|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
2-743 |
0e+00 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 1312.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 2 SIILTFLALFVFLICVFPCITEDT-HKYVYSEICGKGANENESSVYCMKDHKKKNSLYVYKHIMKFFIDKYKSIPNEIAL 80
Cdd:PTZ00342 1 MIIYSLCLFFIYLIYVAPCCTQSLsKGKGYSEICEKATNENESSVYCMKDHKKKSSLYVYKHIMKLLLEKYKLNNNKIAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 81 VEHSYGEPQNYITYDNFFRKVSSFSHTLNTYEGKGIESKKYNEKQNNGIFKLLGIYGSNSINWLASDLSAMMSGVTTLVM 160
Cdd:PTZ00342 81 VEHSCGEPQNYITYGNFFKKVLSFSHSLNTYEGKGIPEKKYNEEQNNGKFKLLGLYGSNSINWLVADLACMLSGVTTLVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 161 HSKFSIDVIVDILNETQLEWLCLDLDLVEGLLNHINELPHLKNLIILDTLSKNKEINLNKEENNNDKKNKSSGNSTSV-- 238
Cdd:PTZ00342 161 HSKFSIDVIVDILNETKLEWLCLDLDLVEGLLERKNELPHLKKLIILDTLIKSKEININKEEKNNGSNVNNNGNKNNKee 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 239 -KGNDLSNMIEITCSGPLEYDKEKLKKYNELKKKCEKCGKKLMLFDDMTKTQTKKFTIKNEDPDFVTSIVYTSGTSGKPK 317
Cdd:PTZ00342 241 qKGNDLSNELEDISLGPLEYDKEKLEKIKDLKEKAKKLGISIILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 318 GVMLSNKNIYNQLFSLYNHSVRERYSFKNHLSYLPISHVFERTFAYSILMYGGTLNVWGKDINYFSKDIYNTKENIMGGV 397
Cdd:PTZ00342 321 GVMLSNKNLYNTVVPLCKHSIFKKYNPKTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 398 PKVFCRIYTNIMTEIDNLPSPKRRLVRKILSLRKSDHNGPFSKFLESIFHISKKIKDKVNPNLEIILSGGGKLSPDIAEE 477
Cdd:PTZ00342 401 PKVFNRIYTNIMTEINNLPPLKRFLVKKILSLRKSNNNGGFSKFLEGITHISSKIKDKVNPNLEVILNGGGKLSPKIAEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 478 FCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPIAPNTKYKVRTWETYKATDTLPKGELLIKSDSMFSGYFLEKE 557
Cdd:PTZ00342 481 LSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPISPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 558 CTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQGEYIETDLLNNLYSQISFINNCVVYGDDSMDGPLAIISVD 637
Cdd:PTZ00342 561 QTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 638 KYLLFLSLKDDNMLEMTGVNEQNYLDKLTDDNINNNIFLDYVKEKMLEVYKETNLNRYNIINNIYLTSKVWDTNNYLTPT 717
Cdd:PTZ00342 641 KYLLFKCLKDDNMLESTGINEKNYLEKLTDETINNNIYVDYVKGKMLEVYKKTNLNRYNIINDIYLTSKVWDTNNYLTPT 720
|
730 740
....*....|....*....|....*.
gi 124807131 718 FKVKRFYVFKDYAFFISQVKEIYNNK 743
Cdd:PTZ00342 721 FKVKRFYVFKDYAFFIDQVKKIYKNK 746
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
282-740 |
2.65e-85 |
|
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: 281.80 E-value: 2.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 282 FDDMTKTQTKKFTIKneDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLYnHSVRERYSF---KNHLSYLPISHVFE 358
Cdd:cd05927 97 FEKLGKKNKVPPPPP--KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVF-KILEILNKInptDVYISYLPLAHIFE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 359 RTFAYSILMYGGTLNVWGKDINYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIDNLPSPKRRLV-----RKILSLRKSD 433
Cdd:cd05927 174 RVVEALFLYHGAKIGFYSGDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFnfalnYKLAELRSGV 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 434 HNgpFSKFLESIfhISKKIKDKVNPNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIG 513
Cdd:cd05927 254 VR--ASPFWDKL--VFNKIKQALGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 514 GPIaPNTKYKVRTWE--TYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKG 591
Cdd:cd05927 330 GPL-PCAEVKLVDVPemNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKN 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 592 LVKLSQGEYIETDLLNNLYSQISFINNCVVYGDDSMDGPLAIISVDKYLLFLSLKDDNMLEMTgvneqnyldklTDDNIN 671
Cdd:cd05927 409 IFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKGGGTGS-----------FEELCK 477
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 672 NNIFLDYVKEKMLEVYKETNLNRYNIINNIYLTSKVWDT-NNYLTPTFKVKRFYVFKdyaFFISQVKEIY 740
Cdd:cd05927 478 NPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVeNGLLTPTFKLKRPQLKK---YYKKQIDEMY 544
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
75-743 |
2.98e-79 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 266.97 E-value: 2.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 75 PNEIALVEHSYGEPQnYITYDNFFRKVSSFSHTLntyEGKGIESkkyNEKqnngifklLGIYGSNSINWLASDLSAMMSG 154
Cdd:COG1022 25 PDRVALREKEDGIWQ-SLTWAEFAERVRALAAGL---LALGVKP---GDR--------VAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 155 VTTLVMHSKFSIDVIVDILNETQLEWL-CLDLDLVEGLLNHINELPHLKNLIILDtlsknkeinlnkeennndkknkssg 233
Cdd:COG1022 90 AVTVPIYPTSSAEEVAYILNDSGAKVLfVEDQEQLDKLLEVRDELPSLRHIVVLD------------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 234 nstsvkgndlsnmieitcsGPLEYDKEKLKKYNELkkkcekcgkkLMLFDDMTKTQTKKFTIKNEDPDFVTSIVYTSGTS 313
Cdd:COG1022 145 -------------------PRGLRDDPRLLSLDEL----------LALGREVADPAELEARRAAVKPDDLATIIYTSGTT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 314 GKPKGVMLSNKNIynqlfsLYN-HSVRERYSFK---NHLSYLPISHVFERTFAYSILMYGGTLNVWGkDINYFSKDIYNT 389
Cdd:COG1022 196 GRPKGVMLTHRNL------LSNaRALLERLPLGpgdRTLSFLPLAHVFERTVSYYALAAGATVAFAE-SPDTLAEDLREV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 390 KENIMGGVPKVFCRIYTNIMTEIDNLPSPKRRL--------VRKILSLRKSDHNGPFSKFLESIFH--ISKKIKDKVNPN 459
Cdd:COG1022 269 KPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLfrwalavgRRYARARLAGKSPSLLLRLKHALADklVFSKLREALGGR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 460 LEIILSGGGKLSPDIAEEFcYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPIaPNTKYKVrtwetykATDtlpkG 539
Cdd:COG1022 349 LRFAVSGGAALGPELARFF-RALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPL-PGVEVKI-------AED----G 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 540 ELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQGEYIETDLLNNLYSQISFINNC 619
Cdd:COG1022 416 EILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQA 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 620 VVYGDDsMDGPLAIISVDkyllFLSLKddNMLEMTGVNEQNYldkltDDNINNNIFLDYVKEkmlEVyKETN--LNRYNI 697
Cdd:COG1022 496 VVVGDG-RPFLAALIVPD----FEALG--EWAEENGLPYTSY-----AELAQDPEVRALIQE---EV-DRANagLSRAEQ 559
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 124807131 698 INNIYLTSKVWDT-NNYLTPTFKVKRFYVFKDYAffiSQVKEIYNNK 743
Cdd:COG1022 560 IKRFRLLPKEFTIeNGELTPTLKLKRKVILEKYA---DLIEALYAGA 603
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
295-722 |
3.45e-71 |
|
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: 242.51 E-value: 3.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 295 IKNEDPDFVTSIVYTSGTSGKPKGVMLSNKN----IYNQLFSLYNH-SVRERYsfknhLSYLPISHVFERTFAYSILMYG 369
Cdd:cd17639 82 FTDGKPDDLACIMYTSGSTGNPKGVMLTHGNlvagIAGLGDRVPELlGPDDRY-----LAYLPLAHIFELAAENVCLYRG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 370 GTlnvwgkdINYFSK-------------DIYNTKENIMGGVPKVFCRIYTNIMTEIDNLPSPKRRLVRKILSLR-KSDHN 435
Cdd:cd17639 157 GT-------IGYGSPrtltdkskrgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKlKALKE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 436 GPFSKFL-ESIFhisKKIKDKVNPNLEIILSGGGKLSPDiAEEFcylLNIKYC---QGYGLTETAGAilGNHADDEHFEY 511
Cdd:cd17639 230 GPGTPLLdELVF---KKVRAALGGRLRYMLSGGAPLSAD-TQEF---LNIVLCpviQGYGLTETCAG--GTVQDPGDLET 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 512 -IGGPIAPNTKYKVRTWETYK-ATDT-LPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDR 588
Cdd:cd17639 301 gRVGPPLPCCEIKLVDWEEGGySTDKpPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDR 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 589 SKGLVKLSQGEYIETDLLNNLYSQISFINNCVVYGDDSMDGPLAIISVDKYLLflslkddnmlemTGVNEQNYLDKLTDD 668
Cdd:cd17639 381 KKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHL------------TKLAEKHGVINSEWE 448
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 124807131 669 NI-NNNIFLDYVKEKMLEVYKETNLNRYNIINNIYLTSKVWdT--NNYLTPTFKVKR 722
Cdd:cd17639 449 ELcEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW-TpeNGLVTAAQKLKR 504
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
298-722 |
4.08e-59 |
|
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: 207.83 E-value: 4.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 298 EDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLfslynHSVRERYSFKN---HLSYLPISHVFERTFA-YSILMYGGTLN 373
Cdd:cd05907 84 EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNA-----LALAERLPATEgdrHLSFLPLAHVFERRAGlYVPLLAGARIY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 374 VWGkDINYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIdnLPSPKRRLVRKIlslrksdhngpfskflesifhiskkik 453
Cdd:cd05907 159 FAS-SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKA--VPGLKRKLFDLA--------------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 454 dkVNPNLEIILSGGGKLSPDIAEeFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPIaPNTKYKVRtwetykat 533
Cdd:cd05907 209 --VGGRLRFAASGGAPLPAELLH-FFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPL-PGVEVRIA-------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 534 dtlPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQGEYIETDLLNNLYSQI 613
Cdd:cd05907 277 ---DDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 614 SFINNCVVYGDDsMDGPLAIISVDkyllFLSLKDdnMLEMTGVNEQNYLDKLTDDNINNNIfldyvkEKMLEVYKETnLN 693
Cdd:cd05907 354 PLISQAVVIGDG-RPFLVALIVPD----PEALEA--WAEEHGIAYTDVAELAANPAVRAEI------EAAVEAANAR-LS 419
|
410 420 430
....*....|....*....|....*....|
gi 124807131 694 RYNIINNIYLTSKVWD-TNNYLTPTFKVKR 722
Cdd:cd05907 420 RYEQIKKFLLLPEPFTiENGELTPTLKLKR 449
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
289-744 |
1.99e-57 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 208.34 E-value: 1.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 289 QTKKFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLYN--HSVRERYSFKN-HLSYLPISHVFERTFAYSI 365
Cdd:PLN02614 211 EGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRllKSANAALTVKDvYLSYLPLAHIFDRVIEECF 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 366 LMYGGTLNVWGKDINYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIDNLPSPKRRLVRKILS-----LRKSDHNGPFSK 440
Cdd:PLN02614 291 IQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSykfgnMKKGQSHVEASP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 441 FLESIfhISKKIKDKVNPNLEIILSGGGKLSPDIaEEFcylLNIKYC----QGYGLTETAGAILGNHADDEHFEYIGGPI 516
Cdd:PLN02614 371 LCDKL--VFNKVKQGLGGNVRIILSGAAPLASHV-ESF---LRVVACchvlQGYGLTESCAGTFVSLPDELDMLGTVGPP 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 517 APNTKYKVRTWE--TYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDdGYFKTGDIVQINDNGSVTFLDRSKGLVK 594
Cdd:PLN02614 445 VPNVDIRLESVPemEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPNGSMKIIDRKKNIFK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 595 LSQGEYIETDLLNNLYSQISFINNCVVYGDdsmdgplaiiSVDKYLLFLSLKDDNMLEMTGVneQNYLDKLTDDNINNNI 674
Cdd:PLN02614 524 LSQGEYVAVENIENIYGEVQAVDSVWVYGN----------SFESFLVAIANPNQQILERWAA--ENGVSGDYNALCQNEK 591
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124807131 675 FLDYVKEKMLEVYKETNLNRYNIINNIYLTSKVWDTN-NYLTPTFKVKRFYVFKDYAFFISQVKEIYNNKL 744
Cdd:PLN02614 592 AKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMErDLLTPTFKKKRPQLLKYYQSVIDEMYKTTNEKL 662
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
303-736 |
9.75e-54 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 197.76 E-value: 9.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 303 VTSIVYTSGTSGKPKGVMLSNKNIY------NQLFSLYNHSVRERYSFknhLSYLPISHVFERTFAYSILMYGGTLNVWG 376
Cdd:PLN02861 222 ICTIMYTSGTTGEPKGVILTNRAIIaevlstDHLLKVTDRVATEEDSY---FSYLPLAHVYDQVIETYCISKGASIGFWQ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 377 KDINYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIDNLPSPKRRLVR-----KILSLRKSDHNGPFSKFLESIfhISKK 451
Cdd:PLN02861 299 GDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDfaynyKLGNLRKGLKQEEASPRLDRL--VFDK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 452 IKDKVNPNLEIILSGGGKLsPDIAEEFcylLNIKYC----QGYGLTETAGAILGNHADDehFEYIGGPIAPNTKYKVRTW 527
Cdd:PLN02861 377 IKEGLGGRVRLLLSGAAPL-PRHVEEF---LRVTSCsvlsQGYGLTESCGGCFTSIANV--FSMVGTVGVPMTTIEARLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 528 ET----YKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDdGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQGEYIET 603
Cdd:PLN02861 451 SVpemgYDALSDVPRGEICLRGNTLFSGYHKRQDLTEEVLID-GWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAV 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 604 DLLNNLYSQISFINNCVVYGDdsmdgplaiiSVDKYLLFLSLKDDNMLEMTGVNEQNyldklTDDN---INNNIFLDYVK 680
Cdd:PLN02861 530 ENLENTYSRCPLIASIWVYGN----------SFESFLVAVVVPDRQALEDWAANNNK-----TGDFkslCKNLKARKYIL 594
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 124807131 681 EKMLEVYKETNLNRYNIINNIYLTSKVWDTNNYL-TPTFKVKRFYVFKDYAFFISQV 736
Cdd:PLN02861 595 DELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLiTPTFKLKRPQLLKYYKDCIDQL 651
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
300-742 |
1.00e-52 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 195.03 E-value: 1.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 300 PDFVTSIVYTSGTSGKPKGVMLSNKN--IYNQLFSLYNHSVRERYSFKN-HLSYLPISHVFERTFAYSILMYGGTLNVWG 376
Cdd:PLN02430 219 PLDICTIMYTSGTSGDPKGVVLTHEAvaTFVRGVDLFMEQFEDKMTHDDvYLSFLPLAHILDRMIEEYFFRKGASVGYYH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 377 KDINYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIDNLpSPKRRLVRKILSLRK---------SDHNGPFSKFLESifh 447
Cdd:PLN02430 299 GDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQEL-NPRRRLIFNALYKYKlawmnrgysHKKASPMADFLAF--- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 448 isKKIKDKVNPNLEIILSGGGKLSPDIaEEFcylLNIKYC----QGYGLTETAGAILGNHADDehFEYIGGPIAPNTKYK 523
Cdd:PLN02430 375 --RKVKAKLGGRLRLLISGGAPLSTEI-EEF---LRVTSCafvvQGYGLTETLGPTTLGFPDE--MCMLGTVGAPAVYNE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 524 VRTWET----YKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDdGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQGE 599
Cdd:PLN02430 447 LRLEEVpemgYDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVMKD-GWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGE 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 600 YIETDLLNNLYSQISFINNCVVYGDDSMDGPLAIISvdkyllflslkddnmlemtgVNEQNyLDKLTDDNINNNIF---- 675
Cdd:PLN02430 526 YVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVV--------------------PNEEN-TNKWAKDNGFTGSFeelc 584
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124807131 676 -LDYVKEKMLEVYKET----NLNRYNIINNIYLTSKVWDTNNYL-TPTFKVKRFYVFKDYAffiSQVKEIYNN 742
Cdd:PLN02430 585 sLPELKEHILSELKSTaeknKLRGFEYIKGVILETKPFDVERDLvTATLKKRRNNLLKYYQ---VEIDEMYRK 654
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
75-596 |
3.97e-51 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 184.82 E-value: 3.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 75 PNEIALVEHSYgepqNYITYDNFFRKVSSFSHTLntyegkgieskkynekQNNGIFK--LLGIYGSNSINWLASDLSAMM 152
Cdd:pfam00501 9 PDKTALEVGEG----RRLTYRELDERANRLAAGL----------------RALGVGKgdRVAILLPNSPEWVVAFLACLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 153 SGVTTLVMHSKFSIDVIVDILNETQLEWL-CLDLDLVEGLLNHINELPHLKNLIILDTLSKNKEINLNKEENNNDKKNKS 231
Cdd:pfam00501 69 AGAVYVPLNPRLPAEELAYILEDSGAKVLiTDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 232 SgnsTSVKGNDLSNMIeitcsgpleydkeklkkynelkkkcekcgkklmlfddmtktqtkkftiknedpdfvtsivYTSG 311
Cdd:pfam00501 149 P---PPPDPDDLAYII------------------------------------------------------------YTSG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 312 TSGKPKGVMLSNKNIYNQLFSLYNHSVRERY--SFKNHLSYLPISHVFERTFA-YSILMYGGTLNVWGK----DINYFSK 384
Cdd:pfam00501 166 TTGKPKGVMLTHRNLVANVLSIKRVRPRGFGlgPDDRVLSTLPLFHDFGLSLGlLGPLLAGATVVLPPGfpalDPAALLE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 385 DIYNTKENIMGGVPkvfcriytnimteidnlpspkrRLVRKILSlrksdhngpfskflesifhiSKKIKDKVNPNLEIIL 464
Cdd:pfam00501 246 LIERYKVTVLYGVP----------------------TLLNMLLE--------------------AGAPKRALLSSLRLVL 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 465 SGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIG--GPIAPNTKYKVRTWET--YKATDTlpKGE 540
Cdd:pfam00501 284 SGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDLRSLGsvGRPLPGTEVKIVDDETgePVPPGE--PGE 361
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 124807131 541 LLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLS 596
Cdd:pfam00501 362 LCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
300-722 |
9.41e-51 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 189.15 E-value: 9.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 300 PDFVTSIVYTSGTSGKPKGVMLSNKNI------YNQLFSLYNHSVrerysfknHLSYLPISHVFERTFAYSILMYGGTLN 373
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLianvagSSLSTKFYPSDV--------HISYLPLAHIYERVNQIVMLHYGVAVG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 374 VWGKDINYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIDNLPSPKRRLVRKIL-SLRKSDHNG-PFSKFLESIfhISKK 451
Cdd:PLN02736 292 FYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYnAKKQALENGkNPSPMWDRL--VFNK 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 452 IKDKVNPNLEIILSGGGKLSPDIAEefcyLLNIkyC------QGYGLTETAGAILGNHADDEHFEYIGGPIaPNTKYK-V 524
Cdd:PLN02736 370 IKAKLGGRVRFMSSGASPLSPDVME----FLRI--CfggrvlEGYGMTETSCVISGMDEGDNLSGHVGSPN-PACEVKlV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 525 RTWE-TYKATDT-LPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQGEYIE 602
Cdd:PLN02736 443 DVPEmNYTSEDQpYPRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIA 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 603 TDLLNNLYSQISFINNCVVYGDDSMDGPLAIISVDKYLLFLSLKDDNMlemtgvnEQNYLDKLTDDninnNIFLDYVKEK 682
Cdd:PLN02736 523 PEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGI-------KYEDLKQLCND----PRVRAAVLAD 591
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 124807131 683 MLEVYKETNLNRYNIINNIYLTSKVWDT-NNYLTPTFKVKR 722
Cdd:PLN02736 592 MDAVGREAQLRGFEFAKAVTLVPEPFTVeNGLLTPTFKVKR 632
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
292-725 |
3.94e-50 |
|
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: 183.33 E-value: 3.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 292 KFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLYNH---SVRERYsfknhLSYLPISHVFERTFAYSILMY 368
Cdd:cd17640 79 VALVVENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIvppQPGDRF-----LSILPIWHSYERSAEYFIFAC 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 369 GGTLNVwgKDINYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIDNLPSPKRRLVRKILSLRksdhngpfskflesifhi 448
Cdd:cd17640 154 GCSQAY--TSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFLSGG------------------ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 449 skkikdkvnpNLEIILSGGGKLsPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPIaPNTKYKVRTWE 528
Cdd:cd17640 214 ----------IFKFGISGGGAL-PPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPL-PGTEIKIVDPE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 529 TYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQGEYIETDLLNN 608
Cdd:cd17640 282 GNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 609 LYSQISFINNCVVYGDDsmdgplaiisvDKYLLFLSLKDDNMLEmTGVNEQNY--LDKLTDDNINNNIFLDYVKEKMLEV 686
Cdd:cd17640 362 ALMRSPFIEQIMVVGQD-----------QKRLGALIVPNFEELE-KWAKESGVklANDRSQLLASKKVLKLYKNEIKDEI 429
|
410 420 430
....*....|....*....|....*....|....*....
gi 124807131 687 YKETNLNRYNIINNIYLTSKVWDTNNYLTPTFKVKRFYV 725
Cdd:cd17640 430 SNRPGFKSFEQIAPFALLEEPFIENGEMTQTMKIKRNVV 468
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
293-689 |
1.18e-38 |
|
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: 150.29 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 293 FTIKNEDpdfVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLynhSVRERYSFKNH-LSYLPISHVFERTFAYSILMYGGT 371
Cdd:cd05914 84 FVSDEDD---VALINYTSGTTGNSKGVMLTYRNIVSNVDGV---KEVVLLGKGDKiLSILPLHHIYPLTFTLLLPLLNGA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 372 LNVWGKDIN---YFSKDIYNTKENIMGGVPKVFCRIYtnIMTEID--NLPSPKRRLVRKILSLrksdhngpfsKFLESIF 446
Cdd:cd05914 158 HVVFLDKIPsakIIALAFAQVTPTLGVPVPLVIEKIF--KMDIIPklTLKKFKFKLAKKINNR----------KIRKLAF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 447 hisKKIKDKVNPNLEIILSGGGKLSPDIaEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPIapnTKYKVRT 526
Cdd:cd05914 226 ---KKVHEAFGGNIKEFVIGGAKINPDV-EEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVI---DGVEVRI 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 527 WETYKATDTlpkGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQG-----EYI 601
Cdd:cd05914 299 DSPDPATGE---GEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGkniypEEI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 602 ETDLLNNLYSQISFinncvvygddsmdgplaIISVDKYLLFLSLKDDNMLEMTGVNEQNYLDKLTDDNIN--NNIFLDYV 679
Cdd:cd05914 376 EAKINNMPFVLESL-----------------VVVQEKKLVALAYIDPDFLDVKALKQRNIIDAIKWEVRDkvNQKVPNYK 438
|
410
....*....|
gi 124807131 680 KEKMLEVYKE 689
Cdd:cd05914 439 KISKVKIVKE 448
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
299-729 |
1.32e-38 |
|
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: 150.70 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLYNH-SVRERysfKNHLSYLPISHVFERTFAYSILMYGGTLNVWGK 377
Cdd:cd05932 135 FPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHiGTEEN---DRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 378 DINYFSKDIYNTKENIMGGVPKVFCRIYTNImteIDNLPSPKRRLVRKIlslrksdhngPFskflesifhISKKIKDKVN 457
Cdd:cd05932 212 SLDTFVEDVQRARPTLFFSVPRLWTKFQQGV---QDKIPQQKLNLLLKI----------PV---------VNSLVKRKVL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 458 PNL-----EIILSGGGKLSPDIAEEFCYL-LNIkyCQGYGLTETAGAILGNHADDEHFEYIGGPIaPNTKYKVRtwetyk 531
Cdd:cd05932 270 KGLgldqcRLAGCGSAPVPPALLEWYRSLgLNI--LEAYGMTENFAYSHLNYPGRDKIGTVGNAG-PGVEVRIS------ 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 532 atdtlPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQGEYIETDLLNNLYS 611
Cdd:cd05932 341 -----EDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 612 QISFINNCVVYGdDSMDGPLAIIsvdkyllflslkddnMLEMTGVNEQNYLDKltddninnniflDYVKEKMLEVYKETN 691
Cdd:cd05932 416 EHDRVEMVCVIG-SGLPAPLALV---------------VLSEEARLRADAFAR------------AELEASLRAHLARVN 467
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 124807131 692 --LNRYNIINNIYLTSKVWDTNN-YLTPTFKVKRFYVFKDY 729
Cdd:cd05932 468 stLDSHEQLAGIVVVKDPWSIDNgILTPTLKIKRNVLEKAY 508
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
306-601 |
1.66e-37 |
|
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: 143.58 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIYNQLFSLYNH-SVRERYSFknhLSYLPISHVFERTFAYSILMYGGTLNVWGK-DINYFS 383
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNLLAAAAALAASgGLTEGDVF---LSTLPLFHIGGLFGLLGALLAGGTVVLLPKfDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 384 KDIYNTKENIMGGVPKVFCRIytnimteIDNLPSPKRRLvrkilslrksdhngpfskflesifhiskkikdkvnPNLEII 463
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARL-------LKAPESAGYDL-----------------------------------SSLRAL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 464 LSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEY--IGGPIaPNTKYKVRTWEtykaTDTLP---K 538
Cdd:cd04433 120 VSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDARKPgsVGRPV-PGVEVRIVDPD----GGELPpgeI 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124807131 539 GELLIKSDSMFSGYFLEKEcTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKlSQGEYI 601
Cdd:cd04433 195 GELVVRGPSVMKGYWNNPE-ATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENV 255
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
298-735 |
3.26e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 146.27 E-value: 3.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 298 EDPDFVTSIVYTSGTSGKPKGVMLSNKNIY-------NQLFSLYN-HSVRERYsfknhLSYLPISHVFERTfAYSILMYG 369
Cdd:PTZ00216 261 ENNDDLALIMYTSGTTGDPKGVMHTHGSLTagilaleDRLNDLIGpPEEDETY-----CSYLPLAHIMEFG-VTNIFLAR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 370 GTLNVWGKD---INYFSK---DIYNTKENIMGGVPKVFCRIYTNIMteiDNLPSP---KRRLVRKILSLR----KSDHNG 436
Cdd:PTZ00216 335 GALIGFGSPrtlTDTFARphgDLTEFRPVFLIGVPRIFDTIKKAVE---AKLPPVgslKRRVFDHAYQSRlralKEGKDT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 437 PFskFLESIFhisKKIKDKVNPNLEIILSGGGKLSPDiAEEFcylLNIKY---CQGYGLTETA--GAI--LGNhaddehF 509
Cdd:PTZ00216 412 PY--WNEKVF---SAPRAVLGGRVRAMLSGGGPLSAA-TQEF---VNVVFgmvIQGWGLTETVccGGIqrTGD------L 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 510 EYIG-GPIAPNTKYKVRTWETYKATDT-LPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLD 587
Cdd:PTZ00216 477 EPNAvGQLLKGVEMKLLDTEEYKHTDTpEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIG 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 588 RSKGLVKLSQGEYIETDLLNNLYSQISF-INNCV---VYGDDSmdgplaiisvdkYLLFLSLKDD----NMLEMTGVnEQ 659
Cdd:PTZ00216 557 RVKALAKNCLGEYIALEALEALYGQNELvVPNGVcvlVHPARS------------YICALVLTDEakamAFAKEHGI-EG 623
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124807131 660 NYLDKLTDDNinnniFLDYVKEKMLEVYKETNLNRYNIINNIYLTSKVWD-TNNYLTPTFKVKRFYVFKDYAFFISQ 735
Cdd:PTZ00216 624 EYPAILKDPE-----FQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTpENGVLTAAMKLKRRVIDERYADLIKE 695
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
302-599 |
6.61e-34 |
|
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: 135.71 E-value: 6.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 302 FVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSL---YNHSVRERYsfknhLSYLPISHVF-ERTFAYSILMYGGTLNVWGK 377
Cdd:COG0318 101 VTALILYTSGTTGRPKGVMLTHRNLLANAAAIaaaLGLTPGDVV-----LVALPLFHVFgLTVGLLAPLLAGATLVLLPR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 378 -DINYFSKDIYNTKENIMGGVPKVFCRIytnimteIDNLPSPKRRLvrkilslrksdhngpfskflesifhiskkikdkv 456
Cdd:COG0318 176 fDPERVLELIERERVTVLFGVPTMLARL-------LRHPEFARYDL---------------------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 457 nPNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNhADDEHFEYIG--GPIAPNTKYKVRTWEtykaTD 534
Cdd:COG0318 215 -SSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVN-PEDPGERRPGsvGRPLPGVEVRIVDED----GR 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124807131 535 TLP---KGELLIKSDSMFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSqGE 599
Cdd:COG0318 289 ELPpgeVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GE 354
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
299-730 |
1.68e-33 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 137.94 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDF-----VTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLYNhSVRERYSFKNHLSYLPISHVFERTfAYSILM------ 367
Cdd:PLN02387 243 DPDLpspndIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMT-VVPKLGKNDVYLAYLPLAHILELA-AESVMAavgaai 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 368 -YGG--TLNVWGKDINYFSK-DIYNTKENIMGGVPKVFCRIYTNIMTEIDNlpspKRRLVRKILSL----RKSDHNGpfS 439
Cdd:PLN02387 321 gYGSplTLTDTSNKIKKGTKgDASALKPTLMTAVPAILDRVRDGVRKKVDA----KGGLAKKLFDIaykrRLAAIEG--S 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 440 KF----LESIFH---ISKKIKDKVNPNLEIILSGGGKLSPDiAEEFcylLNIkyC------QGYGLTET-AGAILGNHaD 505
Cdd:PLN02387 395 WFgawgLEKLLWdalVFKKIRAVLGGRIRFMLSGGAPLSGD-TQRF---INI--ClgapigQGYGLTETcAGATFSEW-D 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 506 DEHFEYIGGPIaPNTKYKVRTWET--YKATDT-LPKGELLIKSDSMFSGYFLEKECTKNAFTDDG----YFKTGDIVQIN 578
Cdd:PLN02387 468 DTSVGRVGPPL-PCCYVKLVSWEEggYLISDKpMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFH 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 579 DNGSVTFLDRSKGLVKLSQGEYIETDLLNNLYSQISFINNCVVYGDDSMDGPLAIISVDKYLLflslkdDNMLEMTGVNE 658
Cdd:PLN02387 547 PDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQAL------EKWAKKAGIDY 620
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124807131 659 QNYLDKLTDDninnniflDYVKE---KMLEVYKETNLNRYNIINNIYLTSKVWDTNNYL-TPTFKVKRFYVFKDYA 730
Cdd:PLN02387 621 SNFAELCEKE--------EAVKEvqqSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLvTAALKLKREQIRKKFK 688
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
299-625 |
1.64e-30 |
|
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: 127.54 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQlfSLYNHSVRERYSFKNHLSYLPISHVFERTFAYSILMYGGTLNVWGKD 378
Cdd:cd17641 156 KGEDVAVLCTTSGTTGKPKLAMLSHGNFLGH--CAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 379 INYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIDNLPSPKRRLVRKILSL-------RKSDHNGPFSKFLESIFH---I 448
Cdd:cd17641 234 PETMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLglraldrGKRGRPVSLWLRLASWLAdalL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 449 SKKIKDKVN-PNLEIILSGGGKLSPDIAEEFCYL-LNIKycQGYGLTETAGAILGNHADDEHFEYIGGPIaPNTKykVRT 526
Cdd:cd17641 314 FRPLRDRLGfSRLRSAATGGAALGPDTFRFFHAIgVPLK--QLYGQTELAGAYTVHRDGDVDPDTVGVPF-PGTE--VRI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 527 WETykatdtlpkGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQGEYIETDLL 606
Cdd:cd17641 389 DEV---------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFI 459
|
330
....*....|....*....
gi 124807131 607 NNLYSQISFINNCVVYGDD 625
Cdd:cd17641 460 ENKLKFSPYIAEAVVLGAG 478
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
282-593 |
3.77e-30 |
|
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: 124.98 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 282 FDDMTKTQTKKFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNIY---NQLFSLYNHSVRERysfKNHLSYLPISHVFE 358
Cdd:cd05936 106 FTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVanaLQIKAWLEDLLEGD---DVVLAALPLFHVFG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 359 RTFAYSILMYGGTLNVW---GKDINYFsKDIYNTKENIMGGVPKvfcrIYTNIMTeidnlpspkrrlvrkilslrksdhn 435
Cdd:cd05936 183 LTVALLLPLALGATIVLiprFRPIGVL-KEIRKHRVTIFPGVPT----MYIALLN------------------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 436 gpFSKFLESIFhiskkikdkvnPNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFE-YIGG 514
Cdd:cd05936 233 --APEFKKRDF-----------SSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPgSIGI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 515 PIaPNTKYKVRTwetyKATDTLPK---GELLIKSDSMFSGYFLEKECTKNAFTdDGYFKTGDIVQINDNGSVTFLDRSKG 591
Cdd:cd05936 300 PL-PGTEVKIVD----DDGEELPPgevGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKD 373
|
..
gi 124807131 592 LV 593
Cdd:cd05936 374 MI 375
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
293-594 |
4.11e-30 |
|
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: 125.02 E-value: 4.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 293 FTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNIYN-----QLFSLYNHSVRERYsfknhLSYLPISHVFERTFAYSILM 367
Cdd:cd05911 138 PPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIAnlsqvQTFLYGNDGSNDVI-----LGFLPLYHIYGLFTTLASLL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 368 YGGTLNVWGK-DINYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIDNLPSpkrrlvrkilslrksdhngpfskflesif 446
Cdd:cd05911 213 NGATVIIMPKfDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSS----------------------------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 447 hiskkikdkvnpnLEIILSGGGKLSPDIAEEFCYLLNIKYC-QGYGLTETAGAILGNHADDEHFEYIGGPIaPNTKYKVR 525
Cdd:cd05911 264 -------------LRVILSGGAPLSKELQELLAKRFPNATIkQGYGMTETGGILTVNPDGDDKPGSVGRLL-PNVEAKIV 329
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124807131 526 TWETYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVK 594
Cdd:cd05911 330 DDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIK 398
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
299-634 |
1.16e-29 |
|
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: 124.88 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNqlFSLYNHSVRERYSFKN-HLSYLPISHVFERTFAYSILMYGGTLNVWGK 377
Cdd:cd17632 221 DDDPLALLIYTSGSTGTPKGAMYTERLVAT--FWLKVSSIQDIRPPASiTLNFMPMSHIAGRISLYGTLARGGTAYFAAA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 378 -DINYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIDnlpspkRRLVrkilslrksdhNGPFSKFLESifHISKKIKDKV 456
Cdd:cd17632 299 sDMSTLFDDLALVRPTELFLVPRVCDMLFQRYQAELD------RRSV-----------AGADAETLAE--RVKAELRERV 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 457 -NPNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNhaddehfeYIGGPiaPNTKYK-VRTWET-YKAT 533
Cdd:cd17632 360 lGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVILDG--------VIVRP--PVLDYKlVDVPELgYFRT 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 534 DT-LPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQGEYIETDLLNNLYSQ 612
Cdd:cd17632 430 DRpHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAA 509
|
330 340
....*....|....*....|..
gi 124807131 613 ISFINNCVVYGDDSMDGPLAII 634
Cdd:cd17632 510 SPLVRQIFVYGNSERAYLLAVV 531
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
300-594 |
1.67e-27 |
|
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: 117.34 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 300 PDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLfSLYNHSVRERYSFKN-HLSYLPISHVFERT-FAYSILMYGGTLNVWGK 377
Cdd:cd05904 157 QDDVAALLYSSGTTGRSKGVMLTHRNLIAMV-AQFVAGEGSNSDSEDvFLCVLPMFHIYGLSsFALGLLRLGATVVVMPR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 378 -DINYFSKDIYNTKENIMGGVPKVfcriytnimteidnlpspkrrlvrkILSLRKSDHNGPFSKflesifhiskkikdkv 456
Cdd:cd05904 236 fDLEELLAAIERYKVTHLPVVPPI-------------------------VLALVKSPIVDKYDL---------------- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 457 nPNLEIILSGGGKLSPDIAEEFCYLL-NIKYCQGYGLTETAGAILGNHADDEHFEYIG--GPIAPNTKYKVRTWETYKAt 533
Cdd:cd05904 275 -SSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGsvGRLVPNVEAKIVDPETGES- 352
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124807131 534 dtLPK---GELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVK 594
Cdd:cd05904 353 --LPPnqtGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIK 414
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
282-601 |
3.69e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 116.44 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 282 FDDMTKTQTKKFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNiynqlfsLYNHSVRERYSFKNH-----LSYLPISHV 356
Cdd:PRK06187 148 YEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRN-------LFLHSLAVCAWLKLSrddvyLVIVPMFHV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 357 FERTFAYSILMYGGTLNVWGK-DINYFSKDIYNTKENIMGGVPkvfcriytNIMTEIDNLPSPKRRlvrKILSLRksdhn 435
Cdd:PRK06187 221 HAWGLPYLALMAGAKQVIPRRfDPENLLDLIETERVTFFFAVP--------TIWQMLLKAPRAYFV---DFSSLR----- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 436 gpfskflesifhiskkikdkvnpnleIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDE---HFEYI 512
Cdd:PRK06187 285 --------------------------LVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQlpgQWTKR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 513 G--GPIAPNTKYKVRTWEtykaTDTLPK-----GELLIKSDSMFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTF 585
Cdd:PRK06187 339 RsaGRPLPGVEARIVDDD----GDELPPdggevGEIIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIDEDGYLYI 413
|
330
....*....|....*.
gi 124807131 586 LDRSKGLVKlSQGEYI 601
Cdd:PRK06187 414 TDRIKDVII-SGGENI 428
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
293-623 |
8.82e-26 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 110.90 E-value: 8.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 293 FTIKNEDPDF--VTSIVYTSGTSGKPKGVMLSNKNIYNQLF-SLYNHSVRERysfKNHLSYLPISHVFertfAYSILM-- 367
Cdd:cd05912 67 FQLKDSDVKLddIATIMYTSGTTGKPKGVQQTFGNHWWSAIgSALNLGLTED---DNWLCALPLFHIS----GLSILMrs 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 368 --YGGTLNVWGK-DINYFSKDIYNTKENIMGGVPKVFCRIytnimteIDNLPSPkrrlvrkilslrksdhngpfskfles 444
Cdd:cd05912 140 viYGMTVYLVDKfDAEQVLHLINSGKVTIISVVPTMLQRL-------LEILGEG-------------------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 445 ifhiskkikdkVNPNLEIILSGGGKLSPDIAEEfCYLLNIKYCQGYGLTETAGAILGNHADDEHfEYIG--GPIAPNTKY 522
Cdd:cd05912 187 -----------YPNNLRCILLGGGPAPKPLLEQ-CKEKGIPVYQSYGMTETCSQIVTLSPEDAL-NKIGsaGKPLFPVEL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 523 KVRTWETYKATDtlpkGELLIKSDSMFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTFLDRSKGLVkLSQGEYIE 602
Cdd:cd05912 254 KIEDDGQPPYEV----GEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIY 327
|
330 340
....*....|....*....|.
gi 124807131 603 TDLLNNLYSQISFINNCVVYG 623
Cdd:cd05912 328 PAEIEEVLLSHPAIKEAGVVG 348
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
306-634 |
1.01e-24 |
|
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: 108.15 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIYNQLFSLynhsVRE-RYSFKNHLSY-LPISHVFERTFAYSI-LMYGGTLNVWGKdinyF 382
Cdd:cd05941 94 ILYTSGTTGRPKGVVLTHANLAANVRAL----VDAwRWTEDDVLLHvLPLHHVHGLVNALLCpLFAGASVEFLPK----F 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 383 SKDIYNTKE-----NIMGGVPKvfcrIYTnimteidnlpspkrRLVRkilslrksdhnGPFSKFLESIFHISKKIKdkvn 457
Cdd:cd05941 166 DPKEVAISRlmpsiTVFMGVPT----IYT--------------RLLQ-----------YYEAHFTDPQFARAAAAE---- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 458 pNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETaGAILGNHADDE-HFEYIGGPIaPNTKYKVRTWETYKATDTL 536
Cdd:cd05941 213 -RLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEI-GMALSNPLDGErRPGTVGMPL-PGVQARIVDEETGEPLPRG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 537 PKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLV------KLSQGEyIETDLLnnly 610
Cdd:cd05941 290 EVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIiksggyKVSALE-IERVLL---- 364
|
330 340
....*....|....*....|....*..
gi 124807131 611 sQISFINNCVVYGDDSMD---GPLAII 634
Cdd:cd05941 365 -AHPGVSECAVIGVPDPDwgeRVVAVV 390
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
295-730 |
1.47e-24 |
|
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: 108.98 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 295 IKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLYNH-SVRERYSFKNHL-SYLPISHVFERTF-AYSILMYGGT 371
Cdd:cd05933 144 ISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHmDLRPATVGQESVvSYLPLSHIAAQILdIWLPIKVGGQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 372 lnVWGKDINYFSKDIYNT----KENIMGGVPkvfcRIYTNIMTEIDNLPSPKRRLVRKILSLRKS---DHN--------G 436
Cdd:cd05933 224 --VYFAQPDALKGTLVKTlrevRPTAFMGVP----RVWEKIQEKMKAVGAKSGTLKRKIASWAKGvglETNlklmggesP 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 437 PFSKFLESIFHISKKIKDKVN-PNLEIILSGGGKLSPDIAEEFCYLlNIKYCQGYGLTETAGAILGNHADDEHFeYIGGP 515
Cdd:cd05933 298 SPLFYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFFLSL-NIPIMELYGMSETSGPHTISNPQAYRL-LSCGK 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 516 IAPNTKYKVRTwetykaTDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKL 595
Cdd:cd05933 376 ALPGCKTKIHN------PDADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIIT 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 596 SQGE-----YIEtdllNNLYSQISFINNCVVYGDDSmdgplaiisvdKYL-LFLSLKdDNMLEMTGVNeqnyLDKLTDDN 669
Cdd:cd05933 450 AGGEnvppvPIE----DAVKKELPIISNAMLIGDKR-----------KFLsMLLTLK-CEVNPETGEP----LDELTEEA 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 670 INNNIFLD-------------------YVKEKMLEVYKETNLNRYNIINNIYLTSKVWDTNNYLTPTFKVKRFYVFKDYA 730
Cdd:cd05933 510 IEFCRKLGsqatrvseiaggkdpkvyeAIEEGIKRVNKKAISNAQKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYK 589
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
280-623 |
4.60e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 103.50 E-value: 4.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 280 MLFDDMTKTQTKKFTIKNE-DPDFVTSIVYTSGTSGKPKGVMLSNKN-IYNQLFSLYNHSVRERYSFknhLSYLPISHVf 357
Cdd:PRK03640 119 VKFAELMNGPKEEAEIQEEfDLDEVATIMYTSGTTGKPKGVIQTYGNhWWSAVGSALNLGLTEDDCW---LAAVPIFHI- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 358 ertFAYSILM----YGGTLNVWGK-DINYFSKDIYNTKENIMGGVPKvfcriytniMTEidnlpspkrRLVRKIlslrks 432
Cdd:PRK03640 195 ---SGLSILMrsviYGMRVVLVEKfDAEKINKLLQTGGVTIISVVST---------MLQ---------RLLERL------ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 433 dHNGPFskflesifhiskkikdkvNPNLEIILSGGGKLSPDIAEEfCYLLNIKYCQGYGLTETAGAILGNHADDEHfEYI 512
Cdd:PRK03640 248 -GEGTY------------------PSSFRCMLLGGGPAPKPLLEQ-CKEKGIPVYQSYGMTETASQIVTLSPEDAL-TKL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 513 GGPIAPNTKYKVRTWETYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTFLDRSKGL 592
Cdd:PRK03640 307 GSAGKPLFPCELKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDL 385
|
330 340 350
....*....|....*....|....*....|.
gi 124807131 593 VkLSQGEYIETDLLNNLYSQISFINNCVVYG 623
Cdd:PRK03640 386 I-ISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
298-621 |
2.17e-21 |
|
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: 97.84 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 298 EDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLfslynHSVRERYSFKNHLSYL---PISHvfertfaYSILMYGGTLNv 374
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASI-----RQYAERLGLGPGDVFLvasPMAH-------QTGFVYGFTLP- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 375 wgkdinyfskdiyntkenIMGGVPKVFCRIYTnimteidnlpsPKRRLVrkILSLRKSDHNGPFSKFLESIFHISKKIKD 454
Cdd:cd05903 157 ------------------LLLGAPVVLQDIWD-----------PDKALA--LMREHGVTFMMGATPFLTDLLNAVEEAGE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 455 KVnPNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAI-LGNHADDEHFEYIGGPIAPNTKYKVrTWETYKAT 533
Cdd:cd05903 206 PL-SRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVtSITPAPEDRRLYTDGRPLPGVEIKV-VDDTGATL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 534 DTLPKGELLIKSDSMFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTFLDRSKGLVkLSQGEYIE-TDLLNNLYSQ 612
Cdd:cd05903 284 APGVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPvLEVEDLLLGH 361
|
....*....
gi 124807131 613 ISFINNCVV 621
Cdd:cd05903 362 PGVIEAAVV 370
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
299-593 |
3.14e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 98.53 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIY-NQLFSLynHSV------RERYsfknhLSYLPISHVFERT----FAYSIlm 367
Cdd:PRK05605 217 TPDDVALILYTSGTTGKPKGAQLTHRNLFaNAAQGK--AWVpglgdgPERV-----LAALPMFHAYGLTlcltLAVSI-- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 368 yGGTLNVWGK-DINYFSKDIYNTKENIMGGVPKvfcrIYTNIMTEidnlpSPKRRLvrKILSLRKSdhngpfskflesif 446
Cdd:PRK05605 288 -GGELVLLPApDIDLILDAMKKHPPTWLPGVPP----LYEKIAEA-----AEERGV--DLSGVRNA-------------- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 447 hiskkikdkvnpnleiiLSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNH-ADDEHFEYIGGPIaPNTKYKVR 525
Cdd:PRK05605 342 -----------------FSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPmSDDRRPGYVGVPF-PDTEVRIV 403
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124807131 526 TWETykATDTLP---KGELLIKSDSMFSGYFLEKECTKNAFTdDGYFKTGDIVQINDNGSVTFLDRSKGLV 593
Cdd:PRK05605 404 DPED--PDETMPdgeEGELLVRGPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELI 471
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
292-601 |
5.76e-21 |
|
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: 97.02 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 292 KFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLYNH-SVRERYSFknhLSYLPISHVFerTFAYSILMygg 370
Cdd:cd05909 138 IFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIfDPNPEDVV---FGALPFFHSF--GLTGCLWL--- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 371 TLNVWGKDINYFS--------KDIYNTKENIMGGVPkVFCRIYTNIMTEIDnLPSpkrrlvrkilslrksdhngpfskfl 442
Cdd:cd05909 210 PLLSGIKVVFHPNpldykkipELIYDKKATILLGTP-TFLRGYARAAHPED-FSS------------------------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 443 esifhiskkikdkvnpnLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHAD-DEHFEYIGGPIaPNTK 521
Cdd:cd05909 263 -----------------LRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPL-PGME 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 522 YKVRTWETYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSqGEYI 601
Cdd:cd05909 325 VKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMV 402
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
306-601 |
2.00e-20 |
|
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: 94.98 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIYNQLFS-LYNHSVRERYSFknhLSYLPISHVFE-RTFAYSILMYGGTLNVWGK-DINYF 382
Cdd:cd17631 103 LMYTSGTTGRPKGAMLTHRNLLWNAVNaLAALDLGPDDVL---LVVAPLFHIGGlGVFTLPTLLRGGTVVILRKfDPETV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 383 SKDIYNTKENIMGGVPkvfcriytNIMTEIDNLPSPKRRlvrkilslrksDHngpfskflesifhiskkikdkvnPNLEI 462
Cdd:cd17631 180 LDLIERHRVTSFFLVP--------TMIQALLQHPRFATT-----------DL-----------------------SSLRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 463 ILSGGGKLSPDIAEEFcYLLNIKYCQGYGLTETAGAILGNHADD--EHFEYIGGPIaPNTKYKVRTwetyKATDTLPK-- 538
Cdd:cd17631 218 VIYGGAPMPERLLRAL-QARGVKFVQGYGMTETSPGVTFLSPEDhrRKLGSAGRPV-FFVEVRIVD----PDGREVPPge 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124807131 539 -GELLIKSDSMFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTFLDRSKGLVKlSQGEYI 601
Cdd:cd17631 292 vGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENV 353
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
283-596 |
2.51e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 92.52 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 283 DDMTKTQTKKFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNIYN---QLFSLYNHSVRErySFKNHLSYLPISHVFER 359
Cdd:PRK05677 189 DALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlQCRALMGSNLNE--GCEILIAPLPLYHIYAF 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 360 TFAYSILMYGGTLNVW---GKDINYFSKDIYNTKENIMGGVPKVFCRIYTNimteidnlpspkrrlvrkiLSLRKSDhng 436
Cdd:PRK05677 267 TFHCMAMMLIGNHNILisnPRDLPAMVKELGKWKFSGFVGLNTLFVALCNN-------------------EAFRKLD--- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 437 pFSKflesifhiskkikdkvnpnLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPI 516
Cdd:PRK05677 325 -FSA-------------------LKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 517 aPNTKYKVrtweTYKATDTLPKG---ELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLV 593
Cdd:PRK05677 385 -PSTLCKV----IDDDGNELPLGevgELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI 459
|
...
gi 124807131 594 KLS 596
Cdd:PRK05677 460 LVS 462
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
306-621 |
6.24e-19 |
|
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: 90.28 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIYNQLFSL---YNHSVRERYSFKNHLSYlpISHVFErTFAYsiLMYGGTLNV----WGKD 378
Cdd:cd05930 98 VIYTSGSTGKPKGVMVEHRGLVNLLLWMqeaYPLTPGDRVLQFTSFSF--DVSVWE-IFGA--LLAGATLVVlpeeVRKD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 379 INYFSKDIYNTKENIMGGVPkvfcriytnimteidnlpspkrrlvrkilSLrksdhngpFSKFLESIfhiskkiKDKVNP 458
Cdd:cd05930 173 PEALADLLAEEGITVLHLTP-----------------------------SL--------LRLLLQEL-------ELAALP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 459 NLEIILSGGGKLSPDIAEEF------CYLLNIkycqgYGLTETAGAILGNHADDEHFEY----IGGPIaPNTKYKVRtwe 528
Cdd:cd05930 209 SLRLVLVGGEALPPDLVRRWrellpgARLVNL-----YGPTEATVDATYYRVPPDDEEDgrvpIGRPI-PNTRVYVL--- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 529 tykatD----TLPK---GELLIKSDSMFSGYFLEKECTKNAFTDDGYF------KTGDIVQINDNGSVTFLDRSKGLVKL 595
Cdd:cd05930 280 -----DenlrPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRIDDQVKI 354
|
330 340 350
....*....|....*....|....*....|.
gi 124807131 596 SQ-----GEyIETDLLnnlysQISFINNCVV 621
Cdd:cd05930 355 RGyrielGE-IEAALL-----AHPGVREAAV 379
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
300-609 |
5.42e-18 |
|
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: 88.07 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 300 PDF----VTSIVYTSGTSGKPKGVMLSNKNIYNQLFSL-----YNHSVRERYsfknhLSYLPISHVFERTFAYSILMYGG 370
Cdd:cd12119 158 PDFdentAAAICYTSGTTGNPKGVVYSHRSLVLHAMAAlltdgLGLSESDVV-----LPVVPMFHVNAWGLPYAAAMVGA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 371 TLNVWGKDINYfsKDIYN--TKEN--IMGGVPKvfcrIYTNIMTEIDNLPspkrrlvRKILSLRKsdhngpfskflesif 446
Cdd:cd12119 233 KLVLPGPYLDP--ASLAEliEREGvtFAAGVPT----VWQGLLDHLEANG-------RDLSSLRR--------------- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 447 hiskkikdkvnpnleiILSGGGKLSPDIAEEFCYLLnIKYCQGYGLTET-----AGAILGNHAD---DEHFEY---IGGP 515
Cdd:cd12119 285 ----------------VVIGGSAVPRSLIEAFEERG-VRVIHAWGMTETsplgtVARPPSEHSNlseDEQLALrakQGRP 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 516 IaPNTKYKVRTWETykatDTLPK-----GELLIKSDSMFSGYFLEKEcTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSK 590
Cdd:cd12119 348 V-PGVELRIVDDDG----RELPWdgkavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSK 421
|
330
....*....|....*....
gi 124807131 591 GLVKlSQGEYIETDLLNNL 609
Cdd:cd12119 422 DVIK-SGGEWISSVELENA 439
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
64-594 |
6.78e-18 |
|
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: 87.97 E-value: 6.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 64 MKFFIDKYKSIPNEIALVEHSYGEPqnyITYDNFFRKVSSFSHTLntyegkgiesKKYNEKQNNGIfkllGIYGSNSINW 143
Cdd:cd17642 20 LHKAMKRYASVPGTIAFTDAHTGVN---YSYAEYLEMSVRLAEAL----------KKYGLKQNDRI----AVCSENSLQF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 144 LASDLSAMMSGVTTLVMHSKFSIDVIVDILNETQLEWLCLDLDLVEGLLNHINELPHLKNLIILDTlsknkeinlnkeen 223
Cdd:cd17642 83 FLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDS-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 224 nndkknkssgnstsvkgndlsnmieitcsgpleydKEKLKKYNELKKKCEKcgkklmlfDDMTKTQTKKFTIKNEDPDFV 303
Cdd:cd17642 149 -----------------------------------KEDYKGYQCLYTFITQ--------NLPPGFNEYDFKPPSFDRDEQ 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 304 TS-IVYTSGTSGKPKGVMLSNKNIYNQLFS----LYNHSVRERYSFknhLSYLPISHVFERTFAYSILMYGGTLNVWGK- 377
Cdd:cd17642 186 VAlIMNSSGSTGLPKGVQLTHKNIVARFSHardpIFGNQIIPDTAI---LTVIPFHHGFGMFTTLGYLICGFRVVLMYKf 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 378 DINYFSKDIYNTKENIMGGVPKVFCRIytnimteidnlpsPKRRLVRKilslrksdhngpfskflesiFHISkkikdkvn 457
Cdd:cd17642 263 EEELFLRSLQDYKVQSALLVPTLFAFF-------------AKSTLVDK--------------------YDLS-------- 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 458 pNLEIILSGGGKLSPDIAEEFCYLLNIKYC-QGYGLTETAGAILgnhADDEHFEYIG--GPIAPNTKYKVRTWETYKATD 534
Cdd:cd17642 302 -NLHEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAIL---ITPEGDDKPGavGKVVPFFYAKVVDLDTGKTLG 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 535 TLPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVK 594
Cdd:cd17642 378 PNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIK 437
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
306-608 |
7.48e-18 |
|
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: 87.38 E-value: 7.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIYNqlfslYNHSVRERYSFKNHLS---YLPISHVFERTFAYSILMYGGTLNVWGKdinyf 382
Cdd:cd17655 142 VIYTSGSTGKPKGVMIEHRGVVN-----LVEWANKVIYQGEHLRvalFASISFDASVTEIFASLLSGNTLYIVRK----- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 383 skdiyntkENIMGGVPkvFCRIYT-NIMTEIDNLPSpkrrlVRKILslrksdhngpfskflesifhisKKIKDKVNPNLE 461
Cdd:cd17655 212 --------ETVLDGQA--LTQYIRqNRITIIDLTPA-----HLKLL----------------------DAADDSEGLSLK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 462 IILSGGGKLSPDIAEEF--CYLLNIKYCQGYGLTETA-GAILGNH---ADDEHFEYIGGPIAPNTKYKVRTWETYKATDT 535
Cdd:cd17655 255 HLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTvDASIYQYepeTDQQVSVPIGKPLGNTRIYILDQYGRPQPVGV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 536 LpkGELLIKSDSMFSGYFLEKECTKNAFTDDGY------FKTGDIVQINDNGSVTFLDRSKGLVK-----LSQGEyIETD 604
Cdd:cd17655 335 A--GELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRIDHQVKirgyrIELGE-IEAR 411
|
....
gi 124807131 605 LLNN 608
Cdd:cd17655 412 LLQH 415
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
306-638 |
2.58e-17 |
|
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: 84.23 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIYNQLFSLYNHsVRERYSFKNHLSYLPISHVFERTFAYSILMYGGTLNVWGKDINYFSkd 385
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKE-GLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKS-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 386 iyntkenimggvpkVFCRIYTNIMTEIDNLPSpkrrLVRKILSLRKSdhngpfskflesifhiskkiKDKVNPNLEIILS 465
Cdd:cd17635 83 --------------LFKILTTNAVTTTCLVPT----LLSKLVSELKS--------------------ANATVPSLRLIGY 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 466 GGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAI-LGNHADDEHFEYIGGPIaPNTKYKVrtwetyKATDTLP-----KG 539
Cdd:cd17635 125 GGSRAIAADVRFIEATGLTNTAQVYGLSETGTALcLPTDDDSIEINAVGRPY-PGVDVYL------AATDGIAgpsasFG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 540 ELLIKSDSMFSGYFLEKECTKNAFTdDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSqGEYIETDLLNNLYSQISFINNC 619
Cdd:cd17635 198 TIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAEGVSGVQEC 275
|
330 340
....*....|....*....|
gi 124807131 620 VVYG-DDSMDGPLAIISVDK 638
Cdd:cd17635 276 ACYEiSDEEFGELVGLAVVA 295
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
299-599 |
4.77e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 84.86 E-value: 4.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNqlfSLYNHSVRERYSfkNHLSYL---PISHVFER-TFAYSILMYGGTLNV 374
Cdd:PRK09088 133 PPERVSLILFTSGTSGQPKGVMLSERNLQQ---TAHNFGVLGRVD--AHSSFLcdaPMFHIIGLiTSVRPVLAVGGSILV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 375 W-----GKDINYFSkdiyntkeNIMGGVPKVFCriytnimteidnLPSPKRRLvrkilsLRKSDHNGPFSKFLESIFhis 449
Cdd:PRK09088 208 SngfepKRTLGRLG--------DPALGITHYFC------------VPQMAQAF------RAQPGFDAAALRHLTALF--- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 450 kkikdkvnpnleiilSGGgklSPDIAEEFCYLLN--IKYCQGYGLTEtAGAILGNHADDEHFEYIGGPI---APNTKYKV 524
Cdd:PRK09088 259 ---------------TGG---APHAAEDILGWLDdgIPMVDGFGMSE-AGTVFGMSVDCDVIRAKAGAAgipTPTVQTRV 319
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124807131 525 RTWETYKATDTLPkGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVkLSQGE 599
Cdd:PRK09088 320 VDDQGNDCPAGVP-GELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGE 392
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
291-588 |
3.46e-16 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 83.43 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 291 KKFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNI------YNQLFSLYNHSVRerysfknhLSYLPISHVFertfays 364
Cdd:PRK08633 772 KRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNIlsnieqISDVFNLRNDDVI--------LSSLPFFHSF------- 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 365 ilmyGGTLNVWGKDINYFS--------------KDIYNTKENIMGGVPkVFCRIYTNimteidnlpspkrrlvrkilslr 430
Cdd:PRK08633 837 ----GLTVTLWLPLLEGIKvvyhpdptdalgiaKLVAKHRATILLGTP-TFLRLYLR----------------------- 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 431 ksdhngpfskflesifhiSKKIKDKVNPNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAI---LGNHADDE 507
Cdd:PRK08633 889 ------------------NKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVAsvnLPDVLAAD 950
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 508 HFEYIGG-------PIaPNTKYKVRTWETYKAtdtLPKGE---LLIKSDSMFSGYFLEKECTKNAFTD---DGYFKTGDI 574
Cdd:PRK08633 951 FKRQTGSkegsvgmPL-PGVAVRIVDPETFEE---LPPGEdglILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDK 1026
|
330
....*....|....
gi 124807131 575 VQINDNGSVTFLDR 588
Cdd:PRK08633 1027 GHLDEDGFLTITDR 1040
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
306-637 |
4.37e-16 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 81.37 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIynqlfsLYNHSVRERYSFKNH----LSYLPISHVFERTFAYSILMYGGT----LNVWGK 377
Cdd:cd05935 89 IPYTSGTTGLPKGCMHTHFSA------AANALQSAVWTGLTPsdviLACLPLFHVTGFVGSLNTAVYVGGtyvlMARWDR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 378 DInyfskdiynTKENImggvPKVFCRIYTNIMTE-IDNLPSPKrrlvrkilsLRKSDhngpFSKflesifhiskkikdkv 456
Cdd:cd05935 163 ET---------ALELI----EKYKVTFWTNIPTMlVDLLATPE---------FKTRD----LSS---------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 457 npnLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPIApNTKYKVRTWETYKATDTL 536
Cdd:cd05935 201 ---LKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*F-GVDARVIDIETGRELPPN 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 537 PKGELLIKSDSMFSGYFLEKECTKNAFTDDG---YFKTGDIVQINDNGSVTFLDRSKGLVKLSQGEYIETDLLNNLYSQI 613
Cdd:cd05935 277 EVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHP 356
|
330 340
....*....|....*....|....*.
gi 124807131 614 SFINNCVVYGDDSMDG--PLAIISVD 637
Cdd:cd05935 357 AI*EVCVISVPDERVGeeVKAFIVLR 382
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
282-594 |
1.81e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 80.27 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 282 FDDMTKTQTKKFTIKNEDPDF----------VTSIVYTSGTSGKPKGVMLSNKNIYN--QLFSLYNHSVRERYSFKN-HL 348
Cdd:PLN02574 169 FDSKRIEFPKFYELIKEDFDFvpkpvikqddVAAIMYSSGTTGASKGVVLTHRNLIAmvELFVRFEASQYEYPGSDNvYL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 349 SYLPISHVFERT-FAYSILMYGGTLNVWGK-DINYFSKDIYNTKENIMGGVPKVfcriytnimteidnlpspkrrlvrki 426
Cdd:PLN02574 249 AALPMFHIYGLSlFVVGLLSLGSTIVVMRRfDASDMVKVIDRFKVTHFPVVPPI-------------------------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 427 lslrksdhngpfskfLESIFHISKKIKDKVNPNLEIILSGGGKLSPDIAEEFCYLL-NIKYCQGYGLTE-TAGAILG-NH 503
Cdd:PLN02574 303 ---------------LMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLpHVDFIQGYGMTEsTAVGTRGfNT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 504 ADDEHFEYIGgPIAPNTKYKVRTWETYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSV 583
Cdd:PLN02574 368 EKLSKYSSVG-LLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYL 446
|
330
....*....|.
gi 124807131 584 TFLDRSKGLVK 594
Cdd:PLN02574 447 YIVDRLKEIIK 457
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
291-596 |
3.53e-15 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 79.29 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 291 KKFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNIY-NQL-FSLYNHSVRERYSFKNHLSY---LPISHVFERTFAYSI 365
Cdd:PRK07059 194 QTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLqMEAWLQPAFEKKPRPDQLNFvcaLPLYHIFALTVCGLL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 366 LMYGGTLNVW---GKDINYFSKDIYNTKENIMGGVPKVFcriytNIMteidnLPSPkrrlvrkilSLRKSDhngpFSKfl 442
Cdd:PRK07059 274 GMRTGGRNILipnPRDIPGFIKELKKYQVHIFPAVNTLY-----NAL-----LNNP---------DFDKLD----FSK-- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 443 esifhiskkikdkvnpnLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFE-YIGGPIaPNTK 521
Cdd:PRK07059 329 -----------------LIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSgTIGLPL-PSTE 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124807131 522 YKVRTwetyKATDTLP---KGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLS 596
Cdd:PRK07059 391 VSIRD----DDGNDLPlgePGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
289-596 |
4.51e-15 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 78.94 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 289 QTKKFTIKNEDPDFVTsivYTSGTSGKPKGVMLSNKNIYNQLF---SLYNHSVRERYSFKnhLSYLPISHVFERTFAYSI 365
Cdd:PRK08974 197 QYVKPELVPEDLAFLQ---YTGGTTGVAKGAMLTHRNMLANLEqakAAYGPLLHPGKELV--VTALPLYHIFALTVNCLL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 366 LMYGGTLNVW---GKDINYFSKDIYNTKENIMGGVPKVFCRIYTNI-MTEIDnlpspkrrlvrkilslrksdhngpFSkf 441
Cdd:PRK08974 272 FIELGGQNLLitnPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEeFQELD------------------------FS-- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 442 lesifhiskkikdkvnpNLEIILSGGGKLSPDIAEEF-----CYLLnikycQGYGLTETAGAILGNHAD-DEHFEYIGGP 515
Cdd:PRK08974 326 -----------------SLKLSVGGGMAVQQAVAERWvkltgQYLL-----EGYGLTECSPLVSVNPYDlDYYSGSIGLP 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 516 IaPNTKYKVRTWETYKATDTLPkGELLIKSDSMFSGYFLEKECTKNAFTDdGYFKTGDIVQINDNGSVTFLDRSKGLVKL 595
Cdd:PRK08974 384 V-PSTEIKLVDDDGNEVPPGEP-GELWVKGPQVMLGYWQRPEATDEVIKD-GWLATGDIAVMDEEGFLRIVDRKKDMILV 460
|
.
gi 124807131 596 S 596
Cdd:PRK08974 461 S 461
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
293-631 |
8.52e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 78.14 E-value: 8.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 293 FTIKNE-DPdfvTSIVYTSGTSGKPKGVMLSNKNIYnqLFSLYNHSVRERYSFKNHLSYLPISHVFERTFAYSILMYGGT 371
Cdd:PLN03102 180 FRIQDEhDP---ISLNYTSGTTADPKGVVISHRGAY--LSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 372 lNVWGKDINyfSKDIYNTKE--NI--MGGVPKVFcriytNIMTEIDnlpspkrrlvrkilSLRKSDHNGPFSkflesifh 447
Cdd:PLN03102 255 -SVCMRHVT--APEIYKNIEmhNVthMCCVPTVF-----NILLKGN--------------SLDLSPRSGPVH-------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 448 iskkikdkvnpnleiILSGGGKlSPDIAEEFCYLLNIKYCQGYGLTETAGAIL-----------GNHADDEHFEYIGGPI 516
Cdd:PLN03102 305 ---------------VLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEATGPVLfcewqdewnrlPENQQMELKARQGVSI 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 517 APNTKYKVRTWETYKAT--DTLPKGELLIKSDSMFSGYFLEKECTKNAFTDdGYFKTGDIVQINDNGSVTFLDRSKGLVk 594
Cdd:PLN03102 369 LGLADVDVKNKETQESVprDGKTMGEIVIKGSSIMKGYLKNPKATSEAFKH-GWLNTGDVGVIHPDGHVEIKDRSKDII- 446
|
330 340 350
....*....|....*....|....*....|....*...
gi 124807131 595 LSQGEYIET-DLLNNLYSQISFINNCVVygddSMDGPL 631
Cdd:PLN03102 447 ISGGENISSvEVENVLYKYPKVLETAVV----AMPHPT 480
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
306-595 |
8.57e-15 |
|
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: 77.97 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIYNqlfSLYNHSVRERYS-------FKNHlsylpishvferTFAYSI------LMYGGTL 372
Cdd:cd05918 111 VIFTSGSTGKPKGVVIEHRALST---SALAHGRALGLTsesrvlqFASY------------TFDVSIleifttLAAGGCL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 373 NVwgkdinyfskdiyNTKENIMGGVPKVFCRIYTN--IMTeidnlPSpkrrlVRKILSLrksdhngpfskflesifhisk 450
Cdd:cd05918 176 CI-------------PSEEDRLNDLAGFINRLRVTwaFLT-----PS-----VARLLDP--------------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 451 kikdKVNPNLEIILSGGGKLSPDIAEEFCY---LLNikycqGYGLTETA-GAILGNHADDEHFEYIGGPIApntkykVRT 526
Cdd:cd05918 212 ----EDVPSLRTLVLGGEALTQSDVDTWADrvrLIN-----AYGPAECTiAATVSPVVPSTDPRNIGRPLG------ATC 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 527 WETYKATDT--LPK---GELLIKSDSMFSGYFLEKECTKNAFTDDGY-------------FKTGDIVQINDNGSVTFLDR 588
Cdd:cd05918 277 WVVDPDNHDrlVPIgavGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGR 356
|
....*..
gi 124807131 589 SKGLVKL 595
Cdd:cd05918 357 KDTQVKI 363
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
301-596 |
1.73e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 77.17 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 301 DFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLY----NHSVRERYSFKN----HLSYLPISHVFERTFAYSILMYGGTL 372
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRaclsQLGPDGQPLMKEgqevMIAPLPLYHIYAFTANCMCMMVSGNH 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 373 NVW---GKDINYFSKDIYNTKENIMGGVPKVFCRIYtnimteidnlpspkrrlvrkilslrksDHNGpFSKFLESifhis 449
Cdd:PRK12492 287 NVLitnPRDIPGFIKELGKWRFSALLGLNTLFVALM---------------------------DHPG-FKDLDFS----- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 450 kkikdkvnpNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGN-HADDEHFEYIGGPIaPNTKYKVrtwe 528
Cdd:PRK12492 334 ---------ALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNpYGELARLGTVGIPV-PGTALKV---- 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124807131 529 TYKATDTLP---KGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLS 596
Cdd:PRK12492 400 IDDDGNELPlgeRGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS 470
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
299-596 |
2.79e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 76.45 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNI---YNQLFSLYNHSVRERYSFKNHLSYLPISHVFERTFAYSILMYGGTLNVW 375
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLvanMQQAHQWLAGTGKLEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 376 ---GKDINYFSKDIYNTKENIMGGVPKVFCRIY-TNIMTEIDnlpspkrrlvrkilslrksdhngpFSkflesifhiskk 451
Cdd:PRK08751 286 isnPRDMPGFVKELKKTRFTAFTGVNTLFNGLLnTPGFDQID------------------------FS------------ 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 452 ikdkvnpNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHAD-DEHFEYIGGPIaPNTKYKVRTwETY 530
Cdd:PRK08751 330 -------SLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTlKEYNGSIGLPI-PSTDACIKD-DAG 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124807131 531 KATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLS 596
Cdd:PRK08751 401 TVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVS 466
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
299-601 |
5.51e-14 |
|
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: 75.41 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDF----------VTSIVYTSGTSGKPKGVMLSNKNIY-NQLFSLYNHSVRERYSFknhLSYLPISHVFERTFAYSILM 367
Cdd:cd12118 121 DPDFewippadewdPIALNYTSGTTGRPKGVVYHHRGAYlNALANILEWEMKQHPVY---LWTLPMFHCNGWCFPWTVAA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 368 YGGTlNVWGKDINYfsKDIYNT--KENI--MGGVPKVFcriytnimTEIDNLPSPKRRlvrkilslrksdhngPFSKfle 443
Cdd:cd12118 198 VGGT-NVCLRKVDA--KAIYDLieKHKVthFCGAPTVL--------NMLANAPPSDAR---------------PLPH--- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 444 sifhiskkikdKVNpnleiILSGGGKLSPDI---AEEfcylLNIKYCQGYGLTETAGAILGNhadDEHFEYIGGPIAPNT 520
Cdd:cd12118 249 -----------RVH-----VMTAGAPPPAAVlakMEE----LGFDVTHVYGLTETYGPATVC---AWKPEWDELPTEERA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 521 KYKVRTWETYKATDTL-----------PK-----GELLIKSDSMFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVT 584
Cdd:cd12118 306 RLKARQGVRYVGLEEVdvldpetmkpvPRdgktiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIE 384
|
330
....*....|....*..
gi 124807131 585 FLDRSKGLVkLSQGEYI 601
Cdd:cd12118 385 IKDRSKDII-ISGGENI 400
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
299-625 |
5.55e-14 |
|
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: 75.02 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLfslynHSVRERYSFKNHLSYLPIShvferTFAYSI--------LMYGG 370
Cdd:cd12116 124 SPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFL-----HSMRERLGLGPGDRLLAVT-----TYAFDIsllelllpLLAGA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 371 TLNVWGKDINY----FSKDIYNTKENIMGGVPkVFCRIYtnimteIDNLPSPKRRLVrkilslrksdhngpfskflesif 446
Cdd:cd12116 194 RVVIAPRETQRdpeaLARLIEAHSITVMQATP-ATWRML------LDAGWQGRAGLT----------------------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 447 hiskkikdkvnpnleiILSGGGKLSPDIAEEFC----YLLNIkycqgYGLTET-----AGAILgnhADDEHFEyIGGPIA 517
Cdd:cd12116 244 ----------------ALCGGEALPPDLAARLLsrvgSLWNL-----YGPTETtiwstAARVT---AAAGPIP-IGRPLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 518 pNTkykvRTWETYKATDTLPKG---ELLIKSDSMFSGYFLEKECTKNAFTDDGY-------FKTGDIVQINDNGSVTFLD 587
Cdd:cd12116 299 -NT----QVYVLDAALRPVPPGvpgELYIGGDGVAQGYLGRPALTAERFVPDPFagpgsrlYRTGDLVRRRADGRLEYLG 373
|
330 340 350
....*....|....*....|....*....|....*...
gi 124807131 588 RSKGLVKLsQGEYIETDLLNNLYSQISFINNCVVYGDD 625
Cdd:cd12116 374 RADGQVKI-RGHRIELGEIEAALAAHPGVAQAAVVVRE 410
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
300-601 |
8.70e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 75.08 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 300 PDFVTSIVYTSGTSGKPKGV------MLSNKNIYNQLFS---LYNHSVrerysfknHLSYLPISHVFERTFAYSILMY-G 369
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVintqrmMCANIAMQEQLRPrepDPPPPV--------SLDWMPWNHTMGGNANFNGLLWgG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 370 GTLNV-WGKDI-NYFSKDIYNTKE---NIMGGVPKVfcriYTNIMTEIDNLPSpkrrlvrkilsLRKSdhngpFSKfles 444
Cdd:PRK12582 291 GTLYIdDGKPLpGMFEETIRNLREispTVYGNVPAG----YAMLAEAMEKDDA-----------LRRS-----FFK---- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 445 ifhiskkikdkvnpNLEIILSGGGKLSPDIAEEFcYLLNIK-------YCQGYGLTETAGAILGNHADDEHFEYIGGPiA 517
Cdd:PRK12582 347 --------------NLRLMAYGGATLSDDLYERM-QALAVRttghripFYTGYGATETAPTTTGTHWDTERVGLIGLP-L 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 518 PNTKYKVrtwetykatdtLPKG---ELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDivqindngSVTFLDR---SKG 591
Cdd:PRK12582 411 PGVELKL-----------APVGdkyEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGD--------AARFVDPddpEKG 471
|
330
....*....|....*....
gi 124807131 592 LV---------KLSQGEYI 601
Cdd:PRK12582 472 LIfdgrvaedfKLSTGTWV 490
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
299-590 |
9.81e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 74.56 E-value: 9.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYnqlfSLYNH-----SVRE--RYsfknhLSYLPISHVFERTFAY-SILMYGG 370
Cdd:PRK07656 164 DPDDVADILFTSGTTGRPKGAMLTHRQLL----SNAADwaeylGLTEgdRY-----LAANPFFHVFGYKAGVnAPLMRGA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 371 TLNVWGKdinyFSKD-----IYNTKENIMGGVPKvfcrIYTNImteidnLPSPKRRlVRKILSLRksdhngpfskflesi 445
Cdd:PRK07656 235 TILPLPV----FDPDevfrlIETERITVLPGPPT----MYNSL------LQHPDRS-AEDLSSLR--------------- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 446 fhiskkikdkvnpnleIILSGGGKLSPDIAEEFCYLLNIKYC-QGYGLTETAGAILGNHADDEhFEYIGGPIA---PNTK 521
Cdd:PRK07656 285 ----------------LAVTGAASMPVALLERFESELGVDIVlTGYGLSEASGVTTFNRLDDD-RKTVAGTIGtaiAGVE 347
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124807131 522 YKV--RTWETYKATDTlpkGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSK 590
Cdd:PRK07656 348 NKIvnELGEEVPVGEV---GELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKK 415
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
305-623 |
1.92e-13 |
|
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: 73.09 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 305 SIVYTSGTSGKPKGVMLSNkniYNQLFSLYNHSVRERYSFKN-HLSYLPISHV-FERTFAYSILMYGGTLNVWGKdinyF 382
Cdd:cd05934 85 SILYTSGTTGPPKGVVITH---ANLTFAGYYSARRFGLGEDDvYLTVLPLFHInAQAVSVLAALSVGATLVLLPR----F 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 383 S-----KDI--YN-TKENIMGGVPKVFCRiytnimTEIDnlPSPKRRLVRKILSlrksdhngpfskflesifhiskkikd 454
Cdd:cd05934 158 SasrfwSDVrrYGaTVTNYLGAMLSYLLA------QPPS--PDDRAHRLRAAYG-------------------------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 455 kvNPNLeiilsgggklsPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPiAPNTKYKVRTWETYKATD 534
Cdd:cd05934 204 --APNP-----------PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRP-APGYEVRIVDDDGQELPA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 535 TLPkGELLIKSD---SMFSGYFLEKECTKNAFTdDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSqGEYIETDLLNNLYS 611
Cdd:cd05934 270 GEP-GELVIRGLrgwGFFKGYYNMPEATAEAMR-NGWFHTGDLGYRDADGFFYFVDRKKDMIRRR-GENISSAEVERAIL 346
|
330
....*....|..
gi 124807131 612 QISFINNCVVYG 623
Cdd:cd05934 347 RHPAVREAAVVA 358
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
308-690 |
2.13e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 73.47 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 308 YTSGTSGKPKGVMLSNKN-IYNQLFSLYnhSVR-ERYSFKNHLSYLPISHVFERT-FAYSILMYGGTLNVWGK-DINYFS 383
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNlVANLCSSLF--SVGpEMIGQVVTLGLIPFFHIYGITgICCATLRNKGKVVVMSRfELRTFL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 384 KDIYNTKENIMGGVPKVFCRIYTN-IMTEIDnlpspkrrlvrkiLSlrksdhngpfskflesifhiskKIKdkvnpnLEI 462
Cdd:PLN02330 269 NALITQEVSFAPIVPPIILNLVKNpIVEEFD-------------LS----------------------KLK------LQA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 463 ILSGGGKLSPDIAEEF-CYLLNIKYCQGYGLTETAGAILgNHADDEHFEYIG-----GPIAPNTKYKVRTWETYKatdTL 536
Cdd:PLN02330 308 IMTAAAPLAPELLTAFeAKFPGVQVQEAYGLTEHSCITL-THGDPEKGHGIAkknsvGFILPNLEVKFIDPDTGR---SL 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 537 PK---GELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSQGEYIETDLLNNLYSQI 613
Cdd:PLN02330 384 PKntpGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHP 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 614 SFINNCVVYGDDSMDG--PLAIISVDKYllfLSLKDDNMLEMTGVNEQNY--------LDKLTdDNINNNIFLDYVKEKM 683
Cdd:PLN02330 464 SVEDAAVVPLPDEEAGeiPAACVVINPK---AKESEEDILNFVAANVAHYkkvrvvqfVDSIP-KSLSGKIMRRLLKEKM 539
|
....*..
gi 124807131 684 LEVYKET 690
Cdd:PLN02330 540 LSINKAN 546
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
300-593 |
3.00e-13 |
|
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: 71.93 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 300 PDFVTSIVYTSGTSGKPKGVMLSNKNIYNQlfslyNHSVRERYSFKNHLSY---LPISHVFERTFAY-SILMYGGTLNVW 375
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-----GYFIGERLGLTEQDRLcipVPLFHCFGSVLGVlACLTHGATMVFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 376 GKDINYFS--KDIYNTKENIMGGVPKVFcriytnimteIDNLPSPKrrlvrkilslrksdhngpFSKFleSIFHISKKIk 453
Cdd:cd05917 76 SPSFDPLAvlEAIEKEKCTALHGVPTMF----------IAELEHPD------------------FDKF--DLSSLRTGI- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 454 dkvnpnleiilSGGGKLSPDIAEEFCYLLNIKYCQ-GYGLTETAGAILGNHADDEHFEYIG--GPIAPNTKYKVRTWETY 530
Cdd:cd05917 125 -----------MAGAPCPPELMKRVIEVMNMKDVTiAYGMTETSPVSTQTRTDDSIEKRVNtvGRIMPHTEAKIVDPEGG 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124807131 531 KATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLV 593
Cdd:cd05917 194 IVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI 256
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
296-601 |
9.03e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 71.43 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 296 KNEDPDFVtsIVYTSGTSGKPKGVMLSNKNIYNQlfSLYNHSVRERYSFKNHLSYLPISHVFE-RTFAYSILMYGGTLNV 374
Cdd:PRK06839 146 KNESASFI--ICYTSGTTGKPKGAVLTQENMFWN--ALNNTFAIDLTMHDRSIVLLPLFHIGGiGLFAFPTLFAGGVIIV 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 375 WGKdinyFSKD-----IYNTKENIMGGVPKVFCRIYTNIMTEIDNLPSpkrrlVRkilslrksdhngpfskflesIFHis 449
Cdd:PRK06839 222 PRK----FEPTkalsmIEKHKVTVVMGVPTIHQALINCSKFETTNLQS-----VR--------------------WFY-- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 450 kkikdkvnpnleiilSGGGKLSPDIAEEFcYLLNIKYCQGYGLTETAGAILGNHADDEHFE--YIGGP--------IAPN 519
Cdd:PRK06839 271 ---------------NGGAPCPEELMREF-IDRGFLFGQGFGMTETSPTVFMLSEEDARRKvgSIGKPvlfcdyelIDEN 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 520 TKyKVRTWETykatdtlpkGELLIKSDSMFSGYFLEKECTKNAFTDdGYFKTGDIVQINDNGSVTFLDRSKGLVkLSQGE 599
Cdd:PRK06839 335 KN-KVEVGEV---------GELLIRGPNVMKEYWNRPDATEETIQD-GWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGE 402
|
..
gi 124807131 600 YI 601
Cdd:PRK06839 403 NI 404
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
299-621 |
2.62e-12 |
|
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: 69.97 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSnkniYNQLFSLYNHSVrERYSFKNHLSYLpisHVFERTFAYSI------LMYGGTL 372
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQIS----HDNLVSFTNWML-SDFPLGPGDVFL---NQAPFSFDLSVmdlypaLASGATL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 373 NVwgkdinyfskdiyntkenimggVPKvfcriytnimTEIDNLpspkRRLVRkilSLRKSDHNGPFSkfLESIFHI---S 449
Cdd:cd05945 167 VP----------------------VPR----------DATADP----KQLFR---FLAEHGITVWVS--TPSFAAMcllS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 450 KKIKDKVNPNLEIILSGGGKLSPDIAEEF------CYLLNIkycqgYGLTETAGAILGNHADDEHFE-----YIGGPIaP 518
Cdd:cd05945 206 PTFTPESLPSLRHFLFCGEVLPHKTARALqqrfpdARIYNT-----YGPTEATVAVTYIEVTPEVLDgydrlPIGYAK-P 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 519 NTKYKVRTwETYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAF-TDDGY--FKTGDIVQINDNGSVTFLDRSKGLVKL 595
Cdd:cd05945 280 GAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKL 358
|
330 340
....*....|....*....|....*.
gi 124807131 596 sQGEYIETDLLNNLYSQISFINNCVV 621
Cdd:cd05945 359 -NGYRIELEEIEAALRQVPGVKEAVV 383
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
458-637 |
4.29e-12 |
|
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: 68.13 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 458 PNLEIILSGGGKLSPDIAEEFCyLLNIKYCQGYGLTETAGAILGNHADDEHFEYiGGPIAPNTKYKVrtwetykatdtLP 537
Cdd:cd17630 111 KSLRAVLLGGAPIPPELLERAA-DRGIPLYTTYGMTETASQVATKRPDGFGRGG-VGVLLPGRELRI-----------VE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 538 KGELLIKSDSMFSGYFleKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVkLSQGEYIETDLLNNLYSQISFIN 617
Cdd:cd17630 178 DGEIWVGGASLAMGYL--RGQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVR 254
|
170 180
....*....|....*....|...
gi 124807131 618 NCVVYG-DDSMDG--PLAIISVD 637
Cdd:cd17630 255 DAFVVGvPDEELGqrPVAVIVGR 277
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
308-596 |
1.60e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 67.75 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 308 YTSGTSGKPKGVMLSNKN-IYNQLFS---LYNHSVRERYSfknhLSYLPISHVFERTFAYSI-LMYGGTLNVWGK-DINY 381
Cdd:PRK06710 213 YTGGTTGFPKGVMLTHKNlVSNTLMGvqwLYNCKEGEEVV----LGVLPFFHVYGMTAVMNLsIMQGYKMVLIPKfDMKM 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 382 FSKDIYNTKENIMGGVPKVFCRIYTN-IMTEIDnlpspkrrlvrkILSLRKSdhngpfskflesifhiskkikdkvnpnl 460
Cdd:PRK06710 289 VFEAIKKHKVTLFPGAPTIYIALLNSpLLKEYD------------ISSIRAC---------------------------- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 461 eiiLSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPIAPNTKYKVRTWETYKATDTLPKGE 540
Cdd:PRK06710 329 ---ISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEALPPGEIGE 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124807131 541 LLIKSDSMFSGYFLEKECTKnAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLS 596
Cdd:PRK06710 406 IVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVAS 460
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
300-623 |
1.79e-11 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 67.40 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 300 PDFVTSIVYTSGTSGKPKGVMLSNKNI-YNQLFSLYNHSVRE--RYsfknhLSYLPISHV-FERTFAYSILMYGGTLNVW 375
Cdd:PRK08008 172 TDDTAEILFTSGTTSRPKGVVITHYNLrFAGYYSAWQCALRDddVY-----LTVMPAFHIdCQCTAAMAAFSAGATFVLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 376 GKdinY----FSKDIYNTKENIMGGVPKVfcriytnIMTEIDNLPSPKRRlvrkilslrksDHngpfsKFLESIF--HIS 449
Cdd:PRK08008 247 EK---YsaraFWGQVCKYRATITECIPMM-------IRTLMVQPPSANDR-----------QH-----CLREVMFylNLS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 450 KKIKDkvnpnleiilsgggklspdiaeEFCYLLNIKYCQGYGLTETAGAILGNHADDE-HFEYIGgpiAPNTKYKVR-TW 527
Cdd:PRK08008 301 DQEKD----------------------AFEERFGVRLLTSYGMTETIVGIIGDRPGDKrRWPSIG---RPGFCYEAEiRD 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 528 ETYKATDTLPKGELLIKS---DSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSqGEYIETD 604
Cdd:PRK08008 356 DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCV 434
|
330
....*....|....*....
gi 124807131 605 LLNNLYSQISFINNCVVYG 623
Cdd:PRK08008 435 ELENIIATHPKIQDIVVVG 453
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
285-604 |
2.30e-11 |
|
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: 66.56 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 285 MTKTQTKKFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLfSLYNHSVRERYSFKNhlsylpiSHVFERTFAYS 364
Cdd:cd17653 89 ILRTSGATLLLTTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYV-SQPPARLDVGPGSRV-------AQVLSIAFDAC 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 365 I------LMYGGTLnVWGKDINYFSKDIyntkenimggvpkvfcriytnimTEIDNLPS-PkrrlvrKILSlrksdhngp 437
Cdd:cd17653 161 IgeifstLCNGGTL-VLADPSDPFAHVA-----------------------RTVDALMStP------SILS--------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 438 fskflesifhiskKIKDKVNPNLEIILSGGGKLSPDIAEEfcYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPIa 517
Cdd:cd17653 202 -------------TLSPQDFPNLKTIFLGGEAVPPSLLDR--WSPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPI- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 518 PNTkyKVRTWEtykaTDTLP-----KGELLIKSDSMFSGYFLEKECTKNAFTDDGY------FKTGDIVQINDNGSVTFL 586
Cdd:cd17653 266 PNS--TCYILD----ADLQPvpegvVGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFL 339
|
330
....*....|....*...
gi 124807131 587 DRSKGLVKLsQGEYIETD 604
Cdd:cd17653 340 GREDNQVKV-RGFRINLE 356
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
299-608 |
5.53e-11 |
|
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: 65.57 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLfslynHSVRERYSFK----NHLSYLPIS-HVFERTFAYSiLMYGGTLN 373
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAA-----HAWRREYELDsfpvRLLQMASFSfDVFAGDFARS-LLNGGTLV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 374 VWGKDINYFSKDIYNT----KENIMGGVPKVfcriytnIMTEIDNLPSPKRRLVRKILSLRKSDhngpfskflesifhiS 449
Cdd:cd17650 165 ICPDEVKLDPAALYDLilksRITLMESTPAL-------IRPVMAYVYRNGLDLSAMRLLIVGSD---------------G 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 450 KKIKDKVnpnleiilsgggklspDIAEEFcyLLNIKYCQGYGLTETAgailgnhADDEHFEY------------IGGPIa 517
Cdd:cd17650 223 CKAQDFK----------------TLAARF--GQGMRIINSYGVTEAT-------IDSTYYEEgrdplgdsanvpIGRPL- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 518 PNTKYKVRTwETYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDDGY------FKTGDIVQINDNGSVTFLDRSKG 591
Cdd:cd17650 277 PNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDH 355
|
330 340
....*....|....*....|..
gi 124807131 592 LVKL-----SQGEyIETDLLNN 608
Cdd:cd17650 356 QVKIrgfriELGE-IESQLARH 376
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
279-625 |
6.59e-11 |
|
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: 65.57 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 279 LMLFDDMTKTQTKKFTIKNEDPDFVTsIVYTSGTSGKPKGVMLSNKNIYNQLFSLYNHSVRERysFKNHLSYLPIShvFE 358
Cdd:cd17656 107 LLEDPSISQEDTSNIDYINNSDDLLY-IIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINF--SDKVLQFATCS--FD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 359 RTFA--YSILMYGGTLnvwgkdinyfskdiYNTKENIMGGVPKVFCRIYTNiMTEIDNLPSPkrrLVRKILSLRksdhnG 436
Cdd:cd17656 182 VCYQeiFSTLLSGGTL--------------YIIREETKRDVEQLFDLVKRH-NIEVVFLPVA---FLKFIFSER-----E 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 437 PFSKFLESIFHiskkikdkvnpnleIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGN-HADDEHFEY--IG 513
Cdd:cd17656 239 FINRFPTCVKH--------------IITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTiNPEAEIPELppIG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 514 GPIApNTKYKVRTWETYKATDTLPkGELLIKSDSMFSGYFLEKECTKNAFTDDGY------FKTGDIVQINDNGSVTFLD 587
Cdd:cd17656 305 KPIS-NTWIYILDQEQQLQPQGIV-GELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLG 382
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 124807131 588 RSKGLVKLsQGEYIETDLLNNLYSQISFINNCVV--YGDD 625
Cdd:cd17656 383 RADHQVKI-RGYRIELGEIEAQLLNHPGVSEAVVldKADD 421
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
299-596 |
7.84e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 65.37 E-value: 7.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFS--LYNHSVRErysfKNHLSYLPISHVferT-FAYSI---LMYGGTL 372
Cdd:PRK08314 188 GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGsvLWSNSTPE----SVVLAVLPLFHV---TgMVHSMnapIYAGATV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 373 NV---WGKDInyfSKDIyntkenimggVPKVFCRIYTNIMTE-IDNLPSPKrrlvrkilsLRKSDhngpfskfLESIFHI 448
Cdd:PRK08314 261 VLmprWDREA---AARL----------IERYRVTHWTNIPTMvVDFLASPG---------LAERD--------LSSLRYI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 449 SkkikdkvnpnleiilsGGGKLSPD-IAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPIApNTKYKVRTW 527
Cdd:PRK08314 311 G----------------GGGAAMPEaVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTF-GVDARVIDP 373
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124807131 528 ETYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTD-DG--YFKTGDIVQINDNGSVTFLDRSKGLVKLS 596
Cdd:PRK08314 374 ETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINAS 445
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
299-590 |
7.89e-11 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 65.46 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSnkniYNQLFSlYNHSVRERYSFKNH---LSYLPISHvfERTFAYSILMyggtlnvw 375
Cdd:PRK13295 195 GPDDVTQLIYTSGTTGEPKGVMHT----ANTLMA-NIVPYAERLGLGADdviLMASPMAH--QTGFMYGLMM-------- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 376 gkdinyfskdiyntkeNIMGGVPKVFCRIYtnimteidnlpSPKR--RLVRkilslrksDHNGPFS----KFLESIFHIS 449
Cdd:PRK13295 260 ----------------PVMLGATAVLQDIW-----------DPARaaELIR--------TEGVTFTmastPFLTDLTRAV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 450 KKiKDKVNPNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEH--FEYIGGPIaPNTKYKVRtw 527
Cdd:PRK13295 305 KE-SGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDEraSTTDGCPL-PGVEVRVV-- 380
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124807131 528 etyKATDT-LPKGE---LLIKSDSMFSGYFleKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSK 590
Cdd:PRK13295 381 ---DADGApLPAGQigrLQVRGCSNFGGYL--KRPQLNGTDADGWFDTGDLARIDADGYIRISGRSK 442
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
297-590 |
1.22e-10 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 64.77 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 297 NEDPDFVTSIVYTSGTSGKPKGVMLSNKNIynqLFSlynhsvrERYsfknhlsylpishvfertfaysilmYGGTLNVWG 376
Cdd:PRK06087 183 TTHGDELAAVLFTSGTEGLPKGVMLTHNNI---LAS-------ERA-------------------------YCARLNLTW 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 377 KDInYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIDNlPSPKRRLVRK---ILSLRKSdhngPFskflesIFHISKKI- 452
Cdd:PRK06087 228 QDV-FMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFT-PDACLALLEQqrcTCMLGAT----PF------IYDLLNLLe 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 453 KDKVN-PNLEIILSGGGKLSPDIAEEfCYLLNIKYCQGYGLTETAGAILGNHADD-EHFEYIGGPIAPNTKYKVrtweTY 530
Cdd:PRK06087 296 KQPADlSALRFFLCGGTTIPKKVARE-CQQRGIKLLSVYGSTESSPHAVVNLDDPlSRFMHTDGYAAAGVEIKV----VD 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124807131 531 KATDTLP---KGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSK 590
Cdd:PRK06087 371 EARKTLPpgcEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKK 433
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
306-621 |
1.41e-10 |
|
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: 64.21 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIYNQLfslynHSVRERYSFK---NHLSYLPISH---VFERTFAysiLMYGGTLNVwgkdi 379
Cdd:TIGR01733 125 VIYTSGSTGRPKGVVVTHRSLVNLL-----AWLARRYGLDpddRVLQFASLSFdasVEEIFGA---LLAGATLVV----- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 380 nyfskdiyntkenIMGGVPKVFCRIYTNIM-----TEIDNLPSPKRRLVRKILSLRKSdhngpfskflesifhiskkikd 454
Cdd:TIGR01733 192 -------------PPEDEERDDAALLAALIaehpvTVLNLTPSLLALLAAALPPALAS---------------------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 455 kvnpnLEIILSGGGKLSPDIAEEFC------YLLNikycqGYGLTETAGAILGN--HADDEHFEY---IGGPIaPNTKYK 523
Cdd:TIGR01733 237 -----LRLVILGGEALTPALVDRWRargpgaRLIN-----LYGPTETTVWSTATlvDPDDAPRESpvpIGRPL-ANTRLY 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 524 VR--------TWETykatdtlpkGELLIKSDSMFSGYFLEKECTKNAFTDDGY--------FKTGDIVQINDNGSVTFLD 587
Cdd:TIGR01733 306 VLdddlrpvpVGVV---------GELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlYRTGDLVRYLPDGNLEFLG 376
|
330 340 350
....*....|....*....|....*....|....*....
gi 124807131 588 RSKGLVKLSQ-----GEyIETDLLnnlysQISFINNCVV 621
Cdd:TIGR01733 377 RIDDQVKIRGyrielGE-IEAALL-----RHPGVREAVV 409
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
298-596 |
1.64e-10 |
|
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: 64.06 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 298 EDPDFvtsIVYTSGTSGKPKGVMLSNKNIYNQLFSlynhsvrERYSFKNHlsylpISHVFERTfAYSILMYGGTLNVWGK 377
Cdd:cd05969 89 EDPTL---LHYTSGTTGTPKGVLHVHDAMIFYYFT-------GKYVLDLH-----PDDIYWCT-ADPGWVTGTVYGIWAP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 378 DINYFSKDIYNTKENIMggvpkvfcRIYTNIMTEIDNL----PSPKRRLVRK-ILSLRKSDhngpfskfLESIFHIskki 452
Cdd:cd05969 153 WLNGVTNVVYEGRFDAE--------SWYGIIERVKVTVwytaPTAIRMLMKEgDELARKYD--------LSSLRFI---- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 453 kdkvnpnleiiLSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNhaddehfeYIGGPIAPNTKYK----VRTWE 528
Cdd:cd05969 213 -----------HSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIAN--------YPCMPIKPGSMGKplpgVKAAV 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124807131 529 TYKATDTLP---KGELLIKSD--SMFSGYFLEKECTKNAFTDdGYFKTGDIVQINDNGSVTFLDRSKGLVKLS 596
Cdd:cd05969 274 VDENGNELPpgtKGILALKPGwpSMFRGIWNDEERYKNSFID-GWYLTGDLAYRDEDGYFWFVGRADDIIKTS 345
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
299-593 |
1.81e-10 |
|
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: 64.23 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIY------NQLFSLYNHSVrerysfknHLSYLPISHVfertfaYSILMYGgtl 372
Cdd:cd05906 165 RPDDLALLMLTSGSTGFPKAVPLTHRNILarsagkIQHNGLTPQDV--------FLNWVPLDHV------GGLVELH--- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 373 nvwgkdinyfSKDIYNTKENImggvpkvfcriytNIMTEiDNLPSPkRRLVRKILSLRKSDHNGP---FSKFLESifhiS 449
Cdd:cd05906 228 ----------LRAVYLGCQQV-------------HVPTE-EILADP-LRWLDLIDRYRVTITWAPnfaFALLNDL----L 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 450 KKIKDKV--NPNLEIILSGGGKLSPDIAEEFCYLLniKYCQ--------GYGLTET-AGAI------LGNHADDEHFEYI 512
Cdd:cd05906 279 EEIEDGTwdLSSLRYLVNAGEAVVAKTIRRLLRLL--EPYGlppdairpAFGMTETcSGVIysrsfpTYDHSQALEFVSL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 513 GGPIaPNTKYKVrTWETYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQInDNGSVTFLDRSKGL 592
Cdd:cd05906 357 GRPI-PGVSMRI-VDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFL-DNGNLTITGRTKDT 433
|
.
gi 124807131 593 V 593
Cdd:cd05906 434 I 434
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
297-629 |
3.52e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 63.23 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 297 NEDPDfVTSIVYTSGTSGKPKGVMLSNKNIynqlfsLYN-HSVRERysFKNH-----LSYLPISHVFERTFAYSILMYGG 370
Cdd:cd05922 114 VSHED-LALLLYTSGSTGSPKLVRLSHQNL------LANaRSIAEY--LGITaddraLTVLPLSYDYGLSVLNTHLLRGA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 371 TL-----NVWGKDinyFSKDIYNTKENIMGGVPKVFCRIytnimteidnlpspkRRLVRKILSLrksdhngpfskflesi 445
Cdd:cd05922 185 TLvltndGVLDDA---FWEDLREHGATGLAGVPSTYAML---------------TRLGFDPAKL---------------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 446 fhiskkikdkvnPNLEIILSGGGKLSPDIAEEFCYLLnikycQG------YGLTE-TAG-AILGNHADDEHFEYIGGPIa 517
Cdd:cd05922 231 ------------PSLRYLTQAGGRLPQETIARLRELL-----PGaqvyvmYGQTEaTRRmTYLPPERILEKPGSIGLAI- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 518 PNTKYKVRTwetYKATDTLPK--GELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKL 595
Cdd:cd05922 293 PGGEFEILD---DDGTPTPPGepGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKL 369
|
330 340 350
....*....|....*....|....*....|....
gi 124807131 596 SqGEYIETDLLNNLYSQISFINNCVVYGDDSMDG 629
Cdd:cd05922 370 F-GNRISPTEIEAAARSIGLIIEAAAVGLPDPLG 402
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
469-596 |
3.92e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 63.14 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 469 KLSPDIAEEFCYLLNIKYCQG-YGLTETAGA---ILGNHADDehFEYIGGPI-----APNTKYKVRTWETykaTDTLP-- 537
Cdd:PRK06178 338 KLNPDYRQRWRALTGSVLAEAaWGMTETHTCdtfTAGFQDDD--FDLLSQPVfvglpVPGTEFKICDFET---GELLPlg 412
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 538 -KGELLIKSDSMFSGYFLEKECTKNAFTDdGYFKTGDIVQINDNGSVTFLDRSKGLVKLS 596
Cdd:PRK06178 413 aEGEIVVRTPSLLKGYWNKPEATAEALRD-GWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
299-593 |
7.31e-10 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 62.20 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLynhsvRERYSFKNH---LSYLPISHV---FERTfaYSILMYGGTL 372
Cdd:PRK07514 154 GADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTL-----VDYWRFTPDdvlIHALPIFHThglFVAT--NVALLAGASM 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 373 nVWgkdinyFSKdiYNTKENI--------MGGVPKVFCRIytnimteidnLPSPkrRLVRKILSlrksdhngpfskfles 444
Cdd:PRK07514 227 -IF------LPK--FDPDAVLalmpratvMMGVPTFYTRL----------LQEP--RLTREAAA---------------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 445 ifhiskkikdkvnpNLEIILSGGGKLSPDIAEEFcyllniKYCQG------YGLTETaGAILGNHADDEHfeyIGGPIA- 517
Cdd:PRK07514 270 --------------HMRLFISGSAPLLAETHREF------QERTGhailerYGMTET-NMNTSNPYDGER---RAGTVGf 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 518 --PNTKYKVRTWETYKatdTLPKGE---LLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGL 592
Cdd:PRK07514 326 plPGVSLRVTDPETGA---ELPPGEigmIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL 402
|
.
gi 124807131 593 V 593
Cdd:PRK07514 403 I 403
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
280-635 |
1.25e-09 |
|
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: 61.42 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 280 MLFDDMTKTQTKkftikneDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNqlFSLYNHSVRERYSFKNHLSYLPIShvFEr 359
Cdd:cd17645 90 MLADSSAKILLT-------NPDDLAYVIYTSGSTGLPKGVMIEHHNLVN--LCEWHRPYFGVTPADKSLVYASFS--FD- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 360 TFAYSILMY---GGTLNVWGKDINYfskDIYNTKEnimggvpkvFCRiyTNIMTeIDNLPSPkrrLVRKILSLRksdhng 436
Cdd:cd17645 158 ASAWEIFPHltaGAALHVVPSERRL---DLDALND---------YFN--QEGIT-ISFLPTG---AAEQFMQLD------ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 437 pfskflesifhiskkikdkvNPNLEIILSGGGKLspDIAEEFCYLLnikyCQGYGLTETAGAILGNHADDEHFEY-IGGP 515
Cdd:cd17645 214 --------------------NQSLRVLLTGGDKL--KKIERKGYKL----VNNYGPTENTVVATSFEIDKPYANIpIGKP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 516 IApntkyKVRTWETYKATDTLP---KGELLIKSDSMFSGYFLEKECTKNAFTDDGY------FKTGDIVQINDNGSVTFL 586
Cdd:cd17645 268 ID-----NTRVYILDEALQLQPigvAGELCIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFLPDGNIEFL 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 124807131 587 DRSKGLVKLsQGEYIETDLLNNLYSQISFINNCVVYGDDSMDGPLAIIS 635
Cdd:cd17645 343 GRLDQQVKI-RGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVA 390
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
305-636 |
2.58e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.57 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 305 SIVYTSGTSGKPKGVMLSNKNIYNQLFSLY---NHSVRERYSFknhLSYLPISHVFERTFAYSILMYGGTLNVWGKDIN- 380
Cdd:PRK05620 185 AICYSTGTTGAPKGVVYSHRSLYLQSLSLRttdSLAVTHGESF---LCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDLSa 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 381 -YFSKDIYNTKENIMGGVPKVFCRIYTNIMTEidnlpSPKRrlvrkiLSLRKsdhngpfskflesifhiskkikdkvnpn 459
Cdd:PRK05620 262 pTLAKIIATAMPRVAHGVPTLWIQLMVHYLKN-----PPER------MSLQE---------------------------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 460 leiILSGGGKLSP---DIAEEFcYLLNIKYCqgYGLTET----------AGAilgNHADDEHFEYIGGPIAPNTKYK-VR 525
Cdd:PRK05620 303 ---IYVGGSAVPPiliKAWEER-YGVDVVHV--WGMTETspvgtvarppSGV---SGEARWAYRVSQGRFPASLEYRiVN 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 526 TWETYKATDTlPKGELLIKSD------------------SMFSGYFLEKECTKnaFTDDGYFKTGDIVQINDNGSVTFLD 587
Cdd:PRK05620 374 DGQVMESTDR-NEGEIQVRGNwvtasyyhspteegggaaSTFRGEDVEDANDR--FTADGWLRTGDVGSVTRDGFLTIHD 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 124807131 588 RSKGLVKlSQGEYIETDLLNNLYSQISFINNCVVYG--DDS-MDGPLAIISV 636
Cdd:PRK05620 451 RARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIGypDDKwGERPLAVTVL 501
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
299-594 |
2.61e-09 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 60.38 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNqlfslynhSVRERYSFKNH----------LSYLPISHVFERTfaySILM- 367
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLVT--------SVAQQVDGENPnlyfhsddviLCVLPMFHIYSLN---SVLLc 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 368 ---YGGTLNVWGK-DINYFSKDIYNTKENIMGGVPKVFCRIYTNIMTEIDNLPSpkrrlVRKILSlrksdhnG--PFSKF 441
Cdd:PLN02246 246 glrVGAAILIMPKfEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSS-----IRMVLS-------GaaPLGKE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 442 LESIFHiSKkikdkvnpnleiilsgggklspdiaeefcyLLNIKYCQGYGLTEtAGAILG---NHAdDEHFEYIGGP--- 515
Cdd:PLN02246 314 LEDAFR-AK------------------------------LPNAVLGQGYGMTE-AGPVLAmclAFA-KEPFPVKSGScgt 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 516 IAPNTKYKVRTWETykaTDTLPK---GELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGL 592
Cdd:PLN02246 361 VVRNAELKIVDPET---GASLPRnqpGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKEL 437
|
..
gi 124807131 593 VK 594
Cdd:PLN02246 438 IK 439
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
300-623 |
5.94e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 59.13 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 300 PDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFslyNHSVRERYSFKNHLSYL-PISHVFERTF-AYSILMYGGTLNVWgK 377
Cdd:PRK06145 148 PTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSI---DHVIALGLTASERLLVVgPLYHVGAFDLpGIAVLWVGGTLRIH-R 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 378 DINYFSKDIYNTKENIMGG--VPKVFCRIYTnimteidnLPSPKRRLVrkilslrksdhngpfSKFLESIfhiskkikdk 455
Cdd:PRK06145 224 EFDPEAVLAAIERHRLTCAwmAPVMLSRVLT--------VPDRDRFDL---------------DSLAWCI---------- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 456 vnpnleiilsGGGKLSPD--IAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEhFEYIG--GPIAPNTKYKVRTwetyK 531
Cdd:PRK06145 271 ----------GGGEKTPEsrIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGRE-IEKIGstGRALAHVEIRIAD----G 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 532 ATDTLP---KGELLIKSDSMFSGYFLEKECTKNAFTDDgYFKTGDIVQINDNGSVTFLDRSKGLVkLSQGEYIETDLLNN 608
Cdd:PRK06145 336 AGRWLPpnmKGEICMRGPKVTKGYWKDPEKTAEAFYGD-WFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVER 413
|
330
....*....|....*
gi 124807131 609 LYSQISFINNCVVYG 623
Cdd:PRK06145 414 VIYELPEVAEAAVIG 428
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
300-601 |
6.11e-09 |
|
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: 59.37 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 300 PDFVTSIVYTSGTSGKPKGV------MLSNKNIYNQLFSLYNHSVRERysfknhLSYLPISHVFERTFAYSILMY-GGTL 372
Cdd:cd05921 164 PDTVAKFLFTSGSTGLPKAVintqrmLCANQAMLEQTYPFFGEEPPVL------VDWLPWNHTFGGNHNFNLVLYnGGTL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 373 NV-WGKDI-NYFSKDIYNTKEnIMggvPKVFcriytnimteiDNLPSPKRRLV---RKILSLRKSdhngpfskFLEsifh 447
Cdd:cd05921 238 YIdDGKPMpGGFEETLRNLRE-IS---PTVY-----------FNVPAGWEMLVaalEKDEALRRR--------FFK---- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 448 iskkikdkvnpNLEIILSGGGKLSPDIAEEFCYLL------NIKYCQGYGLTETAGAILGNHADDEHFEYIGGPiAPNTK 521
Cdd:cd05921 291 -----------RLKLMFYAGAGLSQDVWDRLQALAvatvgeRIPMMAGLGATETAPTATFTHWPTERSGLIGLP-APGTE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 522 YKVrtwetykatdtLPKG---ELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGsvtflDRSKGLV----- 593
Cdd:cd05921 359 LKL-----------VPSGgkyEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADPD-----DPAKGLVfdgrv 422
|
330
....*....|..
gi 124807131 594 ----KLSQGEYI 601
Cdd:cd05921 423 aedfKLASGTWV 434
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
460-590 |
7.76e-09 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 59.00 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 460 LEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTEtaGAILGNHADD--EH-FEYIGGPIAPNTKYKVrtwetYKATDT- 535
Cdd:COG1021 302 LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE--GLVNYTRLDDpeEViLTTQGRPISPDDEVRI-----VDEDGNp 374
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 124807131 536 LPKGE---LLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSK 590
Cdd:COG1021 375 VPPGEvgeLLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAK 432
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
299-602 |
8.07e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.79 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNqlfslYNHSVRERYSF---KNHLSYLPISHVFERTFAYSILMYGGTLNVW 375
Cdd:PRK12467 654 DPDNLAYVIYTSGSTGQPKGVAISHGALAN-----YVCVIAERLQLaadDSMLMVSTFAFDLGVTELFGALASGATLHLL 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 376 GKDINYFSKDIYntkenimggvpkvfCRIYTNIMTEIDNLPSPKRRLVRKILSlrksdhngpfskflesifhiskkikDK 455
Cdd:PRK12467 729 PPDCARDAEAFA--------------ALMADQGVTVLKIVPSHLQALLQASRV-------------------------AL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 456 VNPNLEIILsGGGKLSPDIAEE-FCYLLNIKYCQGYGLTETAGAI----LGNHADDEHFEYIGGPIAPNTKYKVRtwety 530
Cdd:PRK12467 770 PRPQRALVC-GGEALQVDLLARvRALGPGARLINHYGPTETTVGVstyeLSDEERDFGNVPIGQPLANLGLYILD----- 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 531 KATDTLP---KGELLIKSDSMFSGYFLEKECTKNAFTDDGY-------FKTGDIVQINDNGSVTFLDRSKGLVKLsQGEY 600
Cdd:PRK12467 844 HYLNPVPvgvVGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYRADGVIEYLGRMDHQVKI-RGFR 922
|
..
gi 124807131 601 IE 602
Cdd:PRK12467 923 IE 924
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
490-588 |
8.29e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 58.99 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 490 YGLTET-AGAILGNHADDEHFEYIGG--PIAPNTKYKVRTWETYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTDD 566
Cdd:PRK06164 326 YGSSEVqALVALQPATDPVSVRIEGGgrPASPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDD 405
|
90 100
....*....|....*....|..
gi 124807131 567 GYFKTGDIVQINDNGSVTFLDR 588
Cdd:PRK06164 406 GYFRTGDLGYTRGDGQFVYQTR 427
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
298-596 |
1.20e-08 |
|
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: 58.12 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 298 EDPDFvtsIVYTSGTSGKPKGVMlsnkniynqlfslynHSVRerysfknhlsyLPISHvfertfaysiLMYGGT-LNVWG 376
Cdd:cd05972 81 EDPAL---IYFTSGTTGLPKGVL---------------HTHS-----------YPLGH----------IPTAAYwLGLRP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 377 KDINYFSKD---IYNTKENIMG----GVPKVFC-------RIYTNIMTE--IDNL---PSPKRRLVRKILSLRKSDHngp 437
Cdd:cd05972 122 DDIHWNIADpgwAKGAWSSFFGpwllGATVFVYegprfdaERILELLERygVTSFcgpPTAYRMLIKQDLSSYKFSH--- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 438 fskflesifhiskkikdkvnpnLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETaGAILGNHAD-DEHFEYIGGPI 516
Cdd:cd05972 199 ----------------------LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTET-GLTVGNFPDmPVKPGSMGRPT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 517 aPNtkYKVRTweTYKATDTLPKGE-----LLIKSDSMFSGYFLEKECTKNAFTDDgYFKTGDIVQINDNGSVTFLDRSKG 591
Cdd:cd05972 256 -PG--YDVAI--IDDDGRELPPGEegdiaIKLPPPGLFLGYVGDPEKTEASIRGD-YYLTGDRAYRDEDGYFWFVGRADD 329
|
....*
gi 124807131 592 LVKLS 596
Cdd:cd05972 330 IIKSS 334
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
299-607 |
1.29e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 58.08 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLYN-----------HSvrerysfknhlsyLPISHVFERTFA-YSIL 366
Cdd:PRK07787 126 DPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEawqwtaddvlvHG-------------LPLFHVHGLVLGvLGPL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 367 MYGGTLNVWGKdinyFSKDIY----NTKENIMGGVPKVFCRIYTNimTEIDNLPSPKRRLVrkilslrksdhngpfskfl 442
Cdd:PRK07787 193 RIGNRFVHTGR----PTPEAYaqalSEGGTLYFGVPTVWSRIAAD--PEAARALRGARLLV------------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 443 esifhiskkikdkvnpnleiilSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAgAILGNHADDEHFE-YIGGPIApntk 521
Cdd:PRK07787 248 ----------------------SGSAALPVPVFDRLAALTGHRPVERYGMTETL-ITLSTRADGERRPgWVGLPLA---- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 522 yKVRTWETYKATDTLPK-----GELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDR-SKGLVK- 594
Cdd:PRK07787 301 -GVETRLVDEDGGPVPHdgetvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGReSTDLIKs 379
|
330
....*....|....*..
gi 124807131 595 ----LSQGEyIETDLLN 607
Cdd:PRK07787 380 ggyrIGAGE-IETALLG 395
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
287-588 |
2.02e-08 |
|
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: 57.44 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 287 KTQTKKFTIKneDPDFVTSIVYTSGTSGKPKGVMLSNKNIY--NQLFSLYNHSVRERYSFknhlSYLPISH-VFERTFAY 363
Cdd:cd05937 75 KLSGSRFVIV--DPDDPAILIYTSGTTGLPKAAAISWRRTLvtSNLLSHDLNLKNGDRTY----TCMPLYHgTAAFLGAC 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 364 SILMYGGTLNVWGK-DINYFSKDIYNTKENIMGGVPKVfCRIYTNIMteidnlPSPKRRlvrkilslrksDHNgpfskfl 442
Cdd:cd05937 149 NCLMSGGTLALSRKfSASQFWKDVRDSGATIIQYVGEL-CRYLLSTP------PSPYDR-----------DHK------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 443 esifhiskkikdkvnpnleIILSGGGKLSPDIAEEFCYLLNIKYC-QGYGLTE-------------TAGAIlGNHADDEH 508
Cdd:cd05937 204 -------------------VRVAWGNGLRPDIWERFRERFNVPEIgEFYAATEgvfaltnhnvgdfGAGAI-GHHGLIRR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 509 FEYIGG----PIAPNTKYKVRTWETYKAtDTLPKGE-------LLIKSDSMFSGYFLEKECTKNAF-TD-----DGYFKT 571
Cdd:cd05937 264 WKFENQvvlvKMDPETDDPIRDPKTGFC-VRAPVGEpgemlgrVPFKNREAFQGYLHNEDATESKLvRDvfrkgDIYFRT 342
|
330
....*....|....*..
gi 124807131 572 GDIVQINDNGSVTFLDR 588
Cdd:cd05937 343 GDLLRQDADGRWYFLDR 359
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
299-590 |
3.05e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 56.92 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLYnhsvrERYSFKNHLSYL---PISHVfERTFAYSILMYGGTLNVW 375
Cdd:PRK06188 166 LPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQL-----AEWEWPADPRFLmctPLSHA-GGAFFLPTLLRGGTVIVL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 376 GK-DINYFSKDIYNTKENIMGGVPkvfcriyTNIMTEIDNLPSPKRRLvrkilslrksdhngpfskflesifhiskkikd 454
Cdd:PRK06188 240 AKfDPAEVLRAIEEQRITATFLVP-------TMIYALLDHPDLRTRDL-------------------------------- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 455 kvnPNLEIILSGGGKLSPD-IAEEFCYLLNIkYCQGYGLTETAGAIL----GNH--ADDEHFEYIGGPIAPNTkykVRTW 527
Cdd:PRK06188 281 ---SSLETVYYGASPMSPVrLAEAIERFGPI-FAQYYGQTEAPMVITylrkRDHdpDDPKRLTSCGRPTPGLR---VALL 353
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124807131 528 -ETYKATDTLPKGELLIKSDSMFSGYFLEKECTKNAFTdDGYFKTGDIVQINDNGSVTFLDRSK 590
Cdd:PRK06188 354 dEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFR-DGWLHTGDVAREDEDGFYYIVDRKK 416
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
293-609 |
1.10e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 55.21 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 293 FTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKN-IYNQLFSLYNHSVRERYSFknhLSYLPISHVfertfaysilmYGgt 371
Cdd:PRK06334 175 FGVSDKDPEDVAVILFTSGTEKLPKGVPLTHANlLANQRACLKFFSPKEDDVM---MSFLPPFHA-----------YG-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 372 lnvwgkdinyfskdiYN--TKENIMGGVPKVFCRiytnimteidNLPSPKrrlvrKILSLRKSDHN---GPFSKFLESIF 446
Cdd:PRK06334 239 ---------------FNscTLFPLLSGVPVVFAY----------NPLYPK-----KIVEMIDEAKVtflGSTPVFFDYIL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 447 HISKKiKDKVNPNLEIILSGGGKLSPDIAEEFC-YLLNIKYCQGYGLTETAGAILGNHADD-EHFEYIGGPIApNTKYKV 524
Cdd:PRK06334 289 KTAKK-QESCLPSLRFVVIGGDAFKDSLYQEALkTFPHIQLRQGYGTTECSPVITINTVNSpKHESCVGMPIR-GMDVLI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 525 RTWETYKATDTLPKGELLIKSDSMFSGYFLEKE-CTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSqGEYIET 603
Cdd:PRK06334 367 VSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFgQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSL 445
|
....*.
gi 124807131 604 DLLNNL 609
Cdd:PRK06334 446 EALESI 451
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
282-589 |
1.54e-07 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 54.73 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 282 FDDMTKTQTKKFTI---KNEDPDFvtsIVYTSGTSGKPKGVMLSNKNIYNQLfslynhsvreRYSFKNHLSYLP------ 352
Cdd:COG0365 165 WDELLAAASAEFEPeptDADDPLF---ILYTSGTTGKPKGVVHTHGGYLVHA----------ATTAKYVLDLKPgdvfwc 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 353 ISHVFertFAY--------------SILMYGGTLNVWGKDInyFSKDIYNTKENIMGGVPKVfcriYTNIMTEIDNLPSp 418
Cdd:COG0365 232 TADIG---WATghsyivygpllngaTVVLYEGRPDFPDPGR--LWELIEKYGVTVFFTAPTA----IRALMKAGDEPLK- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 419 KRRLVrkilSLRksdhngpfskflesifhiskkikdkvnpnleIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGA 498
Cdd:COG0365 302 KYDLS----SLR-------------------------------LLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 499 ILGNHA---------------------DDEhfeyiGGPIAPNTkykvrtwetykatdtlpKGELLIKSD--SMFSGYFLE 555
Cdd:COG0365 347 FISNLPglpvkpgsmgkpvpgydvavvDED-----GNPVPPGE-----------------EGELVIKGPwpGMFRGYWND 404
|
330 340 350
....*....|....*....|....*....|....*.
gi 124807131 556 KECTKNAF--TDDGYFKTGDIVQINDNGSVTFLDRS 589
Cdd:COG0365 405 PERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRS 440
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
458-606 |
2.05e-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: 54.26 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 458 PNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTEtaGAILGNHADDEHfEYI----GGPIAPNTKykVRTWEtyKAT 533
Cdd:cd05920 255 SSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE--GLLNYTRLDDPD-EVIihtqGRPMSPDDE--IRVVD--EEG 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 534 DTLPKGE---LLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLV-----KLSQGEyIETDL 605
Cdd:cd05920 328 NPVPPGEegeLLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQInrggeKIAAEE-VENLL 406
|
.
gi 124807131 606 L 606
Cdd:cd05920 407 L 407
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
299-598 |
3.91e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 53.73 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGV-----ML-SNKNIYNQLFS--LYNHSVRerysfknhLSYLPISHVFERTFAYSILMY-G 369
Cdd:PRK08180 207 GPDTIAKFLFTSGSTGLPKAVinthrMLcANQQMLAQTFPflAEEPPVL--------VDWLPWNHTFGGNHNLGIVLYnG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 370 GTLnvwgkdinY----------FSKDIYNTKEnimggvpkVFCRIYTNImteidnlpsPK-----RRLVRKILSLRKSdh 434
Cdd:PRK08180 279 GTL--------YiddgkptpggFDETLRNLRE--------ISPTVYFNV---------PKgwemlVPALERDAALRRR-- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 435 ngpfskFLEsifhiskkikdkvnpNLEIILSGGGKLSPDI-------AEEFCYLLnIKYCQGYGLTETAGAILGNHADDE 507
Cdd:PRK08180 332 ------FFS---------------RLKLLFYAGAALSQDVwdrldrvAEATCGER-IRMMTGLGMTETAPSATFTTGPLS 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 508 HFEYIGGPiAPNTKYKVrtwetykatdtLPKG---ELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGsvt 584
Cdd:PRK08180 390 RAGNIGLP-APGCEVKL-----------VPVGgklEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVDPA--- 454
|
330 340
....*....|....*....|...
gi 124807131 585 flDRSKGLV---------KLSQG 598
Cdd:PRK08180 455 --DPERGLMfdgriaedfKLSSG 475
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
296-596 |
4.19e-07 |
|
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: 53.27 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 296 KNEDPdfvtSIVY-TSGTSGKPKgvMLSNKNIY---NQLFSLYNHSVRERysfknhlsylpishvferTFAYSILMYGGT 371
Cdd:cd05970 183 CGEDI----LLVYfSSGTTGMPK--MVEHDFTYplgHIVTAKYWQNVREG------------------GLHLTVADTGWG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 372 LNVWGKdinyfskdIYNtkENIMGgvpkvfCRIYTNIMTEIDnlpsPKRrLVRKILSLRKSDHNGPFSKFLesiFHISKK 451
Cdd:cd05970 239 KAVWGK--------IYG--QWIAG------AAVFVYDYDKFD----PKA-LLEKLSKYGVTTFCAPPTIYR---FLIRED 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 452 IKDKVNPNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAIlgnhADDEHFEYIGGPIA-PNTKYKVRTWETY 530
Cdd:cd05970 295 LSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTI----ATFPWMEPKPGSMGkPAPGYEIDLIDRE 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124807131 531 -KATDTLPKGELLIKSDS-----MFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLS 596
Cdd:cd05970 371 gRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS 441
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
300-593 |
8.35e-07 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 52.65 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 300 PDFVTSIVYTSGTSGKPKGVMLSNKN-IYN----QLFSLYNHSvrerysfKNHLSYLPISHVFErtfAYSILMY----GG 370
Cdd:PRK07529 212 PDDVAAYFHTGGTTGMPKLAQHTHGNeVANawlgALLLGLGPG-------DTVFCGLPLFHVNA---LLVTGLAplarGA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 371 TLnVWG-----KDINYFS---KDIYNTKENIMGGVPKVFcriytnimteidnlpspkrrlvrKILSLRKSD-HNgpfskf 441
Cdd:PRK07529 282 HV-VLAtpqgyRGPGVIAnfwKIVERYRINFLSGVPTVY-----------------------AALLQVPVDgHD------ 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 442 lesifhISkkikdkvnpNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEH-FEYIGGPIaPNT 520
Cdd:PRK07529 332 ------IS---------SLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERrIGSVGLRL-PYQ 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124807131 521 KYKV------RTWETYKATDTLpkGELLIKSDSMFSGYfLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLV 593
Cdd:PRK07529 396 RVRVvilddaGRYLRDCAVDEV--GVLCIAGPNVFSGY-LEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI 471
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
296-593 |
9.83e-07 |
|
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: 52.31 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 296 KNEDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLfslynHSVRERYSFKNH---LSYLPISHVF-ERTFAYSILMYGGt 371
Cdd:cd05926 144 GVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASA-----TNITNTYKLTPDdrtLVVMPLFHVHgLVASLLSTLAAGG- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 372 lNVW---GKDINYFSKDIYNTKenimggvpkvfCRIYTNIMTeidnlpspkrrLVRKILSLRKSDHNGPFSKflesifhi 448
Cdd:cd05926 218 -SVVlppRFSASTFWPDVRDYN-----------ATWYTAVPT-----------IHQILLNRPEPNPESPPPK-------- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 449 skkikdkvnpnLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGN--HADDEHFEYIGGPIAPNTKYKVRT 526
Cdd:cd05926 267 -----------LRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKPVGVEVRILDED 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124807131 527 WETYKATDtlpKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLV 593
Cdd:cd05926 336 GEILPPGV---VGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI 399
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
460-593 |
1.31e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 51.33 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 460 LEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNhaddehfeYIGGPIAP----------NTKYKVRTWET 529
Cdd:cd05944 123 LRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVN--------PPDGPKRPgsvglrlpyaRVRIKVLDGVG 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124807131 530 YKATDTLPK--GELLIKSDSMFSGYfLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLV 593
Cdd:cd05944 195 RLLRDCAPDevGEICVAGPGVFGGY-LYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI 259
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
306-640 |
1.46e-06 |
|
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: 51.63 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIYNQLFSLynhsvRERYSFKNHLSYLPIS---HVFE---RTFAYSiLMYGGTLNVwgkdi 379
Cdd:cd17648 99 AIYTSGTTGKPKGVLVEHGSVVNLRTSL-----SERYFGRDNGDEAVLFfsnYVFDffvEQMTLA-LLNGQKLVV----- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 380 nyfskdiyntKENIMGGVPKVFCR-IYTNIMTEIDNLPSpkrrlVRKILSLRKSDHngpfskflesifhiskkikdkvnp 458
Cdd:cd17648 168 ----------PPDEMRFDPDRFYAyINREKVTYLSGTPS-----VLQQYDLARLPH------------------------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 459 nLEIILSGGGKLSP----DIAEEFCYLLNikycQGYGLTETAgaiLGNH-----ADDEHFEYIGGPIaPNTKYKVRTwet 529
Cdd:cd17648 209 -LKRVDAAGEEFTApvfeKLRSRFAGLII----NAYGPTETT---VTNHkrffpGDQRFDKSLGRPV-RNTKCYVLN--- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 530 yKATDTLP---KGELLIKSDSMFSGYFLEKECTKNAFTDDGY--------------FKTGDIVQINDNGSVTFLDRSKGL 592
Cdd:cd17648 277 -DAMKRVPvgaVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLGRNDFQ 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 124807131 593 VKLsQGEYIETDLLNNLYSQISFINNCVVYGDDSMDGPLAIIsvDKYL 640
Cdd:cd17648 356 VKI-RGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRI--QKYL 400
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
306-595 |
1.50e-06 |
|
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: 52.17 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIYNQLfslynHSVRERYSFKNHLSYL---PISH---VFErtfAYSILMYGGTLNV----W 375
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVNLL-----AWMQRRYGLGPGDRVLqfaSLSFdasVWE---IFGALLSGATLVLappeA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 376 GKDINYFSKDIynTKENImggvpkvfcriytNIMteidNLPsPkrrlvrkilSLrksdhngpFSKFLESIFhiskkikdK 455
Cdd:COG1020 694 RRDPAALAELL--ARHRV-------------TVL----NLT-P---------SL--------LRALLDAAP--------E 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 456 VNPNLEIILSGGGKLSPDIAEEF------CYLLNikycqGYGLTETA-GAILGNHADDEHFEY---IGGPIaPNTKYKVR 525
Cdd:COG1020 729 ALPSLRLVLVGGEALPPELVRRWrarlpgARLVN-----LYGPTETTvDSTYYEVTPPDADGGsvpIGRPI-ANTRVYVL 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 526 twetykatDT----LP---KGELLIKSDSMFSGY----------FLEkectkNAFTDDG--YFKTGDIVQINDNGSVTFL 586
Cdd:COG1020 803 --------DAhlqpVPvgvPGELYIGGAGLARGYlnrpeltaerFVA-----DPFGFPGarLYRTGDLARWLPDGNLEFL 869
|
....*....
gi 124807131 587 DRSKGLVKL 595
Cdd:COG1020 870 GRADDQVKI 878
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
299-601 |
2.66e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 50.93 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQlfslyNHSVRERYSFKNH---LSYLPISHVFERTFAYSILMYGGTLNVW 375
Cdd:PRK12583 199 DRDDPINIQYTSGTTGFPKGATLSHHNILNN-----GYFVAESLGLTEHdrlCVPVPLYHCFGMVLANLGCMTVGACLVY 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 376 GKDinYFSKD-----IYNTKENIMGGVPKVFcriytnimteIDNLPSPKRRLVrKILSLRKSDHNGPfskflESIFHISK 450
Cdd:PRK12583 274 PNE--AFDPLatlqaVEEERCTALYGVPTMF----------IAELDHPQRGNF-DLSSLRTGIMAGA-----PCPIEVMR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 451 KIKDKVN-PNLEIilsgggklspdiaeefcyllnikycqGYGLTETAGAILGNHADDE---HFEYIgGPIAPNTKYKVrt 526
Cdd:PRK12583 336 RVMDEMHmAEVQI--------------------------AYGMTETSPVSLQTTAADDlerRVETV-GRTQPHLEVKV-- 386
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124807131 527 weTYKATDTLPK---GELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSKGLVkLSQGEYI 601
Cdd:PRK12583 387 --VDPDGATVPRgeiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENI 461
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
460-596 |
3.03e-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: 341277 [Multi-domain] Cd Length: 437 Bit Score: 50.59 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 460 LEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETaGAILGNHADDEHFEYIGGPIAPNTKYKVRTWEtyKATDTLPKG 539
Cdd:cd05973 207 LRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTEL-GMVLANHHALEHPVHAGSAGRAMPGWRVAVLD--DDGDELGPG 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124807131 540 ELLI------KSDSM-FSGYFLEKECTknafTDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLS 596
Cdd:cd05973 284 EPGRlaidiaNSPLMwFRGYQLPDTPA----IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMS 343
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
306-621 |
3.82e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 50.28 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNI------YNQLFSLYNHSV---RERYSFKnhLSYLPIshvfertfaYSILMYGGTLNVWG 376
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHDNLvsftnwMLEDFALPEGPQflnQAPYSFD--LSVMDL---------YPTLASGGTLVALP 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 377 KD-INYFsKDIYNTkenimggVPKVFCRIYTNImteidnlPSpkrrlvrkilslrksdhngpfskFLESIFhISKKIKDK 455
Cdd:PRK04813 217 KDmTANF-KQLFET-------LPQLPINVWVST-------PS-----------------------FADMCL-LDPSFNEE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 456 VNPNLEIILSGGGKLSPDIAEEfcyLLNiKYCQG-----YGLTETAGAILGNHADDEHFE-YIGGPIA---PNTKYKVRT 526
Cdd:PRK04813 258 HLPNLTHFLFCGEELPHKTAKK---LLE-RFPSAtiyntYGPTEATVAVTSIEITDEMLDqYKRLPIGyakPDSPLLIID 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 527 WETYKATDTlPKGELLIKSDSMFSGYFLEKECTKNAF-TDDGY--FKTGDIVQInDNGSVTFLDRSKGLVKLSqGEYIET 603
Cdd:PRK04813 334 EEGTKLPDG-EQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYL-EDGLLFYQGRIDFQIKLN-GYRIEL 410
|
330
....*....|....*...
gi 124807131 604 DLLNNLYSQISFINNCVV 621
Cdd:PRK04813 411 EEIEQNLRQSSYVESAVV 428
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
460-601 |
4.79e-06 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 50.14 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 460 LEIILSGGGklSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHfeyiG--GPIAPNTKYKVRTWETYKATDTLP 537
Cdd:PRK06155 296 VRVALGPGV--PAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQRP----GsmGRLAPGFEARVVDEHDQELPDGEP 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124807131 538 kGELLIKSD---SMFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTFLDRSKGLVKlSQGEYI 601
Cdd:PRK06155 370 -GELLLRADepfAFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENI 433
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
303-590 |
5.29e-06 |
|
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: 49.42 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 303 VTSIVYTSGTSGKPKGVMLSNKniynQLFSLY-----NHSVRE--RYSFKNhlsylPISHvferTFAY-----SILMYGG 370
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHR----QTLRAAaawadCADLTEddRYLIIN-----PFFH----TFGYkagivACLLTGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 371 TLnvwgkdinyFSKDIYNtkenimggVPKVFCRIYTNimtEIDNLPspkrrlvrkilslrksdhnGPFSKFLeSIFHISK 450
Cdd:cd17638 69 TV---------VPVAVFD--------VDAILEAIERE---RITVLP-------------------GPPTLFQ-SLLDHPG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 451 KIKDKVNpNLEIILSGGGKLSPDIAEEFCYLLNIK-YCQGYGLTETAGAILGNHADDehFEYI----GGPIApntKYKVR 525
Cdd:cd17638 109 RKKFDLS-SLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVATMCRPGDD--AETVattcGRACP---GFEVR 182
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124807131 526 TWEtykatdtlpKGELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSK 590
Cdd:cd17638 183 IAD---------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLK 238
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
308-601 |
6.84e-06 |
|
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: 49.67 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 308 YTSGTSGKPKGVMLSNKNIYnqlfslynhSVRERYSfKNHLSYLPISHVFERT---FAYSI-------LMYGGT--LNVW 375
Cdd:cd05959 170 YSSGSTGRPKGVVHLHADIY---------WTAELYA-RNVLGIREDDVCFSAAklfFAYGLgnsltfpLSVGATtvLMPE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 376 GKDINYFSKDIYNTKENIMGGVPKVFcriytNIMTEIDNLPSpkrrlvRKILSLRksdhngpfskflesifhiskkikdk 455
Cdd:cd05959 240 RPTPAAVFKRIRRYRPTVFFGVPTLY-----AAMLAAPNLPS------RDLSSLR------------------------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 456 vnpnleIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEYIGGPIaPNTKYKVRTWETYKATDT 535
Cdd:cd05959 284 ------LCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPV-PGYEVELRDEDGGDVADG 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124807131 536 LPkGELLIKSDSMFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLSqGEYI 601
Cdd:cd05959 357 EP-GELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVS-GIWV 419
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
299-602 |
1.23e-05 |
|
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: 48.49 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLfslYNHSVR-ERYSFKNHLSYLPISH--VFERTFAYsiLMYGGTLNV- 374
Cdd:cd17651 134 DADDLAYVIYTSGSTGRPKGVVMPHRSLANLV---AWQARAsSLGPGARTLQFAGLGFdvSVQEIFST--LCAGATLVLp 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 375 ---WGKDINYFSKdiyntkenimggvpkvFCRiyTNIMTEIDnLPSPkrrLVRKILslrksDHNGPFSKFLesifhiskk 451
Cdd:cd17651 209 peeVRTDPPALAA----------------WLD--EQRISRVF-LPTV---ALRALA-----EHGRPLGVRL--------- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 452 ikdkvnPNLEIILSGGGKLS--PDIAEEFCYLLNIKYCQGYGLTE----TAGAILGNHADDEHFEYIGGPIApNTKYKVR 525
Cdd:cd17651 253 ------AALRYLLTGGEQLVltEDLREFCAGLPGLRLHNHYGPTEthvvTALSLPGDPAAWPAPPPIGRPID-NTRVYVL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 526 TWETYKATDTLPkGELLIKSDSMFSGYFLEKECTKNAFTDDGY------FKTGDIVQINDNGSVTFLDRSKGLVKLSqGE 599
Cdd:cd17651 326 DAALRPVPPGVP-GELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGRADDQVKIR-GF 403
|
...
gi 124807131 600 YIE 602
Cdd:cd17651 404 RIE 406
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
282-609 |
1.38e-05 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 48.59 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 282 FDDMTKTQTKKFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNK-NIYNQLFSLYNHSVRERySFKNHLSYLPISHVFERT 360
Cdd:PRK06018 158 YEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRsNVLHALMANNGDALGTS-AADTMLPVVPLFHANSWG 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 361 FAYSILMYGGTLNVWGKDINYFSkdIY----NTKENIMGGVPKVFCRIYTNIMTEidnlpspkrrlvrkilslrksdhng 436
Cdd:PRK06018 237 IAFSAPSMGTKLVMPGAKLDGAS--VYelldTEKVTFTAGVPTVWLMLLQYMEKE------------------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 437 pfskflesifhiskkikDKVNPNLEIILSGGGKLSPDIAEEFcYLLNIKYCQGYGLTE-----TAGAI---LGNHADDEH 508
Cdd:PRK06018 290 -----------------GLKLPHLKMVVCGGSAMPRSMIKAF-EDMGVEVRHAWGMTEmsplgTLAALkppFSKLPGDAR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 509 FEYI---GGPIapntkYKVRTWETYKATDTLPK-----GELLIKSDSMFSGYFLEKectKNAFTDDGYFKTGDIVQINDN 580
Cdd:PRK06018 352 LDVLqkqGYPP-----FGVEMKITDDAGKELPWdgktfGRLKVRGPAVAAAYYRVD---GEILDDDGFFDTGDVATIDAY 423
|
330 340
....*....|....*....|....*....
gi 124807131 581 GSVTFLDRSKGLVKlSQGEYIETDLLNNL 609
Cdd:PRK06018 424 GYMRITDRSKDVIK-SGGEWISSIDLENL 451
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
299-328 |
1.65e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 48.27 E-value: 1.65e-05
10 20 30
....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYN 328
Cdd:PRK08315 197 DPDDPINIQYTSGTTGFPKGATLTHRNILN 226
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
299-595 |
2.13e-05 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 48.04 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSL---YNHSVRERYSFKNHLSYlPIShVFERTFAysiLMYGGTLNV- 374
Cdd:cd17646 136 RPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMqdeYPLGPGDRVLQKTPLSF-DVS-VWELFWP---LVAGARLVVa 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 375 ---WGKDINYFSKDIynTKENImggvpkvfcriytnimTEIDNLPSPKRRLVRkilSLRKSDHngpfskflesifhiskk 451
Cdd:cd17646 211 rpgGHRDPAYLAALI--REHGV----------------TTCHFVPSMLRVFLA---EPAAGSC----------------- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 452 ikdkvnPNLEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAGAILGNHADDEHFEY---IGGPIaPNTkykvrtwE 528
Cdd:cd17646 253 ------ASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPsvpIGRPV-PNT-------R 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124807131 529 TYKATDTL-PK-----GELLIKSDSMFSGYFLEKECTKNAFTDDGY------FKTGDIVQINDNGSVTFLDRSKGLVKL 595
Cdd:cd17646 319 LYVLDDALrPVpvgvpGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFLGRSDDQVKI 397
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
539-647 |
4.58e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 47.08 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 539 GELLIKSDSMFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTFLDRSKGLVkLSQGEYIE-TDLLNNLYSQISFIN 617
Cdd:PRK07786 372 GEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYcAEVENVLASHPDIVE 449
|
90 100 110
....*....|....*....|....*....|..
gi 124807131 618 NCVVYGDDSMDG--PLAIISVDKYLLFLSLKD 647
Cdd:PRK07786 450 VAVIGRADEKWGevPVAVAAVRNDDAALTLED 481
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
460-590 |
4.63e-05 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 46.91 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 460 LEIILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETagaiLGNHA----DDEH-FEYIGGPIAPNTKYKVRTwetyKATD 534
Cdd:PRK10946 302 LKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEG----LVNYTrlddSDERiFTTQGRPMSPDDEVWVAD----ADGN 373
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 124807131 535 TLPKGE---LLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGDIVQINDNGSVTFLDRSK 590
Cdd:PRK10946 374 PLPQGEvgrLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREK 432
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
462-638 |
5.85e-05 |
|
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: 45.86 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 462 IILSGGGKLSPDIAEEFC-YLLNIKYCQGYGLTETAgAILGNHADDEHFEYIGGPIAPNTKYKVRtwetykATDTLPKGE 540
Cdd:cd17633 114 SIFSSGQKLFESTKKKLKnIFPKANLIEFYGTSELS-FITYNFNQESRPPNSVGRPFPNVEIEIR------NADGGEIGK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 541 LLIKSDSMFSGYFLEKECTKnaftdDGYFKTGDIVQINDNGSVTFLDRSKGLVkLSQGEYIETDLLNNLYSQISFINNCV 620
Cdd:cd17633 187 IFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAI 260
|
170 180
....*....|....*....|.
gi 124807131 621 VYG-DDSMDG--PLAIISVDK 638
Cdd:cd17633 261 VVGiPDARFGeiAVALYSGDK 281
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
307-623 |
5.93e-05 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 46.19 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 307 VYTSGTSGKPKGVMLSNKNIYNQLFsLYNHSVRerySFKNHLSY--LPISHVFERTFAY-SILMYGGTLnVWGKDIN--Y 381
Cdd:cd05940 87 IYTSGTTGLPKAAIISHRRAWRGGA-FFAGSGG---ALPSDVLYtcLPLYHSTALIVGWsACLASGATL-VIRKKFSasN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 382 FSKDIYNTKENIMGGVPKVfCRIYTNIMTEIDNlpspKRRLVRKILSlrksdhNGpfskflesifhiskkikdkvnpnle 461
Cdd:cd05940 162 FWDDIRKYQATIFQYIGEL-CRYLLNQPPKPTE----RKHKVRMIFG------NG------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 462 iilsgggkLSPDIAEEFCYLLNI-KYCQGYGLTE----------TAGAIlGNHAddeHFEYIGGPIAPnTKYKVRTWETY 530
Cdd:cd05940 206 --------LRPDIWEEFKERFGVpRIAEFYAATEgnsgfinffgKPGAI-GRNP---SLLRKVAPLAL-VKYDLESGEPI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 531 KATDTL----PKGE--LL---IKSDSMFSGYFLEKECTKNAFTD-----DGYFKTGDIVQINDNGSVTFLDRSkGLVKLS 596
Cdd:cd05940 273 RDAEGRcikvPRGEpgLLisrINPLEPFDGYTDPAATEKKILRDvfkkgDAWFNTGDLMRLDGEGFWYFVDRL-GDTFRW 351
|
330 340
....*....|....*....|....*..
gi 124807131 597 QGEYIETDLLNNLYSQISFINNCVVYG 623
Cdd:cd05940 352 KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
294-585 |
1.28e-04 |
|
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: 45.56 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 294 TIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLFSLYNH---SVRERYsfknhLSYLPISHvfertfaySILMYGG 370
Cdd:cd05908 99 EVLCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNStewKTKDRI-----LSWMPLTH--------DMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 371 TLnvwgkdinyfSKDIYNTKENIMGgvPKVFCRIYTNIMTEIDNlpspkrrlvRKIlSLRKSDHNGpfSKFLESIFHiSK 450
Cdd:cd05908 166 HL----------APLIAGMNQYLMP--TRLFIRRPILWLKKASE---------HKA-TIVSSPNFG--YKYFLKTLK-PE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 451 KIKDKVNPNLEIILSGGGKLSPDIAEEFcyllnIKYCQGYGLTETA------------GAILGNHAD-------DEHFEY 511
Cdd:cd05908 221 KANDWDLSSIRMILNGAEPIDYELCHEF-----LDHMSKYGLKRNAilpvyglaeasvGASLPKAQSpfktitlGRRHVT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 512 IGGPIAPNTKYKVRTW---ETYKATD------------TLPK---GELLIKSDSMFSGYFLEKECTKNAFTDDGYFKTGD 573
Cdd:cd05908 296 HGEPEPEVDKKDSECLtfvEVGKPIDetdiricdednkILPDgyiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGD 375
|
330
....*....|..
gi 124807131 574 IVQINDNGSVTF 585
Cdd:cd05908 376 LGFIRNGRLVIT 387
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
292-326 |
2.26e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 44.96 E-value: 2.26e-04
10 20 30
....*....|....*....|....*....|....*
gi 124807131 292 KFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNI 326
Cdd:PRK06814 784 LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNL 818
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
92-606 |
3.22e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 44.35 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 92 ITYDNFFRKVSSFSHTLntyegkgiesKKYNEKQNNGIFkllgIYGSNSINWLASDLSAMMSGVTTLVMHSKFSIDVIVD 171
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVL----------LNLNISKNDNVL----IYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLID 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 172 ILnETQLEWLCLDLDLveGLLNH--INELPHLKNLIILDTLSKNKEINLNKEENNNDKKNKSSGNSTSVKGNdlsnmiei 249
Cdd:PTZ00237 159 RI-ETITPKLIITTNY--GILNDeiITFTPNLKEAIELSTFKPSNVITLFRNDITSESDLKKIETIPTIPNT-------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 250 tcsgpLEYDKEklkkynelkkkcekcgkklmlfddmtktqTKKFTIKNEDP--DFVT-------SIVYTSGTSGKPKGVM 320
Cdd:PTZ00237 228 -----LSWYDE-----------------------------IKKIKENNQSPfyEYVPvesshplYILYTSGTTGNSKAVV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 321 LSNKniyNQLFSL--YNHSVRERYSFKNHLSYLPISHVFERTFAYSILMYGGTLNVWGKDI---NYFSKDIYNTKENimg 395
Cdd:PTZ00237 274 RSNG---PHLVGLkyYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGIiknKHIEDDLWNTIEK--- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 396 gvPKVFCriytnimteidNLPSPKrrlvrKILSLRKSDHNGpfskflesifhisKKIKDKVN-PNLEIILSGGGKLSPDI 474
Cdd:PTZ00237 348 --HKVTH-----------TLTLPK-----TIRYLIKTDPEA-------------TIIRSKYDlSNLKEIWCGGEVIEESI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 475 AEEFCYLLNIKYCQGYGLTETAGA-ILGNHADDEHFEYIGGPiAPNTKYKVRTwETYKATDTLPKGELLIK---SDSMFS 550
Cdd:PTZ00237 397 PEYIENKLKIKSSRGYGQTEIGITyLYCYGHINIPYNATGVP-SIFIKPSILS-EDGKELNVNEIGEVAFKlpmPPSFAT 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124807131 551 GYFLEKECTKNAFTD-DGYFKTGDIVQINDNGSVTFLDRSKGLVKLS----QGEYIETDLL 606
Cdd:PTZ00237 475 TFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISgnkvQLNTIETSIL 535
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
284-623 |
4.83e-04 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 43.57 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 284 DMTKTQTKKFTIKNEDPDFVTSI--VYTSGTSGKPKGVMLSNkniynqlFSLYNHSVRERYSFKNHLSylpishvfertf 361
Cdd:cd05939 85 DPLLTQSSTEPPSQDDVNFRDKLfyIYTSGTTGLPKAAVIVH-------SRYYRIAAGAYYAFGMRPE------------ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 362 aysilmyggtlnvwgkDINYFSKDIYNTKENIMGgvpkvFCRIYTNIMTEIdnlpspkrrlVRKILSLRK-----SDHNG 436
Cdd:cd05939 146 ----------------DVVYDCLPLYHSAGGIMG-----VGQALLHGSTVV----------IRKKFSASNfwddcVKYNC 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 437 PFSKFLESI--FHISKKIKDKVNPNLEIILSGGGkLSPDIAEEFCYLLNIKYC-QGYGLTEtAGAILGNHadDEHFEYIG 513
Cdd:cd05939 195 TIVQYIGEIcrYLLAQPPSEEEQKHNVRLAVGNG-LRPQIWEQFVRRFGIPQIgEFYGATE-GNSSLVNI--DNHVGACG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 514 -GPIAPNTKYKVR-------TWETYKATDTL-------PKGEL---LIKSDSM--FSGYFLEKECTK----NAFTD-DGY 568
Cdd:cd05939 271 fNSRILPSVYPIRlikvdedTGELIRDSDGLcipcqpgEPGLLvgkIIQNDPLrrFDGYVNEGATNKkiarDVFKKgDSA 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 124807131 569 FKTGDIVQINDNGSVTFLDRSKGLVKLsQGEYIETDLLNNLYSQISFINNCVVYG 623
Cdd:cd05939 351 FLSGDVLVMDELGYLYFKDRTGDTFRW-KGENVSTTEVEGILSNVLGLEDVVVYG 404
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
299-602 |
5.50e-04 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 43.45 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIyNQLFS----LYNHSVRERYSFKNHLSylpishvfertFAYSI------LMY 368
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANV-LALFAatqrWFGFNEDDVWTLFHSYA-----------FDFSVweiwgaLLH 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 369 GGTLNVwgkdinyfskdiyntkenimggVPKvfcriytnimtEIDNLPSPKRRLVRK----ILSLRKSdhngPFSKFLES 444
Cdd:cd17643 159 GGRLVV----------------------VPY-----------EVARSPEDFARLLRDegvtVLNQTPS----AFYQLVEA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 445 IFHiskkiKDKVNPNLEIILSGGGKLSPDI----AEEFCY----LLNikycqGYGLTETA-----GAILGNHADDEHFEY 511
Cdd:cd17643 202 ADR-----DGRDPLALRYVIFGGEALEAAMlrpwAGRFGLdrpqLVN-----MYGITETTvhvtfRPLDAADLPAAAASP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 512 IGGPIApntkykvrTWETYKATDTL---PK---GELLIKSDSMFSGYFLEKECTK-----NAFTDDG--YFKTGDIVQIN 578
Cdd:cd17643 272 IGRPLP--------GLRVYVLDADGrpvPPgvvGELYVSGAGVARGYLGRPELTAerfvaNPFGGPGsrMYRTGDLARRL 343
|
330 340
....*....|....*....|....
gi 124807131 579 DNGSVTFLDRSKGLVKLSqGEYIE 602
Cdd:cd17643 344 PDGELEYLGRADEQVKIR-GFRIE 366
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
297-602 |
8.46e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 43.23 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 297 NEDPDFVTSIVYTSGTSGKPKGVMLSNKNIYNQLfslynHSVRERYSF---KNHLSYLPISHVFERTFAYSILMYGGTLN 373
Cdd:PRK12467 1714 NLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRL-----CATQEAYQLsaaDVVLQFTSFAFDVSVWELFWPLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 374 VWGKDINYFSKDIYNTkenimggvpkvfcrIYTNIMTEIDNLPSpkrrlvrkilslrksdhngPFSKFLESIFHISKKik 453
Cdd:PRK12467 1789 IAPPGAHRDPEQLIQL--------------IERQQVTTLHFVPS-------------------MLQQLLQMDEQVEHP-- 1833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 454 dkvnPNLEIILSGGGKLSPDIAEE-FCYLLNIKYCQGYGLTETAGAI---LGNHADDEHFEY--IGGPIApNTKykvrtw 527
Cdd:PRK12467 1834 ----LSLRRVVCGGEALEVEALRPwLERLPDTGLFNLYGPTETAVDVthwTCRRKDLEGRDSvpIGQPIA-NLS------ 1902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 528 eTYKATDTL---PK---GELLIKSDSMFSGYFLEKECTKNAFTDDGY-------FKTGDIVQINDNGSVTFLDRSKGLVK 594
Cdd:PRK12467 1903 -TYILDASLnpvPIgvaGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRADGVIEYLGRIDHQVK 1981
|
....*...
gi 124807131 595 LsQGEYIE 602
Cdd:PRK12467 1982 I-RGFRIE 1988
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
299-328 |
9.03e-04 |
|
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: 42.64 E-value: 9.03e-04
10 20 30
....*....|....*....|....*....|
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNIYN 328
Cdd:cd12114 124 APDDLAYVIFTSGSTGTPKGVMISHRAALN 153
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
298-320 |
1.96e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 41.66 E-value: 1.96e-03
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
539-599 |
1.97e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 41.46 E-value: 1.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124807131 539 GELLIKSDSMFSGYFLEKECTKNAFTDdGYFKTGDIVQINDNGSVTFLDRSKGLVKlSQGE 599
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAFRG-GWFHSGDLGVMDEEGYITVVDRKKDMIK-TGGE 426
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
299-326 |
2.24e-03 |
|
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: 41.42 E-value: 2.24e-03
10 20
....*....|....*....|....*...
gi 124807131 299 DPDFVTSIVYTSGTSGKPKGVMLSNKNI 326
Cdd:cd12117 134 SPDDLAYVMYTSGSTGRPKGVAVTHRGV 161
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
463-596 |
2.34e-03 |
|
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: 41.40 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 463 ILSGGGKLSPDIAEEFCYLLNIKYCQGYGLTETAgAILGNHAddehfeyiGGPIAPNTK------YKVRTWETykATDTL 536
Cdd:cd05974 205 VVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETT-ALVGNSP--------GQPVKAGSMgrplpgYRVALLDP--DGAPA 273
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124807131 537 PKGEL-LIKSDS----MFSGYFLEKECTKNAFtDDGYFKTGDIVQINDNGSVTFLDRSKGLVKLS 596
Cdd:cd05974 274 TEGEVaLDLGDTrpvgLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSS 337
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
299-326 |
2.34e-03 |
|
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: 41.31 E-value: 2.34e-03
10 20
....*....|....*....|....*...
gi 124807131 299 DPDfVTSIVYTSGTSGKPKGVMLSNKNI 326
Cdd:TIGR03098 162 DSD-MAAILYTSGSTGRPKGVVLSHRNL 188
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
298-320 |
2.40e-03 |
|
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: 41.46 E-value: 2.40e-03
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
279-607 |
3.06e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 40.85 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 279 LMLFDDMTKTQTKKFTIKNEDPDFVTSIVYTSGTSGKPKGVMLSNKNiynQLFSLYNHSVRERYSFKNHLSYLPIS---H 355
Cdd:PRK07008 154 LLCYETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRS---TVLHAYGAALPDAMGLSARDAVLPVVpmfH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 356 VFERTFAYSILMYGGTLNVWGKDINyfSKDIYNTKE----NIMGGVPKVFCRIYTNIMTEidnlpspkrrlvrkilSLRk 431
Cdd:PRK07008 231 VNAWGLPYSAPLTGAKLVLPGPDLD--GKSLYELIEaervTFSAGVPTVWLGLLNHMREA----------------GLR- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 432 sdhngpFSKFLESIFhiskkikdkvnpnleiilsGGGKLSPDIAEEFCYLLNIKYCQGYGLTE-----TAGAILGNH--- 503
Cdd:PRK07008 292 ------FSTLRRTVI-------------------GGSACPPAMIRTFEDEYGVEVIHAWGMTEmsplgTLCKLKWKHsql 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124807131 504 ADDEH---FEYIGGPIapntkYKVRTWETYKATDTLP-----KGELLIKSDSMFSGYFLEKECTknafTDDGYFKTGDIV 575
Cdd:PRK07008 347 PLDEQrklLEKQGRVI-----YGVDMKIVGDDGRELPwdgkaFGDLQVRGPWVIDRYFRGDASP----LVDGWFPTGDVA 417
|
330 340 350
....*....|....*....|....*....|...
gi 124807131 576 QINDNGSVTFLDRSKGLVKlSQGEYIET-DLLN 607
Cdd:PRK07008 418 TIDADGFMQITDRSKDVIK-SGGEWISSiDIEN 449
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
298-320 |
4.51e-03 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 40.62 E-value: 4.51e-03
10 20
....*....|....*....|...
gi 124807131 298 EDPDFvtsIVYTSGTSGKPKGVM 320
Cdd:cd05966 231 EDPLF---ILYTSGSTGKPKGVV 250
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
306-336 |
4.61e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 40.80 E-value: 4.61e-03
10 20 30
....*....|....*....|....*....|.
gi 124807131 306 IVYTSGTSGKPKGVMLSNKNIYNQLFSLYNH 336
Cdd:PRK10252 603 IIFTSGSTGRPKGVMVGQTAIVNRLLWMQNH 633
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
306-324 |
9.96e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 39.15 E-value: 9.96e-03
|
| |
