL----RLYLR-----------NKKLHPlMFAS--------------------LRLV 903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 372 IAkslimskvkqalgfdrvltlasAAAPMSPETKKYF-LSLDLKIVDAFGMSETAGCHTICLPDS--------VG--LNT 440
Cdd:PRK08633 904 VA----------------------GAEKLKPEVADAFeEKFGIRILEGYGATETSPVASVNLPDVlaadfkrqTGskEGS 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 441 IGKTLPGCESKFINKD------ANGHGELCIRGRHVFMGYIDNKEKTEESL---DDDCWLHSGDLGFVDDKGYVSLTGR- 510
Cdd:PRK08633 962 VGMPLPGVAVRIVDPEtfeelpPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRy 1041
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17933690 511 ---SKeiiitAGGENIPPVHIENTIKKELDAISNAFLV--------GEQrkyLTVLITLKTE 561
Cdd:PRK08633 1042 srfAK-----IGGEMVPLGAVEEELAKALGGEEVVFAVtavpdekkGEK---LVVLHTCGAE 1095
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
43-532 |
5.81e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 68.66 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 43 EEPISVPGLLKRTVNNYGDypALRTKNGKNGYHTVTYKQYEQKVHQVAKAFI-KLGLEEHHSVGVLAFNCAE-----WFY 116
Cdd:PRK05620 7 DVPLSLTRILEYGSTVHGD--TTVTTWGGAEQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEhlevlFAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 117 SAMGAIhargiIAGIYTTNSADAVQHVLESSHAQIVVVD--DAKQMDKIHAIRDKL---------PKLKAAIQIQE---- 181
Cdd:PRK05620 85 ACMGAV-----FNPLNKQLMNDQIVHIINHAEDEVIVADprLAEQLGEILKECPCVravvfigpsDADSAAAHMPEgikv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 182 -PYSPYLKKEDGYYRWSEIEsmnvsdvedqymtrlENVAINECcclvYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRV 260
Cdd:PRK05620 160 ySYEALLDGRSTVYDWPELD---------------ETTAAAIC----YSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 261 VVGAESIVSYLPLSHVAAQTVDIytCAFVAGC-IWFADKDALKGTLVKSLQDARPTRFMGVPRVYEKFqerMVavasssg 339
Cdd:PRK05620 221 VTHGESFLCCVPIYHVLSWGVPL--AAFMSGTpLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQL---MV------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 340 slkkmlaswakgitlkHYMVSQGKSsggfrykiaksliMSkvkqalgfdrVLTLASAAAPMSPE-TKKYFLSLDLKIVDA 418
Cdd:PRK05620 289 ----------------HYLKNPPER-------------MS----------LQEIYVGGSAVPPIlIKAWEERYGVDVVHV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 419 FGMSETAGCHTICLPDSvGLN---------TIGKTLPGCESKFINKD--ANGH----GELCIRGRHVFMGYIDNKEKTE- 482
Cdd:PRK05620 330 WGMTETSPVGTVARPPS-GVSgearwayrvSQGRFPASLEYRIVNDGqvMESTdrneGEIQVRGNWVTASYYHSPTEEGg 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17933690 483 ---------------ESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIENTI 532
Cdd:PRK05620 409 gaastfrgedvedanDRFTADGWLRTGDVGSVTRDGFLTIHDRARD-VIRSGGEWIYSAQLENYI 472
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
59-546 |
6.90e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 68.42 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 59 YGDYPALRTKNGkngyhTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNcAEWFYSAMGAIHARGiiAGIYTTN--- 135
Cdd:PRK07788 62 APDRAALIDERG-----TLTYAELDEQSNALARGLLALGVRAGDGVAVLARN-HRGFVLALYAAGKVG--ARIILLNtgf 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 136 SADAVQHVLESSHAQIVVVDDaKQMDKIHAIRDKLPKLKAAIQIQEPYSPylkkedgyyRWSEIESMnvsdveDQYMTRL 215
Cdd:PRK07788 134 SGPQLAEVAAREGVKALVYDD-EFTDLLSALPPDLGRLRAWGGNPDDDEP---------SGSTDETL------DDLIAGS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 216 EN----VAINECCCLVYTSGTVGMPKGVMLSHDNITFDVRGIVkamDRVVVGA-ESIVSYLPLSHvaAQTVDIYTCAFVA 290
Cdd:PRK07788 198 STaplpKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLL---SRVPFRAgETTLLPAPMFH--ATGWAHLTLAMAL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 291 GCiwfadkdalkgTLVksLQ---DARPTRfmgvpRVYEKFQ-ERMVAVASSsgsLKKMLASWAKgiTLKHYMVSqgkssg 366
Cdd:PRK07788 273 GS-----------TVV--LRrrfDPEATL-----EDIAKHKaTALVVVPVM---LSRILDLGPE--VLAKYDTS------ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 367 gfrykiakSLimskvkqalgfdRVLtlASAAAPMSPETKKYFLsldlkivDAFG--------MSETAGChTICLPDSVGL 438
Cdd:PRK07788 324 --------SL------------KII--FVSGSALSPELATRAL-------EAFGpvlynlygSTEVAFA-TIATPEDLAE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 439 N--TIGKTLPGCESKFInkDANGH-------GELCIRGRHVFMGYIDNKEKTEEslddDCWLHSGDLGFVDDKGYVSLTG 509
Cdd:PRK07788 374 ApgTVGRPPKGVTVKIL--DENGNevprgvvGRIFVGNGFPFEGYTDGRDKQII----DGLLSSGDVGYFDEDGLLFVDG 447
|
490 500 510
....*....|....*....|....*....|....*..
gi 17933690 510 RSKEIIITaGGENIPPVHIENTIkKELDAISNAFLVG 546
Cdd:PRK07788 448 RDDDMIVS-GGENVFPAEVEDLL-AGHPDVVEAAVIG 482
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
47-532 |
7.35e-12 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 68.25 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 47 SVPGLLKRTVNNYGDYPALRTkngknGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARG 126
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVF-----GGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 127 IIAGIYTTNSADAVQHVLESSHAQIVVVDdAKQMDKIHAIRDKLPKLKAAIQIQEPYSPYLKKEdgyYRWSEI----ESM 202
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVE-AALLAALEAADPGDLPLPAVWLLDAPASVSVPAG---WSTAPLppldAPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 203 NVSDVEDQymtrlENVAIneccclVYTSGTVGMPKGVMLSHDNitFDVRGIVKAMDRVVVGAESIVSYLPLSHVAAQtvD 282
Cdd:PRK06155 173 PAAAVQPG-----DTAAI------LYTSGTTGPSKGVCCPHAQ--FYWWGRNSAEDLEIGADDVLYTTLPLFHTNAL--N 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 283 IYTCAFVAGCiwfadkdalkgTLVkslqdarptrfmgvprVYEKFqermvavaSSSGSLKKMLASWAKGITLKHYMVSqg 362
Cdd:PRK06155 238 AFFQALLAGA-----------TYV----------------LEPRF--------SASGFWPAVRRHGATVTYLLGAMVS-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 363 kssggfrykiaksLIMSKVKQALgfDRVLTLASAAAPMSPET--KKYFLSLDLKIVDAFGMSET-AGCHTICLPDSVGln 439
Cdd:PRK06155 281 -------------ILLSQPARES--DRAHRVRVALGPGVPAAlhAAFRERFGVDLLDGYGSTETnFVIAVTHGSQRPG-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 440 TIGKTLPGCESKFINKD-----ANGHGELCIRGR--HVFM-GYIDNKEKTEESLDDdCWLHSGDLGFVDDKGYVSLTGRS 511
Cdd:PRK06155 344 SMGRLAPGFEARVVDEHdqelpDGEPGELLLRADepFAFAtGYFGMPEKTVEAWRN-LWFHTGDRVVRDADGWFRFVDRI 422
|
490 500
....*....|....*....|.
gi 17933690 512 KEiIITAGGENIPPVHIENTI 532
Cdd:PRK06155 423 KD-AIRRRGENISSFEVEQVL 442
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
63-532 |
8.62e-12 |
|
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: 67.50 E-value: 8.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 63 PALRTkngknGYHTVTYKQYEQKVHQVAKAFI-KLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQ 141
Cdd:cd05958 2 TCLRS-----PEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 142 HVLESSHAQIVVVDDAkqmdkihairdklpklkaaiqiqepyspylkkedgyyrwseiesmnVSDVEDqymtrlenvain 221
Cdd:cd05958 77 YILDKARITVALCAHA----------------------------------------------LTASDD------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 222 eCCCLVYTSGTVGMPKGVMLSHDnitfDVRGIVKAMDRVVVGAES---IVSYLPLSHV-AAQTVDIYTCAFVAGCIWFAD 297
Cdd:cd05958 99 -ICILAFTSGTTGAPKATMHFHR----DPLASADRYAVNVLRLREddrFVGSPPLAFTfGLGGVLLFPFGVGASGVLLEE 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 298 KDALKgtLVKSLQDARPTRFMGVPRVYEKfqerMVAVASSSGSLkkmlaswakgitlkhymvsqgkssggfrykiaksli 377
Cdd:cd05958 174 ATPDL--LLSAIARYKPTVLFTAPTAYRA----MLAHPDAAGPD------------------------------------ 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 378 mskvkqaLGFDRVLTLASAAAPmSPETKKYFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKDA 457
Cdd:cd05958 212 -------LSSLRKCVSAGEALP-AALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEG 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 458 N----GH-GELCIRGRhvfMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTI 532
Cdd:cd05958 284 NpvpdGTiGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVEDVL 359
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
419-532 |
9.73e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 64.25 E-value: 9.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 419 FGMSETAGCHTICLPDSV--GLNTIGKTLPGCEskfINKDANGHGELCIRGRHVFMGYIDNKEKTEESLDddcwlhSGDL 496
Cdd:PRK07445 261 YGMTETASQIATLKPDDFlaGNNSSGQVLPHAQ---ITIPANQTGNITIQAQSLALGYYPQILDSQGIFE------TDDL 331
|
90 100 110
....*....|....*....|....*....|....*.
gi 17933690 497 GFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTI 532
Cdd:PRK07445 332 GYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAI 366
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
48-542 |
1.09e-10 |
|
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: 64.82 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 48 VPGLLKRTVNNYGDYPALRTKNGKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGI 127
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 128 IAGIYTTNSADAVQHVLESSHAQIVVVDDAkqmdkiHAIRDKLPKLKAAIQIQEPYSPYLKK-------------EDGYY 194
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQDAEAKALITADG------FTRRGREVNLKEEADKACAQCPTVEKvvvvrhlgndftpAKGRD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 195 RWSeiesmnvSDVEDQYMTRLENVAINECCCLVYTSGTVGMPKGVMlsHDNITFDVRGivkAMDrvvvgaesivSYLPLS 274
Cdd:cd05968 217 LSY-------DEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTV--HVHAGFPLKA---AQD----------MYFQFD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 275 HVAAQTVdiytcafvagcIWFADKD------ALKGTLVkslqdARPTRFM--GVP------RVYEKFQERMVAVASSSGS 340
Cdd:cd05968 275 LKPGDLL-----------TWFTDLGwmmgpwLIFGGLI-----LGATMVLydGAPdhpkadRLWRMVEDHEITHLGLSPT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 341 LKKMLASWAKGITLKHymvsqGKSSggfrykiakslimskvkqalgfdrVLTLASAAAPMSPETKKYFLSLDLK----IV 416
Cdd:cd05968 339 LIRALKPRGDAPVNAH-----DLSS------------------------LRVLGSTGEPWNPEPWNWLFETVGKgrnpII 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 417 DAFGMSETAG----CHTICLPDSVGLNTigkTLPGCESKFINKDAN----GHGELCIRGRHVFM--GYIDNKEKTEE--- 483
Cdd:cd05968 390 NYSGGTEISGgilgNVLIKPIKPSSFNG---PVPGMKADVLDESGKparpEVGELVLLAPWPGMtrGFWRDEDRYLEtyw 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 17933690 484 SLDDDCWLHsGDLGFVDDKGYVSLTGRSKEIIITAgGENIPPVHIENTIKKELDAISNA 542
Cdd:cd05968 467 SRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVA-GKRVGPAEIESVLNAHPAVLESA 523
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
75-532 |
1.31e-10 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 64.07 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 75 HTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEwFYSAMGAIHARG-IIAGIYTTNSADAVQHVLESSHAQIVV 153
Cdd:cd05923 27 LRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVE-AVIALLALHRLGaVPALINPRLKAAELAELIERGEMTAAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 154 V-DDAKQMDKIHAIRDKLPKLKAAIQIQEPYSpylkkedgyyrwseiesmnVSDVEDQYMTRLENVAInecccLVYTSGT 232
Cdd:cd05923 106 IaVDAQVMDAIFQSGVRVLALSDLVGLGEPES-------------------AGPLIEDPPREPEQPAF-----VFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 233 VGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESIVSYLPLSHVAAqTVDIYTCAFVAGCIWFADKDALKGTLVKSLQDA 312
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIG-FFAVLVAALALDGTYVVVEEFDPADALKLIEQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 313 RPTRFMGVPRVYEKFqermvaVASSSGSLKKMlaswakgitlkhymvsqgkssggfrykiaKSLimskvkqalgfdRVLT 392
Cdd:cd05923 241 RVTSLFATPTHLDAL------AAAAEFAGLKL-----------------------------SSL------------RHVT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 393 LASAAAPmSPETKKYFLSLDLKIVDAFGMSETAgcHTICLPDSV-------GLNTIGKTLPGCESKFINKDANGHGELCI 465
Cdd:cd05923 274 FAGATMP-DAVLERVNQHLPGEKVNIYGTTEAM--NSLYMRDARtgtemrpGFFSEVRIVRIGGSPDEALANGEEGELIV 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17933690 466 R--GRHVFMGYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTI 532
Cdd:cd05923 351 AaaADAAFTGYLNQPEATAKKLQDG-WYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHPSEIERVL 417
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
221-529 |
2.07e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.87 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 221 NECCCLVYTSGTVGMPKGVMLSHDNITFDVRGI------VKAMDRVVvgaesivSYLPLSH-----------VAAQ-TVD 282
Cdd:PRK09192 176 DDIAYLQYSSGSTRFPRGVIITHRALMANLRAIshdglkVRPGDRCV-------SWLPFYHdmglvgflltpVATQlSVD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 283 -IYTCAFVA-GCIWFADKDALKGTLVKSlqdarPTrfMGvprvYEKFQERMvavasSSGSLKKM-LASW-AKGI------ 352
Cdd:PRK09192 249 yLPTRDFARrPLQWLDLISRNRGTISYS-----PP--FG----YELCARRV-----NSKDLAELdLSCWrVAGIgadmir 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 353 --TLKHYmvSQGKSSGGFR-------YKIAKS---LIMSKVKQALGFDRV----LTLASAAAPMSPETKKYflsldlkiv 416
Cdd:PRK09192 313 pdVLHQF--AEAFAPAGFDdkafmpsYGLAEAtlaVSFSPLGSGIVVEEVdrdrLEYQGKAVAPGAETRRV--------- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 417 dafgmSETAGChticlpdsvglntiGKTLPGCESKFINKDanGH-------GELCIRGRHVFMGYIDNKEkTEESLDDDC 489
Cdd:PRK09192 382 -----RTFVNC--------------GKALPGHEIEIRNEA--GMplpervvGHICVRGPSLMSGYFRDEE-SQDVLAADG 439
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 17933690 490 WLHSGDLGFVDDkGYVSLTGRSKEIIITaGGENIPPVHIE 529
Cdd:PRK09192 440 WLDTGDLGYLLD-GYLYITGRAKDLIII-NGRNIWPQDIE 477
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
419-525 |
2.58e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 63.49 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 419 FGMSETaGCHTICLP-DSVGLNTI-----GKTLPGCESKFINKDANG-----------HGELCIRGRHVFMGYIDNKEKT 481
Cdd:PRK05857 317 YGLSET-GCTALCLPtDDGSIVKIeagavGRPYPGVDVYLAATDGIGptapgagpsasFGTLWIKSPANMLGYWNNPERT 395
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 17933690 482 EESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPP 525
Cdd:PRK05857 396 AEVLIDG-WVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAP 437
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
393-546 |
3.13e-10 |
|
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: 62.73 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 393 LASAAAPMSPETkkyflsLDLKIVDAFGMSETAGCHT-ICLPDSVGLNTIGKTL-PGCESKFINKDAN----GH-GELCI 465
Cdd:cd05920 267 LSPALARRVPPV------LGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVDEEGNpvppGEeGELLT 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 466 RGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIENTIkKELDAISNAFLV 545
Cdd:cd05920 341 RGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKD-QINRGGEKIAAEEVENLL-LRHPAVHDAAVV 418
|
.
gi 17933690 546 G 546
Cdd:cd05920 419 A 419
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
76-576 |
4.39e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 76 TVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHArgiiaGIYTTnsadAVQHVLESSHAQIVVVD 155
Cdd:PRK13390 24 QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRS-----GLYIT----AINHHLTAPEADYIVGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 156 DAKQMDKIHAIRDKL-PKLKAAIQIQEPYSPYLkkeDGYyrwseiesmnvSDVEDQYMTRLENVAINEC-CCLVYTSGTV 233
Cdd:PRK13390 95 SGARVLVASAALDGLaAKVGADLPLRLSFGGEI---DGF-----------GSFEAALAGAGPRLTEQPCgAVMLYSSGTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 234 GMPKGVMLSHDNITFDVRGivkamDRVVVGAESIVSyLPLSHVAAQTVDIYTCAFVAgciWFADKDALKGTLVKSLQ-DA 312
Cdd:PRK13390 161 GFPKGIQPDLPGRDVDAPG-----DPIVAIARAFYD-ISESDIYYSSAPIYHAAPLR---WCSMVHALGGTVVLAKRfDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 313 RPTRfmgvpRVYEKFqeRMVAVASSSGSLKKMLAswakgitlkhymvsqgkssggfrykiakslIMSKVKQALGFDRVLT 392
Cdd:PRK13390 232 QATL-----GHVERY--RITVTQMVPTMFVRLLK------------------------------LDADVRTRYDVSSLRA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 393 LASAAAPMSPETKKYFLS-LDLKIVDAFGMSETAGCHTICLPD------SVGLNTIGkTLPGCESKFINKDANGHGELCI 465
Cdd:PRK13390 275 VIHAAAPCPVDVKHAMIDwLGPIVYEYYSSTEAHGMTFIDSPDwlahpgSVGRSVLG-DLHICDDDGNELPAGRIGTVYF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 466 RGRHVFMGYIDNKEKTEESLD--DDCWLHSGDLGFVDDKGYVSLTGRsKEIIITAGGENIPPVHIENTIKKElDAISNAF 543
Cdd:PRK13390 354 ERDRLPFRYLNDPEKTAAAQHpaHPFWTTVGDLGSVDEDGYLYLADR-KSFMIISGGVNIYPQETENALTMH-PAVHDVA 431
|
490 500 510
....*....|....*....|....*....|....*..
gi 17933690 544 LVG----EQRKYLTVLITLKTEVDkdsgePLDELSHE 576
Cdd:PRK13390 432 VIGvpdpEMGEQVKAVIQLVEGIR-----GSDELARE 463
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
75-530 |
4.60e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 62.61 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 75 HTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEwFYSAMGAihARgiIAGIYTT--N---SADAVQHVLESSHA 149
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPE-FFEVYWA--AR--RSGLYYTpiNwhlTAAEIAYIVDDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 150 QIVVVDdAKQMDKIHAIRDKLPK-LKAAIQIQEPyspylkkEDGYYRWSEIesmnvsdVEDQYMTRLENVAinECCCLVY 228
Cdd:PRK08276 85 KVLIVS-AALADTAAELAAELPAgVPLLLVVAGP-------VPGFRSYEEA-------LAAQPDTPIADET--AGADMLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 229 TSGTVGMPKGVM--LSHDNI----TFDVRGIVKAMDrvvVGAESIvsYL---PLSHvAAQTVdiytcafvagciWFADKD 299
Cdd:PRK08276 148 SSGTTGRPKGIKrpLPGLDPdeapGMMLALLGFGMY---GGPDSV--YLspaPLYH-TAPLR------------FGMSAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 300 ALKGTLVkslqdarptrfmgvprVYEKFQ-ERMVAVASssgslkkmlaswakgitlkhymvsqgkssggfRYKIAKSL-- 376
Cdd:PRK08276 210 ALGGTVV----------------VMEKFDaEEALALIE--------------------------------RYRVTHSQlv 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 377 -IMskvkqalgFDRVLTL----------------ASAAAPMSPETKKyflsldlKIVDAFG--------MSETAGchtIC 431
Cdd:PRK08276 242 pTM--------FVRMLKLpeevrarydvsslrvaIHAAAPCPVEVKR-------AMIDWWGpiiheyyaSSEGGG---VT 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 432 L---------PDSVGLNTIGktlpgcESKFINKDanghGELCIRGR----HVFMG-----YIDNKEKTEESLDDDCWLHS 493
Cdd:PRK08276 304 VitsedwlahPGSVGKAVLG------EVRILDED----GNELPPGEigtvYFEMDgypfeYHNDPEKTAAARNPHGWVTV 373
|
490 500 510
....*....|....*....|....*....|....*..
gi 17933690 494 GDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIEN 530
Cdd:PRK08276 374 GDVGYLDEDGYLYLTDRKSDMIIS-GGVNIYPQEIEN 409
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
104-532 |
5.22e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 62.39 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 104 VGVLAFNCAEwFYSAMGAIHARGII-AGIYTTNSADAVQHVLESSHAQIVVVDDAKqmdkihaiRDKLPKLKAAIQIQEP 182
Cdd:PRK07867 57 VGVLLDNTPE-FSLLLGAAALSGIVpVGLNPTRRGAALARDIAHADCQLVLTESAH--------AELLDGLDPGVRVINV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 183 YSPYLKKEDGYYRWSEIESMNVsDVEDQYMtrlenvainecccLVYTSGTVGMPKGVMLSHDNITFDvrGIVKAmDRVVV 262
Cdd:PRK07867 128 DSPAWADELAAHRDAEPPFRVA-DPDDLFM-------------LIFTSGTSGDPKAVRCTHRKVASA--GVMLA-QRFGL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 263 GAESiVSYL--PLSHVAAQTVDiYTCAFVAGciwfadkdalkGTLvkslqdARPTRFmgvprvyekfqermvavaSSSGS 340
Cdd:PRK07867 191 GPDD-VCYVsmPLFHSNAVMAG-WAVALAAG-----------ASI------ALRRKF------------------SASGF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 341 LKKMLASwakGITLKHYMvsqGKssggfrykiAKSLIMSKVKQALGFDRVLTLA---SAAAPMSPETKKYFlslDLKIVD 417
Cdd:PRK07867 234 LPDVRRY---GATYANYV---GK---------PLSYVLATPERPDDADNPLRIVygnEGAPGDIARFARRF---GCVVVD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 418 AFGMSETAgchtICL-------PDSVGLNTIG------KTLPGCESKFInkDANGH-------GELC-IRGRHVFMGYID 476
Cdd:PRK07867 296 GFGSTEGG----VAItrtpdtpPGALGPLPPGvaivdpDTGTECPPAED--ADGRLlnadeaiGELVnTAGPGGFEGYYN 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 17933690 477 NKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIENTI 532
Cdd:PRK07867 370 DPEADAERMRGG-VYWSGDLAYRDADGYAYFAGRLGD-WMRVDGENLGTAPIERIL 423
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
83-529 |
6.93e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 62.02 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 83 EQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIhargiIAGIYTT-----NSADAVQHVLESSHAQIVVVDDa 157
Cdd:PRK12406 18 AQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAM-----RLGAYAVpvnwhFKPEEIAYILEDSGARVLIAHA- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 158 kqmDKIHAIRDKLPK----LKAAI--QIQEPY--SPYLKKED----GYYRWSEIESMNVSDVEDQYMTrlenvaineccc 225
Cdd:PRK12406 92 ---DLLHGLASALPAgvtvLSVPTppEIAAAYriSPALLTPPagaiDWEGWLAQQEPYDGPPVPQPQS------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVmlSHDNITFDVRGIVKAMDRVVVG-AESIVSYL--PLSHVAAqtvdiYTCAFVAGciwfadkdALK 302
Cdd:PRK12406 157 MIYTSGTTGHPKGV--RRAAPTPEQAAAAEQMRALIYGlKPGIRALLtgPLYHSAP-----NAYGLRAG--------RLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 303 GTLVksLQdarptrfmgvPRvyekFQ-ERMVAvasssgslkkmlaswakgitlkhyMVSQGKSSGGFRYKIAKSLIM--- 378
Cdd:PRK12406 222 GVLV--LQ----------PR----FDpEELLQ------------------------LIERHRITHMHMVPTMFIRLLklp 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 379 SKVKQALGFDRVLTLASAAAPMSPETKKYFLSL-DLKIVDAFGMSETaGCHTICLPDSvGLN---TIGKTLPGCESKFIn 454
Cdd:PRK12406 262 EEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWwGPVIYEYYGSTES-GAVTFATSED-ALShpgTVGKAAPGAELRFV- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 455 kDANGH-------GELCIRGRhvfmGYID----NKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENI 523
Cdd:PRK12406 339 -DEDGRplpqgeiGEIYSRIA----GNPDftyhNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNI 412
|
....*.
gi 17933690 524 PPVHIE 529
Cdd:PRK12406 413 YPAEIE 418
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
388-551 |
1.51e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 60.95 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 388 DRVLTLASAAAPMSPETKKYFLS--LDLKIVDAFGMSE----TAGCHTICL--PDSVGLNTIGKTLPGCeskfinkdaNG 459
Cdd:PRK07638 253 ENKMKIISSGAKWEAEAKEKIKNifPYAKLYEFYGASElsfvTALVDEESErrPNSVGRPFHNVQVRIC---------NE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 460 HGELCIRGR----HV-----FMGYIDNKEKTEEsLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIEN 530
Cdd:PRK07638 324 AGEEVQKGEigtvYVkspqfFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIES 401
|
170 180
....*....|....*....|.
gi 17933690 531 TIkKELDAISNAFLVGEQRKY 551
Cdd:PRK07638 402 VL-HEHPAVDEIVVIGVPDSY 421
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
395-532 |
2.07e-09 |
|
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: 60.56 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 395 SAAAPMSPET-KKYFLSLDLKIVDAFGMSETAgchTICLpDSVGLN----TIGKTLPGCESKFInkDANGH-------GE 462
Cdd:cd05928 298 TGGEPLNPEVlEKWKAQTGLDIYEGYGQTETG---LICA-NFKGMKikpgSMGKASPPYDVQII--DDNGNvlppgteGD 371
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17933690 463 LCIRGRHV-----FMGYIDNKEKTEESLDDDCWLhSGDLGFVDDKGYVSLTGRSKEIIITAgGENIPPVHIENTI 532
Cdd:cd05928 372 IGIRVKPIrpfglFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSS-GYRIGPFEVESAL 444
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
461-572 |
4.33e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 59.37 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 461 GELCIRGRHVFMGYIDNKEKTEESLDDDCWLHSGDLGF-VDDKGYVSLT--GRSkeiiITAGGENIPPVHIENTIkKELD 537
Cdd:PRK06164 378 GEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYtRGDGQFVYQTrmGDS----LRLGGFLVNPAEIEHAL-EALP 452
|
90 100 110
....*....|....*....|....*....|....*
gi 17933690 538 AISNAFLVGEQRKYLTVLITLkteVDKDSGEPLDE 572
Cdd:PRK06164 453 GVAAAQVVGATRDGKTVPVAF---VIPTDGASPDE 484
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
390-626 |
7.71e-09 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 58.89 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 390 VLTLASAAAPMSPETKKYFLSlDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKD-----ANGHGELC 464
Cdd:PRK06060 265 VVSAGEALELGLAERLMEFFG-GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDgttagPGVEGDLW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 465 IRGRHVFMGYIDnkeKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPPVHIENTIKKElDAISNAFL 544
Cdd:PRK06060 344 VRGPAIAKGYWN---RPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVI-GGVNVDPREVERLIIED-EAVAEAAV 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 545 VGEqrKYLTVLITLKTEVDKDSGEPLDElshesSVwVKSLgveHKTVSDILAAGPCPKVWKSIEDAIKRANKQSISNAQK 624
Cdd:PRK06060 419 VAV--RESTGASTLQAFLVATSGATIDG-----SV-MRDL---HRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
..
gi 17933690 625 VQ 626
Cdd:PRK06060 488 KQ 489
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
226-538 |
1.05e-08 |
|
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: 58.16 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVVGAESIvsYL---PLSHVAAQTvdiytcafvagciWFADKDALK 302
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPGADSV--YLspaPLYHAAPFR-------------WSMTALFMG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 303 GTLVkslqdarptrfmgvprVYEKFQ-ERMVAVasssgsLKKMLASWAKGI-TLKHYMVsqgKSSGGFRYKIAksliMSK 380
Cdd:cd05929 195 GTLV----------------LMEKFDpEEFLRL------IERYRVTFAQFVpTMFVRLL---KLPEAVRNAYD----LSS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 381 VKqalgfdrvlTLASAAAPMSPETKKYFLSLDLKIVDAF-GMSETAGChTICL-------PDSVGLNTIGKTlpgcesKF 452
Cdd:cd05929 246 LK---------RVIHAAAPCPPWVKEQWIDWGGPIIWEYyGGTEGQGL-TIINgeewlthPGSVGRAVLGKV------HI 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 453 InkDANGH-------GELCIRGRHVFMgYIDNKEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITaGGENIPP 525
Cdd:cd05929 310 L--DEDGNevppgeiGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIIS-GGVNIYP 385
|
330
....*....|....*.
gi 17933690 526 VHIEN---TIKKELDA 538
Cdd:cd05929 386 QEIENaliAHPKVLDA 401
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
229-529 |
1.64e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 57.47 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 229 TSGTVGMPKGVMLSHDNITFDVRGIVkamDRVVVGAESIV--SYLPLSHVAAQTvdIYTCAFVAGC-IWFADKDALKGTL 305
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLN---ARVGLDAATDVgcSWLPLYHDMGLA--FLLTAALAGApLWLAPTTAFSASP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 306 VKSLQ---DARPTrfmgvprvyekfqerMVAVASSSGSLKKMLASWAKGITLK--HYMVSQGK--SSGGF-RYKIAksli 377
Cdd:PRK05851 235 FRWLSwlsDSRAT---------------LTAAPNFAYNLIGKYARRVSDVDLGalRVALNGGEpvDCDGFeRFATA---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 378 MSKVkqalGFDrvltlASAAAPmspetkkyflsldlkivdAFGMSETAGCHT------------ICLPDSVGLNT---IG 442
Cdd:PRK05851 296 MAPF----GFD-----AGAAAP------------------SYGLAESTCAVTvpvpgiglrvdeVTTDDGSGARRhavLG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 443 KTLPGCESKFINKDA----NGH--GELCIRGRHVFMGYIDnkektEESLDDDCWLHSGDLGFVDDKGYVsLTGRSKEIII 516
Cdd:PRK05851 349 NPIPGMEVRISPGDGaagvAGReiGEIEIRGASMMSGYLG-----QAPIDPDDWFPTGDLGYLVDGGLV-VCGRAKELIT 422
|
330
....*....|...
gi 17933690 517 TAgGENIPPVHIE 529
Cdd:PRK05851 423 VA-GRNIFPTEIE 434
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
76-511 |
3.57e-08 |
|
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: 56.16 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 76 TVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVD 155
Cdd:cd17653 22 SLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 156 DAKqmdkihairdklpklkaaiqiqepyspylkkedgyyrwseiesmnvsdvedqymtrlenvaiNECCCLVYTSGTVGM 235
Cdd:cd17653 102 DSP--------------------------------------------------------------DDLAYIIFTSGSTGI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 236 PKGVMLSHDNITfdvrGIVKAM-DRVVVGAESIVsyLPLSHVA--AQTVDIYTCAFVAGCIWFADKDALKGTLVKS---- 308
Cdd:cd17653 120 PKGVMVPHRGVL----NYVSQPpARLDVGPGSRV--AQVLSIAfdACIGEIFSTLCNGGTLVLADPSDPFAHVARTvdal 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 309 ------LQDARPTRFmgvPRVyekfqeRMVAVASSSGSlKKMLASWAKGITLkhymvsqgkssggfrykiakslimskvk 382
Cdd:cd17653 194 mstpsiLSTLSPQDF---PNL------KTIFLGGEAVP-PSLLDRWSPGRRL---------------------------- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 383 qalgfdrvltlasaaapmspetkkyflsldlkiVDAFGMSETagchTIC------LPDSVglNTIGKTLPGceSKFINKD 456
Cdd:cd17653 236 ---------------------------------YNAYGPTEC----TISstmtelLPGQP--VTIGKPIPN--STCYILD 274
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17933690 457 ANGH-------GELCIRGRHVFMGYIDNKEKTEESLDDDCWLH------SGDLGFVDDKGYVSLTGRS 511
Cdd:cd17653 275 ADLQpvpegvvGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGRE 342
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
418-546 |
4.08e-08 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 55.39 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 418 AFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKDAN----GH-GELCIRGRHVFMGYIDNKEKTEESLDDDcWLH 492
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGRevpdGEvGEIVARGPTVMAGYWNRPEVNARRTRGG-WHH 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 17933690 493 SGDLGFVDDKGYVSLTGrSKEIIITAGGENIPPVHIENTIkKELDAISNAFLVG 546
Cdd:cd17636 221 TNDLGRREPDGSLSFVG-PKTRMIKSGAENIYPAEVERCL-RQHPAVADAAVIG 272
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
52-602 |
4.48e-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: 56.43 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 52 LKRTVNNYGDYPALrTKNGKNG--YHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAM-----GAIHA 124
Cdd:cd17634 59 LDRHLRENGDRTAI-IYEGDDTsqSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLacariGAVHS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 125 RgiiagIYTTNSADAVQHVLESSHAQIVVVDDakqmDKIHAIR--DKLPKLKAAIQIQEPySPY----LKKEDGYYRWSE 198
Cdd:cd17634 138 V-----IFGGFAPEAVAGRIIDSSSRLLITAD----GGVRAGRsvPLKKNVDDALNPNVT-SVEhvivLKRTGSDIDWQE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 199 IESMNVSDVEDQYMTRLENVAIN--ECCCLVYTSGTVGMPKGVMlsHDNITFDVRGIVKAMDRVVVGAEsivsylplshv 276
Cdd:cd17634 208 GRDLWWRDLIAKASPEHQPEAMNaeDPLFILYTSGTTGKPKGVL--HTTGGYLVYAATTMKYVFDYGPG----------- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 277 aaqtvDIYTCA----FVAGCIWFadkdaLKGTLVkslqdARPTRFM--GVPrvyekfqermvaVASSSGSLKKMLAswak 350
Cdd:cd17634 275 -----DIYWCTadvgWVTGHSYL-----LYGPLA-----CGATTLLyeGVP------------NWPTPARMWQVVD---- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 351 gitlKHYMVSQGKSSGGFRykiakSLIMSKVKQALGFDR--VLTLASAAAPMSPETKKYFLSLDLK----IVDAFGMSET 424
Cdd:cd17634 324 ----KHGVNILYTAPTAIR-----ALMAAGDDAIEGTDRssLRILGSVGEPINPEAYEWYWKKIGKekcpVVDTWWQTET 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 425 AGCHTICLPDSVGLNTIGKTLP--GCESKFInkDANGH-------GELCIR-----GRHVFMGYIDNKEKTEESLDDDCW 490
Cdd:cd17634 395 GGFMITPLPGAIELKAGSATRPvfGVQPAVV--DNEGHpqpggteGNLVITdpwpgQTRTLFGDHERFEQTYFSTFKGMY 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 491 LHsGDLGFVDDKGYVSLTGRSKEIIITAgGENIPPVHIENTIKKElDAISNAFLVG------EQRKYLTVliTLKTEVdk 564
Cdd:cd17634 473 FS-GDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIESVLVAH-PKVAEAAVVGiphaikGQAPYAYV--VLNHGV-- 545
|
570 580 590
....*....|....*....|....*....|....*...
gi 17933690 565 dsgEPLDELSHESSVWVKSLGVEHKTVSDILAAGPCPK 602
Cdd:cd17634 546 ---EPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPK 580
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
226-548 |
4.85e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.72 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFD---VR---GIVKAMDRVvvgaesIVSYLPLSHvaaqtvDIytcafvagciwfadkd 299
Cdd:PRK05691 171 LQYTSGSTALPKGVQVSHGNLVANeqlIRhgfGIDLNPDDV------IVSWLPLYH------DM---------------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 300 ALKGTLVKSLqdarptrFMGVPRVY---EKFQERMVavasssgslkkmlaSWAKGITlkHYmvsQGKSSGG--FRYKIAK 374
Cdd:PRK05691 223 GLIGGLLQPI-------FSGVPCVLmspAYFLERPL--------------RWLEAIS--EY---GGTISGGpdFAYRLCS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 375 SLIMSKVKQALGFDRVLTLASAAAPMSPET---------------KKYFLSLDL-------------KIVDAFGMSETAG 426
Cdd:PRK05691 277 ERVSESALERLDLSRWRVAYSGSEPIRQDSlerfaekfaacgfdpDSFFASYGLaeatlfvsggrrgQGIPALELDAEAL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 427 CHTICLP-DSVGLNTIGKTLPGCESKFINK------DANGHGELCIRGRHVFMGYIDNKEKTEES---LDDDCWLHSGDL 496
Cdd:PRK05691 357 ARNRAEPgTGSVLMSCGRSQPGHAVLIVDPqslevlGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDL 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 17933690 497 GFVDDkGYVSLTGRSKEIIITAgGENIPPVHIENTIKKELDAISN----AFLVGEQ 548
Cdd:PRK05691 437 GFLRD-GELFVTGRLKDMLIVR-GHNLYPQDIEKTVEREVEVVRKgrvaAFAVNHQ 490
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
226-550 |
5.86e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 56.13 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRgivKAMDRVVVGAESIV-SYLPLSHvaaqtvdiytcAFvagciwfadkdALKGT 304
Cdd:PRK06814 798 ILFTSGSEGTPKGVVLSHRNLLANRA---QVAARIDFSPEDKVfNALPVFH-----------SF-----------GLTGG 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 305 LVKSLQDARPTRFMGVPRVYEKFQERMVAV-ASSSGSLKKMLASWAkgitlkhymvsqgkssggfRYkiakslimskvkq 383
Cdd:PRK06814 853 LVLPLLSGVKVFLYPSPLHYRIIPELIYDTnATILFGTDTFLNGYA-------------------RY------------- 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 384 ALGFD-RVLTLASAAA-PMSPETKK-YFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKF-----INK 455
Cdd:PRK06814 901 AHPYDfRSLRYVFAGAeKVKEETRQtWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLepvpgIDE 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 456 DanghGELCIRGRHVFMGYID-NKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSK---EIiitaGGENIPPVHIEnT 531
Cdd:PRK06814 981 G----GRLFVRGPNVMLGYLRaENPGVLEPPADG-WYDTGDIVTIDEEGFITIKGRAKrfaKI----AGEMISLAAVE-E 1050
|
330 340
....*....|....*....|.
gi 17933690 532 IKKEL--DAISNAFLVGEQRK 550
Cdd:PRK06814 1051 LAAELwpDALHAAVSIPDARK 1071
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
226-519 |
6.38e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 55.87 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGI-----VKAMDRvvvgaesIVSYLPLSHVAAQTVDIYTcAFVAGCIWFadkda 300
Cdd:PRK08043 370 ILFTSGSEGHPKGVVHSHKSLLANVEQIktiadFTPNDR-------FMSALPLFHSFGLTVGLFT-PLLTGAEVF----- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 301 lkgtLVKSlqdarPTRFMGVPR-VYEkfQERMVAVASSSgslkkmlaswakgiTLKHYmvsqgkssggfrykiakslimS 379
Cdd:PRK08043 437 ----LYPS-----PLHYRIVPElVYD--RNCTVLFGTST--------------FLGNY---------------------A 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 380 KVKQALGFDRVLTLASAAAPMSPETKK-YFLSLDLKIVDAFGMSETAGCHTICLPDSVGLNTIGKTLPGCESKFINKD-- 456
Cdd:PRK08043 471 RFANPYDFARLRYVVAGAEKLQESTKQlWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPgi 550
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17933690 457 ANGhGELCIRGRHVFMGYI-------------DNKEKTEESldddCWLHSGDLGFVDDKGYVSLTGRSKEIIITAG 519
Cdd:PRK08043 551 EQG-GRLQLKGPNIMNGYLrvekpgvlevptaENARGEMER----GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
104-542 |
1.44e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 54.65 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 104 VGVLAFNCAEwFYSAMGAIHARG-IIAGIYTTNSADAVQHVLESSHAQIVVVDDA--KQMDKIHAIRDKL-----PKLKA 175
Cdd:PRK13388 55 VGVLLGNTPE-MLFWLAAAALGGyVLVGLNTTRRGAALAADIRRADCQLLVTDAEhrPLLDGLDLPGVRVldvdtPAYAE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 176 AIQIQEPYSPYlkkedgyyrwSEIesmnvsDVEDQYMtrlenvainecccLVYTSGTVGMPKGVMLSHDNITFDVRGIVK 255
Cdd:PRK13388 134 LVAAAGALTPH----------REV------DAMDPFM-------------LIFTSGTTGAPKAVRCSHGRLAFAGRALTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 256 AMDRVvvgaESIVSYL--PLSHVAAqTVDIYTCAFVAGciwfadkdalkGTLvkslqdARPTRFmgvprvyekfqermva 333
Cdd:PRK13388 185 RFGLT----RDDVCYVsmPLFHSNA-VMAGWAPAVASG-----------AAV------ALPAKF---------------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 334 vaSSSGSLKKMLASwakGITlkhYMVSQGKssggfrykiAKSLIMSKVKQALGFDRVLTLA--SAAapmSPETKKYFLS- 410
Cdd:PRK13388 227 --SASGFLDDVRRY---GAT---YFNYVGK---------PLAYILATPERPDDADNPLRVAfgNEA---SPRDIAEFSRr 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 411 LDLKIVDAFGMSETAGchTICLPDSVGLNTIGKTLPG---------CESKFINKDANGH--------GELCIR-GRHVFM 472
Cdd:PRK13388 287 FGCQVEDGYGSSEGAV--IVVREPGTPPGSIGRGAPGvaiynpetlTECAVARFDAHGAllnadeaiGELVNTaGAGFFE 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 473 GYIDNKEKTEESLDDDcWLHSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIENtIKKELDAISNA 542
Cdd:PRK13388 365 GYYNNPEATAERMRHG-MYWSGDLAYRDADGWIYFAGRTAD-WMRVDGENLSAAPIER-ILLRHPAINRV 431
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
227-526 |
2.60e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 53.13 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 227 VYTSGTVGMPKGVMLSHDNItfdvRGIVKAMDRVVVGAESIVSYLPLSHVAAQTVdiytcafvagciwfadkdalkgtLV 306
Cdd:PRK07824 41 VATSGTTGTPKGAMLTAAAL----TASADATHDRLGGPGQWLLALPAHHIAGLQV-----------------------LV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 307 KSLQ-DARPtrfmgvprvyekfqermVAVASSSGSLKKMLASWAKGITlkhymvsqgkssGGFRYKiakSLIMSKVKQAL 385
Cdd:PRK07824 94 RSVIaGSEP-----------------VELDVSAGFDPTALPRAVAELG------------GGRRYT---SLVPMQLAKAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 386 G----------FDRVLTlasAAAPMSPETKKYFLSLDLKIVDAFGMSETAGChtiCLPDsvglntiGKTLPGCESKFINk 455
Cdd:PRK07824 142 DdpaataalaeLDAVLV---GGGPAPAPVLDAAAAAGINVVRTYGMSETSGG---CVYD-------GVPLDGVRVRVED- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17933690 456 danghGELCIRGRHVFMGY---IDNKEKTEESldddcWLHSGDLGFVDDkGYVSLTGRSKEIIITAGGENIPPV 526
Cdd:PRK07824 208 -----GRIALGGPTLAKGYrnpVDPDPFAEPG-----WFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQV 270
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
61-532 |
3.52e-07 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 53.22 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 61 DYPALRTKNGkngyhTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNcAEWFYSAMGAiHARgIIAGIYTTN---SA 137
Cdd:PRK13382 58 DRPGLIDELG-----TLTWRELDERSDALAAALQALPIGEPRVVGIMCRN-HRGFVEALLA-ANR-IGADILLLNtsfAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 138 DAVQHVLESSHAQIVVVDD--AKQMDKihAIRDKlPKlkaAIQIQEpyspylkkedgyyrWSEIESMNVSDV-------- 207
Cdd:PRK13382 130 PALAEVVTREGVDTVIYDEefSATVDR--ALADC-PQ---ATRIVA--------------WTDEDHDLTVEVliaahagq 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 208 EDQYMTRLENVAIneccclvYTSGTVGMPKGVMLSHDNITFDVRGIvkaMDRVVVGAES-IVSYLPLSHvaaqtvdiytc 286
Cdd:PRK13382 190 RPEPTGRKGRVIL-------LTSGTTGTPKGARRSGPGGIGTLKAI---LDRTPWRAEEpTVIVAPMFH----------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 287 AFVAGCIWFADkdALKGTLVkslqdarpTRfmgvprvyEKFqermvavaSSSGSLKKMLASWAKGITLKHYMVSQgkssg 366
Cdd:PRK13382 249 AWGFSQLVLAA--SLACTIV--------TR--------RRF--------DPEATLDLIDRHRATGLAVVPVMFDR----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 367 gfrykiakslIMSKVKQALGFDRVLTLASAAA---PMSPETKKYFLsldlkivDAFG-------MSETAGCHTICLPDSV 436
Cdd:PRK13382 298 ----------IMDLPAEVRNRYSGRSLRFAAAsgsRMRPDVVIAFM-------DQFGdviynnyNATEAGMIATATPADL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 437 --GLNTIGKTLPGCESKFInkDANGH-------GELCIRGRHVFMGYIDNKEKTEEslddDCWLHSGDLGFVDDKGYVSL 507
Cdd:PRK13382 361 raAPDTAGRPAEGTEIRIL--DQDFRevptgevGTIFVRNDTQFDGYTSGSTKDFH----DGFMASGDVGYLDENGRLFV 434
|
490 500
....*....|....*....|....*
gi 17933690 508 TGRSKEIIITaGGENIPPVHIENTI 532
Cdd:PRK13382 435 VGRDDEMIVS-GGENVYPIEVEKTL 458
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
419-545 |
3.95e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 53.07 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 419 FGMSETAGCHT-ICLPDSVGLNTIGKTL-PGCESKFINKDAN----GH-GELCIRGRHVFMGYIDNKEKTEESLDDDCWL 491
Cdd:PRK10946 332 FGMAEGLVNYTrLDDSDERIFTTQGRPMsPDDEVWVADADGNplpqGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFY 411
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 17933690 492 HSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIENTIKKElDAISNAFLV 545
Cdd:PRK10946 412 CSGDLVSIDPDGYITVVGREKD-QINRGGEKIAAEEIENLLLRH-PAVIHAALV 463
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
461-574 |
5.53e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 52.64 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 461 GELCIRGRHVFMGYIDNKEKTEE----SLDDDC-------WLHSGDLGFVDDkGYVSLTGRSKEIIITAgGENIPPVHIE 529
Cdd:PRK05850 398 GEIWVHGDNVAAGYWQKPEETERtfgaTLVDPSpgtpegpWLRTGDLGFISE-GELFIVGRIKDLLIVD-GRNHYPDDIE 475
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 17933690 530 NTIKK----ELDAISNAFLVGEQrkyLTVLITLKTEVDKDsGEPLDELS 574
Cdd:PRK05850 476 ATIQEitggRVAAISVPDDGTEK---LVAIIELKKRGDSD-EEAMDRLR 520
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
51-510 |
8.01e-07 |
|
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: 52.20 E-value: 8.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 51 LLKRTVNNYGDYPALRTKNGkngyhTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAG 130
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDR-----SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 131 IYTTNSADAVQHVLESSHAQIVVVDdakqmdkiHAIRDKLPKLKAAIQIQEPYSPYlkkedgyyrwSEIESMNVSDVEDq 210
Cdd:cd12117 77 LDPELPAERLAFMLADAGAKVLLTD--------RSLAGRAGGLEVAVVIDEALDAG----------PAGNPAVPVSPDD- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 211 ymtrlenvaineCCCLVYTSGTVGMPKGVMLSHDNITfdvrGIVKAMDRVVVGAESIVsyLPLSHVA--AQTVDIYTCAF 288
Cdd:cd12117 138 ------------LAYVMYTSGSTGRPKGVAVTHRGVV----RLVKNTNYVTLGPDDRV--LQTSPLAfdASTFEIWGALL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 289 VAGCIWFADKDALkgtlvkslqdarptrfMGVPRVYEKFQERMVAVASSSGSLKKMLASWAKGI--TLKHYMVsqgkssG 366
Cdd:cd12117 200 NGARLVLAPKGTL----------------LDPDALGALIAEEGVTVLWLTAALFNQLADEDPECfaGLRELLT------G 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 367 GFRYKIAkslimsKVKQALgfdrvltlasAAAPmspetkkyflslDLKIVDAFGMSET---AGCHTICLPDSVGLNT-IG 442
Cdd:cd12117 258 GEVVSPP------HVRRVL----------AACP------------GLRLVNGYGPTENttfTTSHVVTELDEVAGSIpIG 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 443 KTLPGCESKFInkDANGH-------GELCIRGRHVFMGYIDNKEKTEESLDDDCWL------HSGDLGFVDDKGYVSLTG 509
Cdd:cd12117 310 RPIANTRVYVL--DEDGRpvppgvpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLG 387
|
.
gi 17933690 510 R 510
Cdd:cd12117 388 R 388
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
76-247 |
1.77e-06 |
|
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: 50.94 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 76 TVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVD 155
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 156 DAkqmdkihaIRDKLPKLKAAIQIQEPYspyLKKEDGyyrwSEIESMNVSDvedqymtrlenvainECCCLVYTSGTVGM 235
Cdd:cd17656 93 RH--------LKSKLSFNKSTILLEDPS---ISQEDT----SNIDYINNSD---------------DLLYIIYTSGTTGK 142
|
170
....*....|..
gi 17933690 236 PKGVMLSHDNIT 247
Cdd:cd17656 143 PKGVQLEHKNMV 154
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
76-537 |
2.57e-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: 50.43 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 76 TVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVVD 155
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 156 dakqmdkihairdklpklkaaiqiqepyspylkkedgyyrwseiesmnvsdvedqymtrlenvaineCCCLVYTSGTVGM 235
Cdd:cd05940 83 -------------------------------------------------------------------AALYIYTSGTTGL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 236 PKGVMLSHDNIT-----FDVRGIVKAMDRvvvgaesIVSYLPLSHVAAQTVDIYTCAFVAGCIWFADK--------DALK 302
Cdd:cd05940 96 PKAAIISHRRAWrggafFAGSGGALPSDV-------LYTCLPLYHSTALIVGWSACLASGATLVIRKKfsasnfwdDIRK 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 303 ---------GTLVKSL--QDARPT------RFM---GV-PRVYEKFQERmvavasssgslkkmlasWAKGITLKHYMVSQ 361
Cdd:cd05940 169 yqatifqyiGELCRYLlnQPPKPTerkhkvRMIfgnGLrPDIWEEFKER-----------------FGVPRIAEFYAATE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 362 GKSSggfrykiakSLIMSKVKQALGFDRVLTLASAAApmspETKKYFLSLDLKIVDAFGMSETAGchticlPDSVGLnTI 441
Cdd:cd05940 232 GNSG---------FINFFGKPGAIGRNPSLLRKVAPL----ALVKYDLESGEPIRDAEGRCIKVP------RGEPGL-LI 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 442 GKtlpgceskfinkdanghgelcIRGRHVFMGYIDNKEKTEESLDD-----DCWLHSGDLGFVDDKGYVSL------TGR 510
Cdd:cd05940 292 SR---------------------INPLEPFDGYTDPAATEKKILRDvfkkgDAWFNTGDLMRLDGEGFWYFvdrlgdTFR 350
|
490 500
....*....|....*....|....*..
gi 17933690 511 SKeiiitagGENIPPVHIENTIKKELD 537
Cdd:cd05940 351 WK-------GENVSTTEVAAVLGAFPG 370
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
440-578 |
3.73e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 49.99 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 440 TIGKTLPGCESKFInkDANGH-------GELCIRGRHVFMGYIDNKEKTEEslddDCWLHSGDLGFVDDKGYVSLTGRSK 512
Cdd:PRK13383 346 TVGKPVAGCPVRIL--DRNNRpvgprvtGRIFVGGELAGTRYTDGGGKAVV----DGMTSTGDMGYLDNAGRLFIVGRED 419
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17933690 513 EIIITaGGENIPPVHIENTIKKELDAISNAFL-VGEQR--KYLTVLITLKTEVDKDSGEPLDELSHESS 578
Cdd:PRK13383 420 DMIIS-GGENVYPRAVENALAAHPAVADNAVIgVPDERfgHRLAAFVVLHPGSGVDAAQLRDYLKDRVS 487
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
419-545 |
6.06e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 49.10 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 419 FGMSETAGchTICLPDSVGLNTIGKTLPGCESKFINkdanghGELCIRGRHVFMGYIDNKEKTeeSL-DDDCWLHSGDLG 497
Cdd:PRK09029 271 YGLTEMAS--TVCAKRADGLAGVGSPLPGREVKLVD------GEIWLRGASLALGYWRQGQLV--PLvNDEGWFATRDRG 340
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17933690 498 FVDDkGYVSLTGRSKEIIITaGGENIPPVHIENTIKKeLDAISNAFLV 545
Cdd:PRK09029 341 EWQN-GELTILGRLDNLFFS-GGEGIQPEEIERVINQ-HPLVQQVFVV 385
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
389-546 |
1.76e-05 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 47.51 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 389 RVLTLASAAAPMSPETKKYF-LSLDLKIVDAFGMSETAG--CHTICLPDSVGLNTIGKTLPGCESKFINKDAN--GHGEL 463
Cdd:cd05973 206 RLRRVSSAGEPLTPEVIRWFdAALGVPIHDHYGQTELGMvlANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDelGPGEP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 464 CIRGRHV-------FMGYidnkEKTEESLDDDCWLHSGDLGFVDDKGYVSLTGRSKEIIITAgGENIPPVHIENTIKKEl 536
Cdd:cd05973 286 GRLAIDIansplmwFRGY----QLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEH- 359
|
170
....*....|
gi 17933690 537 DAISNAFLVG 546
Cdd:cd05973 360 PAVAEAAVIG 369
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
44-247 |
4.61e-05 |
|
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: 46.77 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 44 EPISVPGLLKRTVNNYGDYPALRTkngknGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVlafnCAE---WFYSAMG 120
Cdd:COG1020 474 ADATLHELFEAQAARTPDAVAVVF-----GDQSLTYAELNARANRLAHHLRALGVGPGDLVGV----CLErslEMVVALL 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 121 AIHARGiiaGIY----TTNSADAVQHVLESSHAQIVVVDDAkqmdkihaIRDKLPKLKAA-IQIQEPyspylkkedgyyr 195
Cdd:COG1020 545 AVLKAG---AAYvpldPAYPAERLAYMLEDAGARLVLTQSA--------LAARLPELGVPvLALDAL------------- 600
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17933690 196 wsEIESMNVSDVEDQymTRLENVAineccCLVYTSGTVGMPKGVMLSHDNIT 247
Cdd:COG1020 601 --ALAAEPATNPPVP--VTPDDLA-----YVIYTSGSTGRPKGVMVEHRALV 643
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
76-294 |
4.74e-05 |
|
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: 46.52 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 76 TVTYKQYEQKVHQVAKAFIK-LGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIVVV 154
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 155 DdakqmdkihairdklPKLKAAIqiqEPYSPYLKKEDG--YYRWSEIESMNVSDVEDQYMTRLE---------NVAINEC 223
Cdd:cd05938 85 A---------------PELQEAV---EEVLPALRADGVsvWYLSHTSNTEGVISLLDKVDAASDepvpaslraHVTIKSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 224 CCLVYTSGTVGMPKGVMLSHDNI-----TFDVRGivkamdrvvVGAESIV-SYLPLSHVAAQTVDIYTC----------- 286
Cdd:cd05938 147 ALYIYTSGTTGLPKAARISHLRVlqcsgFLSLCG---------VTADDVIyITLPLYHSSGFLLGIGGCielgatcvlkp 217
|
....*...
gi 17933690 287 AFVAGCIW 294
Cdd:cd05938 218 KFSASQFW 225
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
396-545 |
5.37e-05 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 46.02 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 396 AAAPMSPETKKYFLSL-DLKIVDAFGMSETagchTICLPDSVGLN----TIGKTLPGCESKFINKDAN--GHGELCI--- 465
Cdd:cd05974 208 AGEPLNPEVIEQVRRAwGLTIRDGYGQTET----TALVGNSPGQPvkagSMGRPLPGYRVALLDPDGApaTEGEVALdlg 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 466 --RGRHVFMGYIDNKEKTEESLDDDCWlHSGDLGFVDDKGYVSLTGRSKEiIITAGGENIPPVHIENTIkKELDAISNAF 543
Cdd:cd05974 284 dtRPVGLMKGYAGDPDKTAHAMRGGYY-RTGDIAMRDEDGYLTYVGRADD-VFKSSDYRISPFELESVL-IEHPAVAEAA 360
|
..
gi 17933690 544 LV 545
Cdd:cd05974 361 VV 362
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
60-243 |
6.97e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.94 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 60 GDYPALRTKNGKNGYHTVTYKQYEQKVHQVAKAFIKLGLEEhhsvG--VLAF--NCAEwfysAMGAIHARGIIAGIYTTN 135
Cdd:PRK03584 98 DDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGP----GdrVAAYlpNIPE----TVVAMLATASLGAIWSSC 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 136 SAD-AVQHVLESsHAQI-----VVVD-------DAKQMDKIHAIRDKLPKLKAAIQIqepysPYLKKEDGYYR------W 196
Cdd:PRK03584 170 SPDfGVQGVLDR-FGQIepkvlIAVDgyryggkAFDRRAKVAELRAALPSLEHVVVV-----PYLGPAAAAAAlpgallW 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17933690 197 SEIesmnVSDVEDQYMTrLENVAINECCCLVYTSGTVGMPKGVMLSH 243
Cdd:PRK03584 244 EDF----LAPAEAAELE-FEPVPFDHPLWILYSSGTTGLPKCIVHGH 285
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
226-502 |
7.76e-05 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 45.54 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNITFDVRGIVK--AMDRVVVGAESIVSYlplshvaaqTVDIYTCAFVagciwfadKDALKG 303
Cdd:cd17650 98 VIYTSGTTGKPKGVMVEHRNVAHAAHAWRReyELDSFPVRLLQMASF---------SFDVFAGDFA--------RSLLNG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 304 -TLVKSLQDARptrfMGVPRVYEKFQERMVAVASSSGSLKkmlaswakgITLKHYMVSQgkssgGFRYKIAKSLIM-SKV 381
Cdd:cd17650 161 gTLVICPDEVK----LDPAALYDLILKSRITLMESTPALI---------RPVMAYVYRN-----GLDLSAMRLLIVgSDG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 382 KQALgfDRVLTLASAAAPMspetkkyflsldlKIVDAFGMSETAGCHTICLPDSVGLNT-----IGKTLPGCESKFINKD 456
Cdd:cd17650 223 CKAQ--DFKTLAARFGQGM-------------RIINSYGVTEATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLDER 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17933690 457 ANGH-----GELCIRGRHVFMGYIDNKEKTEESLDDD---------------CWLHSGD---LGFVDDK 502
Cdd:cd17650 288 LQPQpvgvaGELYIGGAGVARGYLNRPELTAERFVENpfapgermyrtgdlaRWRADGNvelLGRVDHQ 356
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
369-520 |
7.83e-05 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 45.66 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 369 RYKIAKSLIMSKVKqalgfdRVLtlaSAAAPMSPETKKYFLSL---DLKIVDAFGMSEtagchtiCLP-DSVGLNTI--- 441
Cdd:PRK09274 278 RYGEANGIKLPSLR------RVI---SAGAPVPIAVIERFRAMlppDAEILTPYGATE-------ALPiSSIESREIlfa 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 442 -------------GKTLPGCESKFINKD--------------ANGHGELCIRGRHVFMGYIDNKEKTEES--LDD--DCW 490
Cdd:PRK09274 342 traatdngagicvGRPVDGVEVRIIAISdapipewddalrlaTGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGqgDVW 421
|
170 180 190
....*....|....*....|....*....|
gi 17933690 491 LHSGDLGFVDDKGYVSLTGRSKEIIITAGG 520
Cdd:PRK09274 422 HRMGDLGYLDAQGRLWFCGRKAHRVETAGG 451
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
49-246 |
1.40e-04 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 44.96 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 49 PGLLKRTVNNYGDYPALRTkngknGYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGII 128
Cdd:cd17646 1 HALVAEQAARTPDAPAVVD-----EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 129 AGIYTTNSADAVQHVLESSHAQIVVVDDAkqmdkihaIRDKLPKLKAAiqiqepyspylkKEDGYYRWSEiesmnVSDVE 208
Cdd:cd17646 76 LPLDPGYPADRLAYMLADAGPAVVLTTAD--------LAARLPAGGDV------------ALLGDEALAA-----PPATP 130
|
170 180 190
....*....|....*....|....*....|....*...
gi 17933690 209 DQYMTRLENVAineccCLVYTSGTVGMPKGVMLSHDNI 246
Cdd:cd17646 131 PLVPPRPDNLA-----YVIYTSGSTGRPKGVMVTHAGI 163
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
441-510 |
2.45e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 44.12 E-value: 2.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17933690 441 IGKTLPGCESKFINKDAN-----GHGELCIRGRHVFMGYIDNKEKTEE---SLDDDCWLHSGDLGFVDDkGYVSLTGR 510
Cdd:PRK04813 320 IGYAKPDSPLLIIDEEGTklpdgEQGEIVISGPSVSKGYLNNPEKTAEaffTFDGQPAYHTGDAGYLED-GLLFYQGR 396
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
77-243 |
2.52e-04 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 44.18 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 77 VTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEwfysAMGAIHARGIIAGIYTTNSAD-AVQHVLE---SSHAQIV 152
Cdd:cd05943 99 VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPE----AVVAMLATASIGAIWSSCSPDfGVPGVLDrfgQIEPKVL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 153 VVDDA--------KQMDKIHAIRDKLPKLKAAIQIqePYSPYLKKEDG--YYRWSEIESMnVSDVEDQYMTrLENVAINE 222
Cdd:cd05943 175 FAVDAytyngkrhDVREKVAELVKGLPSLLAVVVV--PYTVAAGQPDLskIAKALTLEDF-LATGAAGELE-FEPLPFDH 250
|
170 180
....*....|....*....|.
gi 17933690 223 CCCLVYTSGTVGMPKGVMLSH 243
Cdd:cd05943 251 PLYILYSSGTTGLPKCIVHGA 271
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
78-286 |
3.33e-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: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 78 TYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGaIHARGIIAGIYTTN-SADAVQHVLESSHAQIVVVDD 156
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLG-LAKIGVETALINSNlRLESLLHCITVSKAKALIFNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 157 AKQMDKihAIRDKLPKLkaaiqiqepyspylkkEDGYYRwseiesmnvsdvedqymTRLenvaineccCLVYTSGTVGMP 236
Cdd:cd05939 84 LDPLLT--QSSTEPPSQ----------------DDVNFR-----------------DKL---------FYIYTSGTTGLP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17933690 237 KGVMLSHDNITFDVRGIVKAM-----DRVVVGaesivsyLPLSHVAAQTVDIYTC 286
Cdd:cd05939 120 KAAVIVHSRYYRIAAGAYYAFgmrpeDVVYDC-------LPLYHSAGGIMGVGQA 167
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
226-247 |
5.06e-04 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 42.91 E-value: 5.06e-04
10 20
....*....|....*....|..
gi 17933690 226 LVYTSGTVGMPKGVMLSHDNIT 247
Cdd:cd05918 111 VIFTSGSTGKPKGVVIEHRALS 132
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
194-510 |
1.16e-03 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 42.11 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 194 YRWSeIESMNVSDVEDqymtrlENVAInecccLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDRVVvgAESIVSYLPL 273
Cdd:PRK06334 168 FEWL-MRWFGVSDKDP------EDVAV-----ILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKE--DDVMMSFLPP 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 274 SHVAAqtvdIYTCAF---VAG-CIWFADKDALKGTLVKSLQDARPTrFMGVPRVYekFQERMVAVASSSGSLKKMLASWA 349
Cdd:PRK06334 234 FHAYG----FNSCTLfplLSGvPVVFAYNPLYPKKIVEMIDEAKVT-FLGSTPVF--FDYILKTAKKQESCLPSLRFVVI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 350 KGITLKHYMVSqgkssggfrykiakslimskvkqalgfdrvltlasaaapmspETKKYFLSLDLKivDAFGMSETAGCHT 429
Cdd:PRK06334 307 GGDAFKDSLYQ------------------------------------------EALKTFPHIQLR--QGYGTTECSPVIT 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 430 ICLPDS------VGLNTIG-KTLPGCESKFINKDANGHGELCIRGRHVFMGYIDNKEKTE-ESLDDDCWLHSGDLGFVDD 501
Cdd:PRK06334 343 INTVNSpkhescVGMPIRGmDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGfVELGGETWYVTGDLGYVDR 422
|
....*....
gi 17933690 502 KGYVSLTGR 510
Cdd:PRK06334 423 HGELFLKGR 431
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
212-258 |
1.38e-03 |
|
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: 41.65 E-value: 1.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 17933690 212 MTRLENVAineccCLVYTSGTVGMPKGVMLSHDNITFDVRGIVKAMD 258
Cdd:cd17644 102 LTQPENLA-----YVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYG 143
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
227-268 |
3.04e-03 |
|
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: 40.70 E-value: 3.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 17933690 227 VYTSGTVGMPKGVMLSHDNITFDVRGIVKAMDrvvVGAESIV 268
Cdd:cd17652 99 IYTSGSTGRPKGVVVTHRGLANLAAAQIAAFD---VGPGSRV 137
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
458-532 |
3.45e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 40.49 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 458 NGH-GELCIRGRHVFMGYIDNKEKTEESL------------------DDDCWLHSGDLGFVDDkGYVSLTGRSKEIIITa 518
Cdd:PRK12476 426 DGEvGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaaDDGTWLRTGDLGVYLD-GELYITGRIADLIVI- 503
|
90
....*....|....
gi 17933690 519 GGENIPPVHIENTI 532
Cdd:PRK12476 504 DGRNHYPQDIEATV 517
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
227-247 |
4.10e-03 |
|
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: 39.98 E-value: 4.10e-03
10 20
....*....|....*....|.
gi 17933690 227 VYTSGTVGMPKGVMLSHDNIT 247
Cdd:cd17643 99 IYTSGSTGRPKGVVVSHANVL 119
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
73-258 |
4.23e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 40.53 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 73 GYHTVTYKQYEQKVHQVAKAFIKLGLEEHHSVGVLAFNCAEWFYSAMGAIHARGIIAGIYTTNSADAVQHVLESSHAQIV 152
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933690 153 VVDD--AKQMDKIHAIRdklpklkaAIQIQEPYSPylkkedgyyrWSEIESMNVSdvedqymtrlENVAINECCCLVYTS 230
Cdd:PRK12467 614 LTQShlLAQLPVPAGLR--------SLCLDEPADL----------LCGYSGHNPE----------VALDPDNLAYVIYTS 665
|
170 180
....*....|....*....|....*...
gi 17933690 231 GTVGMPKGVMLSHDNITFDVRGIVKAMD 258
Cdd:PRK12467 666 GSTGQPKGVAISHGALANYVCVIAERLQ 693
|
|
| |
