|
Name |
Accession |
Description |
Interval |
E-value |
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
3-589 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 755.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 3 VTRLFDILYYQLRNRPIDVSIATKKDGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQI 82
Cdd:COG1022 10 ADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAIL-SDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 83 GAVSVPIYPTMSDDDLTFILNNSESKFCLVSDKKIYDKVHNIKDQCPNITSLFTFDEI-----EGALNWNKIKKKGEEIS 157
Cdd:COG1022 89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRglrddPRLLSLDELLALGREVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 158 NQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDCHVRFVMENDEkfRILSILPICHILERMVDYVFM 237
Cdd:COG1022 169 DPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGD--RTLSFLPLAHVFERTVSYYAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 238 YKSYGIYFAEGMDKLASNFQEVKPDVILVVPRIVEKLYASIYNKGTSGGWLKKQIFLWALSVAKKFEPFKPAS------- 310
Cdd:COG1022 247 AAGATVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLAGkspslll 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 311 -LSHKIADFLVFKKWREAVGNNLQLIICGSAALSENLCRIFNAAGLKISEGYGMTETSPVITVN--GRTKdlfcLGTVGP 387
Cdd:COG1022 327 rLKHALADKLVFSKLREALGGRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNrpGDNR----IGTVGP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 388 LLNSCKVKIAEDGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQIT 466
Cdd:COG1022 403 PLPGVEVKIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELdEDGFLRITGRKKDLIVTSGGKNVAPQPI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 467 ENNLKQSRFIGEAMVVGDGEKMPCALIQPDFEFILKYIKYKNLHMNttiSPEEIVKNKVIRERIMQDVEKVNKLLGKWEQ 546
Cdd:COG1022 483 ENALKASPLIEQAVVVGDGRPFLAALIVPDFEALGEWAEENGLPYT---SYAELAQDPEVRALIQEEVDRANAGLSRAEQ 559
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2537297151 547 IKKIELTPTVWSVESGELTPTLKLKRKYIKEKYINLYNKLYDR 589
Cdd:COG1022 560 IKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
29-575 |
3.14e-175 |
|
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: 503.67 E-value: 3.14e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 29 GSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESK 108
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAIL-SRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 109 FCLVSDkkiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiePDRWVTLIYTSGTTGRPK 188
Cdd:cd05907 80 ALFVED--------------------------------------------------------PDDLATIIYTSGTTGRPK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 189 GVMLSHKNILTNVLDCHVRFVMENDEkfRILSILPICHILE-RMVDYVFMYKSYGIYFAEGMDKLASNFQEVKPDVILVV 267
Cdd:cd05907 104 GVMLSHRNILSNALALAERLPATEGD--RHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAETLLDDLSEVRPTVFLAV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 268 PRIVEKLYASIynKGTSGGWLKKQIFLWAlsvakkfepfkpaslshkiadflvfkkwreaVGNNLQLIICGSAALSENLC 347
Cdd:cd05907 182 PRVWEKVYAAI--KVKAVPGLKRKLFDLA-------------------------------VGGRLRFAASGGAPLPAELL 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 348 RIFNAAGLKISEGYGMTETSPVITVNgrTKDLFCLGTVGPLLNSCKVKIAEDGEILTKGSNVFLGYYKDEEKTREIYTDD 427
Cdd:cd05907 229 HFFRALGIPVYEGYGLTETSAVVTLN--PPGDNRIGTVGKPLPGVEVRIADDGEILVRGPNVMLGYYKNPEATAEALDAD 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 428 GWLKTGDIGYIK-DGFLKITDRKKEIFKTSGGKYIIPQITENNLKQSRFIGEAMVVGDGEKMPCALIQPDFEFILKYIKY 506
Cdd:cd05907 307 GWLHTGDLGEIDeDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPEALEAWAEE 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2537297151 507 KNLhmnTTISPEEIVKNKVIRERIMQDVEKVNKLLGKWEQIKKIELTPTVWSVESGELTPTLKLKRKYI 575
Cdd:cd05907 387 HGI---AYTDVAELAANPAVRAEIEAAVEAANARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
29-587 |
2.06e-122 |
|
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: 371.93 E-value: 2.06e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 29 GSWKKISTQSLIDQVNQVSRGLLNYGIN--PQDRIAlITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSE 106
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKpaPASFVG-IYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 107 SKFCLVSDkkiydkvhNIKdqcpnitsLFTFDEIEgalnwnkikKKGEEisNQQEVENLKnsiePDRWVTLIYTSGTTGR 186
Cdd:cd05927 80 ISIVFCDA--------GVK--------VYSLEEFE---------KLGKK--NKVPPPPPK----PEDLATICYTSGTTGN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 187 PKGVMLSHKNILTNVLDC---HVRFVMENDEkFRILSILPICHILERMVDYVFMYKSYGIYFAEGMDK-LASNFQEVKPD 262
Cdd:cd05927 129 PKGVMLTHGNIVSNVAGVfkiLEILNKINPT-DVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRlLLDDIKALKPT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 263 VILVVPRIVEKLYASIYNKGTSGGWLKKQIFLWALSvAKKFEPFKPASLSHKIADFLVFKKWREAVGNNLQLIICGSAAL 342
Cdd:cd05927 208 VFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALN-YKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLTGSAPL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 343 SENLCRIFNAA-GLKISEGYGMTETSPVITVNgrTKDLFCLGTVGPLLNSCKVKI---------AED----GEILTKGSN 408
Cdd:cd05927 287 SPEVLEFLRVAlGCPVLEGYGQTECTAGATLT--LPGDTSVGHVGGPLPCAEVKLvdvpemnydAKDpnprGEVCIRGPN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 409 VFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQITENNLKQSRFIGEAMVVGDGEK 487
Cdd:cd05927 365 VFSGYYKDPEKTAEALDEDGWLHTGDIGEWlPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLK 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 488 -MPCALIQPDFEFILKYIKYKNLhmnTTISPEEIVKNKVIRERIMQDVEKV---NKLLGkWEQIKKIELTPTVWSVESGE 563
Cdd:cd05927 445 sFLVAIVVPDPDVLKEWAASKGG---GTGSFEELCKNPEVKKAILEDLVRLgkeNGLKG-FEQVKAIHLEPEPFSVENGL 520
|
570 580
....*....|....*....|....
gi 2537297151 564 LTPTLKLKRKYIKEKYINLYNKLY 587
Cdd:cd05927 521 LTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
41-579 |
9.55e-106 |
|
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: 327.89 E-value: 9.55e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 41 DQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSdkkiydK 120
Cdd:cd05932 14 DKARRLAAALRALGLEPGSKIALI-SKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG------K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 121 VHNIKDQCPNI------TSLFTFDEIEGALNWnkikkkgEEISNQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSH 194
Cdd:cd05932 87 LDDWKAMAPGVpeglisISLPPPSAANCQYQW-------DDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 195 KNiLTNVLDCHVRF--VMENDekfRILSILPICHILERMvdYVFMYKSYG---IYFAEGMDKLASNFQEVKPDVILVVPR 269
Cdd:cd05932 160 GS-FAWAAQAGIEHigTEEND---RMLSYLPLAHVTERV--FVEGGSLYGgvlVAFAESLDTFVEDVQRARPTLFFSVPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 270 IVEKLYASIYNKgtsggwLKKQIFLWALSVakkfePFKPASLSHKIADFLVFKKWReavgnnlqLIICGSAALSENLCRI 349
Cdd:cd05932 234 LWTKFQQGVQDK------IPQQKLNLLLKI-----PVVNSLVKRKVLKGLGLDQCR--------LAGCGSAPVPPALLEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 350 FNAAGLKISEGYGMTETSPVITVN--GRTKdlfcLGTVGPLLNSCKVKIAEDGEILTKGSNVFLGYYKDEEKTREIYTDD 427
Cdd:cd05932 295 YRSLGLNILEAYGMTENFAYSHLNypGRDK----IGTVGNAGPGVEVRISEDGEILVRSPALMMGYYKDPEATAEAFTAD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 428 GWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQITENNLKQSRFIGEAMVVGDGEKMPCALIQPDFEFILKYIKY 506
Cdd:cd05932 371 GFLRTGDKGELdADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLSEEARLRADAF 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2537297151 507 knlhmnttispeeivKNKVIRERIMQDVEKVNKLLGKWEQIKKIELTPTVWSVESGELTPTLKLKRKYIKEKY 579
Cdd:cd05932 451 ---------------ARAELEASLRAHLARVNSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
26-587 |
2.87e-102 |
|
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: 321.61 E-value: 2.87e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 26 KKDGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIAlITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNS 105
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVG-ILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 106 ESKFCLVSDKKIYDKVHNIKDQCPNITSLFTF-DEIEGALN----WNKIKKKGEEISNQQEVENLKnSIEPDRWVTLIYT 180
Cdd:cd05933 80 EANILVVENQKQLQKILQIQDKLPHLKAIIQYkEPLKEKEPnlysWDEFMELGRSIPDEQLDAIIS-SQKPNQCCTLIYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 181 SGTTGRPKGVMLSHKNIL--TNVLDCHVRFVMENDEKFRILSILPICHILERMVDyVFMYKSYG--IYFAE---GMDKLA 253
Cdd:cd05933 159 SGTTGMPKGVMLSHDNITwtAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILD-IWLPIKVGgqVYFAQpdaLKGTLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 254 SNFQEVKPDVILVVPRIVEKLYASIYNKGTSGGWLKKQIFLWALSVA-----KKFEPFKPASLSHKIADFLVFKKWREAV 328
Cdd:cd05933 238 KTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGletnlKLMGGESPSPLFYRLAKKLVFKKVRKAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 329 G-NNLQLIICGSAALSENLCRIFNAAGLKISEGYGMTETSPVITVNGrtKDLFCLGTVGPLLNSCKVKIAE-----DGEI 402
Cdd:cd05933 318 GlDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISN--PQAYRLLSCGKALPGCKTKIHNpdadgIGEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 403 LTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQITENNLKQS-RFIGEAM 480
Cdd:cd05933 396 CFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLdEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKElPIISNAM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 481 VVGDGEKMPCALI-----------QPDFEFILKYIKYKNL--HMNTTISpeEIV--KNKVIRERIMQDVEKVN-KLLGKW 544
Cdd:cd05933 476 LIGDKRKFLSMLLtlkcevnpetgEPLDELTEEAIEFCRKlgSQATRVS--EIAggKDPKVYEAIEEGIKRVNkKAISNA 553
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2537297151 545 EQIKKIELTPTVWSVESGELTPTLKLKRKYIKEKYINLYNKLY 587
Cdd:cd05933 554 QKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
26-579 |
8.55e-98 |
|
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: 309.35 E-value: 8.55e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 26 KKDGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNS 105
Cdd:cd17641 4 KDFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGD-NRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 106 ESKFCLVSDKKIYDKVHNIKDQCPNITSLFTFDE------IEGALNW-NKIKKKGEEISNQQ--EVENLKNSIEPDRWVT 176
Cdd:cd17641 83 GARVVIAEDEEQVDKLLEIADRIPSVRYVIYCDPrgmrkyDDPRLISfEDVVALGRALDRRDpgLYEREVAAGKGEDVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 177 LIYTSGTTGRPKGVMLSHKNILTnvldcHVRFVMENDEKFR---ILSILPICHILERMVDYVF-MYKSYGIYFAEGMDKL 252
Cdd:cd17641 163 LCTTSGTTGKPKLAMLSHGNFLG-----HCAAYLAADPLGPgdeYVSVLPLPWIGEQMYSVGQaLVCGFIVNFPEEPETM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 253 ASNFQEVKPDVILVVPRIVEKLYASIYNKGTSGGWLKKQIFLWALSVAKK--------FEPFKPASLSHKIADFLVFKKW 324
Cdd:cd17641 238 MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRaldrgkrgRPVSLWLRLASWLADALLFRPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 325 REAVG-NNLQLIICGSAALSENLCRIFNAAGLKISEGYGMTETSPVITVNgRTKDLFcLGTVGPLLNSCKVKIAEDGEIL 403
Cdd:cd17641 318 RDRLGfSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVH-RDGDVD-PDTVGVPFPGTEVRIDEVGEIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 404 TKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIK-DGFLKITDRKKEIFKTSGGKYIIPQITENNLKQSRFIGEAMVV 482
Cdd:cd17641 396 VRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKeNGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 483 GDGEKMPCALIQPDFEFILKYIKYKNL----HMNTTISPEeivknkvIRERIMQDVEKVNKLLGKWEQIKKIELTPTVWS 558
Cdd:cd17641 476 GAGRPYLTAFICIDYAIVGKWAEQRGIafttYTDLASRPE-------VYELIRKEVEKVNASLPEAQRIRRFLLLYKELD 548
|
570 580
....*....|....*....|.
gi 2537297151 559 VESGELTPTLKLKRKYIKEKY 579
Cdd:cd17641 549 ADDGELTRTRKVRRGVIAEKY 569
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
46-588 |
7.47e-97 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 308.95 E-value: 7.47e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 46 VSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDKKIyDKVHNIK 125
Cdd:PLN02736 91 IGSGLVQHGIPKGACVGLY-FINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTL-NTLLSCL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 126 DQCPNITSLFTFDEIEGALNwNKIKKKGEEISNQQEVENLKNSIE-------PDRWVTLIYTSGTTGRPKGVMLSHKNIL 198
Cdd:PLN02736 169 SEIPSVRLIVVVGGADEPLP-SLPSGTGVEIVTYSKLLAQGRSSPqpfrppkPEDVATICYTSGTTGTPKGVVLTHGNLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 199 TNVLDCHVrfvmenDEKF----RILSILPICHILERMVDYVFMYKSYGIYFAEG-MDKLASNFQEVKPDVILVVPRIVEK 273
Cdd:PLN02736 248 ANVAGSSL------STKFypsdVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGdNLKLMDDLAALRPTIFCSVPRLYNR 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 274 LYASIYNKGTSGGWLKKQIFLWALSVAKK-FEPFKPASlshKIADFLVFKKWREAVGNNLQLIICGSAALSENL---CRI 349
Cdd:PLN02736 322 IYDGITNAVKESGGLKERLFNAAYNAKKQaLENGKNPS---PMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVmefLRI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 350 -FnaaGLKISEGYGMTETSPVITVNgRTKDLFClGTVGPLLNSCKVKIA---------ED-----GEILTKGSNVFLGYY 414
Cdd:PLN02736 399 cF---GGRVLEGYGMTETSCVISGM-DEGDNLS-GHVGSPNPACEVKLVdvpemnytsEDqpyprGEICVRGPIIFKGYY 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 415 KDEEKTREIYTDDGWLKTGDIG-YIKDGFLKITDRKKEIFKTSGGKYIIPQITENNLKQSRFIGEAMVVGDG-EKMPCAL 492
Cdd:PLN02736 474 KDEVQTREVIDEDGWLHTGDIGlWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSlNSSLVAV 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 493 IQPDFEFILKY-----IKYKNLhmnttispEEIVKNKVIRERIMQDVEKVNK--LLGKWEQIKKIELTPTVWSVESGELT 565
Cdd:PLN02736 554 VVVDPEVLKAWaasegIKYEDL--------KQLCNDPRVRAAVLADMDAVGReaQLRGFEFAKAVTLVPEPFTVENGLLT 625
|
570 580
....*....|....*....|...
gi 2537297151 566 PTLKLKRKYIKEKYINLYNKLYD 588
Cdd:PLN02736 626 PTFKVKRPQAKAYFAKAISDMYA 648
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
29-575 |
3.40e-95 |
|
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: 299.27 E-value: 3.40e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 29 GSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESK 108
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALF-ADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 109 FclvsdkkiydkvhnikdqcpnitsLFtfdeiegalnwnkikkkgeeisnqqeVENLKNSIepdrwVTLIYTSGTTGRPK 188
Cdd:cd17640 80 A------------------------LV--------------------------VENDSDDL-----ATIIYTSGTTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 189 GVMLSHKNILTNVLdcHVRFVMENDEKFRILSILPICHILERMVDYVFmyksygiyFAEGMDKLASN-------FQEVKP 261
Cdd:cd17640 105 GVMLTHANLLHQIR--SLSDIVPPQPGDRFLSILPIWHSYERSAEYFI--------FACGCSQAYTSirtlkddLKRVKP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 262 DVILVVPRIVEKLYASIYNKGTSGGWLKKQIFLWALSvakkfepfkpaslshkiadflvfkkwreavGNNLQLIICGSAA 341
Cdd:cd17640 175 HYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFLS------------------------------GGIFKFGISGGGA 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 342 LSENLCRIFNAAGLKISEGYGMTETSPVITVngRTKDLFCLGTVGPLLNSCKVKI-----------AEDGEILTKGSNVF 410
Cdd:cd17640 225 LPPHVDTFFEAIGIEVLNGYGLTETSPVVSA--RRLKCNVRGSVGRPLPGTEIKIvdpegnvvlppGEKGIVWVRGPQVM 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 411 LGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQITENNLKQSRFIGEAMVVGDGEKMP 489
Cdd:cd17640 303 KGYYKNPEATSKVLDSDGWFNTGDLGWLtCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRL 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 490 CALIQPDFEFILKYIKYKNLHMNTtiSPEEIVKNKVIRERIMQDV-EKVNKLLG--KWEQIKKIELT--PtvwSVESGEL 564
Cdd:cd17640 383 GALIVPNFEELEKWAKESGVKLAN--DRSQLLASKKVLKLYKNEIkDEISNRPGfkSFEQIAPFALLeeP---FIENGEM 457
|
570
....*....|.
gi 2537297151 565 TPTLKLKRKYI 575
Cdd:cd17640 458 TQTMKIKRNVV 468
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
29-575 |
2.76e-89 |
|
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: 284.88 E-value: 2.76e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 29 GSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESK 108
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAE-TRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 109 fCLVSDKKiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiePDRWVTLIYTSGTTGRPK 188
Cdd:cd17639 80 -AIFTDGK------------------------------------------------------PDDLACIMYTSGSTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 189 GVMLSHKNILTNV--LDCHVRFVMENDEkfRILSILPICHILERMVDYVFMYKSYGIYFAEG---MDKLASN----FQEV 259
Cdd:cd17639 105 GVMLTHGNLVAGIagLGDRVPELLGPDD--RYLAYLPLAHIFELAAENVCLYRGGTIGYGSPrtlTDKSKRGckgdLTEF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 260 KPDVILVVPRIVEKLYASIYNKGTSGGWLKKQIFLWALSvakkfepFKPASLSHK----IADFLVFKKWREAVGNNLQLI 335
Cdd:cd17639 183 KPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQ-------SKLKALKEGpgtpLLDELVFKKVRAALGGRLRYM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 336 ICGSAALSENLCRIFNAAGLKISEGYGMTETSpvitVNGRTKDLFCL--GTVGPLLNSCKVK---IAE----------DG 400
Cdd:cd17639 256 LSGGAPLSADTQEFLNIVLCPVIQGYGLTETC----AGGTVQDPGDLetGRVGPPLPCCEIKlvdWEEggystdkpppRG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 401 EILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQITENNLKQSRFIGEA 479
Cdd:cd17639 332 EILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFhPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNI 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 480 MVVGDGEK-MPCALIQPDFEFILKYIKYknlHMNTTISPEEIVKNKVIRERIMQDVEKVNKL--LGKWEQIKKIELTPTV 556
Cdd:cd17639 412 CVYADPDKsYPVAIVVPNEKHLTKLAEK---HGVINSEWEELCEDKKLQKAVLKSLAETARAagLEKFEIPQGVVLLDEE 488
|
570
....*....|....*....
gi 2537297151 557 WSVESGELTPTLKLKRKYI 575
Cdd:cd17639 489 WTPENGLVTAAQKLKRKEI 507
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
28-456 |
5.41e-88 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 278.81 E-value: 5.41e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 28 DGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSES 107
Cdd:pfam00501 16 VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLP-NSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 108 KFCLVSDKKIYDKVHNIKDQCPNITSLFTFDeiegALNWNKIKKKGEEISNQQEVENLKNSIEPDRWVTLIYTSGTTGRP 187
Cdd:pfam00501 95 KVLITDDALKLEELLEALGKLEVVKLVLVLD----RDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 188 KGVMLSHKNILTNVLDC----HVRFVMENDEkfRILSILPICHILERMVD-YVFMYKSYGIYFAEG-----MDKLASNFQ 257
Cdd:pfam00501 171 KGVMLTHRNLVANVLSIkrvrPRGFGLGPDD--RVLSTLPLFHDFGLSLGlLGPLLAGATVVLPPGfpaldPAALLELIE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 258 EVKPDVILVVPRIVEKLYASiynkgtsggwlkkqiflwalsvakkfEPFKPASLSHkiadflvfkkwreavgnnLQLIIC 337
Cdd:pfam00501 249 RYKVTVLYGVPTLLNMLLEA--------------------------GAPKRALLSS------------------LRLVLS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 338 GSAALSENLCRIFNAA-GLKISEGYGMTETSPVITVNGRTK-DLFCLGTVGPLLNSCKVKIAED-----------GEILT 404
Cdd:pfam00501 285 GGAPLPPELARRFRELfGGALVNGYGLTETTGVVTTPLPLDeDLRSLGSVGRPLPGTEVKIVDDetgepvppgepGELCV 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2537297151 405 KGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTS 456
Cdd:pfam00501 365 RGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRdEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
33-572 |
2.32e-78 |
|
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: 255.06 E-value: 2.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 33 KISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLV 112
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGE-NRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 113 SDkkiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiePDRWVTLIYTSGTTGRPKGVML 192
Cdd:cd05914 86 SD--------------------------------------------------------EDDVALINYTSGTTGNSKGVML 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 193 SHKNILTNVLDC-HVRFVMENDekfRILSILPICHILERMVDYVF-MYKSYGIYFaegMDKLAS------NFQEVKPDVI 264
Cdd:cd05914 110 TYRNIVSNVDGVkEVVLLGKGD---KILSILPLHHIYPLTFTLLLpLLNGAHVVF---LDKIPSakiialAFAQVTPTLG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 265 LVVPRIVEKLY-ASIYNKgtsggwLKKQIFLWALSVakkfePFKPASLSHkiadfLVFKKWREAVGNNLQLIICGSAALS 343
Cdd:cd05914 184 VPVPLVIEKIFkMDIIPK------LTLKKFKFKLAK-----KINNRKIRK-----LAFKKVHEAFGGNIKEFVIGGAKIN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 344 ENLCRIFNAAGLKISEGYGMTETSPVITVNGrtKDLFCLGTVGPLLNSCKVKIA------EDGEILTKGSNVFLGYYKDE 417
Cdd:cd05914 248 PDVEEFLRTIGFPYTIGYGMTETAPIISYSP--PNRIRLGSAGKVIDGVEVRIDspdpatGEGEIIVRGPNVMKGYYKNP 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 418 EKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQITENNLKQSRFIGEAMV-VGDGEKMPCALIQP 495
Cdd:cd05914 326 EATAEAFDKDGWFHTGDLGKIdAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVvVQEKKLVALAYIDP 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2537297151 496 DFEFILKyikyknlhmnttispeeiVKNKVIRERIMQDV-EKVNKLLGKWEQIKKIELTPtvwsvESGELTPTLKLKR 572
Cdd:cd05914 406 DFLDVKA------------------LKQRNIIDAIKWEVrDKVNQKVPNYKKISKVKIVK-----EEFEKTPKGKIKR 460
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
39-579 |
1.84e-69 |
|
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: 231.24 E-value: 1.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFclvsdkkiy 118
Cdd:COG0318 30 LDARARRLAAALRALGVGPGDRVALLLP-NSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARA--------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 119 dkvhnikdqcpnitsLFTfdeiegalnwnkikkkgeeisnqqevenlknsiepdrwVTLIYTSGTTGRPKGVMLSHKNIL 198
Cdd:COG0318 100 ---------------LVT--------------------------------------ALILYTSGTTGRPKGVMLTHRNLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 199 TNVLDCHVRFVMENDEkfRILSILPICHILErMVDYVFMYKSYG--IYFAEGMD--KLASNFQEVKPDVILVVPRIVEKL 274
Cdd:COG0318 127 ANAAAIAAALGLTPGD--VVLVALPLFHVFG-LTVGLLAPLLAGatLVLLPRFDpeRVLELIERERVTVLFGVPTMLARL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 275 YASiynkgtsggwlkkqiflwalsvakkfEPFKPASLSHkiadflvfkkwreavgnnLQLIICGSAALSENLCRIFNAA- 353
Cdd:COG0318 204 LRH--------------------------PEFARYDLSS------------------LRLVVSGGAPLPPELLERFEERf 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 354 GLKISEGYGMTETSPVITVNGRTKDLFCLGTVGPLLNSCKVKIA----------EDGEILTKGSNVFLGYYKDEEKTREI 423
Cdd:COG0318 240 GVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVdedgrelppgEVGEIVVRGPNVMKGYWNDPEATAEA 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 424 YtDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAMVVG-----DGEKmPCALIQPDF 497
Cdd:COG0318 320 F-RDGWLRTGDLGRLdEDGYLYIVGRKKDMIISGGEN-VYPAEVEEVLAAHPGVAEAAVVGvpdekWGER-VVAFVVLRP 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 498 EfilkyikyknlhmnTTISPEEIVknKVIRERimqdvekvnklLGKWEQIKKIELTPTVwsvesgELTPTLKLKRKYIKE 577
Cdd:COG0318 397 G--------------AELDAEELR--AFLRER-----------LARYKVPRRVEFVDEL------PRTASGKIDRRALRE 443
|
..
gi 2537297151 578 KY 579
Cdd:COG0318 444 RY 445
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
31-586 |
6.59e-69 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 235.48 E-value: 6.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 31 WKkiSTQSLIDQVNQVSRGLLNYGINPQDRIAlITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFC 110
Cdd:PLN02430 76 WK--TYKEVYEEVLQIGSALRASGAEPGSRVG-IYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 111 LVSDKKIYDKVHNIKDQCPNITSLFTF-----DEIEGAL-------NWNKIKKKGEEisNQQEVenlkNSIEPDRWVTLI 178
Cdd:PLN02430 153 FVQDKKIKELLEPDCKSAKRLKAIVSFtsvteEESDKASqigvktySWIDFLHMGKE--NPSET----NPPKPLDICTIM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 179 YTSGTTGRPKGVMLSHKNILTNVLDchVRFVMEN-DEKFRI----LSILPICHILERMVDYVFMYKSYGI-YFAEGMDKL 252
Cdd:PLN02430 227 YTSGTSGDPKGVVLTHEAVATFVRG--VDLFMEQfEDKMTHddvyLSFLPLAHILDRMIEEYFFRKGASVgYYHGDLNAL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 253 ASNFQEVKPDVILVVPRIVEKLYASIYNKGTSGGWLKKQIF--LWALSVAkkfepFKPASLSHK----IADFLVFKKWRE 326
Cdd:PLN02430 305 RDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFnaLYKYKLA-----WMNRGYSHKkaspMADFLAFRKVKA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 327 AVGNNLQLIICGSAALS---ENLCRIFNAAglKISEGYGMTETSPVITVnGRTKDLFCLGTVGPLLNSCKVKIAE----- 398
Cdd:PLN02430 380 KLGGRLRLLISGGAPLSteiEEFLRVTSCA--FVVQGYGLTETLGPTTL-GFPDEMCMLGTVGAPAVYNELRLEEvpemg 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 399 --------DGEILTKGSNVFLGYYKDEEKTREIYTdDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQITENN 469
Cdd:PLN02430 457 ydplgeppRGEICVRGKCLFSGYYKNPELTEEVMK-DGWFHTGDIGEIlPNGVLKIIDRKKNLIKLSQGEYVALEYLENV 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 470 LKQSRFIGEAMVVGDGEK-MPCALIQPDFEFILKYiKYKNLHMNttiSPEEIVKNKVIRERIMQDVEKV---NKLLGkWE 545
Cdd:PLN02430 536 YGQNPIVEDIWVYGDSFKsMLVAVVVPNEENTNKW-AKDNGFTG---SFEELCSLPELKEHILSELKSTaekNKLRG-FE 610
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2537297151 546 QIKKIELTPTVWSVESGELTPTLKLKR----KYIKEKYINLYNKL 586
Cdd:PLN02430 611 YIKGVILETKPFDVERDLVTATLKKRRnnllKYYQVEIDEMYRKL 655
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
23-587 |
8.36e-69 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 235.30 E-value: 8.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 23 IATKKDGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIAlITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFIL 102
Cdd:PLN02614 69 IVDGKPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCG-IYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFII 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 103 NNSESKFCLVSDKKIYDkvhnIKDQCPNIT----SLFTF-----DEIEGA-------LNWNKIKKKGEeiSNQQEVENLK 166
Cdd:PLN02614 148 SHSEVSIVFVEEKKISE----LFKTCPNSTeymkTVVSFggvsrEQKEEAetfglviYAWDEFLKLGE--GKQYDLPIKK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 167 nsiePDRWVTLIYTSGTTGRPKGVMLSHKNILTnVLDCHVRFVMENDEKFRI----LSILPICHILERMVDYVFMYKSYG 242
Cdd:PLN02614 222 ----KSDICTIMYTSGTTGDPKGVMISNESIVT-LIAGVIRLLKSANAALTVkdvyLSYLPLAHIFDRVIEECFIQHGAA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 243 IYFAEGMDKL-ASNFQEVKPDVILVVPRIVEKLYASIYNKGTSGGWLKKQIFLWALSVakKFEPFKPASlSHKIA----D 317
Cdd:PLN02614 297 IGFWRGDVKLlIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSY--KFGNMKKGQ-SHVEAsplcD 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 318 FLVFKKWREAVGNNLQLIICGSAALS---ENLCRIfnAAGLKISEGYGMTEtSPVITVNGRTKDLFCLGTVGPLLNSCKV 394
Cdd:PLN02614 374 KLVFNKVKQGLGGNVRIILSGAAPLAshvESFLRV--VACCHVLQGYGLTE-SCAGTFVSLPDELDMLGTVGPPVPNVDI 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 395 KIAE-------------DGEILTKGSNVFLGYYKDEEKTREIYTdDGWLKTGDIG-YIKDGFLKITDRKKEIFKTSGGKY 460
Cdd:PLN02614 451 RLESvpemeydalastpRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGeWQPNGSMKIIDRKKNIFKLSQGEY 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 461 IIPQITENNLKQSRFIGEAMVVGDG-EKMPCALIQPDFEFILKYIKYKNLHMNTtispEEIVKNKVIRERIMQDVEKV-- 537
Cdd:PLN02614 530 VAVENIENIYGEVQAVDSVWVYGNSfESFLVAIANPNQQILERWAAENGVSGDY----NALCQNEKAKEFILGELVKMak 605
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2537297151 538 -NKLLGkWEQIKKIELTPTVWSVESGELTPTLKLKRKYIKEKYINLYNKLY 587
Cdd:PLN02614 606 eKKMKG-FEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
8-495 |
6.34e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 223.91 E-value: 6.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 8 DILYYQLRNRPIDVSI-ATKKDGSWKKistqsLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVS 86
Cdd:PRK06187 10 RILRHGARKHPDKEAVyFDGRRTTYAE-----LDERVNRLANALRALGVKKGDRVAVFDW-NSHEYLEAYFAVPKIGAVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 87 VPIYPTMSDDDLTFILNNSESKFCLVSDK--KIYDKvhnIKDQCPNITSLFTFDEIEGAlnwNKIKKKG--EEISNQQEV 162
Cdd:PRK06187 84 HPINIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAA---ILPQLPTVRTVIVEGDGPAA---PLAPEVGeyEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 163 ENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDCHVRFVMENDEkfRILSILPICHILERMVDYV-FMYKSY 241
Cdd:PRK06187 158 TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDD--VYLVIVPMFHVHAWGLPYLaLMAGAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 242 GIYFAE-GMDKLASNFQEVKPDVILVVPriveklyaSIYNkgtsggwlkkqiflwalsvakkfepfkpASLSHKIADFLV 320
Cdd:PRK06187 236 QVIPRRfDPENLLDLIETERVTFFFAVP--------TIWQ----------------------------MLLKAPRAYFVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 321 FKKWReavgnnlqLIICGSAALSENLCRIFNA-AGLKISEGYGMTETSPVITVN----GRTKDLFCLGTVGPLLNSCKVK 395
Cdd:PRK06187 280 FSSLR--------LVIYGGAALPPALLREFKEkFGIDLVQGYGMTETSPVVSVLppedQLPGQWTKRRSAGRPLPGVEAR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 396 IAED------------GEILTKGSNVFLGYYKDEEKTREIYtDDGWLKTGDIGYI-KDGFLKITDRKKEIFKtSGGKYII 462
Cdd:PRK06187 352 IVDDdgdelppdggevGEIIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIdEDGYLYITDRIKDVII-SGGENIY 429
|
490 500 510
....*....|....*....|....*....|....*...
gi 2537297151 463 PQITENNLKQSRFIGEAMVVG--D---GEKmPCALIQP 495
Cdd:PRK06187 430 PRELEDALYGHPAVAEVAVIGvpDekwGER-PVAVVVL 466
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
27-587 |
7.84e-64 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 221.64 E-value: 7.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 27 KDGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSE 106
Cdd:PLN02861 71 KVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGS-NCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 107 SKFCLVSDKKIYDKVHNIKDQCPNITSLFTFDEIEGAL------------NWNKIKKKGE---EISNQQevenlKNSIep 171
Cdd:PLN02861 150 VSIAFVQESKISSILSCLPKCSSNLKTIVSFGDVSSEQkeeaeelgvscfSWEEFSLMGSldcELPPKQ-----KTDI-- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 172 drwVTLIYTSGTTGRPKGVMLSHKNILTNVLDC-HVRFVMEN--DEKFRILSILPICHILERMVDYVFMYKSYGIYFAEG 248
Cdd:PLN02861 223 ---CTIMYTSGTTGEPKGVILTNRAIIAEVLSTdHLLKVTDRvaTEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 249 -MDKLASNFQEVKPDVILVVPRIVEKLYASIYNKGTSGGWLKKQIFLWA----LSVAKKFEPFKPASlshKIADFLVFKK 323
Cdd:PLN02861 300 dIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAynykLGNLRKGLKQEEAS---PRLDRLVFDK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 324 WREAVGNNLQLIICGSAALS---ENLCRIFNAAGLkiSEGYGMTET-SPVITVNGrtkDLFCL-GTVGPLLNSCKVKIAE 398
Cdd:PLN02861 377 IKEGLGGRVRLLLSGAAPLPrhvEEFLRVTSCSVL--SQGYGLTEScGGCFTSIA---NVFSMvGTVGVPMTTIEARLES 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 399 -------------DGEILTKGSNVFLGYYKDEEKTREIYTdDGWLKTGDIG-YIKDGFLKITDRKKEIFKTSGGKYIIPQ 464
Cdd:PLN02861 452 vpemgydalsdvpRGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGeWQPNGAMKIIDRKKNIFKLSQGEYVAVE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 465 ITENNLKQSRFIGEAMVVGDG-EKMPCALIQPDFEFILKYIKyknlHMNTTISPEEIVKNKVIRERIMQDVEKVNKLLG- 542
Cdd:PLN02861 531 NLENTYSRCPLIASIWVYGNSfESFLVAVVVPDRQALEDWAA----NNNKTGDFKSLCKNLKARKYILDELNSTGKKLQl 606
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2537297151 543 -KWEQIKKIELTPTVWSVESGELTPTLKLKRKYIKEKYINLYNKLY 587
Cdd:PLN02861 607 rGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
29-587 |
9.59e-62 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 216.52 E-value: 9.59e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 29 GSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIAlITSVNRSEWLImdfAIQ----QIGAVsVPIYPTMSDDDLTFILNN 104
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVA-IFADTRAEWLI---ALQgcfrQNITV-VTIYASLGEEALCHSLNE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 105 SESKfCLVSDKKIYDKVHNIKDQCPNITSLFTFDEIEGALNWNKIKKKGEEISNQQEVENL--KNSIEPDR-----WVTL 177
Cdd:PLN02387 177 TEVT-TVICDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLgkENPVDPDLpspndIAVI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 178 IYTSGTTGRPKGVMLSHKNILTNVldCHVRFVMENDEKFRI-LSILPICHILERMVDYVFMYKSYGIYFAEGM------D 250
Cdd:PLN02387 256 MYTSGSTGLPKGVMMTHGNIVATV--AGVMTVVPKLGKNDVyLAYLPLAHILELAAESVMAAVGAAIGYGSPLtltdtsN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 251 KLA----SNFQEVKPDVILVVPRIVEKLYASIYNKGTSGGWLKKQIFLWALS---VAKKFEPFKPASLSHKIADFLVFKK 323
Cdd:PLN02387 334 KIKkgtkGDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKrrlAAIEGSWFGAWGLEKLLWDALVFKK 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 324 WREAVGNNLQLIICGSAALSENLCRIFNAA-GLKISEGYGMTETSPVITVNgrTKDLFCLGTVGPLLNSCKVKIAE---- 398
Cdd:PLN02387 414 IRAVLGGRIRFMLSGGAPLSGDTQRFINIClGAPIGQGYGLTETCAGATFS--EWDDTSVGRVGPPLPCCYVKLVSweeg 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 399 ----------DGEILTKGSNVFLGYYKDEEKTREIYTDDG----WLKTGDIG-YIKDGFLKITDRKKEIFKTSGGKYIIP 463
Cdd:PLN02387 492 gylisdkpmpRGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGqFHPDGCLEIIDRKKDIVKLQHGEYVSL 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 464 QITENNLKQSRFIGEAMVVGDGEKMPC-ALIQPDFEFILKY-----IKYKNLhmnttisPEEIVKNKVIRErIMQDVEKV 537
Cdd:PLN02387 572 GKVEAALSVSPYVDNIMVHADPFHSYCvALVVPSQQALEKWakkagIDYSNF-------AELCEKEEAVKE-VQQSLSKA 643
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2537297151 538 NKL--LGKWEQIKKIELTPTVWSVESGELTPTLKLKRKYIKEKYINLYNKLY 587
Cdd:PLN02387 644 AKAarLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
32-510 |
4.78e-59 |
|
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: 204.75 E-value: 4.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcL 111
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISP-NSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV-I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VSDKKIYDKVHNIKDQCPNITSLFTFD-------EIEGALNWnkikKKGEEISNQQEVENLKnsiePDRWVTLIYTSGTT 184
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGPKDKIIVLDdkpdgvlSIEDLLSP----TLGEEDEDLPPPLKDG----KDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 185 GRPKGVMLSHKNILTNVLDCHVRFVMENDEKFRILSILPICHI----------LERMVDYVfMYKSYGIYFAEgmdklas 254
Cdd:cd05911 159 GLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIyglfttlaslLNGATVII-MPKFDSELFLD------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 255 NFQEVKPDVILVVPRIVEKLYASiynkgtsggwlkkqiflwalsvakkfepfkPASLSHKIAdflvfkkwreavgnNLQL 334
Cdd:cd05911 231 LIEKYKITFLYLVPPIAAALAKS------------------------------PLLDKYDLS--------------SLRV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 335 IICGSAALSENLCRIFNA--AGLKISEGYGMTETSPVITVNGRTKDLFclGTVGPLLNSCKVKIAED-----------GE 401
Cdd:cd05911 267 ILSGGAPLSKELQELLAKrfPNATIKQGYGMTETGGILTVNPDGDDKP--GSVGRLLPNVEAKIVDDdgkdslgpnepGE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 402 ILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQItENNLKQSRFIGEAM 480
Cdd:cd05911 345 ICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFdEDGYLYIVDRKKELIKYKGFQVAPAEL-EAVLLEHPGVADAA 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2537297151 481 VVG-----DGEKmPCALI--QPDFEF----ILKYI-----KYKNLH 510
Cdd:cd05911 424 VIGipdevSGEL-PRAYVvrKPGEKLtekeVKDYVakkvaSYKQLR 468
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
32-495 |
5.51e-58 |
|
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: 201.25 E-value: 5.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcl 111
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLP-NCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 vsdkkiydkvhnikdqcpnitsLFTFDEIEGALnwnKIKKKGEEisnqqevenlKNSIEPDRWVTLIYTSGTTGRPKGVM 191
Cdd:cd05936 100 ----------------------LIVAVSFTDLL---AAGAPLGE----------RVALTPEDVAVLQYTSGTTGVPKGAM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 192 LSHKNILTNVLDCHVRFVMENDEKFRILSILPICHILERMVDYVfmyksygIYFAEGmdklASNFQEVKPDVILVVPRIV 271
Cdd:cd05936 145 LTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALL-------LPLALG----ATIVLIPRFRPIGVLKEIR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 272 EK----------LYASIYNkgtsggwlkkqiflwalsvakkFEPFKPASLShkiadflvfkkwreavgnNLQLIICGSAA 341
Cdd:cd05936 214 KHrvtifpgvptMYIALLN----------------------APEFKKRDFS------------------SLRLCISGGAP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 342 LSENLCRIFNAA-GLKISEGYGMTETSPVITVN---GRTKdlfcLGTVGPLLNSCKVKIAED----------GEILTKGS 407
Cdd:cd05936 254 LPVEVAERFEELtGVPIVEGYGLTETSPVVAVNpldGPRK----PGSIGIPLPGTEVKIVDDdgeelppgevGELWVRGP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 408 NVFLGYYKDEEKTREIYTdDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVGD-- 484
Cdd:cd05936 330 QVMKGYWNRPEETAEAFV-DGWLRTGDIGYMdEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAEAAVVGVpd 407
|
490
....*....|....
gi 2537297151 485 ---GEkMPCALIQP 495
Cdd:cd05936 408 pysGE-AVKAFVVL 420
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
47-587 |
8.41e-55 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 197.51 E-value: 8.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 47 SRGLLNYGINPQDRIALITSVnRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDKKIYDKVHNIK- 125
Cdd:PTZ00216 135 GRGLAELGLTKGSNVAIYEET-RWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLLRLMKs 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 126 DQCPNiTSLFTFDEIEGALN--------WNKIKKKGEEisnQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNI 197
Cdd:PTZ00216 214 GGMPN-TTIIYLDSLPASVDtegcrlvaWTDVVAKGHS---AGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 198 LTNVLDCHVRFV-----MENDEKFriLSILPICHILERMVDYVFMYKSYGIYFAEG---MDKLA---SNFQEVKPDVILV 266
Cdd:PTZ00216 290 TAGILALEDRLNdligpPEEDETY--CSYLPLAHIMEFGVTNIFLARGALIGFGSPrtlTDTFArphGDLTEFRPVFLIG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 267 VPRIVEKLYASIYNKGTSGGWLKKQIF-------LWALSvAKKFEPFkpasLSHKiadflVFKKWREAVGNNLQLIICGS 339
Cdd:PTZ00216 368 VPRIFDTIKKAVEAKLPPVGSLKRRVFdhayqsrLRALK-EGKDTPY----WNEK-----VFSAPRAVLGGRVRAMLSGG 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 340 AALSENLCRIFNAAGLKISEGYGMTETSPVITVNgRTKDLFClGTVGPLLNSCKVKIAE-------D-----GEILTKGS 407
Cdd:PTZ00216 438 GPLSAATQEFVNVVFGMVIQGWGLTETVCCGGIQ-RTGDLEP-NAVGQLLKGVEMKLLDteeykhtDtpeprGEILLRGP 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 408 NVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQitenNLkqsrfigEAMVVGDGE 486
Cdd:PTZ00216 516 FLFKGYYKQEELTREVLDEDGWFHTGDVGSIaANGTLRIIGRVKALAKNCLGEYIALE----AL-------EALYGQNEL 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 487 KMP---CALIQPDFEFIL--------KYIKYKNLHMNTTISPeEIVKNKVIRERIMQDVEKVNKLLGK--WEQIKKIELT 553
Cdd:PTZ00216 585 VVPngvCVLVHPARSYICalvltdeaKAMAFAKEHGIEGEYP-AILKDPEFQKKATESLQETARAAGRksFEIVRHVRVL 663
|
570 580 590
....*....|....*....|....*....|....
gi 2537297151 554 PTVWSVESGELTPTLKLKRKYIKEKYINLYNKLY 587
Cdd:PTZ00216 664 SDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
39-483 |
3.84e-54 |
|
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: 190.13 E-value: 3.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFclvsdkkiy 118
Cdd:cd17631 26 LDERVNRLAHALRALGVAKGDRVAVL-SKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKV--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 119 dkvhnikdqcpnitslfTFDEIegalnwnkikkkgeeisnqqevenlknsiepdrwVTLIYTSGTTGRPKGVMLSHKNIL 198
Cdd:cd17631 96 -----------------LFDDL----------------------------------ALLMYTSGTTGRPKGAMLTHRNLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 199 TNVLDCHVRFVMENDEKFriLSILPICHILERMVdYVFMYKSYG--IYFAEGMD--KLASNFQEVKPDVILVVPRIVekl 274
Cdd:cd17631 125 WNAVNALAALDLGPDDVL--LVVAPLFHIGGLGV-FTLPTLLRGgtVVILRKFDpeTVLDLIERHRVTSFFLVPTMI--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 275 yasiynkgtsggwlkkqIFLWALSVAKKFEpfkpasLShkiadflvfkkwreavgnNLQLIICGSAALSENLCRIFNAAG 354
Cdd:cd17631 199 -----------------QALLQHPRFATTD------LS------------------SLRAVIYGGAPMPERLLRALQARG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 355 LKISEGYGMTETSPVITVNGRTKDLFCLGTVGPLLNSCKVKI----------AEDGEILTKGSNVFLGYYKDEEKTREIY 424
Cdd:cd17631 238 VKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIvdpdgrevppGEVGEIVVRGPHVMAGYWNRPEATAAAF 317
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 425 tDDGWLKTGDIGYI-KDGFLKITDRKKEIFKtSGGKYIIPQITENNLKQSRFIGEAMVVG 483
Cdd:cd17631 318 -RDGWFHTGDLGRLdEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVIG 375
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
32-483 |
4.52e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 183.57 E-value: 4.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESK--F 109
Cdd:PRK07656 29 QRLTYAELNARVRRAAAALAALGIGKGDRVAIW-APNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKalF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 110 C----LVSDKKIYDKVHNIKDQ--CPNITSlftFDEIEGALNWNKIKKKGEEisNQQEVEnlknsIEPDRWVTLIYTSGT 183
Cdd:PRK07656 108 VlglfLGVDYSATTRLPALEHVviCETEED---DPHTEKMKTFTDFLAAGDP--AERAPE-----VDPDDVADILFTSGT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 184 TGRPKGVMLSHKNILTNVLD-CHVRFVMENDekfRILSILPICHilermvdyVFMYKSyGIY--FAEGmdklASNFQEVK 260
Cdd:PRK07656 178 TGRPKGAMLTHRQLLSNAADwAEYLGLTEGD---RYLAANPFFH--------VFGYKA-GVNapLMRG----ATILPLPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 261 PDVILVVpRIVEKLYASI-------YNkgtsggwlkkqiFLwaLSVAKKfepfKPASLSHkiadflvfkkwreavgnnLQ 333
Cdd:PRK07656 242 FDPDEVF-RLIETERITVlpgpptmYN------------SL--LQHPDR----SAEDLSS------------------LR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 334 LIICGSA----ALSENLCRIFNAAglKISEGYGMTETSPVITVN--GRTKDLFClGTVGPLLNSCKVKIA---------- 397
Cdd:PRK07656 285 LAVTGAAsmpvALLERFESELGVD--IVLTGYGLSEASGVTTFNrlDDDRKTVA-GTIGTAIAGVENKIVnelgeevpvg 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 398 EDGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFI 476
Cdd:PRK07656 362 EVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLdEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAV 440
|
....*..
gi 2537297151 477 GEAMVVG 483
Cdd:PRK07656 441 AEAAVIG 447
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
177-495 |
3.52e-49 |
|
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: 174.01 E-value: 3.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 177 LIYTSGTTGRPKGVMLSHKNILTNVLDC-HVRFVMENDekfRILSILPICHILERMVDYVFMYksYG--IYFAEGMD--K 251
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALaASGGLTEGD---VFLSTLPLFHIGGLFGLLGALL--AGgtVVLLPKFDpeA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 252 LASNFQEVKPDVILVVPRIVEKLyasiynkgtsggwlkkqiflwalsvaKKFEPFKPASLShkiadflvfkkwreavgnN 331
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARL--------------------------LKAPESAGYDLS------------------S 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 332 LQLIICGSAALSENLCRIFNAA-GLKISEGYGMTETSPVITVNGRTKDLFCLGTVGPLLNSCKVKIA----------EDG 400
Cdd:cd04433 116 LRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVdpdggelppgEIG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 401 EILTKGSNVFLGYYKDEEKTREIyTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKtSGGKYIIPQITENNLKQSRFIGEA 479
Cdd:cd04433 196 ELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLdEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAEA 273
|
330 340
....*....|....*....|
gi 2537297151 480 MVVG----DGEKMPCALIQP 495
Cdd:cd04433 274 AVVGvpdpEWGERVVAVVVL 293
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
32-520 |
2.91e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 168.41 E-value: 2.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINPQDRIAlITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCL 111
Cdd:PRK12583 44 LRYTWRQLADAVDRLARGLLALGVQPGDRVG-IWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VSDK-KIYDKVHNIKDQCPNITS------------------LFTFDEIEGALNWNKIKKKGEEISnQQEVENLKNSIEPD 172
Cdd:PRK12583 123 CADAfKTSDYHAMLQELLPGLAEgqpgalacerlpelrgvvSLAPAPPPGFLAWHELQARGETVS-REALAERQASLDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 173 RWVTLIYTSGTTGRPKGVMLSHKNILTNvldchVRFVMEN---DEKFRILSILPICHILErMVDYVFMYKSYG---IYFA 246
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHNILNN-----GYFVAESlglTEHDRLCVPVPLYHCFG-MVLANLGCMTVGaclVYPN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 247 EGMDKLAsnfqevkpdvilVVPRIVEKLYASIYNKGTsggwlkkqIFLwalsvakkfepfkpASLSHKIADFLVFKKWRE 326
Cdd:PRK12583 276 EAFDPLA------------TLQAVEEERCTALYGVPT--------MFI--------------AELDHPQRGNFDLSSLRT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 327 AvgnnlqlIICGSAALSENLCRIFNAAGL-KISEGYGMTETSPVITVNGRTKDL-FCLGTVGPLLNSCKVKI-------- 396
Cdd:PRK12583 322 G-------IMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADDLeRRVETVGRTQPHLEVKVvdpdgatv 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 397 --AEDGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQS 473
Cdd:PRK12583 395 prGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMdEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTH 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2537297151 474 RFIGEAMVVGdgekMPCaliQPDFEFILKYIKyknLHMNTTISPEEI 520
Cdd:PRK12583 474 PAVADVQVFG----VPD---EKYGEEIVAWVR---LHPGHAASEEEL 510
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
114-587 |
1.56e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 166.05 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 114 DKKIYDKVHNIKDQCPNI-TSLFTFDEIegalnwnkIKKKGEEISNQQEvenlknsiEPDRWVTLIYTSGTTGRPKGVML 192
Cdd:PTZ00342 261 DKEKLEKIKDLKEKAKKLgISIILFDDM--------TKNKTTNYKIQNE--------DPDFITSIVYTSGTSGKPKGVML 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 193 SHKNILTNVL---DCHVRFVMENDEKFrilSILPICHILERMVDYVFMYKSYGIY-FAEGMDKLASNFQEVKPDVILVVP 268
Cdd:PTZ00342 325 SNKNLYNTVVplcKHSIFKKYNPKTHL---SYLPISHIYERVIAYLSFMLGGTINiWSKDINYFSKDIYNSKGNILAGVP 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 269 RIVEKLYASIYNKGTSGGWLKKQIFLWALSVAKKFEPFKPASLSHKIadFLVFKKWREAVGNNLQLIICGSAALS----E 344
Cdd:PTZ00342 402 KVFNRIYTNIMTEINNLPPLKRFLVKKILSLRKSNNNGGFSKFLEGI--THISSKIKDKVNPNLEVILNGGGKLSpkiaE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 345 NLCRIFNaagLKISEGYGMTETS-PVITVNGRTKDLFCLGtvGPLLNSCKVKI-------AED----GEILTKGSNVFLG 412
Cdd:PTZ00342 480 ELSVLLN---VNYYQGYGLTETTgPIFVQHADDNNTESIG--GPISPNTKYKVrtwetykATDtlpkGELLIKSDSIFSG 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 413 YYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQITENNLKQSRFIGEAMVVGDgEKM--P 489
Cdd:PTZ00342 555 YFLEKEQTKNAFTEDGYFKTGDIVQInKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGD-DSMdgP 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 490 CALIQPDFEFILKYIKYKNLHMNTTISPEEIVKN------------KVIRERIMQDVEKVNklLGKWEQIKKIELTPTVW 557
Cdd:PTZ00342 634 LAIISVDKYLLFKCLKDDNMLESTGINEKNYLEKltdetinnniyvDYVKGKMLEVYKKTN--LNRYNIINDIYLTSKVW 711
|
490 500 510
....*....|....*....|....*....|...
gi 2537297151 558 SVeSGELTPTLKLKRKYIKEKY---INLYNKLY 587
Cdd:PTZ00342 712 DT-NNYLTPTFKVKRFYVFKDYaffIDQVKKIY 743
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
41-505 |
1.92e-40 |
|
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: 154.33 E-value: 1.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 41 DQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVsDKKIYDK 120
Cdd:cd12119 33 ERARRLANALRRLGVKPGDRVATL-AWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFV-DRDFLPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 121 VHNIKDQCPNITSLFTFDeiegalnwNKIKKKGEEISNQQEVENLKNSIEPD-RWV--------TLIYTSGTTGRPKGVM 191
Cdd:cd12119 111 LEAIAPRLPTVEHVVVMT--------DDAAMPEPAGVGVLAYEELLAAESPEyDWPdfdentaaAICYTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 192 LSHKNI--------LTNVLDCHVRFVmendekfrILSILPICHILermvdyvfmykSYGIYFAEGM-------------- 249
Cdd:cd12119 183 YSHRSLvlhamaalLTDGLGLSESDV--------VLPVVPMFHVN-----------AWGLPYAAAMvgaklvlpgpyldp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 250 DKLASNFQEVKPDVILVVPRIveklyasiynkgtsggWlkkQIFLWALSVakkfepfKPASLSHkiadflvfkkwreavg 329
Cdd:cd12119 244 ASLAELIEREGVTFAAGVPTV----------------W---QGLLDHLEA-------NGRDLSS---------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 330 nnLQLIICGSAALSENLCRIFNAAGLKISEGYGMTETSPVITVNGRTKDLFCLG---------TVGPLLNSCKVKIAED- 399
Cdd:cd12119 282 --LRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARPPSEHSNLSedeqlalraKQGRPVPGVELRIVDDd 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 400 -----------GEILTKGSNVFLGYYKDEEKTREiYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKtSGGKYIIPQITE 467
Cdd:cd12119 360 grelpwdgkavGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIdEDGYLTITDRSKDVIK-SGGEWISSVELE 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2537297151 468 NNLKQSRFIGEAMVVG--D---GEKmPCALI------QPDFEFILKYIK 505
Cdd:cd12119 438 NAIMAHPAVAEAAVIGvpHpkwGER-PLAVVvlkegaTVTAEELLEFLA 485
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
33-493 |
3.08e-40 |
|
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: 151.35 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 33 KISTQSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKfclv 112
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALL-SKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 113 sdkkiYDKVHnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiepdrwvTLIYTSGTTGRPKGVML 192
Cdd:cd05912 76 -----LDDIA-----------------------------------------------------TIMYTSGTTGKPKGVQQ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 193 SHKNILTNVLDChvrfvMEN---DEKFRILSILPICHI--LERMVDYVFmyksYG--IYFAEGMD--KLASNFQEVKPDV 263
Cdd:cd05912 98 TFGNHWWSAIGS-----ALNlglTEDDNWLCALPLFHIsgLSILMRSVI----YGmtVYLVDKFDaeQVLHLINSGKVTI 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 264 ILVVPRIVEKLyASIYNKGTSggwlkkqiflwalsvakkfepfkpaslshkiadflvfkkwreavgNNLQLIICGSAALS 343
Cdd:cd05912 169 ISVVPTMLQRL-LEILGEGYP---------------------------------------------NNLRCILLGGGPAP 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 344 ENLCRIFNAAGLKISEGYGMTET-SPVITVNgrTKDLFC-LGTVGPLLNSCKVKIA-------EDGEILTKGSNVFLGYY 414
Cdd:cd05912 203 KPLLEQCKEKGIPVYQSYGMTETcSQIVTLS--PEDALNkIGSAGKPLFPVELKIEddgqppyEVGEILLKGPNVTKGYL 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 415 KDEEKTREIyTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG--DGE--KMP 489
Cdd:cd05912 281 NRPDATEES-FENGWFKTGDIGYLdEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIKEAGVVGipDDKwgQVP 358
|
....
gi 2537297151 490 CALI 493
Cdd:cd05912 359 VAFV 362
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
41-495 |
5.98e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 153.43 E-value: 5.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 41 DQVNQVSRGLLNYGINPQDRIAlITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDK----- 115
Cdd:PRK08315 51 EEVDALAKGLLALGIEKGDRVG-IWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGfkdsd 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 116 ---KIYDKVHNIKDQCPNITSLFTFDEIE-----------GALNWNKIKKKGEEISnQQEVENLKNSIEPDRWVTLIYTS 181
Cdd:PRK08315 130 yvaMLYELAPELATCEPGQLQSARLPELRrviflgdekhpGMLNFDELLALGRAVD-DAELAARQATLDPDDPINIQYTS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 182 GTTGRPKGVMLSHKNILTNVldchvRFVMEN---DEKFRILSILPICHILErMVDYVFMYKSYG---IYFAEGMDKLAsn 255
Cdd:PRK08315 209 GTTGFPKGATLTHRNILNNG-----YFIGEAmklTEEDRLCIPVPLYHCFG-MVLGNLACVTHGatmVYPGEGFDPLA-- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 256 fqevkpdvilvVPRIVEK-----LYAsiynkgtsggwlkkqiflwalsVAKKFepfkPASLSHKiaDFLVFkkwreavgn 330
Cdd:PRK08315 281 -----------TLAAVEEerctaLYG----------------------VPTMF----IAELDHP--DFARF--------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 331 NLQ-L---IICGSAALSENLCRIFNAAGLK-ISEGYGMTETSPVITVNgRTKDLFCL--GTVGPLLNSCKVKIA------ 397
Cdd:PRK08315 313 DLSsLrtgIMAGSPCPIEVMKRVIDKMHMSeVTIAYGMTETSPVSTQT-RTDDPLEKrvTTVGRALPHLEVKIVdpetge 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 398 -----EDGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKE-IFKtsGGKYIIPQITENNL 470
Cdd:PRK08315 392 tvprgEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMdEEGYVNIVGRIKDmIIR--GGENIYPREIEEFL 469
|
490 500 510
....*....|....*....|....*....|
gi 2537297151 471 KQSRFIGEAMVVG--D---GEKMpCALIQP 495
Cdd:PRK08315 470 YTHPKIQDVQVVGvpDekyGEEV-CAWIIL 498
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
34-457 |
3.31e-39 |
|
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: 150.46 E-value: 3.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 34 ISTQSLIDQVNQVSRGLLNYGINPQDrIALITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcLVS 113
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGD-VVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKL-AFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 114 DKKIYDKVHNIKDQcpniTSLFTFDEIEGALNWNKIKKKGEeiSNQQEVEnlknsIEPDRWVTLIYTSGTTGRPKGVMLS 193
Cdd:cd05904 111 TAELAEKLASLALP----VVLLDSAEFDSLSFSDLLFEADE--AEPPVVV-----IKQDDVAALLYSSGTTGRSKGVMLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 194 HKNILTNVLDCHVRFVMENDEKFRILSILPICHIlermvdyvfmyksYGI-YFAEGMDKLASNfqevkpdvILVVPRIV- 271
Cdd:cd05904 180 HRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHI-------------YGLsSFALGLLRLGAT--------VVVMPRFDl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 272 EKLYASIYNKGTSGGWLKKQIFLwALsvAKkfepfkpaslsHKIADFLVFKKwreavgnnLQLIICGSAALSENLCRIFN 351
Cdd:cd05904 239 EELLAAIERYKVTHLPVVPPIVL-AL--VK-----------SPIVDKYDLSS--------LRQIMSGAAPLGKELIEAFR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 352 AA--GLKISEGYGMTETSPVITVN-GRTKDLFCLGTVGPLLNSCKVKIA-----------EDGEILTKGSNVFLGYYKDE 417
Cdd:cd05904 297 AKfpNVDLGQGYGMTESTGVVAMCfAPEKDRAKYGSVGRLVPNVEAKIVdpetgeslppnQTGELWIRGPSIMKGYLNNP 376
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2537297151 418 EKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:cd05904 377 EATAATIDKEGWLHTGDLCYIdEDGYLFIVDRLKELIKYKG 417
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
35-494 |
2.73e-38 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 146.44 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 35 STQSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVsd 114
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALV-GQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 115 kkiydkvhnikdqcpniTSLFTFDEIEgALNWNKIKKKGEEisnqqeVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSH 194
Cdd:TIGR01923 78 -----------------DSLLEEKDFQ-ADSLDRIEAAGRY------ETSLSASFNMDQIATLMFTSGTTGKPKAVPHTF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 195 KNILTNVLDCHVRF-VMENDekfRILSILPICHIlermvdyvfmyKSYGIyfaegmdklasnfqevkpdvilvvprivek 273
Cdd:TIGR01923 134 RNHYASAVGSKENLgFTEDD---NWLLSLPLYHI-----------SGLSI------------------------------ 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 274 LYASIYNKGTsggwlkkqiflwaLSVAKKFepfkpASLSHKIADFLVFK--------KW--REAVGN-NLQLIICGSAAL 342
Cdd:TIGR01923 170 LFRWLIEGAT-------------LRIVDKF-----NQLLEMIANERVTHislvptqlNRllDEGGHNeNLRKILLGGSAI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 343 SENLCRIFNAAGLKISEGYGMTET-SPVITVNgrTKDLFCLGTVGPLLNSCKVKI-----AEDGEILTKGSNVFLGYYKD 416
Cdd:TIGR01923 232 PAPLIEEAQQYGLPIYLSYGMTETcSQVTTAT--PEMLHARPDVGRPLAGREIKIkvdnkEGHGEIMVKGANLMKGYLYQ 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 417 EEkTREIYTDDGWLKTGDIGYIK-DGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG--DGE--KMPCA 491
Cdd:TIGR01923 310 GE-LTPAFEQQGWFNTGDIGELDgEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVVPkpDAEwgQVPVA 387
|
...
gi 2537297151 492 LIQ 494
Cdd:TIGR01923 388 YIV 390
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
32-493 |
7.31e-38 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 146.26 E-value: 7.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCL 111
Cdd:PRK03640 26 KKVTFMELHEAVVSVAGKLAALGVKKGDRVALL-MKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VSDkkIYDKVHNIKDQcpnitslFTFDEIegalnwnkIKKKGEEISNQQEvenlknsIEPDRWVTLIYTSGTTGRPKGVM 191
Cdd:PRK03640 105 TDD--DFEAKLIPGIS-------VKFAEL--------MNGPKEEAEIQEE-------FDLDEVATIMYTSGTTGKPKGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 192 LSHKN----ILTNVLDCHVRfvmENDekfRILSILPICHI--LERMVDYVFmyksYG--IYFAEGMDKLASNF--QEVKP 261
Cdd:PRK03640 161 QTYGNhwwsAVGSALNLGLT---EDD---CWLAAVPIFHIsgLSILMRSVI----YGmrVVLVEKFDAEKINKllQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 262 DVILVVPRIVEKLYASIYNKGTSggwlkkqiflwalsvakkfepfkpaslshkiadflvfkkwreavgNNLQLIICGSAA 341
Cdd:PRK03640 231 TIISVVSTMLQRLLERLGEGTYP---------------------------------------------SSFRCMLLGGGP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 342 LSENLCRIFNAAGLKISEGYGMTET-SPVITVN---GRTKdlfcLGTVGPLLNSCKVKIAED---------GEILTKGSN 408
Cdd:PRK03640 266 APKPLLEQCKEKGIPVYQSYGMTETaSQIVTLSpedALTK----LGSAGKPLFPCELKIEKDgvvvppfeeGEIVVKGPN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 409 VFLGYYKDEEKTREIYtDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG--DG 485
Cdd:PRK03640 342 VTKGYLNREDATRETF-QDGWFKTGDIGYLdEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVGvpDD 419
|
490
....*....|
gi 2537297151 486 E--KMPCALI 493
Cdd:PRK03640 420 KwgQVPVAFV 429
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
22-496 |
5.76e-37 |
|
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: 142.81 E-value: 5.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 22 SIATKKDGswKKISTQSLIDQVNQVSRGLL-NYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTF 100
Cdd:cd05941 2 RIAIVDDG--DSITYADLVARAARLANRLLaLGKDLRGDRVAFLAP-PSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 101 ILNNSESkfclvsdkkiydkvhnikdqcpnitSLFtfdeIEGALnwnkikkkgeeisnqqevenlknsiepdrwvtLIYT 180
Cdd:cd05941 79 VITDSEP-------------------------SLV----LDPAL--------------------------------ILYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 181 SGTTGRPKGVMLSHKNILTNVlDCHV---RFVmENDekfRILSILPICHIlermvdyvfmyksYGIYFAegmdklasnfq 257
Cdd:cd05941 98 SGTTGRPKGVVLTHANLAANV-RALVdawRWT-EDD---VLLHVLPLHHV-------------HGLVNA----------- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 258 evkpdvilvvprivekLYASIYNKGTSggwlkkqIFLwalsvaKKFEPFKPASLSHKiADFLVF---------------- 321
Cdd:cd05941 149 ----------------LLCPLFAGASV-------EFL------PKFDPKEVAISRLM-PSITVFmgvptiytrllqyyea 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 322 -----KKWREAVGNNLQLIICGSAALS----ENLCRIFnaaGLKISEGYGMTETSPVITV--NGRTKDlfclGTVGPLLN 390
Cdd:cd05941 199 hftdpQFARAAAAERLRLMVSGSAALPvptlEEWEAIT---GHTLLERYGMTEIGMALSNplDGERRP----GTVGMPLP 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 391 SCKVKIAED-----------GEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIK-DGFLKITDRKKEIFKTSGG 458
Cdd:cd05941 272 GVQARIVDEetgeplprgevGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDeDGYYWILGRSSVDIIKSGG 351
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2537297151 459 KYIIPQITENNLKQSRFIGEAMVVGD-----GEKMpCALIQPD 496
Cdd:cd05941 352 YKVSALEIERVLLAHPGVSECAVIGVpdpdwGERV-VAVVVLR 393
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
168-448 |
5.58e-36 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 144.30 E-value: 5.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 168 SIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLdcHVRFVMENDEKFRILSILPICHILERMVDyVFMYKSYGI---Y 244
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE--QISDVFNLRNDDVILSSLPFFHSFGLTVT-LWLPLLEGIkvvY 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 245 FAEGMDKLAsnfqevkpdvilvVPRIVEKLYASIYnKGTSggwlkkqIFLWALSVAKKFEPfkpaslshkiADFlvfkkw 324
Cdd:PRK08633 855 HPDPTDALG-------------IAKLVAKHRATIL-LGTP-------TFLRLYLRNKKLHP----------LMF------ 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 325 reavgNNLQLIICGSAALSENLCRIF-NAAGLKISEGYGMTETSPVITVNgrTKDLFC----------LGTVGPLLNSCK 393
Cdd:PRK08633 898 -----ASLRLVVAGAEKLKPEVADAFeEKFGIRILEGYGATETSPVASVN--LPDVLAadfkrqtgskEGSVGMPLPGVA 970
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 394 VKI-----------AEDGEILTKGSNVFLGYYKDEEKTREIYTD---DGWLKTGDIGYI-KDGFLKITDR 448
Cdd:PRK08633 971 VRIvdpetfeelppGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGHLdEDGFLTITDR 1040
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
18-483 |
6.55e-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: 140.91 E-value: 6.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 18 PIDVSIATkkDGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITsVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDD 97
Cdd:cd05926 1 PDAPALVV--PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIAL-PNGLEFVVAFLAAARAGAVVAPLNPAYKKAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 98 LTFILNNSESKFCLVSDKKIYDKVHNIKDQCPNITSLftfdEIEGALNWNKIKkkGEEISNQQ----EVENLKNSIEPDr 173
Cdd:cd05926 78 FEFYLADLGSKLVLTPKGELGPASRAASKLGLAILEL----ALDVGVLIRAPS--AESLSNLLadkkNAKSEGVPLPDD- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 174 wVTLI-YTSGTTGRPKGVMLSHKNILTNVLdcHVRFVMENDEKFRILSILPICHILERMVDYVFMYKSYG-IYFAEGMDK 251
Cdd:cd05926 151 -LALIlHTSGTTGRPKGVPLTHRNLAASAT--NITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGsVVLPPRFSA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 252 LA--SNFQEVKPDVILVVPRIVeklyasiynkgtsggwlkkQIFLwalsvakKFEPFKPASLSHKiadflvfkkwreavg 329
Cdd:cd05926 228 STfwPDVRDYNATWYTAVPTIH-------------------QILL-------NRPEPNPESPPPK--------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 330 nnLQLIICGSAALSENLCRIFNAA-GLKISEGYGMTETSPVITVN----GRTKdlfcLGTVGP-------LLNS--CKVK 395
Cdd:cd05926 267 --LRFIRSCSASLPPAVLEALEATfGAPVLEAYGMTEAAHQMTSNplppGPRK----PGSVGKpvgvevrILDEdgEILP 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 396 IAEDGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIK-DGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSR 474
Cdd:cd05926 341 PGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDaDGYLFLTGRIKELI-NRGGEKISPLEVDGVLLSHP 419
|
....*....
gi 2537297151 475 FIGEAMVVG 483
Cdd:cd05926 420 AVLEAVAFG 428
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
39-483 |
1.61e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 140.91 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDKkIY 118
Cdd:PRK05605 63 LGKQVRRAAAGLRALGVRPGDRVAIVLP-NCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDK-VA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 119 DKVHNIKDQCPnITSLFTFDEIE-----------------------------GALNWNKIKKkGEEISNQQEVENLKnsI 169
Cdd:PRK05605 141 PTVERLRRTTP-LETIVSVNMIAampllqrlalrlpipalrkaraaltgpapGTVPWETLVD-AAIGGDGSDVSHPR--P 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 170 EPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDCH--VRFVMENDEkfRILSILPICHIlermvdY-VFMYKSYGIYFA 246
Cdd:PRK05605 217 TPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKawVPGLGDGPE--RVLAALPMFHA------YgLTLCLTLAVSIG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 247 EGMDKLAsnfqevKPDVILVvpriveklyasiynkgtsggwlkkqiflwaLSVAKKFEP-FKPA--SLSHKIADflvfkk 323
Cdd:PRK05605 289 GELVLLP------APDIDLI------------------------------LDAMKKHPPtWLPGvpPLYEKIAE------ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 324 wrEAVGNNLQL-----IICGSAALSENLCRIFNAA-GLKISEGYGMTETSPVITVNGRTKDLFClGTVGPLLNSCKVKIA 397
Cdd:PRK05605 327 --AAEERGVDLsgvrnAFSGAMALPVSTVELWEKLtGGLLVEGYGLTETSPIIVGNPMSDDRRP-GYVGVPFPDTEVRIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 398 ------------EDGEILTKGSNVFLGYYKDEEKTREIYTdDGWLKTGDIGYIK-DGFLKITDRKKEIFKTsGGKYIIPQ 464
Cdd:PRK05605 404 dpedpdetmpdgEEGELLVRGPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVMEeDGFIRIVDRIKELIIT-GGFNVYPA 481
|
490
....*....|....*....
gi 2537297151 465 ITENNLKQSRFIGEAMVVG 483
Cdd:PRK05605 482 EVEEVLREHPGVEDAAVVG 500
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
43-505 |
4.29e-35 |
|
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: 137.51 E-value: 4.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 43 VNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDKKiydKVH 122
Cdd:cd05903 11 ADRLAAGLAALGVGPGDVVAFQLP-NWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPERF---RQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 123 NIKDQcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiePDRWVTLIYTSGTTGRPKGVMLSHKNILTNVl 202
Cdd:cd05903 87 DPAAM-------------------------------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASI- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 203 dCHVRFVMENDEKFRILSILPICHILERMvdYVFMyksygIYFAEGMdklASNFQEV-KPDVILvvpRIVEKLYASIYNK 281
Cdd:cd05903 123 -RQYAERLGLGPGDVFLVASPMAHQTGFV--YGFT-----LPLLLGA---PVVLQDIwDPDKAL---ALMREHGVTFMMG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 282 GTSggwlkkqiFLWALSVAKKFEPFKPASLshkiadflvfkkwreavgnnlQLIICGSAALSENLCRIFNAA-GLKISEG 360
Cdd:cd05903 189 ATP--------FLTDLLNAVEEAGEPLSRL---------------------RTFVCGGATVPRSLARRAAELlGAKVCSA 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 361 YGMTETSPVITVNGRTKDLFCLGTVGPLLNSCKVKIAED----------GEILTKGSNVFLGYYKDEEKTREIYtDDGWL 430
Cdd:cd05903 240 YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDtgatlapgveGELLSRGPSVFLGYLDRPDLTADAA-PEGWF 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 431 KTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG--D---GEKMpCALI------QPDFE 498
Cdd:cd05903 319 RTGDLARLdEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAlpDerlGERA-CAVVvtksgaLLTFD 396
|
....*..
gi 2537297151 499 FILKYIK 505
Cdd:cd05903 397 ELVAYLD 403
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
50-541 |
4.35e-35 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 139.11 E-value: 4.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 50 LLNYGINPQDRIALITSVnRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESK--FCLVSDKKI--YDKVHNIK 125
Cdd:PRK06087 66 LLAKGIEPGDRVAFQLPG-WCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKmfFAPTLFKQTrpVDLILPLQ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 126 DQCPNITSLFTFDEIEGALN---WNKIKKKGEEIsnQQEVenlknSIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNvl 202
Cdd:PRK06087 145 NQLPQLQQIVGVDKLAPATSslsLSQIIADYEPL--TTAI-----TTHGDELAAVLFTSGTEGLPKGVMLTHNNILAS-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 203 dchvrfvmendEKFrilsilpICHILERMVDYVFMYKS---YGIYFAEGmdkLASNFqevkpdviLVVPRIVeklYASIY 279
Cdd:PRK06087 216 -----------ERA-------YCARLNLTWQDVFMMPAplgHATGFLHG---VTAPF--------LIGARSV---LLDIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 280 NKGTSGGWLKKQIFLWALSVAkkfePFkpaslshkIADFLVFKKWREAVGNNLQLIICGSAALSENLCRIFNAAGLKISE 359
Cdd:PRK06087 264 TPDACLALLEQQRCTCMLGAT----PF--------IYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 360 GYGMTETSPVITVNGRTKDLFCLGTVGPLLNSCKVKIAED----------GEILTKGSNVFLGYYKDEEKTREIYTDDGW 429
Cdd:PRK06087 332 VYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEarktlppgceGEEASRGPNVFMGYLDEPELTARALDEEGW 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 430 LKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG--D---GEKMpCALI-------QPD 496
Cdd:PRK06087 412 YYSGDLCRMdEAGYIKITGRKKDII-VRGGENISSREVEDILLQHPKIHDACVVAmpDerlGERS-CAYVvlkaphhSLT 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2537297151 497 FEFILKYIKYKnlHMNTTISPEEIVknkVIRERIMQDVEKVNKLL 541
Cdd:PRK06087 490 LEEVVAFFSRK--RVAKYKYPEHIV---VIDKLPRTASGKIQKFL 529
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
46-457 |
5.69e-35 |
|
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: 138.23 E-value: 5.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 46 VSRGLLNYGInPQDRIALI--TSVNRsewLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDKKIYD-KVH 122
Cdd:cd05909 20 LARKLAKMTK-EGENVGVMlpPSAGG---ALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKlKLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 123 NIKDQC--PNITSLftfDEIEGALNWN---KIKKKGEEISNQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNI 197
Cdd:cd05909 96 HLFDVEydARIVYL---EDLRAKISKAdkcKAFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 198 LTNVLDCHVRFvmENDEKFRILSILPICHILERMVDYVFMYKSyGIYFAegmdkLASNFQEVKpdvilVVPRIVEKLYAS 277
Cdd:cd05909 173 LANVEQITAIF--DPNPEDVVFGALPFFHSFGLTGCLWLPLLS-GIKVV-----FHPNPLDYK-----KIPELIYDKKAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 278 IYNkGTSggwlkkqIFLWALSVAKKFEPFKpaslshkiadflvfkkwreavgnNLQLIICGSAALSENLCRIF-NAAGLK 356
Cdd:cd05909 240 ILL-GTP-------TFLRGYARAAHPEDFS-----------------------SLRLVVAGAEKLKDTLRQEFqEKFGIR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 357 ISEGYGMTETSPVITVNGRTKDlFCLGTVGPLL-----------NSCKVKIAEDGEILTKGSNVFLGYYKDEEKTREIYt 425
Cdd:cd05909 289 ILEGYGTTECSPVISVNTPQSP-NKEGTVGRPLpgmevkivsveTHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF- 366
|
410 420 430
....*....|....*....|....*....|...
gi 2537297151 426 DDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:cd05909 367 GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAG 399
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
50-493 |
8.98e-34 |
|
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: 135.35 E-value: 8.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 50 LLNYGINPQDRIALiTSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSdKKIYDKVHNIKDQCP 129
Cdd:cd17642 61 LKKYGLKQNDRIAV-CSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS-KKGLQKVLNVQKKLK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 130 NITSLFTFDEIE---GALNWNKIKKKGEEIsNQQEVENLKNSIEPDRWVTLI-YTSGTTGRPKGVMLSHKNILTNVLDC- 204
Cdd:cd17642 139 IIKTIIILDSKEdykGYQCLYTFITQNLPP-GFNEYDFKPPSFDRDEQVALImNSSGSTGLPKGVQLTHKNIVARFSHAr 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 205 HVRFVMENDEKFRILSILPICHilermvdyvfmykSYGIYFAEGMdkLASNFQevkpdvILVVPRIVEKLYASIynkgts 284
Cdd:cd17642 218 DPIFGNQIIPDTAILTVIPFHH-------------GFGMFTTLGY--LICGFR------VVLMYKFEEELFLRS------ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 285 ggwLKKQIFLWALSVAKKFEPFKPASLSHKIaDFlvfkkwreavgNNLQLIICGSAALS----ENLCRIFNAAGlkISEG 360
Cdd:cd17642 271 ---LQDYKVQSALLVPTLFAFFAKSTLVDKY-DL-----------SNLHEIASGGAPLSkevgEAVAKRFKLPG--IRQG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 361 YGMTETSPVITVngrTKDLFCL-GTVGPLLNSCKVKIA-----------EDGEILTKGSNVFLGYYKDEEKTREIYTDDG 428
Cdd:cd17642 334 YGLTETTSAILI---TPEGDDKpGAVGKVVPFFYAKVVdldtgktlgpnERGELCVKGPMIMKGYVNNPEATKALIDKDG 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 429 WLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAMVVG----DGEKMPCALI 493
Cdd:cd17642 411 WLHSGDIAYYdEDGHFFIVDRLKSLIKYKGYQ-VPPAELESILLQHPKIFDAGVAGipdeDAGELPAAVV 479
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
34-540 |
9.21e-34 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 133.37 E-value: 9.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 34 ISTQSLIDQVNQVSRGLLNYGINPQDRIAlITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVS 113
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVG-ICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 114 dkkiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqQEVENLknsiepdrwVTLIYTSGTTGRPKGVMLS 193
Cdd:cd05935 81 ----------------------------------------------SELDDL---------ALIPYTSGTTGLPKGCMHT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 194 HKNILTNVLDCHVRFVMENDEKFriLSILPICHILErMVDYVFMyksyGIYFAEGMDKLASNFQEVKPDVIlvvprivEK 273
Cdd:cd05935 106 HFSAAANALQSAVWTGLTPSDVI--LACLPLFHVTG-FVGSLNT----AVYVGGTYVLMARWDRETALELI-------EK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 274 LyasiynKGTsggwlkkqiFLWALSVAkkfepfkpaslshkIADFLVFKKWREAVGNNLQLIICGSAALSENLC-RIFNA 352
Cdd:cd05935 172 Y------KVT---------FWTNIPTM--------------LVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAeKLLKL 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 353 AGLKISEGYGMTETSPVITVN--GRTKdLFCLGTVGPLLNSCKVKIA--------EDGEILTKGSNVFLGYYKDEEKTRE 422
Cdd:cd05935 223 TGLRFVEGYGLTETMSQTHTNppLRPK-LQCLGIP*FGVDARVIDIEtgrelppnEVGEIVVRGPQIFKGYWNRPEETEE 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 423 IYTDDG---WLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAMVVGD-----GEKmPCALI 493
Cdd:cd05935 302 SFIEIKgrrFFRTGDLGYMdEEGYFFFVDRVKRMINVSGFK-VWPAEVEAKLYKHPAI*EVCVISVpdervGEE-VKAFI 379
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2537297151 494 QPDFEFILKyikyknlhmnttISPEEIVknKVIRERIM-----QDVEKVNKL 540
Cdd:cd05935 380 VLRPEYRGK------------VTEEDII--EWAREQMAaykypREVEFVDEL 417
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
140-457 |
8.29e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 132.58 E-value: 8.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 140 IEGALNWNKIKKKGEEisnqQEVENLknSIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDChvRFVME---NDEKF 216
Cdd:PRK05677 181 LPQAVKFNDALAKGAG----QPVTEA--NPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQC--RALMGsnlNEGCE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 217 RILSILPICHIlermvdYVFMYKSYGIYFAEGMDKLASNFQEVkpdvilvvPRIVEKLyasiyNKGTSGGWLKKQIFLWA 296
Cdd:PRK05677 253 ILIAPLPLYHI------YAFTFHCMAMMLIGNHNILISNPRDL--------PAMVKEL-----GKWKFSGFVGLNTLFVA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 297 LSVAKKFEPFkpaslshkiaDFlvfkkwreavgNNLQLIICGSAALSENLCRIFNA-AGLKISEGYGMTETSPVITVNGR 375
Cdd:PRK05677 314 LCNNEAFRKL----------DF-----------SALKLTLSGGMALQLATAERWKEvTGCAICEGYGMTETSPVVSVNPS 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 376 tkDLFCLGTVG-PLLNS-CKV--------KIAEDGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIK-DGFLK 444
Cdd:PRK05677 373 --QAIQVGTIGiPVPSTlCKVidddgnelPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQeDGYMR 450
|
330
....*....|...
gi 2537297151 445 ITDRKKEIFKTSG 457
Cdd:PRK05677 451 IVDRKKDMILVSG 463
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
171-552 |
1.32e-32 |
|
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: 128.55 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 171 PDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLdcHVRFVMENDEKFRILSILPICHILErMVDYVFMYKSYG---IYFAE 247
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGY--FIGERLGLTEQDRLCIPVPLFHCFG-SVLGVLACLTHGatmVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 248 GMDKLAsnfqevkpdVILVVPRivEKLYAsIYNKGTsggwlkkqIFLwalsvakkfepfkpASLSHKiaDFLVFKKWREA 327
Cdd:cd05917 78 SFDPLA---------VLEAIEK--EKCTA-LHGVPT--------MFI--------------AELEHP--DFDKFDLSSLR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 328 VGnnlqlIICGSAALSENLCRIFNAAGLK-ISEGYGMTETSPVITVNGRTKDLFC-LGTVGPLLNSCKVKI--------- 396
Cdd:cd05917 122 TG-----IMAGAPCPPELMKRVIEVMNMKdVTIAYGMTETSPVSTQTRTDDSIEKrVNTVGRIMPHTEAKIvdpeggivp 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 397 --AEDGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQS 473
Cdd:cd05917 197 pvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMdEDGYCRIVGRIKDMI-IRGGENIYPREIEEFLHTH 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 474 RFIGEAMVVG--D---GEKMpCALIQpdfefilkyikyknLHMNTTISPEEI---VKNKVIRERIMQDVEKVNKL----L 541
Cdd:cd05917 276 PKVSDVQVVGvpDeryGEEV-CAWIR--------------LKEGAELTEEDIkayCKGKIAHYKVPRYVFFVDEFpltvS 340
|
410
....*....|.
gi 2537297151 542 GKweqIKKIEL 552
Cdd:cd05917 341 GK---IQKFKL 348
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
37-457 |
7.04e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 126.59 E-value: 7.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 37 QSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVsDKK 116
Cdd:PRK08316 40 AELDAAVNRVAAALLDLGLKKGDRVAAL-GHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV-DPA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 117 IYDKVHNIKDQCPNITSLFT--FDEIEGALNWNKIkkkgEEISNQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSH 194
Cdd:PRK08316 118 LAPTAEAALALLPVDTLILSlvLGGREAPGGWLDF----ADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 195 KNILTNVLDCHVRFVMENDEkfRILSILPICHILERmvdYVFMyksyGIYFAEGmdklASNFQEVKPDVILVVPRIVEKL 274
Cdd:PRK08316 194 RALIAEYVSCIVAGDMSADD--IPLHALPLYHCAQL---DVFL----GPYLYVG----ATNVILDAPDPELILRTIEAER 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 275 YASIYNKGTsggwlkkqifLW-ALSVAKKFEPFKPASLSH-----KIADFLVFKKWREAVGNnlqliicgsaalsenlCR 348
Cdd:PRK08316 261 ITSFFAPPT----------VWiSLLRHPDFDTRDLSSLRKgyygaSIMPVEVLKELRERLPG----------------LR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 349 IFNAaglkisegYGMTETSPVITVNGRTKDLFCLGTVG-PLLNsCKVKIAED----------GEILTKGSNVFLGYYKDE 417
Cdd:PRK08316 315 FYNC--------YGQTEIAPLATVLGPEEHLRRPGSAGrPVLN-VETRVVDDdgndvapgevGEIVHRSPQLMLGYWDDP 385
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2537297151 418 EKTREIYTdDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:PRK08316 386 EKTAEAFR-GGWFHSGDLGVMdEEGYITVVDRKKDMIKTGG 425
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
6-483 |
8.10e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 126.13 E-value: 8.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 6 LFDILYY---QLRNRPIDVSIATKKDgSWkkiSTQSLIDQVNQVSRGLLN-YGINPQDRIAlITSVNRSEWLIMDFAIQQ 81
Cdd:PRK06839 1 MQGIAYWiekRAYLHPDRIAIITEEE-EM---TYKQLHEYVSKVAAYLIYeLNVKKGERIA-ILSQNSLEYIVLLFAIAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 82 IGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDkkiydkvhnikdqcpniTSLFTFDEIEGALNWNK-IKKKGEEISNQQ 160
Cdd:PRK06839 76 VECIAVPLNIRLTENELIFQLKDSGTTVLFVEK-----------------TFQNMALSMQKVSYVQRvISITSLKEIEDR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 161 EVENLKNSIEpDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLdcHVRFVMENDEKFRILSILPICHIlermvDYVFMYkS 240
Cdd:PRK06839 139 KIDNFVEKNE-SASFIICYTSGTTGKPKGAVLTQENMFWNAL--NNTFAIDLTMHDRSIVLLPLFHI-----GGIGLF-A 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 241 YGIYFAEGM---------DKLASNFQEVKPDVILVVPRIVEKLYASIynkgtsggwlkkqiflwalsvakkfePFKPASL 311
Cdd:PRK06839 210 FPTLFAGGViivprkfepTKALSMIEKHKVTVVMGVPTIHQALINCS--------------------------KFETTNL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 312 SHkiadflvfkkwreavgnnLQLIICGSAALSENLCRIFNAAGLKISEGYGMTETSPviTVNGRTKDLFC--LGTVG-PL 388
Cdd:PRK06839 264 QS------------------VRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSP--TVFMLSEEDARrkVGSIGkPV 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 389 L---------NSCKVKIAEDGEILTKGSNVFLGYYKDEEKTREIyTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGG 458
Cdd:PRK06839 324 LfcdyelideNKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGWLCTGDLARVdEDGFVYIVGRKKEMI-ISGG 401
|
490 500
....*....|....*....|....*
gi 2537297151 459 KYIIPQITENNLKQSRFIGEAMVVG 483
Cdd:PRK06839 402 ENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
32-483 |
3.08e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 124.23 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCL 111
Cdd:PRK06145 26 QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMK-NSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VSDKkiydkvhnIKDQCPNITSLFTFDEIEGAlNWNKIKKKGEEISNQQEVEnlknsiePDRWVTLIYTSGTTGRPKGVM 191
Cdd:PRK06145 105 VDEE--------FDAIVALETPKIVIDAAAQA-DSRRLAQGGLEIPPQAAVA-------PTDLVRLMYTSGTTDRPKGVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 192 LSHKNILTNVLDCHVRFVMENDEkfRILSILPICHIlermvdYVFMYKSYGIYFAEGMDKLASNFQevkPDVILvvpriv 271
Cdd:PRK06145 169 HSYGNLHWKSIDHVIALGLTASE--RLLVVGPLYHV------GAFDLPGIAVLWVGGTLRIHREFD---PEAVL------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 272 eklyASIYNKGTSGGWlkkqiflwalsvakkfepFKPASLSHKIAdflVFKKWREAVGNnLQLIICGSAALSENLCRIFN 351
Cdd:PRK06145 232 ----AAIERHRLTCAW------------------MAPVMLSRVLT---VPDRDRFDLDS-LAWCIGGGEKTPESRIRDFT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 352 A--AGLKISEGYGMTETSPVITVNGRTKDLFCLGTVGPLLNSCKVKIAED----------GEILTKGSNVFLGYYKDEEK 419
Cdd:PRK06145 286 RvfTRARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGagrwlppnmkGEICMRGPKVTKGYWKDPEK 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2537297151 420 TREIYTDDgWLKTGDIGYIKD-GFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG 483
Cdd:PRK06145 366 TAEAFYGD-WFRSGDVGYLDEeGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
43-485 |
5.38e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 122.93 E-value: 5.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 43 VNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAI----QQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVsDKKIY 118
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILP-NRFTYIELSFAVayagGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLA-DAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 119 DKVHNIKDQCPNITSLFTFDEIEGALnwnkikkkgeeiSNQQEVENlknsiEPDRWVTLIYTSGTTGRPKGVMLSHKNIL 198
Cdd:cd05922 81 DRLRDALPASPDPGTVLDADGIRAAR------------ASAPAHEV-----SHEDLALLLYTSGSTGSPKLVRLSHQNLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 199 TNVLDchVRFVMENDEKFRILSILPichilermvdyvfmyksygIYFAEGMDKLASNFqEVKPDVIL----VVPRIVEKL 274
Cdd:cd05922 144 ANARS--IAEYLGITADDRALTVLP-------------------LSYDYGLSVLNTHL-LRGATLVLtndgVLDDAFWED 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 275 YASiyNKGTSggwLKKQIFLWALSVAKKfepFKPASLSHkiadflvfkkwreavgnnLQLIICGSAALSENLCRIFNAA- 353
Cdd:cd05922 202 LRE--HGATG---LAGVPSTYAMLTRLG---FDPAKLPS------------------LRYLTQAGGRLPQETIARLRELl 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 354 -GLKISEGYGMTETSPVITVNGRTKDLFCLGTVGPLLNSCKVKIAED----------GEILTKGSNVFLGYYKDEEKTRE 422
Cdd:cd05922 256 pGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDdgtptppgepGEIVHRGPNVMKGYWNDPPYRRK 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2537297151 423 IYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAMVVGDG 485
Cdd:cd05922 336 EGRGGGVLHTGDLARRdEDGFLFIVGRRDRMIKLFGNR-ISPTEIEAAARSIGLIIEAAAVGLP 398
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
38-494 |
2.49e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 119.67 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 38 SLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVsVPIYPTMSDDDLTFILNNSESKFcLVS---- 113
Cdd:PRK07529 63 ELLADVTRTANLLHSLGVGPGDVVAFL-LPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKV-LVTlgpf 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 114 -DKKIYDKVHNIKDQCPNITSLFTFDEIEGALNW-------------NKIKKKGEEISNQQEvENLKN--SIEPDRWVTL 177
Cdd:PRK07529 140 pGTDIWQKVAEVLAALPELRTVVEVDLARYLPGPkrlavplirrkahARILDFDAELARQPG-DRLFSgrPIGPDDVAAY 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 178 IYTSGTTGRPKGVMLSHKNILTNVLDCH-VRFVMENDEkfrILSILPICHILERMVdyvfmyksygiyfaEGMDKLASNF 256
Cdd:PRK07529 219 FHTGGTTGMPKLAQHTHGNEVANAWLGAlLLGLGPGDT---VFCGLPLFHVNALLV--------------TGLAPLARGA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 257 QevkpdviLVVPriveklyasiynkgTSGGWLKKQIF--LWALsvakkFEPFKPASLS----------------HKIAdf 318
Cdd:PRK07529 282 H-------VVLA--------------TPQGYRGPGVIanFWKI-----VERYRINFLSgvptvyaallqvpvdgHDIS-- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 319 lvfkkwreavgnNLQLIICGSAALSENLCRIFNAA-GLKISEGYGMTETSPVITVN---GRTKdlfcLGTVGPLLNSCKV 394
Cdd:PRK07529 334 ------------SLRYALCGAAPLPVEVFRRFEAAtGVRIVEGYGLTEATCVSSVNppdGERR----IGSVGLRLPYQRV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 395 KIA---------------EDGEILTKGSNVFLGYYkDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKE-IFKtsG 457
Cdd:PRK07529 398 RVVilddagrylrdcavdEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIdADGYFWLTGRAKDlIIR--G 474
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2537297151 458 GKYIIPQITENNLKQSRFIGEAMVVG--D---GEkMPCALIQ 494
Cdd:PRK07529 475 GHNIDPAAIEEALLRHPAVALAAAVGrpDahaGE-LPVAYVQ 515
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
28-483 |
3.77e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 118.55 E-value: 3.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 28 DGSWkkiSTQSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSES 107
Cdd:PRK06188 35 DTRL---TYGQLADRISRYIQAFEALGLGTGDAVALL-SLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 108 KFCLVSDKKIYDKVHNIKDQCPNITSLFTFDEIEGalnwnkikkkGEEISNQ---QEVENLKNSIEPDRWVTLIYTSGTT 184
Cdd:PRK06188 111 STLIVDPAPFVERALALLARVPSLKHVLTLGPVPD----------GVDLLAAaakFGPAPLVAAALPPDIAGLAYTGGTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 185 GRPKGVMLSHKNILTNVLDCHVRFvmENDEKFRILSILPICHilermvdyvfmyksygiyfAEGmdklasnfqevkpdvI 264
Cdd:PRK06188 181 GKPKGVMGTHRSIATMAQIQLAEW--EWPADPRFLMCTPLSH-------------------AGG---------------A 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 265 LVVPRIVEklyasiynkgtsGGwlkkqiflwALSVAKKFEP--FKPASLSHKI-ADFLV---------FKKWREAVGNNL 332
Cdd:PRK06188 225 FFLPTLLR------------GG---------TVIVLAKFDPaeVLRAIEEQRItATFLVptmiyalldHPDLRTRDLSSL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 333 QLIICGSAALS-----ENLCRIfnaaGLKISEGYGMTETSPVITVngRTKDLFCLGTVGpLLNSC--------------- 392
Cdd:PRK06188 284 ETVYYGASPMSpvrlaEAIERF----GPIFAQYYGQTEAPMVITY--LRKRDHDPDDPK-RLTSCgrptpglrvallded 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 393 --KVKIAEDGEILTKGSNVFLGYYKDEEKTREIYTdDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENN 469
Cdd:PRK06188 357 grEVAQGEVGEICVRGPLVMDGYWNRPEETAEAFR-DGWLHTGDVAREdEDGFYYIVDRKKDMI-VTGGFNVFPREVEDV 434
|
490
....*....|....
gi 2537297151 470 LKQSRFIGEAMVVG 483
Cdd:PRK06188 435 LAEHPAVAQVAVIG 448
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
34-461 |
1.47e-27 |
|
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: 117.17 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 34 ISTQSLIDQVNQVSRGL-LNYGINPQDRIALI--TSVnrsEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFC 110
Cdd:cd17632 68 ITYAELWERVGAVAAAHdPEQPVRPGDFVAVLgfTSP---DYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 111 LVSDKKIYDKVHNIKDQcPNITSLFTFD----------EIEGALNwnKIKKKGEEISNQQEVENLKNSIEP--------- 171
Cdd:cd17632 145 AVSAEHLDLAVEAVLEG-GTPPRLVVFDhrpevdahraALESARE--RLAAVGIPVTTLTLIAVRGRDLPPaplfrpepd 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 172 -DRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDchVRFVMENDEKFRI-LSILPICHILERMVDYVFMYKSYGIYFAEG- 248
Cdd:cd17632 222 dDPLALLIYTSGSTGTPKGAMYTERLVATFWLK--VSSIQDIRPPASItLNFMPMSHIAGRISLYGTLARGGTAYFAAAs 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 249 -MDKLASNFQEVKPDVILVVPRIVEKLYasiynkgtsggwlkkQIFLwALSVAKKFEPFKPASLSHKIADFLvfkkwREA 327
Cdd:cd17632 300 dMSTLFDDLALVRPTELFLVPRVCDMLF---------------QRYQ-AELDRRSVAGADAETLAERVKAEL-----RER 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 328 V-GNNLQLIICGSAALSENLcRIF--NAAGLKISEGYGMTETSPVItVNGRTKDlfclgtvGPLLNSCKVKIAE------ 398
Cdd:cd17632 359 VlGGRLLAAVCGSAPLSAEM-KAFmeSLLDLDLHDGYGSTEAGAVI-LDGVIVR-------PPVLDYKLVDVPElgyfrt 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2537297151 399 -----DGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDI-GYIKDGFLKITDRKKEIFKTSGGKYI 461
Cdd:cd17632 430 drphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVmAELGPDRLVYVDRRNNVLKLSQGEFV 498
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
34-483 |
1.67e-27 |
|
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: 116.42 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 34 ISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcLVS 113
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLD-KRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRL-LVT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 114 DKKIYDKVHNIKDQCPNITSLFTFDEIEGAlnwnKIKKKGEEISNQQEVENLKNSIEPDRWV-----TLIYTSGTTGRPK 188
Cdd:TIGR03098 104 SSERLDLLHPALPGCHDLRTLIIVGDPAHA----SEGHPGEEPASWPKLLALGDADPPHPVIdsdmaAILYTSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 189 GVMLSHKNILTNVLDchVRFVMENDEKFRILSILPIChilermvdyvfmyksygiyFAEGMDKLASNFQeVKPDVIL--- 265
Cdd:TIGR03098 180 GVVLSHRNLVAGAQS--VATYLENRPDDRLLAVLPLS-------------------FDYGFNQLTTAFY-VGATVVLhdy 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 266 VVPRIVEKlyaSIYNKGTSGgwLKKQIFLWAlsvakkfepfKPASLshkiadflvfkKWREAVGNNLQLII-CGSAALSE 344
Cdd:TIGR03098 238 LLPRDVLK---ALEKHGITG--LAAVPPLWA----------QLAQL-----------DWPESAAPSLRYLTnSGGAMPRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 345 NLCRIFNAAGL-KISEGYGMTE-----TSPVITVNGRTkdlfclGTVGPLLNSCKVKIA----------EDGEILTKGSN 408
Cdd:TIGR03098 292 TLSRLRSFLPNaRLFLMYGLTEafrstYLPPEEVDRRP------DSIGKAIPNAEVLVLredgsecapgEEGELVHRGAL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 409 VFLGYYKDEEKTREIYTD----DGWLK-------TGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFI 476
Cdd:TIGR03098 366 VAMGYWNDPEKTAERFRPlppfPGELHlpelavwSGDTVRRdEEGFLYFVGRRDEMIKTSGYR-VSPTEVEEVAYATGLV 444
|
....*..
gi 2537297151 477 GEAMVVG 483
Cdd:TIGR03098 445 AEAVAFG 451
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
28-457 |
7.29e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 114.82 E-value: 7.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 28 DGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSES 107
Cdd:COG0365 34 DGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLP-NIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 108 KFCLVSD------KKI--YDKVHNIKDQCPNITSLFTFD------EIEGALNWNkikkkgEEISNQQEVenlknsiEPDR 173
Cdd:COG0365 113 KVLITADgglrggKVIdlKEKVDEALEELPSLEHVIVVGrtgadvPMEGDLDWD------ELLAAASAE-------FEPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 174 WVT------LIYTSGTTGRPKGVMLSHKNILT-------NVLDCHvrfvmENDekfrilsilpichilermvdyVFMY-- 238
Cdd:COG0365 180 PTDaddplfILYTSGTTGKPKGVVHTHGGYLVhaattakYVLDLK-----PGD---------------------VFWCta 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 239 -------KSYGIYFA----------EGmdklASNFQEvkPDVILvvpRIVEKLYASIYnkGTSGGWLkKQIFLWALSVAK 301
Cdd:COG0365 234 digwatgHSYIVYGPllngatvvlyEG----RPDFPD--PGRLW---ELIEKYGVTVF--FTAPTAI-RALMKAGDEPLK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 302 KF------------EPFKPAslshkiadflVFKKWREAVgnnlqliicgsaalsenlcrifnaaGLKISEGYGMTETSPV 369
Cdd:COG0365 302 KYdlsslrllgsagEPLNPE----------VWEWWYEAV-------------------------GVPIVDGWGQTETGGI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 370 ITVNGRTKDLFcLGTVG-PLLnSCKVKIA-EDGEILTKGS-----------NVFLGYYKDEEKTREIY--TDDGWLKTGD 434
Cdd:COG0365 347 FISNLPGLPVK-PGSMGkPVP-GYDVAVVdEDGNPVPPGEegelvikgpwpGMFRGYWNDPERYRETYfgRFPGWYRTGD 424
|
490 500
....*....|....*....|....
gi 2537297151 435 IGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:COG0365 425 GARRdEDGYFWILGRSDDVINVSG 448
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
39-483 |
9.34e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 113.75 E-value: 9.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDKkiy 118
Cdd:PRK09088 28 LDALVGRLAAVLRRRGCVDGERLAVLAR-NSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 119 dkvhnIKDQCPNITSLFTF-DEIEGAlnwnkikkkgeeisnqqeVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNI 197
Cdd:PRK09088 104 -----VAAGRTDVEDLAAFiASADAL------------------EPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 198 --------LTNVLDCHVRFVMENdekfrilsilPICHILermvdyvfmyksygiyfaegmdKLASNfqeVKPdVILVVPR 269
Cdd:PRK09088 161 qqtahnfgVLGRVDAHSSFLCDA----------PMFHII----------------------GLITS---VRP-VLAVGGS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 270 IvekLYASIYNKGTSGGWLKKQiflwALSVAKKF-----------EP-FKPASLSHKIAdflvfkkwreavgnnlqLIIC 337
Cdd:PRK09088 205 I---LVSNGFEPKRTLGRLGDP----ALGITHYFcvpqmaqafraQPgFDAAALRHLTA-----------------LFTG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 338 GSAALSENLcRIFNAAGLKISEGYGMTETSpviTVNGRTKDlfC------LGTVGPLLNSCKVKIAED----------GE 401
Cdd:PRK09088 261 GAPHAAEDI-LGWLDDGIPMVDGFGMSEAG---TVFGMSVD--CdvirakAGAAGIPTPTVQTRVVDDqgndcpagvpGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 402 ILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIK-DGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAM 480
Cdd:PRK09088 335 LLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDaDGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGIRECA 413
|
...
gi 2537297151 481 VVG 483
Cdd:PRK09088 414 VVG 416
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
53-483 |
1.48e-26 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 114.11 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 53 YGINPQDRIALITsVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKfCLVSDKKIYDKVHNIKDQCPNIT 132
Cdd:PRK05620 59 LGITGDQRVGSMM-YNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDE-VIVADPRLAEQLGEILKECPCVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 133 SLFtfdeIEGAlnwNKIKKKGEEISNQQEVENLKN------------SIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTN 200
Cdd:PRK05620 137 AVV----FIGP---SDADSAAAHMPEGIKVYSYEAlldgrstvydwpELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 201 VLDCHV--RFVMENDEKFriLSILPICHILermvdyvfmykSYGIYFAEGMdklaSNFQEVKPDVILVVPRIVEKLYASI 278
Cdd:PRK05620 210 SLSLRTtdSLAVTHGESF--LCCVPIYHVL-----------SWGVPLAAFM----SGTPLVFPGPDLSAPTLAKIIATAM 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 279 --YNKGTSGGWLkkQIFLwalsvakKFEPFKPASLShkiadflvfkkwreavgnnLQLIICGSAALSENLCRIFNAA-GL 355
Cdd:PRK05620 273 prVAHGVPTLWI--QLMV-------HYLKNPPERMS-------------------LQEIYVGGSAVPPILIKAWEERyGV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 356 KISEGYGMTETSPVITV-------NGRTKDL-------FCLGTVGPLLNSCKVKIAED---GEILTKGSNVFLGYYKDE- 417
Cdd:PRK05620 325 DVVHVWGMTETSPVGTVarppsgvSGEARWAyrvsqgrFPASLEYRIVNDGQVMESTDrneGEIQVRGNWVTASYYHSPt 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 418 ---------------EKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKtSGGKYIIPQITENNLKQSRFIGEAMV 481
Cdd:PRK05620 405 eegggaastfrgedvEDANDRFTADGWLRTGDVGSVtRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAV 483
|
..
gi 2537297151 482 VG 483
Cdd:PRK05620 484 IG 485
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
176-579 |
1.94e-26 |
|
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: 110.11 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 176 TLIYTSGTTGRPKGVMLSHKNILTNVLDCHVRfvMENDEKFRILSILPICHILERMVDYVFMYKSYGIYFAEGMDKLASN 255
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAGLHSR--LGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALAED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 256 FQEVKPDVILVVPRIVEKLYASiynkGTSGGWLKkqiflwalsvakkfepfkpaslshkiadflvfkkwreavgnNLQLI 335
Cdd:cd17630 82 LAPPGVTHVSLVPTQLQRLLDS----GQGPAALK-----------------------------------------SLRAV 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 336 ICGSAALSENLCRIFNAAGLKISEGYGMTETSPVITvnGRTKDLFCLGTVGPLLNSCKVKIAEDGEILTKGSNVFLGYYK 415
Cdd:cd17630 117 LLGGAPIPPELLERAADRGIPLYTTYGMTETASQVA--TKRPDGFGRGGVGVLLPGRELRIVEDGEIWVGGASLAMGYLR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 416 DEEktREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVGDGEK----MPC 490
Cdd:cd17630 195 GQL--VPEFNEDGWFTTKDLGELhADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEelgqRPV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 491 ALIQpdfefilkyikyknlhMNTTISPEEIvknkvirerimqdVEKVNKLLGKWEQIKKIELTPTVwsvesgELTPTLKL 570
Cdd:cd17630 272 AVIV----------------GRGPADPAEL-------------RAWLKDKLARFKLPKRIYPVPEL------PRTGGGKV 316
|
....*....
gi 2537297151 571 KRKYIKEKY 579
Cdd:cd17630 317 DRRALRAWL 325
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
45-457 |
4.27e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 112.38 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 45 QVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcLVSDKKIYDKVHNI 124
Cdd:PLN02246 62 RVAAGLHKLGIRQGDVVMLLLP-NCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKL-IITQSCYVDKLKGL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 125 KDQcPNITSLFTFDEIEGALNWNkikkkgeEISNQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNV--- 201
Cdd:PLN02246 140 AED-DGVTVVTIDDPPEGCLHFS-------ELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVaqq 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 202 -------LDCHvrfvmENDekfRILSILPICHI----------LERMVDYVFMYKsygiyFAegMDKLASNFQEVKPDVI 264
Cdd:PLN02246 212 vdgenpnLYFH-----SDD---VILCVLPMFHIyslnsvllcgLRVGAAILIMPK-----FE--IGALLELIQRHKVTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 265 LVVPRIVeklyasiynkgtsggwlkkqiflwaLSVAKKfepfkPASLSHKIAdflvfkkwreavgnNLQLIICGSAALSE 344
Cdd:PLN02246 277 PFVPPIV-------------------------LAIAKS-----PVVEKYDLS--------------SIRMVLSGAAPLGK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 345 NLCRIFNA--AGLKISEGYGMTETSPVITVN-GRTKDLFCL--GTVGPLLNSCKVKIAED-----------GEILTKGSN 408
Cdd:PLN02246 313 ELEDAFRAklPNAVLGQGYGMTEAGPVLAMClAFAKEPFPVksGSCGTVVRNAELKIVDPetgaslprnqpGEICIRGPQ 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2537297151 409 VFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:PLN02246 393 IMKGYLNDPEATANTIDKDGWLHTGDIGYIdDDDELFIVDRLKELIKYKG 442
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
33-457 |
6.38e-26 |
|
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: 110.46 E-value: 6.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 33 KISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLV 112
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLD-NCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 113 SDkkiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiepdrwVTLIYTSGTTGRPKGVML 192
Cdd:cd05934 82 DP------------------------------------------------------------ASILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 193 SHKNILT-NVLDCHVRFVMENDekfRILSILPICHIlermvDYVFmyksYGIYFAegmdkLASNfqevkpDVILVVPRI- 270
Cdd:cd05934 102 THANLTFaGYYSARRFGLGEDD---VYLTVLPLFHI-----NAQA----VSVLAA-----LSVG------ATLVLLPRFs 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 271 -------VEKLYASIYNK-GTSGGWLKKQiflwalsvakkfePFKPASLSHKIadflvfkkwREAvgnnlqliiCGSAAL 342
Cdd:cd05934 159 asrfwsdVRRYGATVTNYlGAMLSYLLAQ-------------PPSPDDRAHRL---------RAA---------YGAPNP 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 343 SENLCRIFNAAGLKISEGYGMTETS-PVITVNGRTKDLFCLGTVGPllnSCKVKIAED----------GEILTK---GSN 408
Cdd:cd05934 208 PELHEEFEERFGVRLLEGYGMTETIvGVIGPRDEPRRPGSIGRPAP---GYEVRIVDDdgqelpagepGELVIRglrGWG 284
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2537297151 409 VFLGYYKDEEKTREIYTdDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:cd05934 285 FFKGYYNMPEATAEAMR-NGWFHTGDLGYRdADGFFYFVDRKKDMIRRRG 333
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
34-483 |
7.76e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 111.59 E-value: 7.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 34 ISTQSLIDQVNQVSRGLLN-YGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLV 112
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQeCGVRKGDRVLLY-MQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 113 SDKkIYDK--------------VHNIKDQCPnitslftfDEIEGAL-NWNKIKKKGEEISNQQEV---ENLKNSIEP--- 171
Cdd:PRK08314 115 GSE-LAPKvapavgnlrlrhviVAQYSDYLP--------AEPEIAVpAWLRAEPPLQALAPGGVVawkEALAAGLAPpph 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 172 ----DRWVTLIYTSGTTGRPKGVMLSHKNILTNVLdCHVRFVMENDEKfRILSILPICHILermvdyvfmyksygiyfae 247
Cdd:PRK08314 186 tagpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAV-GSVLWSNSTPES-VVLAVLPLFHVT------------------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 248 GMdklasnfqevkpdvilvvpriVEKLYASIYNKGT----------SGGWL--KKQIFLWAlsvakkfepfkpaSLSHKI 315
Cdd:PRK08314 245 GM---------------------VHSMNAPIYAGATvvlmprwdreAAARLieRYRVTHWT-------------NIPTMV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 316 ADFLVFKKWREAVGNNLQLIICGSAALSENLC-RIFNAAGLKISEGYGMTETSPVITVN--GRTKdLFCLGTvgPLLNS- 391
Cdd:PRK08314 291 VDFLASPGLAERDLSSLRYIGGGGAAMPEAVAeRLKELTGLDYVEGYGLTETMAQTHSNppDRPK-LQCLGI--PTFGVd 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 392 ---------CKVKIAEDGEILTKGSNVFLGYYKDEEKTREIYTD-DG--WLKTGDIGYI-KDGFLKITDRKKEIFKTSGG 458
Cdd:PRK08314 368 arvidpetlEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMdEEGYFFITDRLKRMINASGF 447
|
490 500
....*....|....*....|....*
gi 2537297151 459 KyIIPQITENNLKQSRFIGEAMVVG 483
Cdd:PRK08314 448 K-VWPAEVENLLYKHPAIQEACVIA 471
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
32-536 |
1.19e-25 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 111.22 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINpQDRIALITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcL 111
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLR-KGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKL-I 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VSDKKIYDKVHNIkdQCPNItsLFTFDEIEGALNWNKIKKKGEEISNQQEVENLKNSiepdRWVTLIYTSGTTGRPKGVM 191
Cdd:PLN02330 132 VTNDTNYGKVKGL--GLPVI--VLGEEKIEGAVNWKELLEAADRAGDTSDNEEILQT----DLCALPFSSGTTGISKGVM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 192 LSHKNILTNVldCHVRFVM--ENDEKFRILSILPICHIlermvdyvfmyksYGIyfaegmdklasnfqevkpdvilvvpr 269
Cdd:PLN02330 204 LTHRNLVANL--CSSLFSVgpEMIGQVVTLGLIPFFHI-------------YGI-------------------------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 270 iVEKLYASIYNKG--TSGGWLKKQIFLWALSVAK-KFEPFKP----ASLSHKIADFLVFKKWReavgnnLQLIICGSAAL 342
Cdd:PLN02330 243 -TGICCATLRNKGkvVVMSRFELRTFLNALITQEvSFAPIVPpiilNLVKNPIVEEFDLSKLK------LQAIMTAAAPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 343 SENLCRIFNAA--GLKISEGYGMTETSPVITVNG---RTKDLFCLGTVGPLLNSCKVKIAE-----------DGEILTKG 406
Cdd:PLN02330 316 APELLTAFEAKfpGVQVQEAYGLTEHSCITLTHGdpeKGHGIAKKNSVGFILPNLEVKFIDpdtgrslpkntPGELCVRS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 407 SNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAMVV--G 483
Cdd:PLN02330 396 QCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIdDDGDIFIVDRIKELIKYKGFQ-VAPAELEAILLTHPSVEDAAVVplP 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2537297151 484 DGE--KMP--CALIQPDF----EFILKYI--------KYKNLHMNTTI--SPEEIVKNKVIRERIMQDVEK 536
Cdd:PLN02330 475 DEEagEIPaaCVVINPKAkeseEDILNFVaanvahykKVRVVQFVDSIpkSLSGKIMRRLLKEKMLSINKA 545
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
166-457 |
1.47e-25 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 110.91 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 166 KNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDCHVRF--VMENDEKFRILSiLPICHILERMVD-YVFMYKSyg 242
Cdd:PRK08974 200 KPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYgpLLHPGKELVVTA-LPLYHIFALTVNcLLFIELG-- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 243 iyfaeGMDKLASNfqevkpdvilvvPRIVEKLYASiynkgtsggwLKKQIFLWALSVAKKFEPFKPASLSHKIaDFlvfk 322
Cdd:PRK08974 277 -----GQNLLITN------------PRDIPGFVKE----------LKKYPFTAITGVNTLFNALLNNEEFQEL-DF---- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 323 kwreavgNNLQLIICGSAALSENLC-RIFNAAGLKISEGYGMTETSPVITVNGRTKDLFClGTVGPLLNSCKVKIAED-- 399
Cdd:PRK08974 325 -------SSLKLSVGGGMAVQQAVAeRWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYS-GSIGLPVPSTEIKLVDDdg 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2537297151 400 --------GEILTKGSNVFLGYYKDEEKTREIYTdDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:PRK08974 397 nevppgepGELWVKGPQVMLGYWQRPEATDEVIK-DGWLATGDIAVMdEEGFLRIVDRKKDMILVSG 462
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
177-488 |
2.66e-25 |
|
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: 106.82 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 177 LIYTSGTTGRPKGVMLSHK-NILTNVLDCHVRFVMENDekfRILSILPICHilermvdyVFMYKSyGIyfaegmdkLASN 255
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRqTLRAAAAWADCADLTEDD---RYLIINPFFH--------TFGYKA-GI--------VACL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 256 FQ--EVKPDVILVVPRIVEKLYasiynkgtsggwlKKQIflwalsvakKFEPfKPASLSHKIADFLVFKKWREAvgnNLQ 333
Cdd:cd17638 65 LTgaTVVPVAVFDVDAILEAIE-------------RERI---------TVLP-GPPTLFQSLLDHPGRKKFDLS---SLR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 334 LIICGSAALSENLC-RIFNAAGLK-ISEGYGMTETspVITVNGRTKDLFCL--GTVGPLLNSCKVKIAEDGEILTKGSNV 409
Cdd:cd17638 119 AAVTGAATVPVELVrRMRSELGFEtVLTAYGLTEA--GVATMCRPGDDAETvaTTCGRACPGFEVRIADDGEVLVRGYNV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 410 FLGYYKDEEKTREIYTDDGWLKTGDIGYIKD-GFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG-DGEK 487
Cdd:cd17638 197 MQGYLDDPEATAEAIDADGWLHTGDVGELDErGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHPGVAQVAVIGvPDER 275
|
.
gi 2537297151 488 M 488
Cdd:cd17638 276 M 276
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
41-521 |
3.85e-25 |
|
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: 108.93 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 41 DQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDKKIYDK 120
Cdd:cd12118 37 DRCRRLASALAALGISRGDTVAVL-APNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFEYED 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 121 VHNIKDqcPNITSLFTFDEiegalnWNKIkkkgeeisnqqevenlknsiepdrwvTLIYTSGTTGRPKGVMLSHKNILTN 200
Cdd:cd12118 116 LLAEGD--PDFEWIPPADE------WDPI--------------------------ALNYTSGTTGRPKGVVYHHRGAYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 201 VLDCHVRFVMENDEKFriLSILPichilermvdyvfMYKSYGIYFAEGMDKLASN---FQEVKPDVIlvvpriveklYAS 277
Cdd:cd12118 162 ALANILEWEMKQHPVY--LWTLP-------------MFHCNGWCFPWTVAAVGGTnvcLRKVDAKAI----------YDL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 278 IYNKGTS--GGwlkKQIFLWALSVAKkfePFKPASLSHKIadflvfkkwreavgnnlQLIICGSAALSENLCRIfNAAGL 355
Cdd:cd12118 217 IEKHKVThfCG---APTVLNMLANAP---PSDARPLPHRV-----------------HVMTAGAPPPAAVLAKM-EELGF 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 356 KISEGYGMTETSPVITVNG------------RTKDLFCLGTVGPLLNSCKVK-------IAED----GEILTKGSNVFLG 412
Cdd:cd12118 273 DVTHVYGLTETYGPATVCAwkpewdelpteeRARLKARQGVRYVGLEEVDVLdpetmkpVPRDgktiGEIVFRGNIVMKG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 413 YYKDEEKTREIYtDDGWLKTGDIGYIK-DGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG--D---GE 486
Cdd:cd12118 353 YLKNPEATAEAF-RGGWFHSGDLAVIHpDGYIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLEAAVVArpDekwGE 430
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2537297151 487 kMPCALI------QPDFEFILKYIKyknLHMNTTISPEEIV 521
Cdd:cd12118 431 -VPCAFVelkegaKVTEEEIIAFCR---EHLAGFMVPKTVV 467
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
29-483 |
5.99e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 108.62 E-value: 5.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 29 GSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESK 108
Cdd:PRK08008 33 GVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLD-NCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 109 FCLVSDK--KIYDKVHNIKDQCPNITSLF--TFDEIEGALNWNKIKkkgeeisNQQEVE-NLKNSIEPDRWVTLIYTSGT 183
Cdd:PRK08008 112 LLVTSAQfyPMYRQIQQEDATPLRHICLTrvALPADDGVSSFTQLK-------AQQPATlCYAPPLSTDDTAEILFTSGT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 184 TGRPKGVMLSHKNIL----TNVLDCHVRfvmENDekfRILSILPICHIlermvdyvfmyksygiyfaegmdklasNFQ-- 257
Cdd:PRK08008 185 TSRPKGVVITHYNLRfagyYSAWQCALR---DDD---VYLTVMPAFHI---------------------------DCQct 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 258 ------EVKPDVILvvpriVEKLYASIYnkgtsggWlkKQIFLWALSVAK---------KFEPFKPASLSHKIADFLVFk 322
Cdd:PRK08008 232 aamaafSAGATFVL-----LEKYSARAF-------W--GQVCKYRATITEcipmmirtlMVQPPSANDRQHCLREVMFY- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 323 kwreavgnnLQLiicgSAALSENLCRIFnaaGLKISEGYGMTETSpVITVNGRTKDLFCLGTVGPLLNSCKVKIAED--- 399
Cdd:PRK08008 297 ---------LNL----SDQEKDAFEERF---GVRLLTSYGMTETI-VGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDhnr 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 400 -------GEILTK---GSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKYIIPQItEN 468
Cdd:PRK08008 360 plpageiGEICIKgvpGKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVdEEGFFYFVDRRCNMIKRGGENVSCVEL-EN 438
|
490
....*....|....*
gi 2537297151 469 NLKQSRFIGEAMVVG 483
Cdd:PRK08008 439 IIATHPKIQDIVVVG 453
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
32-483 |
6.76e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 108.97 E-value: 6.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCL 111
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLP-NCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VSDKkIYDKVHNIKDQCP----NITSLFTFDEIEGALNWNKIKKKGEEI---SNQQEVENLKNSIEPDR----------- 173
Cdd:PRK06710 127 CLDL-VFPRVTNVQSATKiehvIVTRIADFLPFPKNLLYPFVQKKQSNLvvkVSESETIHLWNSVEKEVntgvevpcdpe 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 174 --WVTLIYTSGTTGRPKGVMLSHKNILTNVL-DCHVRFVMENDEKFrILSILPICHIlermvdyvfmyksYGIyfaegmd 250
Cdd:PRK06710 206 ndLALLQYTGGTTGFPKGVMLTHKNLVSNTLmGVQWLYNCKEGEEV-VLGVLPFFHV-------------YGM------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 251 KLASNFQEVKPDVILVVPRIVEKLYASIYNKGtsggwlKKQIFlwalsvakkfepfkPASLSHKIAdFLVFKKWREAVGN 330
Cdd:PRK06710 265 TAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKH------KVTLF--------------PGAPTIYIA-LLNSPLLKEYDIS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 331 NLQLIICGSAALSENLCRIFNA-AGLKISEGYGMTETSPVITVNGRTKDLFClGTVGPLLNSCKVKI-----------AE 398
Cdd:PRK06710 324 SIRACISGSAPLPVEVQEKFETvTGGKLVEGYGLTESSPVTHSNFLWEKRVP-GSIGVPWPDTEAMImsletgealppGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 399 DGEILTKGSNVFLGYYKDEEKTREIYtDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIG 477
Cdd:PRK06710 403 IGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMdEDGFFYVKDRKKDMIVASGFN-VYPREVEEVLYEHEKVQ 480
|
....*.
gi 2537297151 478 EAMVVG 483
Cdd:PRK06710 481 EVVTIG 486
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
168-457 |
1.67e-24 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 107.80 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 168 SIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDCHV--RFVMEN---DEKFRILSILPICHILERMVDYvFMYKSYG 242
Cdd:PRK07059 200 KLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAwlQPAFEKkprPDQLNFVCALPLYHIFALTVCG-LLGMRTG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 243 iyfaeGMDKLASN-------FQEVKPDVILVVPRIveklyASIYNkgtsggwlkkqiflwalsvakkfepfkpASLSHKI 315
Cdd:PRK07059 279 -----GRNILIPNprdipgfIKELKKYQVHIFPAV-----NTLYN----------------------------ALLNNPD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 316 ADFLVFKKWREAVGnnlqliicGSAALSENLC-RIFNAAGLKISEGYGMTETSPVITVNGRTKDLFClGTVGPLLNSCKV 394
Cdd:PRK07059 321 FDKLDFSKLIVANG--------GGMAVQRPVAeRWLEMTGCPITEGYGLSETSPVATCNPVDATEFS-GTIGLPLPSTEV 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2537297151 395 KIAED----------GEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:PRK07059 392 SIRDDdgndlplgepGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMdERGYTKIVDRKKDMILVSG 465
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
177-497 |
2.12e-24 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 106.88 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 177 LIYTSGTTGRPKGVMLSHKNILTNVLDCHV--RFVmendEKFRILSILPICHilermvdyvfmykSYGIYfaegmdkLAS 254
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSNALTLVDywRFT----PDDVLIHALPIFH-------------THGLF-------VAT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 255 NfqevkpdVILVvpriveklyasiynkgtSGGwlkKQIFLwalsvaKKFEP-----FKPAS-------------LSHKIA 316
Cdd:PRK07514 217 N-------VALL-----------------AGA---SMIFL------PKFDPdavlaLMPRAtvmmgvptfytrlLQEPRL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 317 DflvfkkwREAVGNnLQLIICGSAALSENLCRIFNA-AGLKISEGYGMTETSpVITVN---GRTKDlfclGTVGPLLNSC 392
Cdd:PRK07514 264 T-------REAAAH-MRLFISGSAPLLAETHREFQErTGHAILERYGMTETN-MNTSNpydGERRA----GTVGFPLPGV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 393 KVKIA--EDGEILT---------KGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKY 460
Cdd:PRK07514 331 SLRVTdpETGAELPpgeigmievKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIdERGYVHIVGRGKDLI-ISGGYN 409
|
330 340 350
....*....|....*....|....*....|....*..
gi 2537297151 461 IIPQITENNLKQSRFIGEAMVVGdgekMPcaliQPDF 497
Cdd:PRK07514 410 VYPKEVEGEIDELPGVVESAVIG----VP----HPDF 438
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
15-565 |
8.99e-24 |
|
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: 105.59 E-value: 8.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 15 RNRPIDVSIATKK-DGSWKKISTQSLIDQVNQVSRGLLNYGINPqDRIALITSVNRSEWLIMDFAIQQIGAVSVPI---Y 90
Cdd:cd05921 6 RQAPDRTWLAEREgNGGWRRVTYAEALRQVRAIAQGLLDLGLSA-ERPLLILSGNSIEHALMALAAMYAGVPAAPVspaY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 91 PTMSDD--DLTFILNNSESKFCLVSDKKIYDK-----------VHNIKDQCPNITSlFTFDEIEgalnwnkikkkgeEIS 157
Cdd:cd05921 85 SLMSQDlaKLKHLFELLKPGLVFAQDAAPFARalaaifplgtpLVVSRNAVAGRGA-ISFAELA-------------ATP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 158 NQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTN---VLDCHVRFvmeNDEKFRILSILPICHILE----- 229
Cdd:cd05921 151 PTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANqamLEQTYPFF---GEEPPVLVDWLPWNHTFGgnhnf 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 230 RMVDYV--FMYKSYGIYFAEGMDKLASNFQEVKPDVILVVPRIVEKLYASIYNKGTsggwLKKQIFlwalsvAK-KFEPF 306
Cdd:cd05921 228 NLVLYNggTLYIDDGKPMPGGFEETLRNLREISPTVYFNVPAGWEMLVAALEKDEA----LRRRFF------KRlKLMFY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 307 KPASLSHKIADFLvfkkwreavgnnlqliicgsAALSENLC--RIFNAAGlkisegYGMTETSPVITVNgrTKDLFCLGT 384
Cdd:cd05921 298 AGAGLSQDVWDRL--------------------QALAVATVgeRIPMMAG------LGATETAPTATFT--HWPTERSGL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 385 VGPLLNSCKVKIAEDG---EILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDI-----------GYIKDGflkitdRKK 450
Cdd:cd05921 350 IGLPAPGTELKLVPSGgkyEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAakladpddpakGLVFDG------RVA 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 451 EIFKTSGGKYII--PQITENNLKQSRFIGEAMVVGDGEKMPCALIQPDFEFIlkyikyKNLHMNTTISPEEIVKNKVIRE 528
Cdd:cd05921 424 EDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGEDRAEVGALVFPDLLAC------RRLVGLQEASDAEVLRHAKVRA 497
|
570 580 590
....*....|....*....|....*....|....*...
gi 2537297151 529 RIMQDVEKVNK-LLGKWEQIKKIELTPTVWSVESGELT 565
Cdd:cd05921 498 AFRDRLAALNGeATGSSSRIARALLLDEPPSIDKGEIT 535
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
177-457 |
1.91e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 104.52 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 177 LIYTSGTTGRPKGVMLSHKNILTNVLDCHVRF---------VMENDEKFRIlSILPICHIlermvdYVFMyksygiyfAE 247
Cdd:PRK12492 212 LQYTGGTTGLAKGAMLTHGNLVANMLQVRACLsqlgpdgqpLMKEGQEVMI-APLPLYHI------YAFT--------AN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 248 GMDKLASNfqevKPDVILVVPRIVeklyasiynkgtsGGWLKkQIFLWALSVAKKFEPFKPASLSH---KIADFlvfkkw 324
Cdd:PRK12492 277 CMCMMVSG----NHNVLITNPRDI-------------PGFIK-ELGKWRFSALLGLNTLFVALMDHpgfKDLDF------ 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 325 reavgNNLQLIICGSAALSENLC-RIFNAAGLKISEGYGMTETSPVITVNGRtKDLFCLGTVGPLLNSCKVKIAED---- 399
Cdd:PRK12492 333 -----SALKLTNSGGTALVKATAeRWEQLTGCTIVEGYGLTETSPVASTNPY-GELARLGTVGIPVPGTALKVIDDdgne 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2537297151 400 ------GEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:PRK12492 407 lplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIdPDGFVRIVDRKKDLIIVSG 471
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
28-465 |
1.02e-22 |
|
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: 101.98 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 28 DGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSVNRS--EWLimdFAIQQIGAVSVPIYPTMSDDdltfILNNS 105
Cdd:cd05906 34 DGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDfiPAF---WACVLAGFVPAPLTVPPTYD----EPNAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 106 ESKFClvsdkkiydKVHNIKDQCPNITSLFTFDEIEGALNWNKIKK-KGEEISNQQEVENLKNSI--EPDRWVTLIYTSG 182
Cdd:cd05906 107 LRKLR---------HIWQLLGSPVVLTDAELVAEFAGLETLSGLPGiRVLSIEELLDTAADHDLPqsRPDDLALLMLTSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 183 TTGRPKGVMLSHKNILT----NVLDCHVrfvmenDEKFRILSILPICHilermVDYVFMYKSYGIYFaeGMDKLasnfqE 258
Cdd:cd05906 178 STGFPKAVPLTHRNILArsagKIQHNGL------TPQDVFLNWVPLDH-----VGGLVELHLRAVYL--GCQQV-----H 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 259 VKPDVILVVP----RIVEKLYASIynkgtsgGWLKKqiFLWALSV--AKKFEPFKpASLShkiadflvfkkwreavgnNL 332
Cdd:cd05906 240 VPTEEILADPlrwlDLIDRYRVTI-------TWAPN--FAFALLNdlLEEIEDGT-WDLS------------------SL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 333 QLIICGSAALSENLCRIFNAA----GLK---ISEGYGMTETSPVITVN-------GRTKDLF-CLGTVGPllnSCKVKI- 396
Cdd:cd05906 292 RYLVNAGEAVVAKTIRRLLRLlepyGLPpdaIRPAFGMTETCSGVIYSrsfptydHSQALEFvSLGRPIP---GVSMRIv 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2537297151 397 ---------AEDGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIKDGFLKITDRKKEIFKTSGGKYIIPQI 465
Cdd:cd05906 369 ddegqllpeGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEI 446
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
171-520 |
1.14e-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: 99.86 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 171 PDRWVTLIYTSGTTGRPKGVMLSHKNILTNVldchvrFVMENDEKFR----ILSILPICHILERMVdyvfmyksygiyfa 246
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNA------WMLALNSLFDpddvLLCGLPLFHVNGSVV-------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 247 EGMDKLASNFQevkpdviLVVPriveklyasiynkgTSGGWLKKQIF--LWALsvakkFEPFKPASLSH---KIADFLVF 321
Cdd:cd05944 61 TLLTPLASGAH-------VVLA--------------GPAGYRNPGLFdnFWKL-----VERYRITSLSTvptVYAALLQV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 322 KKWREAvgNNLQLIICGSAALSENLCRIF-NAAGLKISEGYGMTETSPVITVNGRTKDLFcLGTVGPLLNSCKVKIA--- 397
Cdd:cd05944 115 PVNADI--SSLRFAMSGAAPLPVELRARFeDATGLPVVEGYGLTEATCLVAVNPPDGPKR-PGSVGLRLPYARVRIKvld 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 398 ------------EDGEILTKGSNVFLGYYKDEEKtREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQ 464
Cdd:cd05944 192 gvgrllrdcapdEVGEICVAGPGVFGGYLYTEGN-KNAFVADGWLNTGDLGRLdADGYLFITGRAKDLI-IRGGHNIDPA 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2537297151 465 ITENNLKQSRFIGEAMVVGD-----GEkMPCALIQpdfefilkyikyknLHMNTTISPEEI 520
Cdd:cd05944 270 LIEEALLRHPAVAFAGAVGQpdahaGE-LPVAYVQ--------------LKPGAVVEEEEL 315
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
45-483 |
6.16e-22 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 99.44 E-value: 6.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 45 QVSRGLLNYGINPQDRIALI---TSVNRSEWlimdFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKfCLVSDKKIYDKV 121
Cdd:PRK06018 51 KVSQALDRDGIKLGDRVATIawnTWRHLEAW----YGIMGIGAICHTVNPRLFPEQIAWIINHAEDR-VVITDLTFVPIL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 122 HNIKDQCPNITSLFTFDE--------IEGALNWnkikkkgEEISNQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLS 193
Cdd:PRK06018 126 EKIADKLPSVERYVVLTDaahmpqttLKNAVAY-------EEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 194 HKnilTNVLdcHVRFVMEND-----EKFRILSILPICHIlermvdyvfmyKSYGIYFAEGmdklASNFQEVKPDVILVVP 268
Cdd:PRK06018 199 HR---SNVL--HALMANNGDalgtsAADTMLPVVPLFHA-----------NSWGIAFSAP----SMGTKLVMPGAKLDGA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 269 RIVEKLYAS--IYNKGTSGGWLkkqIFLWALSVAKKFEPfkpaslshkiadflvfkkwreavgnNLQLIICGSAALSENL 346
Cdd:PRK06018 259 SVYELLDTEkvTFTAGVPTVWL---MLLQYMEKEGLKLP-------------------------HLKMVVCGGSAMPRSM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 347 CRIFNAAGLKISEGYGMTETSPVITVNGRT---------KDLFCLGTVGPLLNSCKVKIAED------------GEILTK 405
Cdd:PRK06018 311 IKAFEDMGVEVRHAWGMTEMSPLGTLAALKppfsklpgdARLDVLQKQGYPPFGVEMKITDDagkelpwdgktfGRLKVR 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2537297151 406 GSNVFLGYYKDEEktrEIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKtSGGKYIIPQITENNLKQSRFIGEAMVVG 483
Cdd:PRK06018 391 GPAVAAAYYRVDG---EILDDDGFFDTGDVATIdAYGYMRITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
169-457 |
9.52e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 99.18 E-value: 9.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 169 IEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDCHVRFVMEN---DEKFRILSILPICHIlermvdyvFMYKSYGIYF 245
Cdd:PRK08751 205 IEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGkleEGCEVVITALPLYHI--------FALTANGLVF 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 246 AE--GMDKLASNFQEVkpdvilvvPRIVEKLyasiynkgtsggwlKKQIFLWALSVAKKFEPFkpasLSHKIADFLVFKK 323
Cdd:PRK08751 277 MKigGCNHLISNPRDM--------PGFVKEL--------------KKTRFTAFTGVNTLFNGL----LNTPGFDQIDFSS 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 324 WREAVGNNLQLiicgSAALSENLCRIfnaAGLKISEGYGMTETSPVITVNGRTKDLFClGTVGPLLNSCKVKIAED---- 399
Cdd:PRK08751 331 LKMTLGGGMAV----QRSVAERWKQV---TGLTLVEAYGLTETSPAACINPLTLKEYN-GSIGLPIPSTDACIKDDagtv 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2537297151 400 ------GEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:PRK08751 403 laigeiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMdEQGFVYIVDRKKDMILVSG 467
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
171-460 |
1.36e-21 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 98.33 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 171 PDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDchVRFVMENDEKFRILSILPICHILERM----------VDYVFMYKS 240
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFA--ILNSTEWKTKDRILSWMPLTHDMGLIafhlapliagMNQYLMPTR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 241 YGIYFAEGMDKLASNFQEVkpdvILVVPRIVEKLYASIYNKGTSGGWLKKQIFLwalsVAKKFEPFKPaSLSHKIADFLV 320
Cdd:cd05908 183 LFIRRPILWLKKASEHKAT----IVSSPNFGYKYFLKTLKPEKANDWDLSSIRM----ILNGAEPIDY-ELCHEFLDHMS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 321 FKKWREavgnNLQLIICGSAALSENLCriFNAAGLKISEGY----GMTETSPVITVNGRTKDLFCLGTVGPLLNSCKVKI 396
Cdd:cd05908 254 KYGLKR----NAILPVYGLAEASVGAS--LPKAQSPFKTITlgrrHVTHGEPEPEVDKKDSECLTFVEVGKPIDETDIRI 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2537297151 397 AED----------GEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIKDGFLKITDRKKEIFKTSGGKY 460
Cdd:cd05908 328 CDEdnkilpdgyiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRNGRLVITGREKDIIFVNGQNV 401
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
43-509 |
2.29e-21 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 97.82 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 43 VNQVSRGLLNYGINPQDRIAlITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDK-KIYDK- 120
Cdd:PRK13295 65 VDRVAVGLARLGVGRGDVVS-CQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTfRGFDHa 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 121 --VHNIKDQCPNITSLFTFDEiEGALNWNK--IKKKGEEISNQQEVenLKNS-IEPDRWVTLIYTSGTTGRPKGVMLSHK 195
Cdd:PRK13295 144 amARRLRPELPALRHVVVVGG-DGADSFEAllITPAWEQEPDAPAI--LARLrPGPDDVTQLIYTSGTTGEPKGVMHTAN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 196 NILTNVLDCHVRFVMENDEKfrILSILPICHILErmvdyvFMYKsygiyfaegmdklasnfqevkpdviLVVPRIVEK-- 273
Cdd:PRK13295 221 TLMANIVPYAERLGLGADDV--ILMASPMAHQTG------FMYG-------------------------LMMPVMLGAta 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 274 LYASIYNKGTSGGWLKKQIFLWALSVAkkfePFkpaslshkIADFLVFKKWREAVGNNLQLIICGSA----ALSENLCRI 349
Cdd:PRK13295 268 VLQDIWDPARAAELIRTEGVTFTMAST----PF--------LTDLTRAVKESGRPVSSLRTFLCAGApipgALVERARAA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 350 FnaaGLKISEGYGMTETSPVITVNGRTKDLFCLGTVGPLLNSCKVKI----------AEDGEILTKGSNVFLGYYKDEEK 419
Cdd:PRK13295 336 L---GAKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVvdadgaplpaGQIGRLQVRGCSNFGGYLKRPQL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 420 TReiyTD-DGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG--D---GEKMpCAL 492
Cdd:PRK13295 413 NG---TDaDGWFDTGDLARIdADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVAypDerlGERA-CAF 487
|
490 500
....*....|....*....|...
gi 2537297151 493 IQP------DFEFILKYIKYKNL 509
Cdd:PRK13295 488 VVPrpgqslDFEEMVEFLKAQKV 510
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
39-483 |
1.16e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 95.61 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIaLITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKfCLVSDKKIY 118
Cdd:PRK07786 48 LDDRVAALAGALSRRGVGFGDRV-LILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAH-VVVTEAALA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 119 DKVHNIKDQCPNITSLFTF--DEIEGALNWNKIKKKGEEISNQQEVENlknsiepDRWVTLIYTSGTTGRPKGVMLSHKN 196
Cdd:PRK07786 126 PVATAVRDIVPLLSTVVVAggSSDDSVLGYEDLLAEAGPAHAPVDIPN-------DSPALIMYTSGTTGRPKGAVLTHAN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 197 ILTNVLDCHVRFVMENDEKFRILSIlPICHIlermvdyvfmyksygiyfaegmdklaSNFQEVKPDVILVVPRIVEKLYA 276
Cdd:PRK07786 199 LTGQAMTCLRTNGADINSDVGFVGV-PLFHI--------------------------AGIGSMLPGLLLGAPTVIYPLGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 277 siynkgtsggwlkkqiflwalsvakkfepFKPASL-----SHKIAD-FLVFKKWR------EAVGNNLQL--IICGSAAL 342
Cdd:PRK07786 252 -----------------------------FDPGQLldvleAEKVTGiFLVPAQWQavcaeqQARPRDLALrvLSWGAAPA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 343 SENLCRIFNAA--GLKISEGYGMTETSPVITVNGRTKDLFCLGTVGPLLNSCKVKIAED----------GEILTKGSNVF 410
Cdd:PRK07786 303 SDTLLRQMAATfpEAQILAAFGQTEMSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVDEnmndvpvgevGEIVYRAPTLM 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2537297151 411 LGYYKDEEKTREIYtDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG 483
Cdd:PRK07786 383 SGYWNNPEATAEAF-AGGWFHSGDLVRQdEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIG 454
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
171-457 |
1.24e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 96.57 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 171 PDRWVTLIYTSGTTGRPKGVMLSHKNILTN------VLDCHVrfvmeNDEKFRIL-----------SILPICHILErmvd 233
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANraqvaaRIDFSP-----EDKVFNALpvfhsfgltggLVLPLLSGVK---- 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 234 yVFMYKS---YGIyfaegmdklasnfqevkpdvilvVPRIVEKLYASIYnKGTSggwlkkqIFLWALsvAKKFEPFkpas 310
Cdd:PRK06814 863 -VFLYPSplhYRI-----------------------IPELIYDTNATIL-FGTD-------TFLNGY--ARYAHPY---- 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 311 lshkiaDFlvfkkwreavgNNLQLIICGSAALSENLCRIF-NAAGLKISEGYGMTETSPVITVNgrTKDLFCLGTVGPLL 389
Cdd:PRK06814 905 ------DF-----------RSLRYVFAGAEKVKEETRQTWmEKFGIRILEGYGVTETAPVIALN--TPMHNKAGTVGRLL 965
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2537297151 390 NSCKVK------IAEDGEILTKGSNVFLGYYKdEEKTREIY-TDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:PRK06814 966 PGIEYRlepvpgIDEGGRLFVRGPNVMLGYLR-AENPGVLEpPADGWYDTGDIVTIdEEGFITIKGRAKRFAKIAG 1040
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
32-483 |
2.35e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 94.87 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINPQDRIAlITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcL 111
Cdd:PLN02860 31 RRRTGHEFVDGVLSLAAGLLRLGLRNGDVVA-IAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVM-L 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VSDKKI---YDKVHNikDQCPNI--------TSLFTFDEIEGALNWNKIKKKGeeISNQqeveNLKNSIEPDRWVTLIYT 180
Cdd:PLN02860 109 VTDETCsswYEELQN--DRLPSLmwqvflesPSSSVFIFLNSFLTTEMLKQRA--LGTT----ELDYAWAPDDAVLICFT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 181 SGTTGRPKGVMLSHKNILTNVLdCHVRFVMENDEKFrILSILPICHI--LERMVDYVfMYKSYGIYFAEGMDKLAsnFQE 258
Cdd:PLN02860 181 SGTTGRPKGVTISHSALIVQSL-AKIAIVGYGEDDV-YLHTAPLCHIggLSSALAML-MVGACHVLLPKFDAKAA--LQA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 259 VKPDVI---LVVPRIVEKLYASIYNKGTSggwlkkqiflwalsvakkfepfkpaslshkiadflvfkkwreAVGNNLQLI 335
Cdd:PLN02860 256 IKQHNVtsmITVPAMMADLISLTRKSMTW------------------------------------------KVFPSVRKI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 336 ICGSAALSENLC----RIFNAAglKISEGYGMTETSPVIT-------------VNGRTKDLFCLGTVGPLLNSC------ 392
Cdd:PLN02860 294 LNGGGSLSSRLLpdakKLFPNA--KLFSAYGMTEACSSLTfmtlhdptlespkQTLQTVNQTKSSSVHQPQGVCvgkpap 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 393 --KVKIAED-----GEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIKD-GFLKITDRKKEIFKTsGGKYIIPQ 464
Cdd:PLN02860 372 hvELKIGLDessrvGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKaGNLWLIGRSNDRIKT-GGENVYPE 450
|
490
....*....|....*....
gi 2537297151 465 ITENNLKQSRFIGEAMVVG 483
Cdd:PLN02860 451 EVEAVLSQHPGVASVVVVG 469
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
39-496 |
2.48e-20 |
|
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: 93.75 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALItsVNRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVsdkki 117
Cdd:cd05930 18 LDARANRLARYLRERGVGPGDLVAVL--LERSlEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLT----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 118 ydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiEPDRWVTLIYTSGTTGRPKGVMLSHKNI 197
Cdd:cd05930 91 ----------------------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 198 LtNVLDCHVR--FVMENDekfRILSILPIC---HILErmvdyVFMYKSYG--IYFAEG-----MDKLASNFQEVKPDVIL 265
Cdd:cd05930 119 V-NLLLWMQEayPLTPGD---RVLQFTSFSfdvSVWE-----IFGALLAGatLVVLPEevrkdPEALADLLAEEGITVLH 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 266 VVPriveklyasiynkgtsggwlkkqiflwalSVAKKFepfkpasLSHkiADFLVFKKWReavgnnlqLIICGSAALSEN 345
Cdd:cd05930 190 LTP-----------------------------SLLRLL-------LQE--LELAALPSLR--------LVLVGGEALPPD 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 346 LCRIFNAA--GLKISEGYGMTETSPVITVNGRTKDLFCLGTV--G-PLLNS---------CKVKIAEDGEILTKGSNVFL 411
Cdd:cd05930 224 LVRRWRELlpGARLVNLYGPTEATVDATYYRVPPDDEEDGRVpiGrPIPNTrvyvldenlRPVPPGVPGELYIGGAGLAR 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 412 GYYKDEEKTREIYTDDGWL------KTGDIGYIK-DG---FL-------KItdrkkeifktsGGKYIIPQITENNLKQSR 474
Cdd:cd05930 304 GYLNRPELTAERFVPNPFGpgermyRTGDLVRWLpDGnleFLgriddqvKI-----------RGYRIELGEIEAALLAHP 372
|
490 500
....*....|....*....|....*.
gi 2537297151 475 FIGEAMVV----GDGEKMPCALIQPD 496
Cdd:cd05930 373 GVREAAVVaredGDGEKRLVAYVVPD 398
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
34-540 |
3.08e-20 |
|
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: 93.97 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 34 ISTQSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVS 113
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLI-MLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 114 dkkiydkvhniKDQCPNI--------TSLFTFDEIEGALNWNKIKKKGEEISNQQEVENLKNSI--EPDRWvtlIYTSGT 183
Cdd:cd05959 109 -----------GELAPVLaaaltkseHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAATHadDPAFW---LYSSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 184 TGRPKGVMLSHKNIlTNVLDCHVRFVMENDEKFRILSILPICHilermvdyvfmykSYGI----YFAEGM---------- 249
Cdd:cd05959 175 TGRPKGVVHLHADI-YWTAELYARNVLGIREDDVCFSAAKLFF-------------AYGLgnslTFPLSVgattvlmper 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 250 ---DKLASNFQEVKPDVILVVPriveKLYASIYNKGTSGGWLKKQIFLwALSVAkkfEPFkPASlshkiadflVFKKWRe 326
Cdd:cd05959 241 ptpAAVFKRIRRYRPTVFFGVP----TLYAAMLAAPNLPSRDLSSLRL-CVSAG---EAL-PAE---------VGERWK- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 327 avgnnlqliicgsaalsenlcrifNAAGLKISEGYGMTETSPVITVN--GRTKdlfcLGTVGPLLNSCKVKI-------- 396
Cdd:cd05959 302 ------------------------ARFGLDILDGIGSTEMLHIFLSNrpGRVR----YGTTGKPVPGYEVELrdedggdv 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 397 --AEDGEILTKGSNVFLGYYKDEEKTREIYtDDGWLKTGDiGYIK--DGFLKITDRKKEIFKTSgGKYIIPQITENNLKQ 472
Cdd:cd05959 354 adGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGD-KYVRddDGFYTYAGRADDMLKVS-GIWVSPFEVESALVQ 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2537297151 473 SRFIGEAMVVgdGEKMPCALIQPdfefiLKYIKYKNLHMNTTISPEEI---VKNKVIRERIMQDVEKVNKL 540
Cdd:cd05959 431 HPAVLEAAVV--GVEDEDGLTKP-----KAFVVLRPGYEDSEALEEELkefVKDRLAPYKYPRWIVFVDEL 494
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
169-487 |
2.23e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 91.83 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 169 IEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVlDCHVRF---VMENDEKFRI-LSILPICHIlermvdyvfmyksYGI- 243
Cdd:PLN02574 195 IKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMV-ELFVRFeasQYEYPGSDNVyLAALPMFHI-------------YGLs 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 244 YFAEGMDKLASnfqevkpdvilvvpriveklyasiynkgtsggwlkkqiflwALSVAKKFEPFKPASLSH--KIADFLVF 321
Cdd:PLN02574 261 LFVVGLLSLGS-----------------------------------------TIVVMRRFDASDMVKVIDrfKVTHFPVV 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 322 --------KKWREAVGN---NLQLIICGSAALSENLCRIFNAA--GLKISEGYGMTETSPVITVNGRTKDLFCLGTVGPL 388
Cdd:PLN02574 300 ppilmaltKKAKGVCGEvlkSLKQVSCGAAPLSGKFIQDFVQTlpHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 389 LNSCKVKIAE-----------DGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTS 456
Cdd:PLN02574 380 APNMQAKVVDwstgcllppgnCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFdEDGYLYIVDRLKEIIKYK 459
|
330 340 350
....*....|....*....|....*....|.
gi 2537297151 457 GGKyIIPQITENNLKQSRFIGEAMVVGDGEK 487
Cdd:PLN02574 460 GFQ-IAPADLEAVLISHPEIIDAAVTAVPDK 489
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-573 |
2.51e-18 |
|
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: 87.87 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 28 DGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSES 107
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLS-QGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 108 KfCLVSDkkiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiEPDRWVTLIYTSGTTGRP 187
Cdd:cd05971 80 S-ALVTD-------------------------------------------------------GSDDPALIIYTSGTTGPP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 188 KGVMLSHKNILTNvldchvrfvmendekfriLSILPICHILERMVDYVFMYKS--------YGIYFAE---GMDKLASNF 256
Cdd:cd05971 104 KGALHAHRVLLGH------------------LPGVQFPFNLFPRDGDLYWTPAdwawigglLDVLLPSlyfGVPVLAHRM 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 257 QEVKPDVILVVpriveklyasiynkgtsggwlkkqifLWALSVAKKFEPfkPASLshKIADFLvfKKWREAVGNNLQLII 336
Cdd:cd05971 166 TKFDPKAALDL--------------------------MSRYGVTTAFLP--PTAL--KMMRQQ--GEQLKHAQVKLRAIA 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 337 CGSAALSENLCR-IFNAAGLKISEGYGMTETSPVItvnGRTKDLFCL--GTVGPLLNSCKVKIAED-GEILTKG------ 406
Cdd:cd05971 214 TGGESLGEELLGwAREQFGVEVNEFYGQTECNLVI---GNCSALFPIkpGSMGKPIPGHRVAIVDDnGTPLPPGevgeia 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 407 -----SNVFLGYYKDEEKTREIYTDDgWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAM 480
Cdd:cd05971 291 velpdPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKdSDGYFWYVGRDDDVITSSGYR-IGPAEIEECLLKHPAVLMAA 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 481 VVGdgekmpcaliQPD---FEFILKYIkyknlHMNTTISPEEIVKnKVIRERimqdvekVNKLLGKWEQIKKIELtptvw 557
Cdd:cd05971 369 VVG----------IPDpirGEIVKAFV-----VLNPGETPSDALA-REIQEL-------VKTRLAAHEYPREIEF----- 420
|
570
....*....|....*.
gi 2537297151 558 sVESGELTPTLKLKRK 573
Cdd:cd05971 421 -VNELPRTATGKIRRR 435
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
177-572 |
2.89e-18 |
|
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: 86.55 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 177 LIYTSGTTGRPKGVMLSHKNILTnVLDCHVRFVMENDEKFRILSILPICHILERMVDYVFMYKSYGIYFAEGMDKLASNF 256
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFA-VPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKSLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 257 QEV---KPDVILVVPRIVEKLYASIYNkgtsggwlkkqiflwALSVAKKfepfkpaslshkiadflvfkkwreavgnnLQ 333
Cdd:cd17635 85 KILttnAVTTTCLVPTLLSKLVSELKS---------------ANATVPS-----------------------------LR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 334 LIICGSAALSENLCRIFNAAGL-KISEGYGMTETSPVITVNgRTKDLFCLGTVGPLLNSCKVKI----------AEDGEI 402
Cdd:cd17635 121 LIGYGGSRAIAADVRFIEATGLtNTAQVYGLSETGTALCLP-TDDDSIEINAVGRPYPGVDVYLaatdgiagpsASFGTI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 403 LTKGSNVFLGYYKDEEKTREIYTdDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAmv 481
Cdd:cd17635 200 WIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERrEDGFLFITGRSSESI-NCGGVKIAPDEVERIAEGVSGVQEC-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 482 vgdgekmPCALIqPDFEFILKYIKYknlhmntTISPEEIVKNkvireRIMQDVEKVNKLLGKWEQIKKIELtptvwsVES 561
Cdd:cd17635 276 -------ACYEI-SDEEFGELVGLA-------VVASAELDEN-----AIRALKHTIRRELEPYARPSTIVI------VTD 329
|
410
....*....|.
gi 2537297151 562 GELTPTLKLKR 572
Cdd:cd17635 330 IPRTQSGKVKR 340
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
5-565 |
3.27e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 88.18 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 5 RLFDILYYQLRNRPIDVSIATKK--DGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIAlITSVNRSEWLIMDFAIQQI 82
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAQREpgHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVM-ILSGNSIEHALMTLAAMQA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 83 GAVSVPI---YPTMSDD--DLTFILNNSESKFCLVSDKKIYDK-VHNIKDQCPNITSLFTFDEIEGALNWNKI--KKKGE 154
Cdd:PRK12582 129 GVPAAPVspaYSLMSHDhaKLKHLFDLVKPRVVFAQSGAPFARaLAALDLLDVTVVHVTGPGEGIASIAFADLaaTPPTA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 155 EisnqqeVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNV-LDCHVRFVMENDEKFRILSILPICHILERMVD 233
Cdd:PRK12582 209 A------VAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIaMQEQLRPREPDPPPPVSLDWMPWNHTMGGNAN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 234 YVFMYKSYGIYF-------AEGMDKLASNFQEVKPDVILVVPriveklyasiynkgtsggwlkkqIFLWALSVAKKFEPF 306
Cdd:PRK12582 283 FNGLLWGGGTLYiddgkplPGMFEETIRNLREISPTVYGNVP-----------------------AGYAMLAEAMEKDDA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 307 KPASlshkiadflVFKkwreavgnNLQLIICGSAALSENLCRIFNAAGLK-------ISEGYGMTETSPVIT-VNGRTKD 378
Cdd:PRK12582 340 LRRS---------FFK--------NLRLMAYGGATLSDDLYERMQALAVRttghripFYTGYGATETAPTTTgTHWDTER 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 379 LfclGTVGPLLNSCKVKIAEDG---EILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIKD------GfLKITDRK 449
Cdd:PRK12582 403 V---GLIGLPLPGVELKLAPVGdkyEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVDpddpekG-LIFDGRV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 450 KEIFKTSGGKYI-IPQITENNLKQSR-FIGEAMVVGDGEKMPCALIQPDFEfilkyiKYKNLHMNTTISPEEIVKNKVIR 527
Cdd:PRK12582 479 AEDFKLSTGTWVsVGTLRPDAVAACSpVIHDAVVAGQDRAFIGLLAWPNPA------ACRQLAGDPDAAPEDVVKHPAVL 552
|
570 580 590
....*....|....*....|....*....|....*....
gi 2537297151 528 ERIMQDVEKVNKLLGKWE-QIKKIELTPTVWSVESGELT 565
Cdd:PRK12582 553 AILREGLSAHNAEAGGSSsRIARALLMTEPPSIDAGEIT 591
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
7-483 |
8.82e-18 |
|
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: 86.78 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 7 FDILYYQLRNRPIDVSIATKKD-GSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSVNRSEWLIMdFAIQQIGAV 85
Cdd:cd05970 20 YDVVDAMAKEYPDKLALVWCDDaGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSL-LALHKLGAI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 86 SVPIYPTMSDDDLTFILNNSESKFCLVSDKK-IYDKVHNIKDQCPNITSLFTF--DEIEGalnWnkikkkgeeISNQQEV 162
Cdd:cd05970 99 AIPATHQLTAKDIVYRIESADIKMIVAIAEDnIPEEIEKAAPECPSKPKLVWVgdPVPEG---W---------IDFRKLI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 163 ENLKNSIEP---------DRWVTLIYTSGTTGRPKgvMLSHKNILtnvldchvrfvmendekfrilsilPICHILErmvd 233
Cdd:cd05970 167 KNASPDFERptansypcgEDILLVYFSSGTTGMPK--MVEHDFTY------------------------PLGHIVT---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 234 yvfmyksygiyfaegmdklASNFQEVKPDVI-LVVPRI--VEKLYASIYnkgtsGGWLK-KQIFLWalsvakKFEPFKPA 309
Cdd:cd05970 217 -------------------AKYWQNVREGGLhLTVADTgwGKAVWGKIY-----GQWIAgAAVFVY------DYDKFDPK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 310 SLSHKIAD--------------FLVFKKWREAVGNNLQLIICGSAALSENLCRIFNAA-GLKISEGYGMTETspVITVN- 373
Cdd:cd05970 267 ALLEKLSKygvttfcapptiyrFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKtGIKLMEGFGQTET--TLTIAt 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 374 -----------GRTKDLFCLGTVGPLLNSCKVkiAEDGEILTKGSN-----VFLGYYKDEEKTREIYtDDGWLKTGDIGY 437
Cdd:cd05970 345 fpwmepkpgsmGKPAPGYEIDLIDREGRSCEA--GEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAW 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2537297151 438 I-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAMVVG 483
Cdd:cd05970 422 MdEDGYLWFVGRTDDLIKSSGYR-IGPFEVESALIQHPAVLECAVTG 467
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
28-457 |
1.26e-17 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 85.44 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 28 DGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITsvNRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSE 106
Cdd:cd17653 17 ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLS--DRSlEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 107 SKFCLVSDKkiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiePDRWVTLIYTSGTTGR 186
Cdd:cd17653 95 ATLLLTTDS-------------------------------------------------------PDDLAYIIFTSGSTGI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 187 PKGVMLSHKNILTNVLDCHVRF-VMENDEKFRILSILPICHILErmvdyVFMYKSYG--IYFAEGMDKLASNFQEVkpDV 263
Cdd:cd17653 120 PKGVMVPHRGVLNYVSQPPARLdVGPGSRVAQVLSIAFDACIGE-----IFSTLCNGgtLVLADPSDPFAHVARTV--DA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 264 ILVVPRIVEKLYASIYNKgtsggwLKKqIFLWALSVakkfepfkPASLShkiadflvfKKWREAVgnnlqliicgsaals 343
Cdd:cd17653 193 LMSTPSILSTLSPQDFPN------LKT-IFLGGEAV--------PPSLL---------DRWSPGR--------------- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 344 enlcRIFNAaglkisegYGMTETSPVITVNGRTKDLFClgTVG-PLLNS-C--------KVKIAEDGEILTKGSNVFLGY 413
Cdd:cd17653 234 ----RLYNA--------YGPTECTISSTMTELLPGQPV--TIGkPIPNStCyildadlqPVPEGVVGEICISGVQVARGY 299
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2537297151 414 YKDEEKT----REIYTDDGWL--KTGDIGYI-KDGFLKITDRKKEIFKTSG 457
Cdd:cd17653 300 LGNPALTaskfVPDPFWPGSRmyRTGDYGRWtEDGGLEFLGREDNQVKVRG 350
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
39-441 |
3.94e-17 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 83.85 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNY-GINPQDRIALitSVNRSEWLIMDF-AIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDkk 116
Cdd:TIGR01733 5 LDERANRLARHLRAAgGVGPGDRVAV--LLERSAELVVAIlAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 117 iydkvHNIKDQCPNITSLFTFDEIEGALNWNkikkkgeeiSNQQEVENLKNSiePDRWVTLIYTSGTTGRPKGVMLSHKN 196
Cdd:TIGR01733 81 -----ALASRLAGLVLPVILLDPLELAALDD---------APAPPPPDAPSG--PDDLAYVIYTSGSTGRPKGVVVTHRS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 197 ILTNVLDCHVRFVMENDEkfRILSILPICHilermvdyvfmyksygiyfaegmdklasnfqevkpDVilvvprIVEKLYA 276
Cdd:TIGR01733 145 LVNLLAWLARRYGLDPDD--RVLQFASLSF-----------------------------------DA------SVEEIFG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 277 SIYNKGT----SGGWLKKQIFLWALSVAKkfepfkpaslsHKI-------ADFLVFKKWREAVGNNLQLIICGSAALSEN 345
Cdd:TIGR01733 182 ALLAGATlvvpPEDEERDDAALLAALIAE-----------HPVtvlnltpSLLALLAAALPPALASLRLVILGGEALTPA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 346 LCRIFNAA--GLKISEGYGMTETSPVITVNGRTKD------LFCLGTvgPLLNS---------CKVKIAEDGEILTKGSN 408
Cdd:TIGR01733 251 LVDRWRARgpGARLINLYGPTETTVWSTATLVDPDdapresPVPIGR--PLANTrlyvldddlRPVPVGVVGELYIGGPG 328
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2537297151 409 VFLGYYKDEEKTREIYTDDG--------WLKTGDIG-YIKDG 441
Cdd:TIGR01733 329 VARGYLNRPELTAERFVPDPfaggdgarLYRTGDLVrYLPDG 370
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
334-483 |
5.18e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 83.89 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 334 LIICGSAALSENLC-RIFNAAGLKISEGYGMTETspVITVNGRTKDLFCLGTVGPLLNSCKVKIAED------------G 400
Cdd:PRK07787 245 LLVSGSAALPVPVFdRLAALTGHRPVERYGMTET--LITLSTRADGERRPGWVGLPLAGVETRLVDEdggpvphdgetvG 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 401 EILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIK-DGFLKITDRKKEIFKTSGGKYIIPQITENNLKQSRFIGEA 479
Cdd:PRK07787 323 ELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDpDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREA 402
|
....
gi 2537297151 480 MVVG 483
Cdd:PRK07787 403 AVVG 406
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
29-495 |
6.80e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 83.59 E-value: 6.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 29 GSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESK 108
Cdd:PRK13391 20 STGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFME-NNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 109 FCLVSDKKiYDKVHNIKDQCPNITSLFTFDEiEGALnwnkikkkgEEISNQQE-VENLKNSIEPDRW--VTLIYTSGTTG 185
Cdd:PRK13391 99 ALITSAAK-LDVARALLKQCPGVRHRLVLDG-DGEL---------EGFVGYAEaVAGLPATPIADESlgTDMLYSSGTTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 186 RPKGVM--LSHKNILTNvldchvrfvmendekfrilsiLPICHILERMVDYvfmyksygiyfaegmdklasnfqevKPDV 263
Cdd:PRK13391 168 RPKGIKrpLPEQPPDTP---------------------LPLTAFLQRLWGF-------------------------RSDM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 264 ILVVPriveklyASIYNKGTSGGWLKKQIFLWALSVAKKFEPFKPASL--SHKI-------ADFLVFKKWREAVGN---- 330
Cdd:PRK13391 202 VYLSP-------APLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALieEYGVthtqlvpTMFSRMLKLPEEVRDkydl 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 331 -NLQLIICGSAAlsenlC------RIFNAAGLKISEGYGMTETSPVITVNGRtKDLFCLGTVG-PLLNscKVKIAED--- 399
Cdd:PRK13391 275 sSLEVAIHAAAP-----CppqvkeQMIDWWGPIIHEYYAATEGLGFTACDSE-EWLAHPGTVGrAMFG--DLHILDDdga 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 400 -------GEILTKGSNVFlGYYKDEEKTREIYTDDG-WLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNL 470
Cdd:PRK13391 347 elppgepGTIWFEGGRPF-EYLNDPAKTAEARHPDGtWSTVGDIGYVdEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLL 424
|
490 500 510
....*....|....*....|....*....|
gi 2537297151 471 KQSRFIGEAMVVGD-----GEKMPcALIQP 495
Cdd:PRK13391 425 ITHPKVADAAVFGVpnedlGEEVK-AVVQP 453
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
33-505 |
1.30e-16 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 82.76 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 33 KISTQSLIDQVNQVSRGLLNYGINPqDRIALITsVNRSEWLIMD-FAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcL 111
Cdd:cd17655 22 TLTYRELNERANQLARTLREKGVGP-DTIVGIM-AERSLEMIVGiLGILKAGGAYLPIDPDYPEERIQYILEDSGADI-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VSDKKIYDKVHNIKDqcpnitslftfdeiegalnwnkIKKKGEEISNQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVM 191
Cdd:cd17655 99 LTQSHLQPPIAFIGL----------------------IDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 192 LSHKNiLTNVLDCHVRfVMENDEKFRILSILPIchILERMVDYVFMYKSYG----IYFAEGM---DKLASNFQEVKPDVI 264
Cdd:cd17655 157 IEHRG-VVNLVEWANK-VIYQGEHLRVALFASI--SFDASVTEIFASLLSGntlyIVRKETVldgQALTQYIRQNRITII 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 265 LVVPRIVEKLyasIYNKGTSGGWLKKqiflwaLSVAKKfepfkpaSLSHKIAdflvfKKWREAVGNNlqliicgsaalse 344
Cdd:cd17655 233 DLTPAHLKLL---DAADDSEGLSLKH------LIVGGE-------ALSTELA-----KKIIELFGTN------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 345 nlCRIFNAaglkisegYGMTET-----SPVITVNGRTKDLFCLGTvgPLLNScKVKIAED----------GEILTKGSNV 409
Cdd:cd17655 279 --PTITNA--------YGPTETtvdasIYQYEPETDQQVSVPIGK--PLGNT-RIYILDQygrpqpvgvaGELYIGGEGV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 410 FLGYYKDEEKTREIYTDDGWL------KTGDIG-YIKDGFLKITDRKKEIFKTSGGKYIIPQItENNLKQSRFIGEAMVV 482
Cdd:cd17655 346 ARGYLNRPELTAEKFVDDPFVpgermyRTGDLArWLPDGNIEFLGRIDHQVKIRGYRIELGEI-EARLLQHPDIKEAVVI 424
|
490 500
....*....|....*....|....*..
gi 2537297151 483 G----DGEKMPCALIQPDFEFILKYIK 505
Cdd:cd17655 425 ArkdeQGQNYLCAYIVSEKELPVAQLR 451
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
177-483 |
1.43e-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: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 177 LIYTSGTTGRPKGVMLSHKNILTNVLdcHVRFVMENDEKFRILSILPICHILermvdyvfmyksygiyfaeGMDKLASNF 256
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANL--QLIHAMGLTEADVYLNMLPLFHIA-------------------GLNLALATF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 257 QevkpdvilvvpriveklyasiynkgtSGGwlkKQIflwalsVAKKFEPFKPASL--SHKIADFLVFKKwreAVGNNLQL 334
Cdd:cd17637 64 H--------------------------AGG---ANV------VMEKFDPAEALELieEEKVTLMGSFPP---ILSNLLDA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 335 IICGSAALS-----------ENLCRIFNAAGLKISEGYGMTETSPVITVNGRTKDLFCLGTVGPLlnsCKVKIAED---- 399
Cdd:cd17637 106 AEKSGVDLSslrhvlgldapETIQRFEETTGATFWSLYGQTETSGLVTLSPYRERPGSAGRPGPL---VRVRIVDDndrp 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 400 ------GEILTKGSNVFLGYYKDEEKTReiYT-DDGWLKTGDIGYI-KDGFLKITDRK--KEIFKTsGGKYIIPQITENN 469
Cdd:cd17637 183 vpagetGEIVVRGPLVFQGYWNLPELTA--YTfRNGWHHTGDLGRFdEDGYLWYAGRKpeKELIKP-GGENVYPAEVEKV 259
|
330
....*....|....
gi 2537297151 470 LKQSRFIGEAMVVG 483
Cdd:cd17637 260 ILEHPAIAEVCVIG 273
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
45-461 |
2.74e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 82.06 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 45 QVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcLVSDKKIYDKVHNI 124
Cdd:PRK07008 51 QLAQALAALGVEPGDRVGTL-AWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRY-VLFDLTFLPLVDAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 125 KDQCPNI----------------TSLFTFDEI----EGALNWNKIKkkgeeisnqqevENLKNSiepdrwvtLIYTSGTT 184
Cdd:PRK07008 129 APQCPNVkgwvamtdaahlpagsTPLLCYETLvgaqDGDYDWPRFD------------ENQASS--------LCYTSGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 185 GRPKGVMLSHKNI--------LTNVLDCHVRFVmendekfrILSILPICHIlermvdyvfmyKSYGIYFAEGMdklasnf 256
Cdd:PRK07008 189 GNPKGALYSHRSTvlhaygaaLPDAMGLSARDA--------VLPVVPMFHV-----------NAWGLPYSAPL------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 257 qeVKPDVILVVPRIVEK-LYASIYNKG--TSGG----WLkkqiflwalsvakkfepfkpASLSHKIADFLVFKKWREAVg 329
Cdd:PRK07008 243 --TGAKLVLPGPDLDGKsLYELIEAERvtFSAGvptvWL--------------------GLLNHMREAGLRFSTLRRTV- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 330 nnlqliICGSAAlSENLCRIFNAA-GLKISEGYGMTETSPVITV-------NGRTKD--LFCLGTVGPLLNSCKVKIAED 399
Cdd:PRK07008 300 ------IGGSAC-PPAMIRTFEDEyGVEVIHAWGMTEMSPLGTLcklkwkhSQLPLDeqRKLLEKQGRVIYGVDMKIVGD 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2537297151 400 ------------GEILTKGSNVFLGYYKDEEKTreiyTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKtSGGKYI 461
Cdd:PRK07008 373 dgrelpwdgkafGDLQVRGPWVIDRYFRGDASP----LVDGWFPTGDVATIdADGFMQITDRSKDVIK-SGGEWI 442
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
50-495 |
6.55e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 80.86 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 50 LLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDKkIYDKVHNIKDQC- 128
Cdd:PRK06178 75 LRQRGVGAGDRVAVFLP-NCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQ-LAPVVEQVRAETs 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 129 -------------PNITSLFTFDEIEGAlnwnKIKKKG-----EEISNQQeVENLKNSIEPDRWVTLIYTSGTTGRPKGV 190
Cdd:PRK06178 153 lrhvivtsladvlPAEPTLPLPDSLRAP----RLAAAGaidllPALRACT-APVPLPPPALDALAALNYTGGTTGMPKGC 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 191 MLSHKN-ILTNVLDCHVRFVMENDEKFriLSILPICHI-------------------LERMVDYVFM--YKSYGIYFAEG 248
Cdd:PRK06178 228 EHTQRDmVYTAAAAYAVAVVGGEDSVF--LSFLPEFWIagenfgllfplfsgatlvlLARWDAVAFMaaVERYRVTRTVM 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 249 mdkLASNFQEvkpdvILVVPRIVEKLYASIYNKGtsggwlkkqiflwALSVAKKFEPfkpaslshkiaDFLvfKKWREAV 328
Cdd:PRK06178 306 ---LVDNAVE-----LMDHPRFAEYDLSSLRQVR-------------VVSFVKKLNP-----------DYR--QRWRALT 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 329 GnnlqliicgsaalsenlCRIFNAAglkisegYGMTET--SPVITVNGRTKDL-------FC-LGTVGPLLNSCK----- 393
Cdd:PRK06178 352 G-----------------SVLAEAA-------WGMTEThtCDTFTAGFQDDDFdllsqpvFVgLPVPGTEFKICDfetge 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 394 -VKIAEDGEILTKGSNVFLGYYKDEEKTREIYTDdGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLK 471
Cdd:PRK06178 408 lLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD-GWLHTGDIGKIdEQGFLHYLGRRKEMLKVNGMS-VFPSEVEALLG 485
|
490 500
....*....|....*....|....*...
gi 2537297151 472 QSRFIGEAMVVG--DGEK--MPCALIQP 495
Cdd:PRK06178 486 QHPAVLGSAVVGrpDPDKgqVPVAFVQL 513
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
39-483 |
1.24e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 79.93 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKfCLVSDKKIY 118
Cdd:PRK07798 34 LEERANRLAHYLIAQGLGPGDHVGIY-ARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAV-ALVYEREFA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 119 DKVHNIKDQCPNitsLFTFDEIE---------GALNWnkikkkgEEISNQQEVENLKNSIEPDRwVTLIYTSGTTGRPKG 189
Cdd:PRK07798 112 PRVAEVLPRLPK---LRTLVVVEdgsgndllpGAVDY-------EDALAAGSPERDFGERSPDD-LYLLYTGGTTGMPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 190 VMLSHKNI--------------LTNVLDCHVRFVMENDEkFRILSILPICHilermvdYVFMYKSYGIYFAEGMDKLASN 255
Cdd:PRK07798 181 VMWRQEDIfrvllggrdfatgePIEDEEELAKRAAAGPG-MRRFPAPPLMH-------GAGQWAAFAALFSGQTVVLLPD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 256 fQEVKPDVILvvpRIVEKlyasiyNKGTSggwlkkqIFL----WALSVAKKFEPFKPASLShkiadflvfkkwreavgnN 331
Cdd:PRK07798 253 -VRFDADEVW---RTIER------EKVNV-------ITIvgdaMARPLLDALEARGPYDLS------------------S 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 332 LQLIICGSAALSENLCRIFNAA--GLKISEGYGMTET---SPVITVNGRTKDLFCLGTVGPllnSCKVkIAEDGEILTKG 406
Cdd:PRK07798 298 LFAIASGGALFSPSVKEALLELlpNVVLTDSIGSSETgfgGSGTVAKGAVHTGGPRFTIGP---RTVV-LDEDGNPVEPG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 407 S----------NVFLGYYKDEEKTREIY-TDDG--WLKTGDIGYI-KDGFLKITDRKKEIFKTsGGKYIIPQITENNLKQ 472
Cdd:PRK07798 374 SgeigwiarrgHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVeADGTITLLGRGSVCINT-GGEKVFPEEVEEALKA 452
|
490
....*....|.
gi 2537297151 473 SRFIGEAMVVG 483
Cdd:PRK07798 453 HPDVADALVVG 463
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
39-498 |
2.01e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 79.18 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKfCLVSDKKIY 118
Cdd:PRK08276 17 LEARSNRLAHGLRALGLREGDVVAILLE-NNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAK-VLIVSAALA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 119 DKVHNIKDQCPNITSLFTFD--EIEGALNWnkikkkgEEISNQQEVENLKNsiEPDRWvTLIYTSGTTGRPKGvmlshkn 196
Cdd:PRK08276 95 DTAAELAAELPAGVPLLLVVagPVPGFRSY-------EEALAAQPDTPIAD--ETAGA-DMLYSSGTTGRPKG------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 197 iltnvldchvrfvmendekfrILSILPICHILERMVDYVFMyksygiyFAEGMDklasnfqeVKPDVILVVPriveklyA 276
Cdd:PRK08276 158 ---------------------IKRPLPGLDPDEAPGMMLAL-------LGFGMY--------GGPDSVYLSP-------A 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 277 SIYNKGTSggwlkkqifLWALSVAK---------KFEPFKPASL--SHKIAD-------FLVFKKWREAVGN-----NLQ 333
Cdd:PRK08276 195 PLYHTAPL---------RFGMSALAlggtvvvmeKFDAEEALALieRYRVTHsqlvptmFVRMLKLPEEVRArydvsSLR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 334 LIICGSAAlsenlC------RIFNAAGLKISEGYGMTETSPVITVNGR---TKDlfclGTVG-PLLnsCKVKI-AEDGEI 402
Cdd:PRK08276 266 VAIHAAAP-----CpvevkrAMIDWWGPIIHEYYASSEGGGVTVITSEdwlAHP----GSVGkAVL--GEVRIlDEDGNE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 403 LTKGS--NVFL-------GYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQ 472
Cdd:PRK08276 335 LPPGEigTVYFemdgypfEYHNDPEKTAAARNPHGWVTVGDVGYLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVT 413
|
490 500 510
....*....|....*....|....*....|....*...
gi 2537297151 473 SRFIGEAMVVG--D---GEK-------MPCALIQPDFE 498
Cdd:PRK08276 414 HPKVADVAVFGvpDeemGERvkavvqpADGADAGDALA 451
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
39-225 |
2.16e-15 |
|
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: 79.90 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALitSVNRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKfCLVSDKKI 117
Cdd:COG1020 507 LNARANRLAHHLRALGVGPGDLVGV--CLERSlEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGAR-LVLTQSAL 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 118 YDKVHNIKDQCpnitslFTFDEIEGAlnwnkikkkgeeisnQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNI 197
Cdd:COG1020 584 AARLPELGVPV------LALDALALA---------------AEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL 642
|
170 180
....*....|....*....|....*...
gi 2537297151 198 LTNVLDCHVRFVMENDEkfRILSILPIC 225
Cdd:COG1020 643 VNLLAWMQRRYGLGPGD--RVLQFASLS 668
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
168-453 |
3.22e-15 |
|
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: 78.43 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 168 SIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDCHVRFvmENDEKFRILSILPICHILErMVDYVF--MYKSYGIYF 245
Cdd:cd05931 145 SPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAY--GLDPGDVVVSWLPLYHDMG-LIGGLLtpLYSGGPSVL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 246 AEGMDKLAsnfqevKPdvilvvpriveklyasiynkgtsGGWLKkQI------------FLWALsVAKKFEPFKPAS--L 311
Cdd:cd05931 222 MSPAAFLR------RP-----------------------LRWLR-LIsryratisaapnFAYDL-CVRRVRDEDLEGldL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 312 SHkiadflvfkkWReavgnnlqLIICGS----AALSENLCRIFNAAGLK---ISEGYGMTE-----------TSPVIT-- 371
Cdd:cd05931 271 SS----------WR--------VALNGAepvrPATLRRFAEAFAPFGFRpeaFRPSYGLAEatlfvsggppgTGPVVLrv 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 372 -----------VNGRTKDLFCLGTVGPLLNSCKVKIAED-----------GEILTKGSNVFLGYYKDEEKTREIY----- 424
Cdd:cd05931 333 drdalagravaVAADDPAARELVSCGRPLPDQEVRIVDPetgrelpdgevGEIWVRGPSVASGYWGRPEATAETFgalaa 412
|
330 340 350
....*....|....*....|....*....|
gi 2537297151 425 -TDDGWLKTGDIGYIKDGFLKITDRKKEIF 453
Cdd:cd05931 413 tDEGGWLRTGDLGFLHDGELYITGRLKDLI 442
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
33-491 |
3.46e-15 |
|
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: 78.28 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 33 KISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvnRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCL 111
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSIVAIMME--RSaEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VsdkkiydkvhnikdqCPNITSLFTFDEIEGALNWNKIkkkgeeisNQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVM 191
Cdd:cd17656 91 T---------------QRHLKSKLSFNKSTILLEDPSI--------SQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 192 LSHKNIlTNVLDcHVRFVMENDEKFRILSilpichilermvdyvFMYKSYGIYFAEGMDKLASNFQevkpdvILVVP--- 268
Cdd:cd17656 148 LEHKNM-VNLLH-FEREKTNINFSDKVLQ---------------FATCSFDVCYQEIFSTLLSGGT------LYIIReet 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 269 -RIVEKLYASIYNKGTSGGWLK----KQIFlwalSVAKKFEPFkPASLSHKIadflvfkkwreAVGNnlQLIIcgsaalS 343
Cdd:cd17656 205 kRDVEQLFDLVKRHNIEVVFLPvaflKFIF----SEREFINRF-PTCVKHII-----------TAGE--QLVI------T 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 344 ENLCRIFNAAGLKISEGYGMTETSPVITVNGRTKDLF-CLGTVGP--------LLNSCK--VKIAEDGEILTKGSNVFLG 412
Cdd:cd17656 261 NEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIpELPPIGKpisntwiyILDQEQqlQPQGIVGELYISGASVARG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 413 YYKDEEKTREIYTDDGW------LKTGDIG-YIKDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAMVV--- 482
Cdd:cd17656 341 YLNRQELTAEKFFPDPFdpnermYRTGDLArYLPDGNIEFLGRADHQVKIRGYR-IELGEIEAQLLNHPGVSEAVVLdka 419
|
490
....*....|
gi 2537297151 483 -GDGEKMPCA 491
Cdd:cd17656 420 dDKGEKYLCA 429
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
33-483 |
4.02e-15 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 77.93 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 33 KISTQSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLV 112
Cdd:cd05923 28 RLTYSELRARIEAVAARLHARGLRPGQRVAVV-LPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 113 SDkkiydkvhnIKDQCPNITSLFTFDEIEGALNwnkikKKGEEISNQQEVENLKNSIEPDRWVtlIYTSGTTGRPKGVML 192
Cdd:cd05923 107 AV---------DAQVMDAIFQSGVRVLALSDLV-----GLGEPESAGPLIEDPPREPEQPAFV--FYTSGTTGLPKGAVI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 193 SHKNILTNVL----DCHVRFVMENdekfRILSILPICHILERMVDYVFMYKSYGIYFAEGMDKLASNFQevkpdviLVVP 268
Cdd:cd05923 171 PQRAAESRVLfmstQAGLRHGRHN----VVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALK-------LIEQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 269 RIVEKLYASiynkgtsggwlkkQIFLWALSVAKKFEPFKPASLSHkiadflvfkkwreavgnnlqLIICGSAALSENLCR 348
Cdd:cd05923 240 ERVTSLFAT-------------PTHLDALAAAAEFAGLKLSSLRH--------------------VTFAGATMPDAVLER 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 349 IFNAAGLKISEGYGMTET-SPVITVNGRTkdlfclGTVG-PLLNScKVKIA-------------EDGEILTK--GSNVFL 411
Cdd:cd05923 287 VNQHLPGEKVNIYGTTEAmNSLYMRDART------GTEMrPGFFS-EVRIVriggspdealangEEGELIVAaaADAAFT 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2537297151 412 GYYKDEEKTREiYTDDGWLKTGDIGYIK-DGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG 483
Cdd:cd05923 360 GYLNQPEATAK-KLQDGWYRTGDVGYVDpSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
37-540 |
9.06e-15 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 76.77 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 37 QSLIDQVNQVSRGLLNYGINPQDRIALITSVNRSEWLIMdFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSdkk 116
Cdd:cd05969 4 AQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSM-LGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 117 iydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKN 196
Cdd:cd05969 80 ----------------------------------------------EELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 197 ILTNVLDCHVRFVMENDEKFRILS------------ILPICHILERMVDYvfmyksyGIYFAEgmdKLASNFQEVKPDVI 264
Cdd:cd05969 114 MIFYYFTGKYVLDLHPDDIYWCTAdpgwvtgtvygiWAPWLNGVTNVVYE-------GRFDAE---SWYGIIERVKVTVW 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 265 LVVPRIVEKLYASiynkgtsGGWLKKQIFLWALSVAKKF-EPFKPASLshkiadflvfkKWREavgnnlqliicgsaals 343
Cdd:cd05969 184 YTAPTAIRMLMKE-------GDELARKYDLSSLRFIHSVgEPLNPEAI-----------RWGM----------------- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 344 enlcrifNAAGLKISEGYGMTETSPVITVNGRTKDLfCLGTVG-PLLNSCKVKIAEDGEILTKGS-----------NVFL 411
Cdd:cd05969 229 -------EVFGVPIHDTWWQTETGSIMIANYPCMPI-KPGSMGkPLPGVKAAVVDENGNELPPGTkgilalkpgwpSMFR 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 412 GYYKDEEKTREiYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAMVVGD-----G 485
Cdd:cd05969 301 GIWNDEERYKN-SFIDGWYLTGDLAYRdEDGYFWFVGRADDIIKTSGHR-VGPFEVESALMEHPAVAEAGVIGKpdplrG 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2537297151 486 EkMPCALI--QPDFE-------FILKYIKYknlHMNTTISPEEI--VKN--KVIRERIMQDVEKVNKL 540
Cdd:cd05969 379 E-IIKAFIslKEGFEpsdelkeEIINFVRQ---KLGAHVAPREIefVDNlpKTRSGKIMRRVLKAKEL 442
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
28-434 |
1.84e-14 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 76.46 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 28 DGSWKKISTQSLIDQVNQVSRGLLNYGInPQDRIALITSVNRSEWLIMDFAIQQIGAVSVPI---YPTMSDD--DLTFIL 102
Cdd:PRK08180 64 DGGWRRLTYAEALERVRAIAQALLDRGL-SAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSQDfgKLRHVL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 103 NNSESKFCLVSDKKIYDK--------------VHNIkDQCPNITSlftFDEIEGAlnwnkikkkgeeiSNQQEVENLKNS 168
Cdd:PRK08180 143 ELLTPGLVFADDGAAFARalaavvpadvevvaVRGA-VPGRAATP---FAALLAT-------------PPTAAVDAAHAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 169 IEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDCHVRFVMENDEKFRILSILPICHilermvdyVF------------ 236
Cdd:PRK08180 206 VGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVDWLPWNH--------TFggnhnlgivlyn 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 237 ---MYKSYGIYFAEGMDKLASNFQEVKPDVILVVPRiveklyasiynkgtsgGW------------LKKQIFlwalSVAK 301
Cdd:PRK08180 278 ggtLYIDDGKPTPGGFDETLRNLREISPTVYFNVPK----------------GWemlvpalerdaaLRRRFF----SRLK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 302 KFEpFKPASLSHKIADFLvfkkwreavgnnlqliicgsAALSENLC--RIFnaaglkISEGYGMTETSPVIT-VNGRTKD 378
Cdd:PRK08180 338 LLF-YAGAALSQDVWDRL--------------------DRVAEATCgeRIR------MMTGLGMTETAPSATfTTGPLSR 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2537297151 379 LFCLGTVGPllnSCKVKIAEDG---EILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGD 434
Cdd:PRK08180 391 AGNIGLPAP---GCEVKLVPVGgklEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGD 446
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
41-500 |
1.86e-14 |
|
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: 75.58 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 41 DQVNQVSRGLLNYGINPQDRIALITsVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDKKIydk 120
Cdd:cd05919 18 DGANRLGSALRNLGVSSGDRVLLLM-LDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSADDI--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 121 vhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiepdrwVTLIYTSGTTGRPKGVMLSHKNILTN 200
Cdd:cd05919 94 ------------------------------------------------------AYLLYSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 201 VlDCHVRFVMENDEKFRILSIlpichilERMvdyvfmyksygiYFAEGM-----------------------DKLASNFQ 257
Cdd:cd05919 120 A-DAMAREALGLTPGDRVFSS-------AKM------------FFGYGLgnslwfplavgasavlnpgwptaERVLATLA 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 258 EVKPDVILVVPRIveklYASIYNKGTsggwlkkqiflwalsvakkfepFKPASLShkiadflvfkkwreavgnNLQLIIC 337
Cdd:cd05919 180 RFRPTVLYGVPTF----YANLLDSCA----------------------GSPDALR------------------SLRLCVS 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 338 GSAALSENLCRIFNAA-GLKISEGYGMTETSPVITVNgrTKDLFCLGTVGPLLNSCKVKIAED----------GEILTKG 406
Cdd:cd05919 216 AGEALPRGLGERWMEHfGGPILDGIGATEVGHIFLSN--RPGAWRLGSTGRPVPGYEIRLVDEeghtippgeeGDLLVRG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 407 SNVFLGYYKDEEKTREIYTdDGWLKTGDIGYI-KDGFLKITDRKKEIFKTsGGKYIIPQITENNLKQSRFIGEAMVVG-- 483
Cdd:cd05919 294 PSAAVGYWNNPEKSRATFN-GGWYRTGDKFCRdADGWYTHAGRADDMLKV-GGQWVSPVEVESLIIQHPAVAEAAVVAvp 371
|
490
....*....|....*....
gi 2537297151 484 --DGEKMPCALIQPDFEFI 500
Cdd:cd05919 372 esTGLSRLTAFVVLKSPAA 390
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
39-505 |
2.34e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 75.89 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDkkiy 118
Cdd:PRK12406 17 LAQRAARAAGGLAALGVRPGDCVALLMR-NDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 119 DKVHNIKDQCP---NITSLFTFDEI--------------EGALNWnkikkkgEEISNQQEVENLKNSIEPDrwvTLIYTS 181
Cdd:PRK12406 92 DLLHGLASALPagvTVLSVPTPPEIaaayrispalltppAGAIDW-------EGWLAQQEPYDGPPVPQPQ---SMIYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 182 GTTGRPKGVMlshkniltnvldchvRF--VMENDEKFrilsilpichilERMVDYVfmyksYGIyfaegmdklasnfqev 259
Cdd:PRK12406 162 GTTGHPKGVR---------------RAapTPEQAAAA------------EQMRALI-----YGL---------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 260 KPDVILVVPrivEKLYASIYN-----KGTSGGwlkkqiflwALSVAKKFEPFKPASL--SHKIAD-------FLVFKKWR 325
Cdd:PRK12406 194 KPGIRALLT---GPLYHSAPNayglrAGRLGG---------VLVLQPRFDPEELLQLieRHRITHmhmvptmFIRLLKLP 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 326 EAVGN-----NLQLIICGSAALSENLCR-IFNAAGLKISEGYGMTETSpVITVNGRTKDLFCLGTVGPLLNSCKVK-IAE 398
Cdd:PRK12406 262 EEVRAkydvsSLRHVIHAAAPCPADVKRaMIEWWGPVIYEYYGSTESG-AVTFATSEDALSHPGTVGKAAPGAELRfVDE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 399 DGEILTKGS----------NVFLGYYKDEEKTREIyTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITE 467
Cdd:PRK12406 341 DGRPLPQGEigeiysriagNPDFTYHNKPEKRAEI-DRGGFITSGDVGYLdADGYLFLCDRKRDMV-ISGGVNIYPAEIE 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2537297151 468 NNLKQSRFIGEAMVVG--D---GEKMpCALIQP------DFEFILKYIK 505
Cdd:PRK12406 419 AVLHAVPGVHDCAVFGipDaefGEAL-MAVVEPqpgatlDEADIRAQLK 466
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
30-483 |
3.24e-14 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 74.82 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 30 SWKKISTQSLIDQVNQVSRGLLnyGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKF 109
Cdd:cd05958 10 EWTYRDLLALANRIANVLVGEL--GIVPGNRVLLRGS-NSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 110 CLVSDKkiydkvhnikdqcpnitsLFTFDEIegalnwnkikkkgeeisnqqevenlknsiepdrwVTLIYTSGTTGRPKG 189
Cdd:cd05958 87 ALCAHA------------------LTASDDI----------------------------------CILAFTSGTTGAPKA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 190 VMLSHKNILTnVLDCHVRFVMENDEKFRILSILPICHILERMVDYVFMYK--SYGIYFAEGM-DKLASNFQEVKPDVILV 266
Cdd:cd05958 115 TMHFHRDPLA-SADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGvgASGVLLEEATpDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 267 VPRIVEKLYASIYNKGTSGGWLKKqiflwALSVAKKFepfkPASLshkiadflvFKKWREAVGNNlqlIICGSAAlSENL 346
Cdd:cd05958 194 APTAYRAMLAHPDAAGPDLSSLRK-----CVSAGEAL----PAAL---------HRAWKEATGIP---IIDGIGS-TEMF 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 347 cRIF----------NAAGlKISEGYgmteTSPVITVNGRTKDLfclGTVGPLLnsckvkiaedgeilTKGSNvflGYYKD 416
Cdd:cd05958 252 -HIFisarpgdarpGATG-KPVPGY----EAKVVDDEGNPVPD---GTIGRLA--------------VRGPT---GCRYL 305
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2537297151 417 EEKTREIYTDDGWLKTGDIGYIK-DGFLKITDRKKEIFKtSGGKYIIPQITENNLKQSRFIGEAMVVG 483
Cdd:cd05958 306 ADKRQRTYVQGGWNITGDTYSRDpDGYFRHQGRSDDMIV-SGGYNIAPPEVEDVLLQHPAVAECAVVG 372
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
39-483 |
5.75e-14 |
|
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: 74.30 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKfCLVSDKkiy 118
Cdd:cd05972 6 LKRESAKAANVLAKLGLRKGDRVAVLLP-RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAK-AIVTDA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 119 dkvhnikdqcpnitslftfdeiegalnwnkikkkgEEISnqqevenlknsiepdrwvTLIYTSGTTGRPKGVMLSHKnil 198
Cdd:cd05972 81 -----------------------------------EDPA------------------LIYFTSGTTGLPKGVLHTHS--- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 199 tnvldchvrfvmendekfrilsiLPICHILErmvdyvfmyksygiyfaegmdklASNFQEVKPDvilvvpriveKLYASI 278
Cdd:cd05972 105 -----------------------YPLGHIPT-----------------------AAYWLGLRPD----------DIHWNI 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 279 YNKGTSGGWLKKQIFLWALSVA------KKFEPFKPASL--SHKIADFL----VFKKWREA-----VGNNLQLIICGSAA 341
Cdd:cd05972 129 ADPGWAKGAWSSFFGPWLLGATvfvyegPRFDAERILELleRYGVTSFCgpptAYRMLIKQdlssyKFSHLRLVVSAGEP 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 342 LSENLCRIFNAA-GLKISEGYGMTETspVITVNgrtkDLFCL----GTVGPLLNSCKVKIA----------EDGEILTKG 406
Cdd:cd05972 209 LNPEVIEWWRAAtGLPIRDGYGQTET--GLTVG----NFPDMpvkpGSMGRPTPGYDVAIIdddgrelppgEEGDIAIKL 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 407 SNV--FLGYYKDEEKTREIYTDDgWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAMVVG 483
Cdd:cd05972 283 PPPglFLGYVGDPEKTEASIRGD-YYLTGDRAYRdEDGYFWFVGRADDIIKSSGYR-IGPFEVESALLEHPAVAEAAVVG 360
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
5-488 |
2.22e-13 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 72.61 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 5 RLFDILYYQLRNRPIDVSIATKKDGSwkKISTQSLIDQVNQVSRGLLNYGINPQDRIALItSVNRSEWLIMDFAIQQIGA 84
Cdd:PRK05852 17 RIADLVEVAATRLPEAPALVVTADRI--AISYRDLARLVDDLAGQLTRSGLLPGDRVALR-MGSNAEFVVALLAASRADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 85 VSVPIYPTMSDDDLTFILNNSESKFCLVSDKKIYDKVHNIKDQCPNITSLFTFDEIEGALNWNKIKKKGEEISNQQEVEN 164
Cdd:PRK05852 94 VVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 165 LKnsiePDRwVTLIYTSGTTGRPKGVMLSHKNILTNVLdchvrfvmendekfrilSILPICHILERMVDYVFM--YKSYG 242
Cdd:PRK05852 174 LR----PDD-AMIMFTGGTTGLPKMVPWTHANIASSVR-----------------AIITGYRLSPRDATVAVMplYHGHG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 243 IyFAEGMDKLASNfqevkpDVILVVPRiveklyasiynkgtsgGWLKKQIFlWALSVAKKFEPFKPASLSHKI----ADF 318
Cdd:PRK05852 232 L-IAALLATLASG------GAVLLPAR----------------GRFSAHTF-WDDIKAVGATWYTAVPTIHQIllerAAT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 319 LVFKKWREAvgnnLQLIICGSAAL----SENLCRIFNAAGLkisEGYGMTETSPVIT---VNGRTKDLFCLGTVGPLLNS 391
Cdd:PRK05852 288 EPSGRKPAA----LRFIRSCSAPLtaetAQALQTEFAAPVV---CAFGMTEATHQVTttqIEGIGQTENPVVSTGLVGRS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 392 CKVKI------------AEDGEILTKGSNVFLGYYKDEEKTREIYTDdGWLKTGDIGYIK-DGFLKITDRKKEIFKTSGG 458
Cdd:PRK05852 361 TGAQIrivgsdglplpaGAVGEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSaAGDLSIRGRIKELINRGGE 439
|
490 500 510
....*....|....*....|....*....|
gi 2537297151 459 KyIIPQITENNLKQSRFIGEAMVVGDGEKM 488
Cdd:PRK05852 440 K-ISPERVEGVLASHPNVMEAAVFGVPDQL 468
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
28-483 |
2.55e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 72.38 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 28 DGSWkkisTQSLID-QVNQVSRGLLNYGINPQDRIaLITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSE 106
Cdd:PRK07470 30 DRSW----TWREIDaRVDALAAALAARGVRKGDRI-LVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 107 SKFCLVsDKKIYDKVHNIKDQCPNITSLFTFDEIEGALNWNKIKKK--GEEISNQQevenlknsIEPDRWVTLIYTSGTT 184
Cdd:PRK07470 105 ARAMIC-HADFPEHAAAVRAASPDLTHVVAIGGARAGLDYEALVARhlGARVANAA--------VDHDDPCWFFFTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 185 GRPKGVMLSHKN---ILTNvldcHVRFVM----ENDekfRILSILPICHilermvdyvfmykSYGIY----FAEGMdklA 253
Cdd:PRK07470 176 GRPKAAVLTHGQmafVITN----HLADLMpgttEQD---ASLVVAPLSH-------------GAGIHqlcqVARGA---A 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 254 SNFQEVKPDVILVVPRIVEKLYASiyNKGTSGGWLKkqIFLWALSVAKkfepFKPASLSHkiadflvfkkwreavgnnlq 333
Cdd:PRK07470 233 TVLLPSERFDPAEVWALVERHRVT--NLFTVPTILK--MLVEHPAVDR----YDHSSLRY-------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 334 LIICGSAALSENLCRIFNAAGLKISEGYGMTETSPVITV------------NGRtkdlfcLGTVGPLLNSCKVKIAED-- 399
Cdd:PRK07470 285 VIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVlppalhdaedgpDAR------IGTCGFERTGMEVQIQDDeg 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 400 --------GEILTKGSNVFLGYYKDEEKTREIYTdDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNL 470
Cdd:PRK07470 359 relppgetGEICVIGPAVFAGYYNNPEANAKAFR-DGWFRTGDLGHLdARGFLYITGRASDMY-ISGGSNVYPREIEEKL 436
|
490
....*....|...
gi 2537297151 471 KQSRFIGEAMVVG 483
Cdd:PRK07470 437 LTHPAVSEVAVLG 449
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
170-457 |
3.31e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 72.44 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 170 EPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLdcHVRFVMENDEKFRILSILPICHILERMVDY---------VFMYKS 240
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKSLLANVE--QIKTIADFTPNDRFMSALPLFHSFGLTVGLftplltgaeVFLYPS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 241 YGIYfaegmdklasnfqevkpdvilvvpRIVEKLyasIYNK------GTSggwlkkqIFLWalSVAKKFEPFkpaslshk 314
Cdd:PRK08043 441 PLHY------------------------RIVPEL---VYDRnctvlfGTS-------TFLG--NYARFANPY-------- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 315 iaDFLvfkkwreavgnNLQLIICGSAALSENLCRI-FNAAGLKISEGYGMTETSPVITVN--GRTKdlfcLGTVGPLLNS 391
Cdd:PRK08043 477 --DFA-----------RLRYVVAGAEKLQESTKQLwQDKFGLRILEGYGVTECAPVVSINvpMAAK----PGTVGRILPG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 392 CKVK------IAEDGEILTKGSNVFLGYYKDEE---------KTREIYTDDGWLKTGDIGYIKD-GFLKITDRKKEIFKT 455
Cdd:PRK08043 540 MDARllsvpgIEQGGRLQLKGPNIMNGYLRVEKpgvlevptaENARGEMERGWYDTGDIVRFDEqGFVQIQGRAKRFAKI 619
|
..
gi 2537297151 456 SG 457
Cdd:PRK08043 620 AG 621
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
35-204 |
3.61e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 71.94 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 35 STQSLIDQVNQVSRGLLNYGINPQDRIALItsVNRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESkFCLVS 113
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVY--LPRSaRLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEP-ALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 114 DkkiydkvhnikdqcpnitslftfDEIEGALNWN--KIKKKGEEISNQqeVENLKNSIEPDRWVTLIYTSGTTGRPKGVM 191
Cdd:cd12116 91 D-----------------------DALPDRLPAGlpVLLLALAAAAAA--PAAPRTPVSPDDLAYVIYTSGSTGRPKGVV 145
|
170
....*....|...
gi 2537297151 192 LSHKNiLTNVLDC 204
Cdd:cd12116 146 VSHRN-LVNFLHS 157
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
41-493 |
5.97e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 71.59 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 41 DQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVsDKKIYDK 120
Cdd:PLN03102 47 DRCCRLAASLISLNITKNDVVSVLAP-NTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFV-DRSFEPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 121 VHNI------KDQCPNITSLFtFDEIEGA-------LNWNKIKKKGEEI-SNQQEVENLKNSIEPdrwVTLIYTSGTTGR 186
Cdd:PLN03102 125 AREVlhllssEDSNLNLPVIF-IHEIDFPkrpsseeLDYECLIQRGEPTpSLVARMFRIQDEHDP---ISLNYTSGTTAD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 187 PKGVMLSHKNILTNVLDCHVRFVMendekfrilSILPIchilermvdYVF---MYKSYGIYFAEGMDKLASNFQEVKPdv 263
Cdd:PLN03102 201 PKGVVISHRGAYLSTLSAIIGWEM---------GTCPV---------YLWtlpMFHCNGWTFTWGTAARGGTSVCMRH-- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 264 iLVVPRIveklYASIYNKGTSGGWLKKQIFLWALSVAKkfepfkpASLSHKiadflvfkkwreavGNNLQLIICGS---A 340
Cdd:PLN03102 261 -VTAPEI----YKNIEMHNVTHMCCVPTVFNILLKGNS-------LDLSPR--------------SGPVHVLTGGSpppA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 341 ALSENLCRIfnaaGLKISEGYGMTE-TSPVitvngrtkdLFC--------------------LGTVGPLLNSCKVKIAED 399
Cdd:PLN03102 315 ALVKKVQRL----GFQVMHAYGLTEaTGPV---------LFCewqdewnrlpenqqmelkarQGVSILGLADVDVKNKET 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 400 -----------GEILTKGSNVFLGYYKDEEKTREIYTdDGWLKTGDIGYIK-DGFLKITDRKKEIFkTSGGKYIIPQITE 467
Cdd:PLN03102 382 qesvprdgktmGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHpDGHVEIKDRSKDII-ISGGENISSVEVE 459
|
490 500 510
....*....|....*....|....*....|.
gi 2537297151 468 NNLKQSRFIGEAMVVGD-----GEkMPCALI 493
Cdd:PLN03102 460 NVLYKYPKVLETAVVAMphptwGE-TPCAFV 489
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
330-483 |
1.21e-12 |
|
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: 68.97 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 330 NNLQLIICGSAALSE----NLCRIFNAAglKISEGYGMTETSpVITVNGrTKDLFCLGTVGPLLNSCKVKI--AEDGEIL 403
Cdd:cd17633 110 SKIKSIFSSGQKLFEstkkKLKNIFPKA--NLIEFYGTSELS-FITYNF-NQESRPPNSVGRPFPNVEIEIrnADGGEIG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 404 T---KGSNVFLGYYKDEEktreiYTDDGWLKTGDIGYIK-DGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEA 479
Cdd:cd17633 186 KifvKSEMVFSGYVRGGF-----SNPDGWMSVGDIGYVDeEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEA 259
|
....
gi 2537297151 480 MVVG 483
Cdd:cd17633 260 IVVG 263
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
354-495 |
1.72e-12 |
|
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: 69.71 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 354 GLKISEGYGMTETSPVITVNGrTKDLFCLGTVGPLLNScKVKI----------AEDGEILTKGSNVFLgYYKDEEKTREI 423
Cdd:cd05929 269 GPIIWEYYGGTEGQGLTIING-EEWLTHPGSVGRAVLG-KVHIldedgnevppGEIGEVYFANGPGFE-YTNDPEKTAAA 345
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2537297151 424 YTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG--DGE--KMPCALIQP 495
Cdd:cd05929 346 RNEGGWSTLGDVGYLdEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpDEElgQRVHAVVQP 421
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
34-493 |
4.63e-12 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 68.45 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 34 ISTQSLIDQVNQVSRGLLNYGINPQDRIALItsVNRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLV 112
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVT--LPKGpEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 113 sdkkiyDKVHNIKDQCPNITSLFTFDEIEGALnwnkikkkgeeisnqqevENLKNSIEPDRWVTLIYTSGTTGRPKGVML 192
Cdd:cd12114 91 ------DGPDAQLDVAVFDVLILDLDALAAPA------------------PPPPVDVAPDDLAYVIFTSGSTGTPKGVMI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 193 SHKNILTNVLDCHVRFVMenDEKFRILSILPICHILErmvdyvfmykSYGIYFAegmdkLASNFQevkpdviLVVPRIVE 272
Cdd:cd12114 147 SHRAALNTILDINRRFAV--GPDDRVLALSSLSFDLS----------VYDIFGA-----LSAGAT-------LVLPDEAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 273 KLYASIYNKgtsggWLKK-QIFLWAlSVakkfepfkPAslshkIADFLVfkKWREAVGN---NLQLIICG----SAALSE 344
Cdd:cd12114 203 RRDPAHWAE-----LIERhGVTLWN-SV--------PA-----LLEMLL--DVLEAAQAllpSLRLVLLSgdwiPLDLPA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 345 NLCRIFNAAGLkISEGyGMTETS------PVITVN--------GRtkdlfclgtvgPLLN-SCKV--KIAED------GE 401
Cdd:cd12114 262 RLRALAPDARL-ISLG-GATEASiwsiyhPIDEVPpdwrsipyGR-----------PLANqRYRVldPRGRDcpdwvpGE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 402 ILTKGSNVFLGYYKDEEKTREIYTDDG----WLKTGDIG-YIKDGFLKITDRKKEIFKTSGGKYIIPQItENNLKQSRFI 476
Cdd:cd12114 329 LWIGGRGVALGYLGDPELTAARFVTHPdgerLYRTGDLGrYRPDGTLEFLGRRDGQVKVRGYRIELGEI-EAALQAHPGV 407
|
490
....*....|....*..
gi 2537297151 477 GEAMVVGDGEKMPCALI 493
Cdd:cd12114 408 ARAVVVVLGDPGGKRLA 424
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
44-203 |
6.00e-12 |
|
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: 68.00 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 44 NQVSRGLLNYGINPQDRIALITSvnRSEWLIMDF-AIQQIGAVSVPIYPTMSDDDLTFILNNSESKfCLVSDKKIYDKVH 122
Cdd:cd12117 33 NRLARRLRAAGVGPGDVVGVLAE--RSPELVVALlAVLKAGAAYVPLDPELPAERLAFMLADAGAK-VLLTDRSLAGRAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 123 NikDQCPNITslftfdeiegalnwnkikkkgEEISNQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVL 202
Cdd:cd12117 110 G--LEVAVVI---------------------DEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK 166
|
.
gi 2537297151 203 D 203
Cdd:cd12117 167 N 167
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
45-521 |
2.55e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 66.12 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 45 QVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVsDKKIYDKVHNI 124
Cdd:PRK08162 55 RLASALARRGIGRGDTVAVLLP-NIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIV-DTEFAEVAREA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 125 KDQCPNiTSLFTFDEIEGALnwnkikKKGEEISnQQEVENLKNSIEP--------DRW--VTLIYTSGTTGRPKGVMLSH 194
Cdd:PRK08162 133 LALLPG-PKPLVIDVDDPEY------PGGRFIG-ALDYEAFLASGDPdfawtlpaDEWdaIALNYTSGTTGNPKGVVYHH 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 195 K----NILTNVLDCHvrfvMENDEKFriLSILPICHilermvdyvfmyksygiyfaegmdklasnfqevkpdvilvvpri 270
Cdd:PRK08162 205 RgaylNALSNILAWG----MPKHPVY--LWTLPMFH-------------------------------------------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 271 veklyasiynkgtSGGWlkkqIFLWALSVA-------KKFEPFKPASL--SHKIADF----LVF-------KKWREAVGN 330
Cdd:PRK08162 235 -------------CNGW----CFPWTVAARagtnvclRKVDPKLIFDLirEHGVTHYcgapIVLsalinapAEWRAGIDH 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 331 NLQLIICGSA---ALSENLCRIfnaaGLKISEGYGMTETSPVITV------------------NGRTkdlfclGTVGPLL 389
Cdd:PRK08162 298 PVHAMVAGAAppaAVIAKMEEI----GFDLTHVYGLTETYGPATVcawqpewdalplderaqlKARQ------GVRYPLQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 390 NSCKV-------KIAED----GEILTKGSNVFLGYYKDEEKTREIYTdDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSG 457
Cdd:PRK08162 368 EGVTVldpdtmqPVPADgetiGEIMFRGNIVMKGYLKNPKATEEAFA-GGWFHTGDLAVLhPDGYIKIKDRSKDII-ISG 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2537297151 458 GKYIIPQITENNLKQSRFIGEAMVVGD-----GEkMPCALIQpdfefilkyikyknLHMNTTISPEEIV 521
Cdd:PRK08162 446 GENISSIEVEDVLYRHPAVLVAAVVAKpdpkwGE-VPCAFVE--------------LKDGASATEEEII 499
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
400-494 |
2.75e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 66.18 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 400 GEILTKGSNVFLGYYKDEEKTREIYTDdGWLKTGDIGYIKDGFLKITDRKKEIFKTSgGKYIIPQITENNLKQ-----SR 474
Cdd:PRK09192 412 GHICVRGPSLMSGYFRDEESQDVLAAD-GWLDTGDLGYLLDGYLYITGRAKDLIIIN-GRNIWPQDIEWIAEQepelrSG 489
|
90 100
....*....|....*....|
gi 2537297151 475 FIGEAMVVGDGEKMPCALIQ 494
Cdd:PRK09192 490 DAAAFSIAQENGEKIVLLVQ 509
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
177-489 |
3.59e-11 |
|
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: 65.35 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 177 LIYTSGTTGRPKGVMLSHKNILTnvldchvrFV--MENDEKF----RILSILPichilermvdYVFMYKSYGIYFAegmd 250
Cdd:cd05945 102 IIFTSGSTGRPKGVQISHDNLVS--------FTnwMLSDFPLgpgdVFLNQAP----------FSFDLSVMDLYPA---- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 251 kLASNfqevkpDVILVVPRIVEKLYASIYNkgtsggWLKK-QIFLW-----ALSVAKKFEPFKPASLShkiadflvfkkw 324
Cdd:cd05945 160 -LASG------ATLVPVPRDATADPKQLFR------FLAEhGITVWvstpsFAAMCLLSPTFTPESLP------------ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 325 reavgnNL-QLIICG-------SAALSENL--CRIFNAaglkisegYGMTETSPVITVNGRTKD-LFCLGTV--GPLLNS 391
Cdd:cd05945 215 ------SLrHFLFCGevlphktARALQQRFpdARIYNT--------YGPTEATVAVTYIEVTPEvLDGYDRLpiGYAKPG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 392 CKVKI----------AEDGEILTKGSNVFLGYYKDEEKTRE-IYTDDG--WLKTGDIGYIK-DGFLKITDRKKEIFKTSG 457
Cdd:cd05945 281 AKLVIldedgrpvppGEKGELVISGPSVSKGYLNNPEKTAAaFFPDEGqrAYRTGDLVRLEaDGLLFYRGRLDFQVKLNG 360
|
330 340 350
....*....|....*....|....*....|....
gi 2537297151 458 GKYIIPQItENNLKQSRFIGEAMVV--GDGEKMP 489
Cdd:cd05945 361 YRIELEEI-EAALRQVPGVKEAVVVpkYKGEKVT 393
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
54-457 |
9.26e-11 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 64.39 E-value: 9.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 54 GINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcLVSDKKIYDKVHNIKDQCPNITS 133
Cdd:PRK06155 67 GVKRGDRVALMCG-NRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARL-LVVEAALLAALEAADPGDLPLPA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 134 LFTFDEiEGALNWNKIKKKGEEISNQQEVEnlKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNILtnVLDCHVRFVMEND 213
Cdd:PRK06155 145 VWLLDA-PASVSVPAGWSTAPLPPLDAPAP--AAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFY--WWGRNSAEDLEIG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 214 EKFRILSILPICHIlermvdyvfmyksygiyfaegmDKLASNFQEVKPDVILVV-PRI-VEKLYASIYNKGTSGGWLKKQ 291
Cdd:PRK06155 220 ADDVLYTTLPLFHT----------------------NALNAFFQALLAGATYVLePRFsASGFWPAVRRHGATVTYLLGA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 292 IFLWALSvakkfEPFKPASLSHKIadflvfkkwREAVGnnlqliICGSAALSENLCRIFnaaGLKISEGYGMTETSPVIT 371
Cdd:PRK06155 278 MVSILLS-----QPARESDRAHRV---------RVALG------PGVPAALHAAFRERF---GVDLLDGYGSTETNFVIA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 372 VNGRTKDlfcLGTVGPLLNSCKVKIAED----------GEILTKGSNVFL---GYYKDEEKTREIYtDDGWLKTGDIGYI 438
Cdd:PRK06155 335 VTHGSQR---PGSMGRLAPGFEARVVDEhdqelpdgepGELLLRADEPFAfatGYFGMPEKTVEAW-RNLWFHTGDRVVR 410
|
410 420
....*....|....*....|
gi 2537297151 439 K-DGFLKITDRKKEIFKTSG 457
Cdd:PRK06155 411 DaDGWFRFVDRIKDAIRRRG 430
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
34-214 |
1.84e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.41 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 34 ISTQSLIDQVNQVSRGLLNYGINPQDRIALitSVNRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcLV 112
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGI--AVERSiEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRL-LL 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 113 SDKKIYDKVhnikDQCPNITSLFtfdeiegalnwnkIKKKGEEISNQQEvENLKNSIEPDRWVTLIYTSGTTGRPKGVML 192
Cdd:PRK12467 615 TQSHLLAQL----PVPAGLRSLC-------------LDEPADLLCGYSG-HNPEVALDPDNLAYVIYTSGSTGQPKGVAI 676
|
170 180
....*....|....*....|..
gi 2537297151 193 SHKNILTNVLDCHVRFVMENDE 214
Cdd:PRK12467 677 SHGALANYVCVIAERLQLAADD 698
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
172-495 |
2.53e-10 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 63.32 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 172 DRW--VTLIYTSGTTGRPKGVMLSHKNILTNVLDCHVrfVMENDEKFRILSILPichilermvdyvfMYKSYGIYFAEGM 249
Cdd:PLN02479 193 DEWqsIALGYTSGTTASPKGVVLHHRGAYLMALSNAL--IWGMNEGAVYLWTLP-------------MFHCNGWCFTWTL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 250 DKLASN---FQEVKPDVIlvvpriveklYASIYNKGTSGgWLKKQIFLWALSVAKKFEPFKPasLSHKIAdflvfkkwre 326
Cdd:PLN02479 258 AALCGTnicLRQVTAKAI----------YSAIANYGVTH-FCAAPVVLNTIVNAPKSETILP--LPRVVH---------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 327 avgnnlqlIICGSAALSENLCRIFNAAGLKISEGYGMTETS---------------PVIT---VNGRTK---------DL 379
Cdd:PLN02479 315 --------VMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETYgpstvcawkpewdslPPEEqarLNARQGvryigleglDV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 380 FCLGTVGPLLNSCKVKiaedGEILTKGSNVFLGYYKDEEKTREIYTdDGWLKTGDIGyIK--DGFLKITDRKKEIFkTSG 457
Cdd:PLN02479 387 VDTKTMKPVPADGKTM----GEIVMRGNMVMKGYLKNPKANEEAFA-NGWFHSGDLG-VKhpDGYIEIKDRSKDII-ISG 459
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2537297151 458 GKYIIPQITENNLKQSRFIGEAMVVGD-----GEKmPCALIQP 495
Cdd:PLN02479 460 GENISSLEVENVVYTHPAVLEASVVARpderwGES-PCAFVTL 501
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
168-453 |
2.65e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 62.91 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 168 SIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDChVRFV--MENDEkfrILSILPICHilermvdyvfmykSYGiYF 245
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRAC-LKFFspKEDDV---MMSFLPPFH-------------AYG-FN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 246 AEGMDKLASNFQEVKPDVILVVPRIVEKLYASiynKGTSGGwlKKQIFL-WALSVAKKFEpfkpASLShkiadflvfkkw 324
Cdd:PRK06334 241 SCTLFPLLSGVPVVFAYNPLYPKKIVEMIDEA---KVTFLG--STPVFFdYILKTAKKQE----SCLP------------ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 325 reavgnNLQLIICGSAALSENL----CRIFNAAGLKisEGYGMTETSPVITVNGRT--KDLFCLGT----VGPLLNSCKV 394
Cdd:PRK06334 300 ------SLRFVVIGGDAFKDSLyqeaLKTFPHIQLR--QGYGTTECSPVITINTVNspKHESCVGMpirgMDVLIVSEET 371
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2537297151 395 KI----AEDGEILTKGSNVFLGYYKDEEKTREIYTD-DGWLKTGDIGYIkdgflkitDRKKEIF 453
Cdd:PRK06334 372 KVpvssGETGLVLTRGTSLFSGYLGEDFGQGFVELGgETWYVTGDLGYV--------DRHGELF 427
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
58-488 |
2.75e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 62.87 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 58 QDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSDKKIYDkvhnikdqcpnitslftF 137
Cdd:PRK07638 50 NKTIAILLE-NRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLND-----------------L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 138 DEIEGA-LNWNKIKkkgEEISNQQEVENLKNSIEPDRWVtLIYTSGTTGRPKGVMLSHKNILTNvLDCHVR-FVMENDEK 215
Cdd:PRK07638 112 PDEEGRvIEIDEWK---RMIEKYLPTYAPIENVQNAPFY-MGFTSGSTGKPKAFLRAQQSWLHS-FDCNVHdFHMKREDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 216 FRILSILPICHILERMVDYVFMYKSYGIyfaegMDKLASN-----FQEVKPDVILVVPRIVEKLY---ASIYNKGT---S 284
Cdd:PRK07638 187 VLIAGTLVHSLFLYGAISTLYVGQTVHL-----MRKFIPNqvldkLETENISVMYTVPTMLESLYkenRVIENKMKiisS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 285 GG-WLK------KQIFLWAlsvaKKFEPFKPASLShkIADFLV---FKKWREAVG---NNLQLIICgsaalsenlcrifN 351
Cdd:PRK07638 262 GAkWEAeakekiKNIFPYA----KLYEFYGASELS--FVTALVdeeSERRPNSVGrpfHNVQVRIC-------------N 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 352 AAGLKISEGygmtetspvitvngrtkdlfclgtvgpllnsckvkiaEDGEILTKGSNVFLGYYKDEEKTREIyTDDGWLK 431
Cdd:PRK07638 323 EAGEEVQKG-------------------------------------EIGTVYVKSPQFFMGYIIGGVLAREL-NADGWMT 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2537297151 432 TGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVGD-----GEKM 488
Cdd:PRK07638 365 VRDVGYEdEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIGVpdsywGEKP 426
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
30-482 |
5.28e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 61.81 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 30 SWkkistQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKF 109
Cdd:PRK09029 30 TW-----QQLCARIDQLAAGFAQQGVVEGSGVALRGK-NSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 110 CLVSDkkiydkvhnikdQCPNITSLftfdeieGALNWNkikkkgeEISNQQEVenlknSIEPDRWVTLIYTSGTTGRPKG 189
Cdd:PRK09029 104 ALVLE------------GENTFSAL-------TSLHLQ-------LVEGAHAV-----AWQPQRLATMTLTSGSTGLPKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 190 VMLSHKNILTN---VLDChvrfvMENDEKFRILSILPICH-----ILERmvdyvfmyksygiYFAEGmdklASnfqevkp 261
Cdd:PRK09029 153 AVHTAQAHLASaegVLSL-----MPFTAQDSWLLSLPLFHvsgqgIVWR-------------WLYAG----AT------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 262 dviLVVPRIvEKLYASIyNKGTSGGWLKKQifLWALSVakkfEPFKPASLSHkiadflvfkkwreavgnnlqlIICGSAA 341
Cdd:PRK09029 204 ---LVVRDK-QPLEQAL-AGCTHASLVPTQ--LWRLLD----NRSEPLSLKA---------------------VLLGGAA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 342 LSENLCRIFNAAGLKISEGYGMTETSPVITVngrtKDLFCLGTVGPLLNSCKVKIaEDGEILTKGSNVFLGYYKDeEKTR 421
Cdd:PRK09029 252 IPVELTEQAEQQGIRCWCGYGLTEMASTVCA----KRADGLAGVGSPLPGREVKL-VDGEIWLRGASLALGYWRQ-GQLV 325
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2537297151 422 EIYTDDGWLKTGDIGYIKDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVV 482
Cdd:PRK09029 326 PLVNDEGWFATRDRGEWQNGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFVV 385
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
180-463 |
5.67e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.94 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 180 TSGTTGRPKGVMLSHKNILTNVLDCHVR--FVMENDekfRILSILPICHILErMVDY--VFMYKSYGIYFAEGMDKLASn 255
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAaeFDVETD---VMVSWLPLFHDMG-MVGFltVPMYFGAELVKVTPMDFLRD- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 256 fqevkpdvILVVPRIVEKLYASI-------YN-------KGTSGGWLKKQIFLWALSVAkkfEPFKPASLshkiadflvf 321
Cdd:PRK07768 235 --------PLLWAELISKYRGTMtaapnfaYAllarrlrRQAKPGAFDLSSLRFALNGA---EPIDPADV---------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 322 kkwreavgnnlqliicgsaalsENLCRIFNAAGLK---ISEGYGMTETSPVITV----NGRTKDLFC------------- 381
Cdd:PRK07768 294 ----------------------EDLLDAGARFGLRpeaILPAYGMAEATLAVSFspcgAGLVVDEVDadllaalrravpa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 382 -------LGTVGPLLNSCKVKIAED----------GEILTKGSNVFLGYyKDEEKTREIYTDDGWLKTGDIGYIKD-GFL 443
Cdd:PRK07768 352 tkgntrrLATLGPPLPGLEVRVVDEdgqvlpprgvGVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEeGEV 430
|
330 340
....*....|....*....|
gi 2537297151 444 KITDRKKEIFkTSGGKYIIP 463
Cdd:PRK07768 431 VVCGRVKDVI-IMAGRNIYP 449
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
169-483 |
7.66e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 60.83 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 169 IEPDrwVTLIY-TSGTTGRPKGVMLSHKNILTNVLDCHVRFVMENdekfRILSILPICHI-----LERMVdyVFMYKSYG 242
Cdd:PRK07824 33 IDDD--VALVVaTSGTTGTPKGAMLTAAALTASADATHDRLGGPG----QWLLALPAHHIaglqvLVRSV--IAGSEPVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 243 IYFAEGMD--KLASNFQEVKPDvilvvpriveKLYASiynkgtsggwlkkqifLWALSVAKKF-EPFKPASLshkiADFl 319
Cdd:PRK07824 105 LDVSAGFDptALPRAVAELGGG----------RRYTS----------------LVPMQLAKALdDPAATAAL----AEL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 320 vfkkwrEAVgnnlqLIicGSAALSENLCRIFNAAGLKISEGYGMTETSPVITVNGRTkdlfclgtvgplLNSCKVKIaED 399
Cdd:PRK07824 154 ------DAV-----LV--GGGPAPAPVLDAAAAAGINVVRTYGMSETSGGCVYDGVP------------LDGVRVRV-ED 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 400 GEILTKGSNVFLGYYKDEEKtrEIYTDDGWLKTGDIGYIKDGFLKITDRKKEIFKTsGGKYIIPQITENNLKQSRFIGEA 479
Cdd:PRK07824 208 GRIALGGPTLAKGYRNPVDP--DPFAEPGWFRTDDLGALDDGVLTVLGRADDAIST-GGLTVLPQVVEAALATHPAVADC 284
|
....
gi 2537297151 480 MVVG 483
Cdd:PRK07824 285 AVFG 288
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
33-199 |
9.89e-10 |
|
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: 60.78 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 33 KISTQSLIDQVNQVSRGLLNYGINPQDRIALitSVNRSEWLIMD-FAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCL 111
Cdd:cd17643 12 RLTYGELDARANRLARTLRAEGVGPGDRVAL--ALPRSAELIVAlLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VsdkkiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiEPDRWVTLIYTSGTTGRPKGVM 191
Cdd:cd17643 90 T---------------------------------------------------------DPDDLAYVIYTSGSTGRPKGVV 112
|
....*...
gi 2537297151 192 LSHKNILT 199
Cdd:cd17643 113 VSHANVLA 120
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
42-443 |
1.04e-09 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 61.21 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 42 QVNQVSRGLLNYGINPQDRIALItsVNRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESkFCLVSDkkiydk 120
Cdd:cd17651 29 RANRLAHRLRARGVGPGDLVALC--ARRSaELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGP-VLVLTH------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 121 vhnikdqcPNITSLFTFDEIEGALNwnkikkkGEEISNQQEVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNiLTN 200
Cdd:cd17651 100 --------PALAGELAVELVAVTLL-------DQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS-LAN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 201 VLDCHVRfVMENDEKFRILSILPIChiLERMVDYVFMYKSYGiyfaeGMDKLASNfqEVKPDvilvvpriVEKLYAsiyn 280
Cdd:cd17651 164 LVAWQAR-ASSLGPGARTLQFAGLG--FDVSVQEIFSTLCAG-----ATLVLPPE--EVRTD--------PPALAA---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 281 kgtsggWLKKQ---------IFLWALSVAKKFEPFKPASLSHkiadflvfkkwreavgnnlqLIICGSAALSENLCRIFN 351
Cdd:cd17651 222 ------WLDEQrisrvflptVALRALAEHGRPLGVRLAALRY--------------------LLTGGEQLVLTEDLREFC 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 352 AA--GLKISEGYGMTETSPV--ITVNGRTKDLFCLGTVGPLLNSCKVKIAED----------GEILTKGSNVFLGYYKDE 417
Cdd:cd17651 276 AGlpGLRLHNHYGPTETHVVtaLSLPGDPAAWPAPPPIGRPIDNTRVYVLDAalrpvppgvpGELYIGGAGLARGYLNRP 355
|
410 420 430
....*....|....*....|....*....|...
gi 2537297151 418 EKTREIYTDDGWL------KTGDIG-YIKDGFL 443
Cdd:cd17651 356 ELTAERFVPDPFVpgarmyRTGDLArWLPDGEL 388
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
156-482 |
1.60e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 60.29 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 156 ISNQQEVENLKNSIEPDRWVT------LIYTSGTTGRPKGVMLSHKNILTnvldchvrFV--MEND----EKFRILSILP 223
Cdd:PRK04813 121 LDELKDIFATGNPYDFDHAVKgddnyyIIFTSGTTGKPKGVQISHDNLVS--------FTnwMLEDfalpEGPQFLNQAP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 224 ichilermvdYVF----MYksygIY--FAEG-----MDKLASN-----FQEVK----------P---DVILVVPRIVEKL 274
Cdd:PRK04813 193 ----------YSFdlsvMD----LYptLASGgtlvaLPKDMTAnfkqlFETLPqlpinvwvstPsfaDMCLLDPSFNEEH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 275 YASiynkgtsggwLKKqiFLwalsvakkfepFKPASLSHKIADFLVfKKWREAvgnnlqliicgsaalsenlcRIFNAag 354
Cdd:PRK04813 259 LPN----------LTH--FL-----------FCGEELPHKTAKKLL-ERFPSA--------------------TIYNT-- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 355 lkisegYGMTE-----TSPVITVN----------GRTK---DLFCLGTVGPllnscKVKIAEDGEILTKGSNVFLGYYKD 416
Cdd:PRK04813 293 ------YGPTEatvavTSIEITDEmldqykrlpiGYAKpdsPLLIIDEEGT-----KLPDGEQGEIVISGPSVSKGYLNN 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 417 EEKTREI-YTDDGW--LKTGDIGYIKDGFLKITDRKKEIFKTSGgkYIIP-QITENNLKQSRFIGEAMVV 482
Cdd:PRK04813 362 PEKTAEAfFTFDGQpaYHTGDAGYLEDGLLFYQGRIDFQIKLNG--YRIElEEIEQNLRQSSYVESAVVV 429
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
54-483 |
2.80e-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: 59.79 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 54 GINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKfCLVSDKKIYDKVHNIKDQCPNI-T 132
Cdd:cd05928 63 GLQRGDRVAVILP-RVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAK-CIVTSDELAPEVDSVASECPSLkT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 133 SLFTFDE-IEGALNWNKIKKKGEEISNQQEVEnlknSIEPdrwVTLIYTSGTTGRPKGVMLSHKNILTNVLDCHvrfvme 211
Cdd:cd05928 141 KLLVSEKsRDGWLNFKELLNEASTEHHCVETG----SQEP---MAIYFTSGTTGSPKMAEHSHSSLGLGLKVNG------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 212 ndekfRILSILPICHILERMVDYVFMYKSYGIYFA---EGMDKLASNFQEVKPDVILVV----PRIVEKLYASIYNkgts 284
Cdd:cd05928 208 -----RYWLDLTASDIMWNTSDTGWIKSAWSSLFEpwiQGACVFVHHLPRFDPLVILKTlssyPITTFCGAPTVYR---- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 285 ggwlkkqiflwaLSVAKKFEPFKPASLSHkiadflvfkkwreavgnnlqLIICGSAALSENLCRIFNAAGLKISEGYGMT 364
Cdd:cd05928 279 ------------MLVQQDLSSYKFPSLQH--------------------CVTGGEPLNPEVLEKWKAQTGLDIYEGYGQT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 365 ETSpVITVNGRTKDLFClGTVGPLLNSCKVKIAED-GEILTKGSN--------------VFLGYYKDEEKTREIYTDDGW 429
Cdd:cd05928 327 ETG-LICANFKGMKIKP-GSMGKASPPYDVQIIDDnGNVLPPGTEgdigirvkpirpfgLFSGYVDNPEKTAATIRGDFY 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2537297151 430 LkTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAMVVG 483
Cdd:cd05928 405 L-TGDRGIMdEDGYFWFMGRADDVINSSGYR-IGPFEVESALIEHPAVVESAVVS 457
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
27-194 |
3.11e-09 |
|
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: 59.81 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 27 KDGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSVNRSEWLIMdFAIQQIGAVSVPIYPTMSDDDLTFILNNSE 106
Cdd:cd05968 85 EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAF-LAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 107 SKFCLVSD---KKiyDKVHNIKD-------QCPNITSLFTFDEIEGALNWNKikkkGEEISNQQEVENLKNSIE---PDR 173
Cdd:cd05968 164 AKALITADgftRR--GREVNLKEeadkacaQCPTVEKVVVVRHLGNDFTPAK----GRDLSYDEEKETAGDGAErteSED 237
|
170 180
....*....|....*....|.
gi 2537297151 174 WVTLIYTSGTTGRPKGVMLSH 194
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVH 258
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
32-235 |
3.42e-09 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 59.34 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYG-INPQDRIALItsVNRSEWLIMD-FAIQQIGAVSVPIYPTMSDDDLTFILNNSESKF 109
Cdd:cd17648 11 KRLTYRELNERANRLAHYLLSVAeIRPDDLVGLV--LDKSELMIIAiLAVWKAGAAYVPIDPSYPDERIQFILEDTGARV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 110 CLVsdkkiydkvhnikdqcpNITSLftfdeiegalnwnkikkkgeeisnqqevenlknsiepdrwVTLIYTSGTTGRPKG 189
Cdd:cd17648 89 VIT-----------------NSTDL----------------------------------------AYAIYTSGTTGKPKG 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2537297151 190 VMLSHKNILTNVLDCHVRFVMENDEKFRILSILPIC--HILERMVDYV 235
Cdd:cd17648 112 VLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFSNYVfdFFVEQMTLAL 159
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
34-496 |
3.73e-09 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 59.39 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 34 ISTQSLIDQVNQVSRGLLNYGINPQDRiALITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVS 113
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGDR-VVVQLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 114 DKkiYDK------VHNIKDQCPNITSLFTFDEIEGALNWNKIKkkgeeisnQQEVENLKNSIEPDRWVTLIYTSGTTGRP 187
Cdd:COG1021 130 DR--HRGfdyralARELQAEVPSLRHVLVVGDAGEFTSLDALL--------AAPADLSEPRPDPDDVAFFQLSGGTTGLP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 188 KGVMLSHKNILTNVLDChVRfVMENDEKFRILSILPICHilermvdyVFMYKSYGI---YFAEGMDKLASNFqevKPDVI 264
Cdd:COG1021 200 KLIPRTHDDYLYSVRAS-AE-ICGLDADTVYLAALPAAH--------NFPLSSPGVlgvLYAGGTVVLAPDP---SPDTA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 265 L------------VVPRIVeklyasiynkgtsGGWLKkqiflwalsvAKKFEPFKPASLshkiadflvfkkwreavgnnl 332
Cdd:COG1021 267 FplierervtvtaLVPPLA-------------LLWLD----------AAERSRYDLSSL--------------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 333 QLIICGSAALSENL-CRIFNAAGLKISEGYGMTE-----TSP------VITVNGRtkdlfclgtvgPLLNSCKVKIAED- 399
Cdd:COG1021 303 RVLQVGGAKLSPELaRRVRPALGCTLQQVFGMAEglvnyTRLddpeevILTTQGR-----------PISPDDEVRIVDEd 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 400 ---------GEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKE-IFKtsGGKYIIPQITEN 468
Cdd:COG1021 372 gnpvppgevGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRtPDGYLVVEGRAKDqINR--GGEKIAAEEVEN 449
|
490 500 510
....*....|....*....|....*....|...
gi 2537297151 469 NLKQSRFIGEAMVVG--D---GEKMpCALIQPD 496
Cdd:COG1021 450 LLLAHPAVHDAAVVAmpDeylGERS-CAFVVPR 481
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
6-496 |
9.78e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 58.22 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 6 LFDILYYQLRNRPIDVsiATKKDGswKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITsVNRSEWLIMDFAIQQIGAV 85
Cdd:PRK06164 12 LASLLDAHARARPDAV--ALIDED--RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWL-PNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 86 SVPIYPTMSDDDLTFILNNSESKFCLVSDK-------KIYDKVHniKDQCPNITSLFTFDEIEGAL--NWNKIKKKGEEI 156
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidfaAILAAVP--PDALPPLRAIAVVDDAADATpaPAPGARVQLFAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 157 SNQQEVENL-KNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLDCHVRFVMENDEkfRILSILPICHilermvdyV 235
Cdd:PRK06164 165 PDPAPPAAAgERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGA--VLLAALPFCG--------V 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 236 FMYKSYGIYFAEGMDKLASNFQEVKPDVILVVPRIVEKLYASiynkgtsggwlkKQIFLWALSVAKKFEPFKPASLsHKI 315
Cdd:PRK06164 235 FGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGN------------DEMLRRILDTAGERADFPSARL-FGF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 316 ADFLvfKKWREAVGNNLQ----------------LIICGSAALSENLcRIfNAAGLKISegygmtetsPVITVNGRTKDl 379
Cdd:PRK06164 302 ASFA--PALGELAALARArgvpltglygssevqaLVALQPATDPVSV-RI-EGGGRPAS---------PEARVRARDPQ- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 380 fclgtVGPLLNSckvkiAEDGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIK-DGFLKITDRKKEIFKTsGG 458
Cdd:PRK06164 368 -----DGALLPD-----GESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRgDGQFVYQTRMGDSLRL-GG 436
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2537297151 459 KYIIPQITENNLKQSRFIGEAMVVG---DGEKMPCALIQPD 496
Cdd:PRK06164 437 FLVNPAEIEHALEALPGVAAAQVVGatrDGKTVPVAFVIPT 477
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
83-472 |
1.34e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.26 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 83 GAVSVPIYPTMS-----DDDLTFILNNSESKFcLVSDKKIYDKVHNIKD-QCPNITSLFTFDEIEGAL--NWNKIKKKGE 154
Cdd:PRK05691 88 GVIAVPAYPPESarrhhQERLLSIIADAEPRL-LLTVADLRDSLLQMEElAAANAPELLCVDTLDPALaeAWQEPALQPD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 155 EISNQQevenlknsiepdrwvtliYTSGTTGRPKGVMLSHKNILTNVLDCHVRFVMENDEKFRILSILPICHilermvdy 234
Cdd:PRK05691 167 DIAFLQ------------------YTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVSWLPLYH-------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 235 vfmyksygiyfaeGMDKLASNFQEVKPDV--ILVVP-----RIVEKLYA-SIYNKGTSGGwlkkQIFLWALSVAKKFEpf 306
Cdd:PRK05691 221 -------------DMGLIGGLLQPIFSGVpcVLMSPayfleRPLRWLEAiSEYGGTISGG----PDFAYRLCSERVSE-- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 307 kpASLSHkiadfLVFKKWREAVGnnlqliicGSAALSENLCRIF----NAAGLKISE---GYGMTETSPVITVNGRTKDL 379
Cdd:PRK05691 282 --SALER-----LDLSRWRVAYS--------GSEPIRQDSLERFaekfAACGFDPDSffaSYGLAEATLFVSGGRRGQGI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 380 FCL--------------GTvGPLLNSC-------KVKIAED-----------GEILTKGSNVFLGYYKDEEKTREIYTD- 426
Cdd:PRK05691 347 PALeldaealarnraepGT-GSVLMSCgrsqpghAVLIVDPqslevlgdnrvGEIWASGPSIAHGYWRNPEASAKTFVEh 425
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2537297151 427 DG--WLKTGDIGYIKDGFLKITDRKKEIFKTSgGKYIIPQITENNLKQ 472
Cdd:PRK05691 426 DGrtWLRTGDLGFLRDGELFVTGRLKDMLIVR-GHNLYPQDIEKTVER 472
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
44-203 |
1.74e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.04 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 44 NQVSRGLLNYGINPQDRIALitSVNRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcLVSDKKIYDKVh 122
Cdd:PRK12316 547 NRLAHALIERGVGPDVLVGV--AMERSiEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQL-LLSQSHLGRKL- 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 123 nikdQCPNITSLFTFDEIegalnwnkikkkGEEISNQQEvENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNiLTNVL 202
Cdd:PRK12316 623 ----PLAAGVQVLDLDRP------------AAWLEGYSE-ENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRA-LSNRL 684
|
.
gi 2537297151 203 D 203
Cdd:PRK12316 685 C 685
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
39-197 |
2.01e-08 |
|
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: 56.90 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALitSVNRSEWLIMD-FAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcLVSDKKI 117
Cdd:cd17646 29 LDERANRLAHLLRARGVGPEDRVAV--LLPRSADLVVAlLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAV-VLTTADL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 118 YDK---VHNIKDQCPNITSLFTFDEiegalnwnkikkkgeeisnqqevenLKNSIEPDRWVTLIYTSGTTGRPKGVMLSH 194
Cdd:cd17646 106 AARlpaGGDVALLGDEALAAPPATP-------------------------PLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
|
...
gi 2537297151 195 KNI 197
Cdd:cd17646 161 AGI 163
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
10-498 |
2.10e-08 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 56.79 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 10 LYYQLRNRPIDVSIATKKDGSWkkiSTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPI 89
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSL---TYKQLNEKANQLARHLRGKGVKPDDQVGIMLD-KSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 90 YPTMSDDDLTFILNNSESKFCLVsdkkiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsi 169
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLT--------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 170 EPDRWVTLIYTSGTTGRPKGVMLSHKNiLTNVLDCHVRF--VMENDEKFRILSILPICHILErmvdyVFMYKSYGIyfae 247
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHN-LVNLCEWHRPYfgVTPADKSLVYASFSFDASAWE-----IFPHLTAGA---- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 248 gmdKLASNFQEVKPDvilvvpriVEKLYASIYNKGTSGGWLKKQiflwalsVAKKFEPFKPASlshkiadflvfkkwrea 327
Cdd:cd17645 172 ---ALHVVPSERRLD--------LDALNDYFNQEGITISFLPTG-------AAEQFMQLDNQS----------------- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 328 vgnnLQLIICGSAALsenlcRIFNAAGLKISEGYGMTETSPVITVN-----------GRTKDLFCLGTVGPLLNSCKVKI 396
Cdd:cd17645 217 ----LRVLLTGGDKL-----KKIERKGYKLVNNYGPTENTVVATSFeidkpyanipiGKPIDNTRVYILDEALQLQPIGV 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 397 AedGEILTKGSNVFLGYYKDEEKTREIYTDDGWL------KTGDIG-YIKDGFLKITDRKKEIFKTSGGKyIIPQITENN 469
Cdd:cd17645 288 A--GELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAkFLPDGNIEFLGRLDQQVKIRGYR-IEPGEIEPF 364
|
490 500 510
....*....|....*....|....*....|...
gi 2537297151 470 LKQSRFIGEAMVV----GDGEKMPCALIQPDFE 498
Cdd:cd17645 365 LMNHPLIELAAVLakedADGRKYLVAYVTAPEE 397
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
13-463 |
3.81e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 56.17 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 13 QLRNRPidVSIATKKDGSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIaLITSVNRSEWLIMDFAIQQIGAVSVpiypt 92
Cdd:PRK05857 23 QARQQP--EAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRV-LVISDNGPETYLSVLACAKLGAIAV----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 93 MSDDDLTfilNNSESKFCLVSD----------KKIYDKVHNIKDQCPNITSLFTFDEIEGALNWNKIKKKGEEISNQqev 162
Cdd:PRK05857 95 MADGNLP---IAAIERFCQITDpaaalvapgsKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGS--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 163 enlknsiepDRWVTLIYTSGTTGRPKGVMLSHK------NILTNVLDCHVRFVmENDEKFrilSILPICHI--LERMVDy 234
Cdd:PRK05857 169 ---------EDPLAMIFTSGTTGEPKAVLLANRtffavpDILQKEGLNWVTWV-VGETTY---SPLPATHIggLWWILT- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 235 VFMYKSYGIYFAEGMDKLASNFQEVKPDVILVVPRIVEKLYASIYNKGTSGGWLKkqiflwalsvakkfepfkpaslshk 314
Cdd:PRK05857 235 CLMHGGLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLR------------------------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 315 iadFLVFKkwreavgnnlqliicGSAALSENLcRIFNAAGLKISEGYGMTETSPVI----TVNGRTKDLFClGTVGPLLN 390
Cdd:PRK05857 290 ---LVGYG---------------GSRAIAADV-RFIEATGVRTAQVYGLSETGCTAlclpTDDGSIVKIEA-GAVGRPYP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 391 SCKVKIAED----------------GEILTKGSNVFLGYYKDEEKTREIYTdDGWLKTGD-IGYIKDGFLKITDRKKEIF 453
Cdd:PRK05857 350 GVDVYLAATdgigptapgagpsasfGTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDlLERREDGFFYIKGRSSEMI 428
|
490
....*....|
gi 2537297151 454 kTSGGKYIIP 463
Cdd:PRK05857 429 -ICGGVNIAP 437
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
42-198 |
4.49e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 56.71 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 42 QVNQVSRGLLNYGINPQDRIALitSVNRSEWLIMDF-AIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSdkkiydk 120
Cdd:PRK12467 1608 RANRLAHRLIALGVGPEVLVGI--AVERSLEMVVGLlAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ------- 1678
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2537297151 121 vHNIKDQCPNITSLFTFdEIEGALNWnkikkkgeeISNQQEvENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNIL 198
Cdd:PRK12467 1679 -SHLQARLPLPDGLRSL-VLDQEDDW---------LEGYSD-SNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALV 1744
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
6-449 |
6.98e-08 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 55.24 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 6 LFDILYYQLRNRPIDVSIATKkDGSWkkiSTQSLIDQVNQVSRGLLNYGINPQDRIALitSVNRSEWLI--MdFAIQQIG 83
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAW-DGSL---TYAELDRLSSRLAHHLRSLGVGPGVFVPL--CFEKSKWAVvaM-LAVLKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 84 AVSVPIYPTMSDDDLTFILNNSESKFCLVSDkkiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqeve 163
Cdd:cd05918 74 GAFVPLDPSHPLQRLQEILQDTGAKVVLTSS------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 164 nlknsiePDRWVTLIYTSGTTGRPKGVMLSHKNILTNVLdCHVRFvMENDEKFRIL---------SILPICHIL------ 228
Cdd:cd05918 105 -------PSDAAYVIFTSGSTGKPKGVVIEHRALSTSAL-AHGRA-LGLTSESRVLqfasytfdvSILEIFTTLaaggcl 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 229 ------ERMVDyvfmyksygiyfaegmdkLASNFQEVKPDVILVVPriveklyasiynkgtsggwlkkqiflwalSVAKK 302
Cdd:cd05918 176 cipseeDRLND------------------LAGFINRLRVTWAFLTP-----------------------------SVARL 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 303 FEPfkpaslshkiadflvfkkwrEAVgNNLQLIICGSAALSENLCRIFnAAGLKISEGYGMTETSpVITVNGRTKDLFCL 382
Cdd:cd05918 209 LDP--------------------EDV-PSLRTLVLGGEALTQSDVDTW-ADRVRLINAYGPAECT-IAATVSPVVPSTDP 265
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 383 GTVG-PLLNSCKVKIAED----------GEILTKGSNVFLGYYKDEEKTREIYTDD-GWL------------KTGDIG-Y 437
Cdd:cd05918 266 RNIGrPLGATCWVVDPDNhdrlvpigavGELLIEGPILARGYLNDPEKTAAAFIEDpAWLkqegsgrgrrlyRTGDLVrY 345
|
490
....*....|..
gi 2537297151 438 IKDGFLKITDRK 449
Cdd:cd05918 346 NPDGSLEYVGRK 357
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
353-483 |
8.65e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 55.00 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 353 AGLKISEGYGMTET-SPVITVngrTKDLFCLG--TVGPLLNSCKVKIAE--DGEILTKGSNVFLGYYKDEEKTREIytdd 427
Cdd:PRK07445 253 LQLRLAPTYGMTETaSQIATL---KPDDFLAGnnSSGQVLPHAQITIPAnqTGNITIQAQSLALGYYPQILDSQGI---- 325
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2537297151 428 gwLKTGDIGYI-KDGFLKITDR--KKEIfktSGGKYIIPQITENNLKQSRFIGEAMVVG 483
Cdd:PRK07445 326 --FETDDLGYLdAQGYLHILGRnsQKII---TGGENVYPAEVEAAILATGLVQDVCVLG 379
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
34-214 |
9.43e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.56 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 34 ISTQSLIDQVNQVSRGLLNYGINPQDRIALitSVNRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcLV 112
Cdd:PRK05691 2214 LSYAELDARANRLARALRERGVGPQVRVGL--ALERSlEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGL-LL 2290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 113 SDKKIYDkvhnikdqcpnitslfTFDEIEGALNWNKIKKKGEEISNQQEVEnLKNSIEPDRWVTLIYTSGTTGRPKGVML 192
Cdd:PRK05691 2291 SDRALFE----------------ALGELPAGVARWCLEDDAAALAAYSDAP-LPFLSLPQHQAYLIYTSGSTGKPKGVVV 2353
|
170 180
....*....|....*....|..
gi 2537297151 193 SHKNILTNVLDCHVRFVMENDE 214
Cdd:PRK05691 2354 SHGEIAMHCQAVIERFGMRADD 2375
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
34-194 |
9.99e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.35 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 34 ISTQSLIDQVNQVSRGLLNYGINPQDRIALitSVNRSEWLIMDF-AIQQIGAVSVPIYPTMSDDDLTFILNNSESKFcLV 112
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAI--AAERSFELVVALlAVLKAGGAYVPLDPNYPAERLAYMLEDSGAAL-LL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 113 SDKkiydkvhNIKDQCPNITSLFTFDeIEGALNWNKIKKKGEEisnqqevenlkNSIEPDRWVTLIYTSGTTGRPKGVML 192
Cdd:PRK12316 2106 TQR-------HLLERLPLPAGVARLP-LDRDAEWADYPDTAPA-----------VQLAGENLAYVIYTSGSTGLPKGVAV 2166
|
..
gi 2537297151 193 SH 194
Cdd:PRK12316 2167 SH 2168
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
28-495 |
1.08e-07 |
|
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: 54.64 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 28 DGSWkkiSTQSLIDQVNQVSRGLLNYGINPQDRiALITSVNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSES 107
Cdd:cd05920 38 DRRL---TYRELDRRADRLAAGLRGLGIRPGDR-VVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 108 KFCLVSDKkiydkvhnikdqcpnitsLFTFDEIEGALnwnkikkkgEEISNQQEVENLKNSiepdrwvtliytSGTTGRP 187
Cdd:cd05920 114 VAYIVPDR------------------HAGFDHRALAR---------ELAESIPEVALFLLS------------GGTTGTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 188 KGVMLSHK----NILTNVLDCHVrfvmenDEKFRILSILPICHilermvdyVFMYKSYGIY---FAEGMDKLASNfqeVK 260
Cdd:cd05920 155 KLIPRTHNdyayNVRASAEVCGL------DQDTVYLAVLPAAH--------NFPLACPGVLgtlLAGGRVVLAPD---PS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 261 PD------------VILVVPRIVEklyasiynkgtsggwlkkqifLWALSVAkkfepfkpaslshkiadflvfkkWREAV 328
Cdd:cd05920 218 PDaafplieregvtVTALVPALVS---------------------LWLDAAA-----------------------SRRAD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 329 GNNLQLIICGSAALSENLCRIFNAA-GLKISEGYGMTE-----TSP------VITVNGRtkdlfclgtvgPLLNSCKVKI 396
Cdd:cd05920 254 LSSLRLLQVGGARLSPALARRVPPVlGCTLQQVFGMAEgllnyTRLddpdevIIHTQGR-----------PMSPDDEIRV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 397 A----------EDGEILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQI 465
Cdd:cd05920 323 VdeegnpvppgEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRtPDGYLVVEGRIKDQI-NRGGEKIAAEE 401
|
490 500 510
....*....|....*....|....*....|....*
gi 2537297151 466 TENNLKQSRFIGEAMVVG--D---GEKMpCALIQP 495
Cdd:cd05920 402 VENLLLRHPAVHDAAVVAmpDellGERS-CAFVVL 435
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
33-205 |
1.23e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 54.52 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 33 KISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvnRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKfCL 111
Cdd:PRK04319 73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMP--RIpELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAK-VL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VSDKKIYDKVhnIKDQCPNITSLFTFDE----IEGALNWNKIKkkgEEISNQQEVENLknsiEPDRWVTLIYTSGTTGRP 187
Cdd:PRK04319 150 ITTPALLERK--PADDLPSLKHVLLVGEdveeGPGTLDFNALM---EQASDEFDIEWT----DREDGAILHYTSGSTGKP 220
|
170 180
....*....|....*....|....
gi 2537297151 188 KGVMLSHKNILTN------VLDCH 205
Cdd:PRK04319 221 KGVLHVHNAMLQHyqtgkyVLDLH 244
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
42-486 |
2.21e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 54.40 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 42 QVNQVSRGLLNYGINPQDRIALitSVNRSEWLIMDF-AIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLVSdkkiydk 120
Cdd:PRK12467 3129 RANRLAHRLIAIGVGPDVLVGV--AVERSVEMIVALlAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ------- 3199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 121 vHNIKDQCPNITSLFTFDEIEGALNwnkikkkGEEisnqqeVENLKNSIEPDRWVTLIYTSGTTGRPKGVMLSHKNiLTN 200
Cdd:PRK12467 3200 -AHLLEQLPAPAGDTALTLDRLDLN-------GYS------ENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGA-LAN 3264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 201 VLdCHVRFVMENDEKFRILSILPIChilermVDyVFMYKSYGIYFAEGMDKLASNFQevkpdvilvvpRIVEKLYASIYN 280
Cdd:PRK12467 3265 HL-CWIAEAYELDANDRVLLFMSFS------FD-GAQERFLWTLICGGCLVVRDNDL-----------WDPEELWQAIHA 3325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 281 KGtsggwlkkqiflwaLSVAKkfepFKPASLShkiaDFLVFKKWREavGNNLQLIICGSAALSE-NLCRIFNAAG-LKIS 358
Cdd:PRK12467 3326 HR--------------ISIAC----FPPAYLQ----QFAEDAGGAD--CASLDIYVFGGEAVPPaAFEQVKRKLKpRGLT 3381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 359 EGYGMTETSPVITVNGRTKDLFCLGTVGPL---------------LNSCKVKIAedGEILTKGSNVFLGYYKDEEKTREI 423
Cdd:PRK12467 3382 NGYGPTEAVVTVTLWKCGGDAVCEAPYAPIgrpvagrsiyvldgqLNPVPVGVA--GELYIGGVGLARGYHQRPSLTAER 3459
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2537297151 424 YTDDGWL-------KTGDIG-YIKDGFLKITDRKKEIFKTSGGKYIIPQItENNLKQSRFIGEAMVVG-DGE 486
Cdd:PRK12467 3460 FVADPFSgsggrlyRTGDLArYRADGVIEYLGRIDHQVKIRGFRIELGEI-EARLLQHPSVREAVVLArDGA 3530
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
7-194 |
2.26e-07 |
|
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: 53.73 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 7 FDILYYQLRNRPIDVS-IATKKDGSW-KKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSVnRSEWLIMDFAIQQIGA 84
Cdd:cd17634 56 ANALDRHLRENGDRTAiIYEGDDTSQsRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPM-IPEAAVAMLACARIGA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 85 VSVPIYPTMSDDDLTFILNNSESKFCLVSD-----------KKIYDKVHNIkdQCPNITSLFTFDEIEGALNWNKikkkG 153
Cdd:cd17634 135 VHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvplKKNVDDALNP--NVTSVEHVIVLKRTGSDIDWQE----G 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2537297151 154 EEISNQQEVENLKNSIEPDRW-----VTLIYTSGTTGRPKGVMLSH 194
Cdd:cd17634 209 RDLWWRDLIAKASPEHQPEAMnaedpLFILYTSGTTGKPKGVLHTT 254
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
32-496 |
2.85e-07 |
|
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: 53.24 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINPQDRIALItsVNRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFC 110
Cdd:cd17650 11 RQLTYRELNERANQLARTLRGLGVAPGSVVGVC--ADRSlDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 111 LvsdkkiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsIEPDRWVTLIYTSGTTGRPKGV 190
Cdd:cd17650 89 L---------------------------------------------------------TQPEDLAYVIYTSGTTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 191 MLSHKNILtnvldcHVRFVMEndekfRILSILPICHILERMVDYVFmyksygiyfaegmDKLASNFQE--VKPDVILVVP 268
Cdd:cd17650 112 MVEHRNVA------HAAHAWR-----REYELDSFPVRLLQMASFSF-------------DVFAGDFARslLNGGTLVICP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 269 RIVEKLYASIYNKgtsggwLKKQIFLWALSVakkfepfkPAsLSHKIADFLvfkKWREAVGNNLQLIICGS----AALSE 344
Cdd:cd17650 168 DEVKLDPAALYDL------ILKSRITLMEST--------PA-LIRPVMAYV---YRNGLDLSAMRLLIVGSdgckAQDFK 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 345 NLCRIFnAAGLKISEGYGMTETSPVITVNGRTKDLFCLGT---VG-PLLNSC---------KVKIAEDGEILTKGSNVFL 411
Cdd:cd17650 230 TLAARF-GQGMRIINSYGVTEATIDSTYYEEGRDPLGDSAnvpIGrPLPNTAmyvlderlqPQPVGVAGELYIGGAGVAR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 412 GYYKDEEKTREIYTDDGW------LKTGDIG-YIKDGFLKITDRKKEIFKTSGGKYIIPQItENNLKQSRFIGEAMVV-- 482
Cdd:cd17650 309 GYLNRPELTAERFVENPFapgermYRTGDLArWRADGNVELLGRVDHQVKIRGFRIELGEI-ESQLARHPAIDEAVVAvr 387
|
490
....*....|....*.
gi 2537297151 483 --GDGEKMPCALIQPD 496
Cdd:cd17650 388 edKGGEARLCAYVVAA 403
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
33-501 |
4.69e-07 |
|
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: 52.44 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 33 KISTQSLIDQVNQVSRGLLNYGINPQDRIALItsVNRSEWLIMDF-AIQQIGAVSVPIYPTMSDDDLTFILNNSEskfcl 111
Cdd:cd17644 25 QLTYEELNTKANQLAHYLQSLGVKSESLVGIC--VERSLEMIIGLlAILKAGGAYVPLDPNYPQERLTYILEDAQ----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 vsdkkiydkvhnikdqcpnITSLFTfdeiegalnwnkikkkgeeisnQQEveNLknsiepdrwVTLIYTSGTTGRPKGVM 191
Cdd:cd17644 98 -------------------ISVLLT----------------------QPE--NL---------AYVIYTSGSTGKPKGVM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 192 LSHKNILTNVLDCH-VRFVMENDekfRILSILPICHILERMVDYVFMYKSYGIYFAEGmdklasnfqEVKPDvilvVPRI 270
Cdd:cd17644 126 IEHQSLVNLSHGLIkEYGITSSD---RVLQFASIAFDVAAEEIYVTLLSGATLVLRPE---------EMRSS----LEDF 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 271 VEKLYasiynkgtsggwlKKQIFLWALsvakkfepfkPASLSHKIADFLVFKKWreAVGNNLQLIICGSAALSENLCRI- 349
Cdd:cd17644 190 VQYIQ-------------QWQLTVLSL----------PPAYWHLLVLELLLSTI--DLPSSLRLVIVGGEAVQPELVRQw 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 350 FNAAGLKIS--EGYGMTETSPVITVNGRTKDLFCLGT---VG-PLLNSC---------KVKIAEDGEILTKGSNVFLGYY 414
Cdd:cd17644 245 QKNVGNFIQliNVYGPTEATIAATVCRLTQLTERNITsvpIGrPIANTQvyildenlqPVPVGVPGELHIGGVGLARGYL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 415 KDEEKTREIYTDDGWL--------KTGDIG-YIKDGFLKITDRKKEIFKTSGGKYIIPQItENNLKQSRFIGEAMVVG-- 483
Cdd:cd17644 325 NRPELTAEKFISHPFNsseserlyKTGDLArYLPDGNIEYLGRIDNQVKIRGFRIELGEI-EAVLSQHNDVKTAVVIVre 403
|
490 500
....*....|....*....|
gi 2537297151 484 --DGEKMPCALIQPDFEFIL 501
Cdd:cd17644 404 dqPGNKRLVAYIVPHYEESP 423
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
13-191 |
5.06e-07 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 52.63 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 13 QLRNRPIDVSIATKKD--GSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSVnRSEWLIMDFAIQQIGAVSVPIY 90
Cdd:TIGR02188 66 HLEARPDKVAIIWEGDepGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPM-IPEAAIAMLACARIGAIHSVVF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 91 PTMSDDDLTFILNNSESKFCLVSDKKIY-DKVHNIKD-------QCPnitslftfDEIEGALnwnKIKKKGEEISNQQE- 161
Cdd:TIGR02188 145 GGFSAEALADRINDAGAKLVITADEGLRgGKVIPLKAivdealeKCP--------VSVEHVL---VVRRTGNPVVPWVEg 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2537297151 162 --------VENLKNSIEPDrWVT------LIYTSGTTGRPKGVM 191
Cdd:TIGR02188 214 rdvwwhdlMAKASAYCEPE-PMDsedplfILYTSGSTGKPKGVL 256
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
44-197 |
6.02e-07 |
|
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: 52.26 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 44 NQVSRGLLNYGINPQDRIALitSVNRS-EWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILnnSESKFCLVsdkkiydkvh 122
Cdd:cd17652 23 NRLARLLAARGVGPERLVAL--ALPRSaELVVAILAVLKAGAAYLPLDPAYPAERIAYML--ADARPALL---------- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2537297151 123 nikdqcpnITSlftfdeiegalnwnkikkkgeeisnqqevenlknsiePDRWVTLIYTSGTTGRPKGVMLSHKNI 197
Cdd:cd17652 89 --------LTT-------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGL 118
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
39-495 |
1.50e-06 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 50.83 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 39 LIDQVNQVSRGLLNYGINPQDRIALitSVNRSEWLIMDF-AIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCLvsdkki 117
Cdd:cd17649 18 LDARANRLAHRLRALGVGPEVRVGI--ALERSLEMVVALlAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLL------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 118 ydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknSIEPDRWVTLIYTSGTTGRPKGVMLSHKNI 197
Cdd:cd17649 90 --------------------------------------------------THHPRQLAYVIYTSGSTGTPKGVAVSHGPL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 198 LTnvldcHVRFVMEndekfrILSILPICHILErmvdyvFMYKSYGIYFAEGMDKLASNFQEVKPDVILVVPriVEKLYAS 277
Cdd:cd17649 120 AA-----HCQATAE------RYGLTPGDRELQ------FASFNFDGAHEQLLPPLICGACVVLRPDELWAS--ADELAEM 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 278 IYNKGtsggwlkkqiflwaLSVAKkfepFKPASLsHKIADFLVFKKWREAVgnNLQLIICGSAALSENLCRIFNAAGLKI 357
Cdd:cd17649 181 VRELG--------------VTVLD----LPPAYL-QQLAEEADRTGDGRPP--SLRLYIFGGEALSPELLRRWLKAPVRL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 358 SEGYGMTETSPVITVNGRTKDLFCLGTVGPL---------------LNSCKVKIAedGEILTKGSNVFLGYYKDEEKTRE 422
Cdd:cd17649 240 FNAYGPTEATVTPLVWKCEAGAARAGASMPIgrplggrsayildadLNPVPVGVT--GELYIGGEGLARGYLGRPELTAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 423 IYTDDG-------WLKTGDIG-YIKDG---FLKITDRKKEIfktsGGKYIIPQITENNLKQSRFIGEAMVV---GDGEKM 488
Cdd:cd17649 318 RFVPDPfgapgsrLYRTGDLArWRDDGvieYLGRVDHQVKI----RGFRIELGEIEAALLEHPGVREAAVValdGAGGKQ 393
|
....*..
gi 2537297151 489 PCALIQP 495
Cdd:cd17649 394 LVAYVVL 400
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
32-482 |
3.14e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.73 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINPQDRIALitSVNRSEWLIMDF-AIQQIGAVSVPIYPTMSDDDLTFILNNSESKFC 110
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARGVGPEVLVGI--AMERSAEMMVGLlAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALL 4652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 111 LVSDkkiydkvhNIKDQCP---NITSLFtfdeIEGALNWNKIKKkgeeisnqqevENLKNSIEPDRWVTLIYTSGTTGRP 187
Cdd:PRK12316 4653 LTQS--------HLLQRLPipdGLASLA----LDRDEDWEGFPA-----------HDPAVRLHPDNLAYVIYTSGSTGRP 4709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 188 KGVMLSHKNILTNVLDCHVRFVMENDEkfRILSilpichilermvdyvFMYKSYGIYFAEGMDKLASNFQEVKPDVILVV 267
Cdd:PRK12316 4710 KGVAVSHGSLVNHLHATGERYELTPDD--RVLQ---------------FMSFSFDGSHEGLYHPLINGASVVIRDDSLWD 4772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 268 PrivEKLYASIYNKGtsggwlkkqiflwaLSVAKkfepFKPASLSHKIADFlvfkkwrEAVGN--NLQLIICGSAALS-E 344
Cdd:PRK12316 4773 P---ERLYAEIHEHR--------------VTVLV----FPPVYLQQLAEHA-------ERDGEppSLRVYCFGGEAVAqA 4824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 345 NLCRIFNAAGLK-ISEGYGMTETSPVITVNGRTKDLFCLGTVGPL---------------LNSCKVKIAedGEILTKGSN 408
Cdd:PRK12316 4825 SYDLAWRALKPVyLFNGYGPTETTVTVLLWKARDGDACGAAYMPIgtplgnrsgyvldgqLNPLPVGVA--GELYLGGEG 4902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 409 VFLGYYKDEEKTREIYTDDGW-------LKTGDIG-YIKDGFLKITDRKKEIFKTSGGKYIIPQItENNLKQSRFIGEAM 480
Cdd:PRK12316 4903 VARGYLERPALTAERFVPDPFgapggrlYRTGDLArYRADGVIDYLGRVDHQVKIRGFRIELGEI-EARLREHPAVREAV 4981
|
..
gi 2537297151 481 VV 482
Cdd:PRK12316 4982 VI 4983
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
331-483 |
3.74e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 49.93 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 331 NLQLIICGSAALSENLCRIFNAA-GLKISEGYGMTETSpVITVNGRtKDL-FCLGTVGPLLNSCKVKIAED--------- 399
Cdd:PRK07788 324 SLKIIFVSGSALSPELATRALEAfGPVLYNLYGSTEVA-FATIATP-EDLaEAPGTVGRPPKGVTVKILDEngnevprgv 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 400 -GEILTKGSNVFLGYYKDEEKTREiytdDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIG 477
Cdd:PRK07788 402 vGRIFVGNGFPFEGYTDGRDKQII----DGLLSSGDVGYFdEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVV 476
|
....*.
gi 2537297151 478 EAMVVG 483
Cdd:PRK07788 477 EAAVIG 482
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
33-202 |
3.79e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.04 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 33 KISTQSLIDQVNQVSRGLLNYGINPQDRIALitSVNRSEWLIMDF-AIQQIGAVSVPIYPTMSDDDLTFILNNSESKfCL 111
Cdd:PRK10252 483 QFSYREMREQVVALANLLRERGVKPGDSVAV--ALPRSVFLTLALhAIVEAGAAWLPLDTGYPDDRLKMMLEDARPS-LL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VSDKKIYDKVHNIkdqcPNITSLfTFDEIEGAlnwnkikkkgeeisnqQEVENLKNSiEPDRWVTLIYTSGTTGRPKGVM 191
Cdd:PRK10252 560 ITTADQLPRFADV----PDLTSL-CYNAPLAP----------------QGAAPLQLS-QPHHTAYIIFTSGSTGRPKGVM 617
|
170
....*....|.
gi 2537297151 192 LSHKNILTNVL 202
Cdd:PRK10252 618 VGQTAIVNRLL 628
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
29-194 |
4.09e-06 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 49.87 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 29 GSWKKISTQSLIDQVNQVSRGLLNYGINPQDRIAL----ITsvnrsEWLIMDFAIQQIGAV-SVpIYPTMSDDDLTFILN 103
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIympmIP-----ELVIAMLACARIGAVhSV-VFAGFSAESLADRIN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 104 NSESKFCLVSD-----------KKIYDKVhniKDQCPNITSLFTFDEIEGALNWNKikkkGEEISNQQEVENLKNSIEPD 172
Cdd:cd05966 154 DAQCKLVITADggyrggkviplKEIVDEA---LEKCPSVEKVLVVKRTGGEVPMTE----GRDLWWHDLMAKQSPECEPE 226
|
170 180
....*....|....*....|....*...
gi 2537297151 173 rWVT------LIYTSGTTGRPKGVMLSH 194
Cdd:cd05966 227 -WMDsedplfILYTSGSTGKPKGVVHTT 253
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
388-494 |
4.24e-06 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 49.74 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 388 LLNSCKVKIAEDGE----ILTKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYIK-DGFLKITDRKKEIFkTSGGKYII 462
Cdd:cd05915 345 VADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDeEGYVEIKDRLKDLI-KSGGEWIS 423
|
90 100 110
....*....|....*....|....*....|....*..
gi 2537297151 463 PQITENNLKQSRFIGEAMVVGD-----GEKMpCALIQ 494
Cdd:cd05915 424 SVDLENALMGHPKVKEAAVVAIphpkwQERP-LAVVV 459
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
348-482 |
6.75e-06 |
|
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: 48.72 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 348 RIFNAAGLKISEGYGMTETSpvITVNGRTKDLFCLGTVGPLLNSCKVKI-------AEDGEI-LTKGSN----VFLGYYK 415
Cdd:cd05974 219 QVRRAWGLTIRDGYGQTETT--ALVGNSPGQPVKAGSMGRPLPGYRVALldpdgapATEGEVaLDLGDTrpvgLMKGYAG 296
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2537297151 416 DEEKTREIyTDDGWLKTGDIGYI-KDGFLKITDRKKEIFKTSGGKyIIPQITENNLKQSRFIGEAMVV 482
Cdd:cd05974 297 DPDKTAHA-MRGGYYRTGDIAMRdEDGYLTYVGRADDVFKSSDYR-ISPFELESVLIEHPAVAEAAVV 362
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
360-483 |
6.94e-06 |
|
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: 48.45 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 360 GYGMTETSPVITVNGRTKDlfCLGTVG---PLlnsCKVKI----------AEDGEILTKGSNVFLGYY-KDEEKTREiyT 425
Cdd:cd17636 142 GYGQTEVMGLATFAALGGG--AIGGAGrpsPL---VQVRIldedgrevpdGEVGEIVARGPTVMAGYWnRPEVNARR--T 214
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2537297151 426 DDGWLKTGDIGY-IKDGFLKITDRKKEIFKtSGGKYIIPQITENNLKQSRFIGEAMVVG 483
Cdd:cd17636 215 RGGWHHTNDLGRrEPDGSLSFVGPKTRMIK-SGAENIYPAEVERCLRQHPAVADAAVIG 272
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
398-497 |
8.67e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.61 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 398 EDGEILTKGSNVFLGYYKDEEKTReiytdDGWLKTGDIGYIKDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIG 477
Cdd:PRK05851 371 EIGEIEIRGASMMSGYLGQAPIDP-----DDWFPTGDLGYLVDGGLVVCGRAKELI-TVAGRNIFPTEIERVAAQVRGVR 444
|
90 100
....*....|....*....|....
gi 2537297151 478 EAMVV----GDGEKMPCALIQPDF 497
Cdd:PRK05851 445 EGAVVavgtGEGSARPGLVIAAEF 468
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-483 |
2.75e-05 |
|
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: 46.61 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 177 LIYTSGTTGRPKGVMLSHKNI---LTNVLDchvrFVMENDEKFRI----------LSILPICHILermvdyvfmyksYGI 243
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmLMGGAD----FGTGEFTPSEDahkaaaaaagTVMFPAPPLM------------HGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 244 YFAEGMDKLASNFQEVKPDVILV---VPRIVEKlyasiyNKGTSggwlkkqIFL----WALSVAKKFEPFKPASLShkia 316
Cdd:cd05924 72 GSWTAFGGLLGGQTVVLPDDRFDpeeVWRTIEK------HKVTS-------MTIvgdaMARPLIDALRDAGPYDLS---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 317 dflvfkkwreavgnNLQLIICGSAALS----ENLCR------IFNAAGlkISE----GYGMT-----ETSPVITVNGRTk 377
Cdd:cd05924 135 --------------SLFAISSGGALLSpevkQGLLElvpnitLVDAFG--SSEtgftGSGHSagsgpETGPFTRANPDT- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 378 dlfCLgtVGPLLNSCKVKIAEDGEILTKGsNVFLGYYKDEEKTREIY-TDDG--WLKTGDIG-YIKDGFLKITDRKKEIF 453
Cdd:cd05924 198 ---VV--LDDDGRVVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRAtVEADGTVTLLGRGSVCI 271
|
330 340 350
....*....|....*....|....*....|
gi 2537297151 454 KTsGGKYIIPQITENNLKQSRFIGEAMVVG 483
Cdd:cd05924 272 NT-GGEKVFPEEVEEALKSHPAVYDVLVVG 300
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
177-201 |
4.29e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 46.47 E-value: 4.29e-05
10 20
....*....|....*....|....*
gi 2537297151 177 LIYTSGTTGRPKGVMLSHKNILTNV 201
Cdd:PRK05850 165 LQYTSGSTRTPAGVMVSHRNVIANF 189
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
400-451 |
6.44e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 45.70 E-value: 6.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2537297151 400 GEILTKGSNVFLGYYKDEEKTREIY----------TDDG-WLKTGDIGYIKDGFLKITDRKKE 451
Cdd:PRK05850 398 GEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFISEGELFIVGRIKD 460
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
413-483 |
6.90e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 45.77 E-value: 6.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2537297151 413 YYKDEEKTREIY--TDDGWLKTGDIGYI-KDGFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFIGEAMVVG 483
Cdd:PRK13390 362 YLNDPEKTAAAQhpAHPFWTTVGDLGSVdEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAVHDVAVIG 434
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
354-449 |
7.00e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 45.79 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 354 GLKISEGYGMTETSPVIT-------------------VNGRTKDLfC----LGTVGPLLNsckvkiAED--GEIL-TKGS 407
Cdd:PRK13388 288 GCQVEDGYGSSEGAVIVVrepgtppgsigrgapgvaiYNPETLTE-CavarFDAHGALLN------ADEaiGELVnTAGA 360
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2537297151 408 NVFLGYYKDEEKTREiYTDDGWLKTGDIGYI-KDGFLKITDRK 449
Cdd:PRK13388 361 GFFEGYYNNPEATAE-RMRHGMYWSGDLAYRdADGWIYFAGRT 402
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
332-493 |
1.02e-04 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 44.98 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 332 LQLIICGSAALSENLCR-IFNAAGLKISEGYGMTE---------TSP--VITVNGRtkdlfclgtvgPLLNSCKVKIA-E 398
Cdd:PRK10946 302 LKLLQVGGARLSETLARrIPAELGCQLQQVFGMAEglvnytrldDSDerIFTTQGR-----------PMSPDDEVWVAdA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 399 DGEIL---------TKGSNVFLGYYKDEEKTREIYTDDGWLKTGDIGYI-KDGFLKITDRKK-EIfkTSGGKYIIPQITE 467
Cdd:PRK10946 371 DGNPLpqgevgrlmTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIdPDGYITVVGREKdQI--NRGGEKIAAEEIE 448
|
170 180 190
....*....|....*....|....*....|.
gi 2537297151 468 NNLKQSRFIGEAMVVG--D---GEKmPCALI 493
Cdd:PRK10946 449 NLLLRHPAVIHAALVSmeDelmGEK-SCAFL 478
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
30-226 |
1.02e-04 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 45.12 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 30 SWKKISTQSLIDQVNQVSRGllNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKF 109
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLHD--DLGVQAGDFVAIDLT-NSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 110 CLVsdkkiydkvhnikdqcpnitslftfdeiegalnwnkikkkgeeisnqqevenlknsiEPDRWVTLIYTSGTTGRPKG 189
Cdd:cd05937 82 VIV---------------------------------------------------------DPDDPAILIYTSGTTGLPKA 104
|
170 180 190
....*....|....*....|....*....|....*..
gi 2537297151 190 VMLSHKNILTNVLDCHVRFVMENDEkfRILSILPICH 226
Cdd:cd05937 105 AAISWRRTLVTSNLLSHDLNLKNGD--RTYTCMPLYH 139
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
177-452 |
1.35e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 44.72 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 177 LIYTSGTTGRPKGVMLSHKNILTNVLdcHVRFVMENDEKFRILSILPICH-------ILERMVDYVFMYKSYGIYF---A 246
Cdd:PRK07769 185 LQYTSGSTRIPAGVQITHLNLPTNVL--QVIDALEGQEGDRGVSWLPFFHdmglitvLLPALLGHYITFMSPAAFVrrpG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 247 EGMDKLAsnfqeVKPD----VILVVPRIVEKLYAsiynkgtsggwlkkqiflwALSVAKKFEPfkPASLShkiadflvfk 322
Cdd:PRK07769 263 RWIRELA-----RKPGgtggTFSAAPNFAFEHAA-------------------ARGLPKDGEP--PLDLS---------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 323 kwreavgnNLQLIICGSAALSENLCRIFNAA----GLK---ISEGYGMTE------TSP------VITVNgrtKDLFCLG 383
Cdd:PRK07769 307 --------NVKGLLNGSEPVSPASMRKFNEAfapyGLPptaIKPSYGMAEatlfvsTTPmdeeptVIYVD---RDELNAG 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 384 TVGPLLN---------SC-KVKIAE-----D------------GEILTKGSNVFLGYYKDEEKTREIY------------ 424
Cdd:PRK07769 376 RFVEVPAdapnavaqvSAgKVGVSEwavivDpetaselpdgqiGEIWLHGNNIGTGYWGKPEETAATFqnilksrlsesh 455
|
330 340 350
....*....|....*....|....*....|...
gi 2537297151 425 -----TDDGWLKTGDIGYIKDGFLKITDRKKEI 452
Cdd:PRK07769 456 aegapDDALWVRTGDYGVYFDGELYITGRVKDL 488
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
398-483 |
2.16e-04 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 43.98 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 398 EDGEILTKGSNVFLGYYKDeeKTREIYtdDGWLKTGDIGYIKD-GFLKITDRKKEIFkTSGGKYIIPQITENNLKQSRFI 476
Cdd:PRK13382 390 EVGTIFVRNDTQFDGYTSG--STKDFH--DGFMASGDVGYLDEnGRLFVVGRDDEMI-VSGGENVYPIEVEKTLATHPDV 464
|
....*..
gi 2537297151 477 GEAMVVG 483
Cdd:PRK13382 465 AEAAVIG 471
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
32-199 |
2.37e-04 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 44.09 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 32 KKISTQSLIDQVNQVSRGLLNYGINPQDRIALITSvNRSEWLIMDFAIQQIGAVSVPIYPTMSDDDLTFILNNSESKFCL 111
Cdd:PRK08279 61 QSISYAELNARANRYAHWAAARGVGKGDVVALLME-NRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 112 VSDkkiyDKVHnikdqcpnitslfTFDEIEGALN-----WnkiKKKGEEISNQQEVENLKNSIE--PDRW------VT-- 176
Cdd:PRK08279 140 VGE----ELVE-------------AFEEARADLArpprlW---VAGGDTLDDPEGYEDLAAAAAgaPTTNpasrsgVTak 199
|
170 180
....*....|....*....|....*..
gi 2537297151 177 ----LIYTSGTTGRPKGVMLSHKNILT 199
Cdd:PRK08279 200 dtafYIYTSGTTGLPKAAVMSHMRWLK 226
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
170-196 |
2.55e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 43.85 E-value: 2.55e-04
10 20
....*....|....*....|....*..
gi 2537297151 170 EPDRWVTLIYTSGTTGRPKGVMLSHKN 196
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRN 129
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
171-202 |
6.30e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 6.30e-04
10 20 30
....*....|....*....|....*....|..
gi 2537297151 171 PDRWVTLIYTSGTTGRPKGVMLSHKNILTNVL 202
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQL 3899
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
400-457 |
1.48e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 41.65 E-value: 1.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2537297151 400 GEILTKGSNVFLGYYKDEEKTREIY------------------TDDGWLKTGDIGYIKDGFLKITDRKKEIFKTSG 457
Cdd:PRK12476 430 GEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaaDDGTWLRTGDLGVYLDGELYITGRIADLIVIDG 505
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
354-443 |
2.86e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 40.43 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537297151 354 GLKISEGYGMTETSPVITvngRTKDLfCLGTVGPL-----------LNSCKVKIAED----------GEIL-TKGSNVFL 411
Cdd:PRK07867 290 GCVVVDGFGSTEGGVAIT---RTPDT-PPGALGPLppgvaivdpdtGTECPPAEDADgrllnadeaiGELVnTAGPGGFE 365
|
90 100 110
....*....|....*....|....*....|...
gi 2537297151 412 GYYKDEEKTREiYTDDGWLKTGDIGYI-KDGFL 443
Cdd:PRK07867 366 GYYNDPEADAE-RMRGGVYWSGDLAYRdADGYA 397
|
|
| |
