|
Name |
Accession |
Description |
Interval |
E-value |
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
9-601 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 719.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDYKTetWIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:COG1022 16 LLRRRAARFPDRVALREKEDGI--WQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAFRVMQLGSQLKRIIIFDREVKRDerDQTSIYFDDFLKLGEGHPHQA 168
Cdd:COG1022 94 PIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGLRD--DPRLLSLDELLALGREVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 169 EVDKRISESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTHVFERAWTCWCLSMGC 248
Cdd:COG1022 172 ELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP-LGPGDRTLSFLPLAHVFERTVSYYALAAGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 249 TLSINLRPADIQKTIKEIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLMLDAIKVGREHNlEYVYKGLTPPPVLHMK 328
Cdd:COG1022 251 TVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYA-RARLAGKSPSLLLRLK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 329 YKFYEKTIYSLLKKTIGiENGRFFPTAGAAIPPAVQEFVLSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQ 408
Cdd:COG1022 330 HALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 409 VKIGENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE-HLFLTERIKDLFKTSNGKYIAPQAIEAKLVV 487
Cdd:COG1022 409 VKIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDgFLRITGRKKDLIVTSGGKNVAPQPIENALKA 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 488 DRYIDQISIIADERKFVSALIIPEYKLVKEYADKKGIHYGSMEDLLRKPEIIELFKERIDTLQQQFAHYEQIKKFTLLPQ 567
Cdd:COG1022 489 SPLIEQAVVVGDGRPFLAALIVPDFEALGEWAEENGLPYTSYAELAQDPEVRALIQEEVDRANAGLSRAEQIKRFRLLPK 568
|
570 580 590
....*....|....*....|....*....|....
gi 2786809754 568 PFSMERGELTNTLKIKRSVLNKNYAVEIEKMYEE 601
Cdd:COG1022 569 EFTIENGELTPTLKLKRKVILEKYADLIEALYAG 602
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
33-587 |
1.80e-175 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 504.82 E-value: 1.80e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 33 WIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIF 112
Cdd:cd05907 3 WQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 113 VGeqlqydvafrvmqlgsqlkriiifdrevkrderdqtsiyfddflklgegHPhqaevdkrisesgnGDLANILYTSGTT 192
Cdd:cd05907 83 VE-------------------------------------------------DP--------------DDLATIIYTSGTT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 193 GDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTHVFE-RAWTCWCLSMGCTLSINLRPADIQKTIKEIRPTAM 271
Cdd:cd05907 100 GRPKGVMLSHRNILSNALALAERLP-ATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAETLLDDLSEVRPTVF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 272 CSVPRFWEKVYAGVqeKINETTGLKKKLMLDAIkvgrehnleyvykgltpppvlhmkykfyektiysllkktigIENGRF 351
Cdd:cd05907 179 LAVPRVWEKVYAAI--KVKAVPGLKRKLFDLAV-----------------------------------------GGRLRF 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 352 FPTAGAAIPPAVQEFVLSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKIGENNEIMLRGEGITHGYYKK 431
Cdd:cd05907 216 AASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADDGEILVRGPNVMLGYYKN 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 432 EAATKAAFTEDGWFHTGDAGYIKDE-HLFLTERIKDLFKTSNGKYIAPQAIEAKLVVDRYIDQISIIADERKFVSALIIP 510
Cdd:cd05907 296 PEATAEALDADGWLHTGDLGEIDEDgFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVP 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786809754 511 EYKLVKEYADKKGIHYGSMEDLLRKPEIIELFKERIDTLQQQFAHYEQIKKFTLLPQPFSMERGELTNTLKIKRSVL 587
Cdd:cd05907 376 DPEALEAWAEEHGIAYTDVAELAANPAVRAEIEAAVEAANARLSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
23-591 |
9.33e-114 |
|
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: 350.95 E-value: 9.33e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 23 LRYRDYKTetWIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYM 102
Cdd:cd17641 1 LREKDFGI--WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 103 VGDAEIRYIFVGEQLQYDVAFRVMQLGSQLKRIIIFDREVKRDERDQTSIYFDDFLKLGEGHP--HQAEVDKRISESGNG 180
Cdd:cd17641 79 LNYTGARVVIAEDEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDrrDPGLYEREVAAGKGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCY---EAAIPAHNERFPqlGDQDVimNFLPFTHVFERAWTCwCLSMGCTLSINL--R 255
Cdd:cd17641 159 DVAVLCTTSGTTGKPKLAMLSHGNFlghCAAYLAADPLGP--GDEYV--SVLPLPWIGEQMYSV-GQALVCGFIVNFpeE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 256 PADIQKTIKEIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLMLDAIKVGREhNLEYVYKGLTPPPVLHMKYKFYEKT 335
Cdd:cd17641 234 PETMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLR-ALDRGKRGRPVSLWLRLASWLADAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 336 IYSLLKKTIGIENGRFFPTAGAAIPPAVQEFVLSVGINMVAGYGLTESTA--TVACENDYDHvvGSVGRLMPHVQVKIGE 413
Cdd:cd17641 313 LFRPLRDRLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGayTVHRDGDVDP--DTVGVPFPGTEVRIDE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 414 NNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIK-DEHLFLTERIKDLFKTSNGKYIAPQAIEAKLVVDRYID 492
Cdd:cd17641 391 VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKeNGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 493 QISIIADERKFVSALIIPEYKLVKEYADKKGIHYGSMEDLLRKPEIIELFKERIDTLQQQFAHYEQIKKFTLLPQPFSME 572
Cdd:cd17641 471 EAVVLGAGRPYLTAFICIDYAIVGKWAEQRGIAFTTYTDLASRPEVYELIRKEVEKVNASLPEAQRIRRFLLLYKELDAD 550
|
570
....*....|....*....
gi 2786809754 573 RGELTNTLKIKRSVLNKNY 591
Cdd:cd17641 551 DGELTRTRKVRRGVIAEKY 569
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
27-599 |
7.47e-106 |
|
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: 329.56 E-value: 7.47e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 27 DYKtetWIpvSWNQFAATVKTVSNALIELGIGIQEN--IAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVG 104
Cdd:cd05927 2 PYE---WI--SYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 105 DAEIRyifvgeqlqydvafrvmqlgsqlkrIIIFDREVKrderdqtsIY-FDDFLKLGEGHPHQAEVDKRisesgnGDLA 183
Cdd:cd05927 77 HAEIS-------------------------IVFCDAGVK--------VYsLEEFEKLGKKNKVPPPPPKP------EDLA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 184 NILYTSGTTGDSKGVMLHHSCYEAAIPAHN---ERFPQLGDQDVIMNFLPFTHVFERAWTCWCLSMGCtlSINLRPADIQ 260
Cdd:cd05927 118 TICYTSGTTGNPKGVMLTHGNIVSNVAGVFkilEILNKINPTDVYISYLPLAHIFERVVEALFLYHGA--KIGFYSGDIR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 261 K---TIKEIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLmldaIKVGREHNLEYVYKGltpppvlHMKYK-FYEKTI 336
Cdd:cd05927 196 LlldDIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKL----FNFALNYKLAELRSG-------VVRASpFWDKLV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 337 YSLLKKTIGiENGRFFPTAGAAIPPAVQEFVLSV-GINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKI---- 411
Cdd:cd05927 265 FNKIKQALG-GNVRLMLTGSAPLSPEVLEFLRVAlGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLvdvp 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 -------GENN--EIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFKTSNGKYIAPQAI 481
Cdd:cd05927 344 emnydakDPNPrgEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWlPNGTLKIIDRKKNIFKLSQGEYVAPEKI 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 482 EAKLVVDRYIDQISIIAD-ERKFVSALIIPEYKLVKEYADKKGIHYGSMEDLLRKPEIIELFKERIDTL--QQQFAHYEQ 558
Cdd:cd05927 424 ENIYARSPFVAQIFVYGDsLKSFLVAIVVPDPDVLKEWAASKGGGTGSFEELCKNPEVKKAILEDLVRLgkENGLKGFEQ 503
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2786809754 559 IKKFTLLPQPFSMERGELTNTLKIKRSVLNKNYAVEIEKMY 599
Cdd:cd05927 504 VKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
33-599 |
1.91e-95 |
|
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: 304.28 E-value: 1.91e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 33 WIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIF 112
Cdd:cd05933 6 WHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 113 VGEQLQYDvafRVMQLGSQL---KRIIIFDREVKRDERDQTSiyFDDFLKLGEGHPhQAEVDKRISESGNGDLANILYTS 189
Cdd:cd05933 86 VENQKQLQ---KILQIQDKLphlKAIIQYKEPLKEKEPNLYS--WDEFMELGRSIP-DEQLDAIISSQKPNQCCTLIYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 190 GTTGDSKGVMLHH---SCYEAAIPAHNERFPQLGDQDVIMNFLPFTHVFERAWTCW-CLSMGCTLSINLRPA---DIQKT 262
Cdd:cd05933 160 GTTGMPKGVMLSHdniTWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWlPIKVGGQVYFAQPDAlkgTLVKT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 263 IKEIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLMLDAIKVGREHNLEYVyKGLTPPPvlhMKYKFYEKTIYSLLKK 342
Cdd:cd05933 240 LREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLM-GGESPSP---LFYRLAKKLVFKKVRK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 343 TIGIENGRFFPTAGAAIPPAVQEFVLSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKIGENN-----EI 417
Cdd:cd05933 316 ALGLDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDadgigEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 418 MLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFKTSNGKYIAPQAIEAklVVDRYIDQIS- 495
Cdd:cd05933 396 CFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLdEDGFLYITGRIKELIITAGGENVPPVPIED--AVKKELPIISn 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 496 --IIADERKFVSALI-----------IPEYKL---VKEYADKKGIHYGSMEDLL--RKPEIIELFKERIDTLQQQFAHYE 557
Cdd:cd05933 474 amLIGDKRKFLSMLLtlkcevnpetgEPLDELteeAIEFCRKLGSQATRVSEIAggKDPKVYEAIEEGIKRVNKKAISNA 553
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2786809754 558 Q-IKKFTLLPQPFSMERGELTNTLKIKRSVLNKNYAVEIEKMY 599
Cdd:cd05933 554 QkIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
36-586 |
4.45e-87 |
|
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: 278.47 E-value: 4.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 36 VSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVge 115
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 116 qlqydvafrvmqlgsqlkriiifdrevkrderdqtsiyfddflklgeghphqaevdkrisESGNGDLANILYTSGTTGDS 195
Cdd:cd17640 84 ------------------------------------------------------------ENDSDDLATIIYTSGTTGNP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 196 KGVMLHH--------SCYEAAIPAHNERFpqlgdqdviMNFLPFTHVFERAWTCWCLSMGCTL---SINLRPADIQKtik 264
Cdd:cd17640 104 KGVMLTHanllhqirSLSDIVPPQPGDRF---------LSILPIWHSYERSAEYFIFACGCSQaytSIRTLKDDLKR--- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 265 eIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLMLDAIKVGrehnleyvykgltpppvlhmkykfyektiysllkkti 344
Cdd:cd17640 172 -VKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFLSGG------------------------------------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 345 gieNGRFFPTAGAAIPPAVQEFVLSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKI-----------GE 413
Cdd:cd17640 214 ---IFKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIvdpegnvvlppGE 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 414 NNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFKTSNGKYIAPQAIEAKLVVDRYID 492
Cdd:cd17640 291 KGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLtCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIE 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 493 QISIIADERKFVSALIIPEYKLVKEYADKKGIHYGS-MEDLLRKPEIIELFKERIDTLQQQ---FAHYEQIKKFTLLPQP 568
Cdd:cd17640 371 QIMVVGQDQKRLGALIVPNFEELEKWAKESGVKLANdRSQLLASKKVLKLYKNEIKDEISNrpgFKSFEQIAPFALLEEP 450
|
570
....*....|....*...
gi 2786809754 569 FsMERGELTNTLKIKRSV 586
Cdd:cd17640 451 F-IENGEMTQTMKIKRNV 467
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
166-587 |
9.04e-82 |
|
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: 265.62 E-value: 9.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 166 HQAEVDKRISESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQ-LGDQDVIMNFLPFTHVFERAWTCWCL 244
Cdd:cd17639 74 NETECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPElLGPDDRYLAYLPLAHIFELAAENVCL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 245 SMGCTLSINlRPADIQKTIK--------EIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLMLDAIkvgrEHNLEYVY 316
Cdd:cd17639 154 YRGGTIGYG-SPRTLTDKSKrgckgdltEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAY----QSKLKALK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 317 KGLTPPpvlhmkykFYEKTIYSLLKKTIGiENGRFFPTAGAAIPPAVQEFVLSVGINMVAGYGLTESTAtVACENDYDHV 396
Cdd:cd17639 229 EGPGTP--------LLDELVFKKVRAALG-GRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCA-GGTVQDPGDL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 397 -VGSVGRLMPHVQVKI------GENN-------EIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLT 461
Cdd:cd17639 299 eTGRVGPPLPCCEIKLvdweegGYSTdkppprgEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFhPDGTLKII 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 462 ERIKDLFKTSNGKYIAPQAIEAKLVVDRYIDQISIIADERK-FVSALIIPEYKLVKEYADKKGIHYGSMEDLLRKPEIIE 540
Cdd:cd17639 379 DRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKsYPVAIVVPNEKHLTKLAEKHGVINSEWEELCEDKKLQK 458
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2786809754 541 L-FKERIDT-LQQQFAHYEQIKKFTLLPQPFSMERGELTNTLKIKRSVL 587
Cdd:cd17639 459 AvLKSLAETaRAAGLEKFEIPQGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
10-471 |
2.76e-81 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 261.86 E-value: 2.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 10 IQRQARKYGDRVVLRYRDYKTetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVP 89
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRR-----LTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 90 FYATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAFRVMQLGSQLKRIIIFDrevkRDERDQTSIYFDDFLKLGEGHPHQAE 169
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLD----RDPVLKEEPLPEEAKPADVPPPPPPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 170 VDKRisesgngDLANILYTSGTTGDSKGVMLHH---SCYEAAIPAHNERFPQLGDQDVIMNFLPFTHVFERAWTCWC-LS 245
Cdd:pfam00501 152 PDPD-------DLAYIIYTSGTTGKPKGVMLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGpLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 246 MGCTL-----SINLRPADIQKTIKEIRPTAMCSVPRFWEKVYAGVQEKINETTGLkkklmldaikvgrehnleyvykglt 320
Cdd:pfam00501 225 AGATVvlppgFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSL------------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 321 pppvlhmkykfyektiysllkktigiengRFFPTAGAAIPPAVQEFVLSVGINMVA-GYGLTESTATVAC---ENDYDHV 396
Cdd:pfam00501 280 -----------------------------RLVLSGGAPLPPELARRFRELFGGALVnGYGLTETTGVVTTplpLDEDLRS 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 397 VGSVGRLMPHVQVKI-----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERI 464
Cdd:pfam00501 331 LGSVGRPLPGTEVKIvddetgepvppGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRdEDGYLEIVGRK 410
|
....*..
gi 2786809754 465 KDLFKTS 471
Cdd:pfam00501 411 KDQIKLG 417
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
42-601 |
2.31e-78 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 260.80 E-value: 2.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 42 AATVKT-VSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGEQ-LQY 119
Cdd:PLN02736 84 AGTARTaIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQtLNT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 120 DVAFrVMQLGSqLKRIIIfdreVKRDERDQTS---------IYFDDFLKLGEGHPHQAEVDKrisesgNGDLANILYTSG 190
Cdd:PLN02736 164 LLSC-LSEIPS-VRLIVV----VGGADEPLPSlpsgtgveiVTYSKLLAQGRSSPQPFRPPK------PEDVATICYTSG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 191 TTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTHVFERAWTCWCLSMGctLSINLRPADIQK---TIKEIR 267
Cdd:PLN02736 232 TTGTPKGVVLTHGNLIANVAGSSLSTK-FYPSDVHISYLPLAHIYERVNQIVMLHYG--VAVGFYQGDNLKlmdDLAALR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 268 PTAMCSVPRFWEKVYAGVQEKINETTGLKKKLMLDAIKVGReHNLEyvyKGLTPPPVlhmkykfYEKTIYSLLKKTIGie 347
Cdd:PLN02736 309 PTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKK-QALE---NGKNPSPM-------WDRLVFNKIKAKLG-- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 348 nGRF-FPTAGAA-IPPAVQEFV-LSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVK---IGENN------ 415
Cdd:PLN02736 376 -GRVrFMSSGASpLSPDVMEFLrICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKlvdVPEMNytsedq 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 416 -----EIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAG-YIKDEHLFLTERIKDLFKTSNGKYIAPQAIEAKLVVDR 489
Cdd:PLN02736 455 pyprgEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGlWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCK 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 490 YIDQISIIADE-RKFVSALIIPEYKLVKEYADKKGIHYGSMEDLLRKPEIIELFKERIDTL--QQQFAHYEQIKKFTLLP 566
Cdd:PLN02736 535 FVAQCFVYGDSlNSSLVAVVVVDPEVLKAWAASEGIKYEDLKQLCNDPRVRAAVLADMDAVgrEAQLRGFEFAKAVTLVP 614
|
570 580 590
....*....|....*....|....*....|....*
gi 2786809754 567 QPFSMERGELTNTLKIKRSVLNKNYAVEIEKMYEE 601
Cdd:PLN02736 615 EPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAE 649
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
37-591 |
1.06e-76 |
|
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: 252.39 E-value: 1.06e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 37 SWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGEQ 116
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 117 LQYDVAFRVmqLGSQLKRIIIFDREVKRDERDqtsiyFDDFLK----LGEGHPHQAEvdkrisesgngDLANILYTSGTT 192
Cdd:cd05932 88 DDWKAMAPG--VPEGLISISLPPPSAANCQYQ-----WDDLIAqhppLEERPTRFPE-----------QLATLIYTSGTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 193 GDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFTHVFERAWT--CWCLSmGCTL----SINLRPADIQKTikei 266
Cdd:cd05932 150 GQPKGVMLTFGSFAWAAQAGIEHI-GTEENDRMLSYLPLAHVTERVFVegGSLYG-GVLVafaeSLDTFVEDVQRA---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 267 RPTAMCSVPRFWEKVYAGVQEKINettglKKKLMLdaikvgrehnleyvykgLTPPPVLHmkykfyeKTIYSLLKKTIGI 346
Cdd:cd05932 224 RPTLFFSVPRLWTKFQQGVQDKIP-----QQKLNL-----------------LLKIPVVN-------SLVKRKVLKGLGL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 347 ENGRFFPTAGAAIPPAVQEFVLSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKIGENNEIMLRGEGITH 426
Cdd:cd05932 275 DQCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISEDGEILVRSPALMM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 427 GYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFKTSNGKYIAPQAIEAKLVVDRYIDQISIIADERKFVS 505
Cdd:cd05932 355 GYYKDPEATAEAFTADGFLRTGDKGELdADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPL 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 506 ALIIPEyklvkeyadkKGIHYGSmeDLLRKPEIIELFKERIDTLQQQFAHYEQIKKFTLLPQPFSMERGELTNTLKIKRS 585
Cdd:cd05932 435 ALVVLS----------EEARLRA--DAFARAELEASLRAHLARVNSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKRN 502
|
....*.
gi 2786809754 586 VLNKNY 591
Cdd:cd05932 503 VLEKAY 508
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
38-600 |
1.17e-66 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 230.39 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 38 WNQFAATVKTVSN---ALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVG 114
Cdd:PLN02387 106 WITYGQVFERVCNfasGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 115 -EQLQydvafRVMQLGSQL---KRIIIFDREVKRDE------RDQTSIYFDDFLKLGEGHPHQAEVDKRisesgnGDLAN 184
Cdd:PLN02387 186 sKQLK-----KLIDISSQLetvKRVIYMDDEGVDSDsslsgsSNWTVSSFSEVEKLGKENPVDPDLPSP------NDIAV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 185 ILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGDQDVIMNFLPFTHVFERAWTCWCLSMGCTLSIN--LRPADIQKT 262
Cdd:PLN02387 255 IMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVYLAYLPLAHILELAAESVMAAVGAAIGYGspLTLTDTSNK 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 263 IK--------EIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLMLDAIKvGREHNLEYVYKGLTPPpvlhmkykfyEK 334
Cdd:PLN02387 335 IKkgtkgdasALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYK-RRLAAIEGSWFGAWGL----------EK 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 335 TIYSLL--KKTIGIENG--RFFPTAGAAIPPAVQEFV-LSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQV 409
Cdd:PLN02387 404 LLWDALvfKKIRAVLGGriRFMLSGGAPLSGDTQRFInICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYV 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 410 KI---GENN-----------EIMLRGEGITHGYYKKEAATKAAFTEDG----WFHTGDAG-YIKDEHLFLTERIKDLFKT 470
Cdd:PLN02387 484 KLvswEEGGylisdkpmprgEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGqFHPDGCLEIIDRKKDIVKL 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 471 SNGKYIAPQAIEAKLVVDRYIDQISIIADE-RKFVSALIIPEYKLVKEYADKKGIHYGSMEDLLRKPEIIelfKERIDTL 549
Cdd:PLN02387 564 QHGEYVSLGKVEAALSVSPYVDNIMVHADPfHSYCVALVVPSQQALEKWAKKAGIDYSNFAELCEKEEAV---KEVQQSL 640
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2786809754 550 -----QQQFAHYEQIKKFTLLPQPFSMERGELTNTLKIKRSVLNKNYAVEIEKMYE 600
Cdd:PLN02387 641 skaakAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
9-485 |
5.57e-66 |
|
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: 222.38 E-value: 5.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDyktETWipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:COG0318 4 LLRRAAARHPDRPALVFGG---RRL---TYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVgeqlqydvafrvmqlgsqlkriiifdrevkrderdqtsiyfddflklgeghphqa 168
Cdd:COG0318 78 PLNPRLTAEELAYILEDSGARALVT------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 169 evdkrisesgngdlANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTHVFerAWTC---WCLS 245
Cdd:COG0318 103 --------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG-LTPGDVVLVALPLFHVF--GLTVgllAPLL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 246 MGCTLSI--NLRPADIQKTIKEIRPTAMCSVPRFWEkvyagvqekinettglkkkLMLDAIKVGREHnleyvykgltppp 323
Cdd:COG0318 166 AGATLVLlpRFDPERVLELIERERVTVLFGVPTMLA-------------------RLLRHPEFARYD------------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 324 vlhmkykfyektIYSLlkktigiengRFFPTAGAAIPPAV-QEFVLSVGINMVAGYGLTESTATVAC--ENDYDHVVGSV 400
Cdd:COG0318 214 ------------LSSL----------RLVVSGGAPLPPELlERFEERFGVRIVEGYGLTETSPVVTVnpEDPGERRPGSV 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 401 GRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYI-KDEHLFLTERIKDLFK 469
Cdd:COG0318 272 GRPLPGVEVRIvdedgrelppGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLdEDGYLYIVGRKKDMII 350
|
490
....*....|....*.
gi 2786809754 470 tSNGKYIAPQAIEAKL 485
Cdd:COG0318 351 -SGGENVYPAEVEEVL 365
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
34-584 |
8.13e-64 |
|
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: 216.92 E-value: 8.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 34 IPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFV 113
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 114 GEqlqydvafrvmqlgsqlkriiifdrevkrderdqtsiyfddflklgeghphqaevdkrisesgNGDLANILYTSGTTG 193
Cdd:cd05914 86 SD---------------------------------------------------------------EDDVALINYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 194 DSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTHVFERAWT-CWCLSMGCTLSINLRPAD---IQKTIKEIRPT 269
Cdd:cd05914 103 NSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTlLLPLLNGAHVVFLDKIPSakiIALAFAQVTPT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 270 AMCSVPRFWEKVYagVQEKINETTGLKKKLMLDAikvgrehnleyvykgltppPVLHMKYKfyeKTIYSLLKKTIGiENG 349
Cdd:cd05914 182 LGVPVPLVIEKIF--KMDIIPKLTLKKFKFKLAK-------------------KINNRKIR---KLAFKKVHEAFG-GNI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 350 RFFPTAGAAIPPAVQEFVLSVGINMVAGYGLTEsTATVACENDYDHVV-GSVGRLMPHVQVKI------GENNEIMLRGE 422
Cdd:cd05914 237 KEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTE-TAPIISYSPPNRIRlGSAGKVIDGVEVRIdspdpaTGEGEIIVRGP 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 423 GITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE-HLFLTERIKDLFKTSNGKYIAPQAIEAKLVVDRYIDQISIIADER 501
Cdd:cd05914 316 NVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEgYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEK 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 502 KFVsALIIPEYKLVKEYAdkkgihygsmedlLRKPEIIELFK-ERIDTLQQQFAHYEQIKKFTLLPQPFsmergELTNTL 580
Cdd:cd05914 396 KLV-ALAYIDPDFLDVKA-------------LKQRNIIDAIKwEVRDKVNQKVPNYKKISKVKIVKEEF-----EKTPKG 456
|
....
gi 2786809754 581 KIKR 584
Cdd:cd05914 457 KIKR 460
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
16-600 |
5.07e-63 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 219.89 E-value: 5.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 16 KYGDRVVLRYR---DYKTETWIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLyVDFGAFGVRAV-TVPFY 91
Cdd:PLN02614 57 KYPNNPMLGRReivDGKPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWI-ISMEACNAHGLyCVPLY 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 92 ATSSEAQVHYMVGDAEIRYIFVgEQLQYDVAFRVMQLGSQLKRIIIFDREVKRDERDQTSIY------FDDFLKLGEGHP 165
Cdd:PLN02614 136 DTLGAGAVEFIISHSEVSIVFV-EEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFglviyaWDEFLKLGEGKQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 166 HQAEVDKRisesgnGDLANILYTSGTTGDSKGVMLHHSCYeAAIPAHNERF-----PQLGDQDVIMNFLPFTHVFERAWT 240
Cdd:PLN02614 215 YDLPIKKK------SDICTIMYTSGTTGDPKGVMISNESI-VTLIAGVIRLlksanAALTVKDVYLSYLPLAHIFDRVIE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 241 CWCLSMGCtlSINLRPADIQKTIK---EIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLMldaiKVGREHNLEYVYK 317
Cdd:PLN02614 288 ECFIQHGA--AIGFWRGDVKLLIEdlgELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVF----DSAFSYKFGNMKK 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 318 GLTpppvlHMKYK-FYEKTIYSLLKKTIGiENGRFFPTAGAAIPPAVQEFVLSVG-INMVAGYGLTESTA-TVACENDYD 394
Cdd:PLN02614 362 GQS-----HVEASpLCDKLVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVAcCHVLQGYGLTESCAgTFVSLPDEL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 395 HVVGSVGRLMPHVQVKIGE-------------NNEIMLRGEGITHGYYKKEAATKAAFTeDGWFHTGDAG-YIKDEHLFL 460
Cdd:PLN02614 436 DMLGTVGPPVPNVDIRLESvpemeydalastpRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGeWQPNGSMKI 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 461 TERIKDLFKTSNGKYIAPQAIEAKLVVDRYIDQISIIADE-RKFVSALIIPEYKLVKEYADKKGIHyGSMEDLLRKPEII 539
Cdd:PLN02614 515 IDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSfESFLVAIANPNQQILERWAAENGVS-GDYNALCQNEKAK 593
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786809754 540 E-LFKERIDTLQQ-QFAHYEQIKKFTLLPQPFSMERGELTNTLKIKRSVLNKNYAVEIEKMYE 600
Cdd:PLN02614 594 EfILGELVKMAKEkKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYK 656
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
14-600 |
1.62e-58 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 207.36 E-value: 1.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 14 ARKYGDRVVLRYRDYKTETWIPVSWNQFAAT---VKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPF 90
Cdd:PLN02430 52 VEKYPDNKMLGWRRIVDGKVGPYMWKTYKEVyeeVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 91 YATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAFRVMQLGSQLKRIIIFDR--EVKRDERDQTSI---YFDDFLKLGEGHP 165
Cdd:PLN02430 132 YDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLKAIVSFTSvtEEESDKASQIGVktySWIDFLHMGKENP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 166 HQAEVDKRIsesgngDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGDQ----DVIMNFLPFTHVFERAWTC 241
Cdd:PLN02430 212 SETNPPKPL------DICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQFEDKmthdDVYLSFLPLAHILDRMIEE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 242 WCLSMGCTL-----SINLRPADIQktikEIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKkLMLDAIKVGREHNLEYVY 316
Cdd:PLN02430 286 YFFRKGASVgyyhgDLNALRDDLM----ELKPTLLAGVPRVFERIHEGIQKALQELNPRRR-LIFNALYKYKLAWMNRGY 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 317 KGLTPPPVLHMkykfyekTIYSLLKKTIGienGR--FFPTAGAAIPPAVQEF--VLSVGInMVAGYGLTESTA-TVACEN 391
Cdd:PLN02430 361 SHKKASPMADF-------LAFRKVKAKLG---GRlrLLISGGAPLSTEIEEFlrVTSCAF-VVQGYGLTETLGpTTLGFP 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 392 DYDHVVGSVGRLMPHVQVKI-----------GEN--NEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYI-KDEH 457
Cdd:PLN02430 430 DEMCMLGTVGAPAVYNELRLeevpemgydplGEPprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEIlPNGV 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 458 LFLTERIKDLFKTSNGKYIAPQAIEAKLVVDRYIDQISIIADE-RKFVSALIIPEYKLVKEYADKKGiHYGSMEDLLRKP 536
Cdd:PLN02430 509 LKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSfKSMLVAVVVPNEENTNKWAKDNG-FTGSFEELCSLP 587
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786809754 537 EIIELFKERIDTL--QQQFAHYEQIKKFTLLPQPFSMERGELTNTLKIKRSVLNKNYAVEIEKMYE 600
Cdd:PLN02430 588 ELKEHILSELKSTaeKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYR 653
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
7-601 |
2.22e-58 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 207.00 E-value: 2.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 7 SVLIQRQARKYGDRVVLryrDYKTETWIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLyVDFGAFGVRAV 86
Cdd:PLN02861 52 AVKKYPNNQMLGRRQVT---DSKVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWI-IAMEACNSQGI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 87 T-VPFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAFRVMQLGSQLKRIIIFDR---EVKRDERDQTSIYF--DDFLKL 160
Cdd:PLN02861 128 TyVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLPKCSSNLKTIVSFGDvssEQKEEAEELGVSCFswEEFSLM 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 161 GEghphqaeVDKRISESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAhNERFPQLGD-----QDVIMNFLPFTHVF 235
Cdd:PLN02861 208 GS-------LDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLS-TDHLLKVTDrvateEDSYFSYLPLAHVY 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 236 ERAWTCWCLSMGCtlSINLRPADIQ---KTIKEIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLMLDAIKvgreHNL 312
Cdd:PLN02861 280 DQVIETYCISKGA--SIGFWQGDIRylmEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYN----YKL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 313 EYVYKGLTPppvlHMKYKFYEKTIYSLLKKTIGiENGRFFPTAGAAIPPAVQEFV-LSVGINMVAGYGLTESTAtvACEN 391
Cdd:PLN02861 354 GNLRKGLKQ----EEASPRLDRLVFDKIKEGLG-GRVRLLLSGAAPLPRHVEEFLrVTSCSVLSQGYGLTESCG--GCFT 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 392 DYDHV---VGSVGRLMPHVQVKIGE-------------NNEIMLRGEGITHGYYKKEAATKAAFTeDGWFHTGDAG-YIK 454
Cdd:PLN02861 427 SIANVfsmVGTVGVPMTTIEARLESvpemgydalsdvpRGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGeWQP 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 455 DEHLFLTERIKDLFKTSNGKYIAPQAIEAKLVVDRYIDQISIIADE-RKFVSALIIPEYKLVKEYADKKGIHyGSMEDLL 533
Cdd:PLN02861 506 NGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSfESFLVAVVVPDRQALEDWAANNNKT-GDFKSLC 584
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 534 RKPEIIELFKERIDT--LQQQFAHYEQIKKFTLLPQPFSMERGELTNTLKIKRSVLNKNYAVEIEKMYEE 601
Cdd:PLN02861 585 KNLKARKYILDELNStgKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSE 654
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
36-601 |
1.28e-56 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 202.90 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 36 VSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGE 115
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 116 QLQYDVaFRVMQLGSQLKRIIIFDREVKR--DERDQTSIYFDDFLKLGEGHphQAEVDKRISESgNGDLANILYTSGTTG 193
Cdd:PTZ00216 202 KNVPNL-LRLMKSGGMPNTTIIYLDSLPAsvDTEGCRLVAWTDVVAKGHSA--GSHHPLNIPEN-NDDLALIMYTSGTTG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 194 DSKGVMLHHSCYEAAIPAHNERFPQL----GDQDVIMNFLPFTHVFERAWTCWCLSMGC--------TLS-INLRP-ADI 259
Cdd:PTZ00216 278 DPKGVMHTHGSLTAGILALEDRLNDLigppEEDETYCSYLPLAHIMEFGVTNIFLARGAligfgsprTLTdTFARPhGDL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 260 qktiKEIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLM-------LDAIKVGREhnleyvykglTPppvlhmkykFY 332
Cdd:PTZ00216 358 ----TEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFdhayqsrLRALKEGKD----------TP---------YW 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 333 EKTIYSLLKKTIGiENGRFFPTAGAAIPPAVQEFVLSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKIG 412
Cdd:PTZ00216 415 NEKVFSAPRAVLG-GRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLL 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 413 ENN------------EIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE-HLFLTERIKDLFKTSNGKYIAPQ 479
Cdd:PTZ00216 494 DTEeykhtdtpeprgEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANgTLRIIGRVKALAKNCLGEYIALE 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 480 AIEA-----KLVVDryiDQISIIADERK-FVSALIIPEYKLVKEYADKKGIHyGSMEDLLRKPEiielFKERIDTLQQQF 553
Cdd:PTZ00216 574 ALEAlygqnELVVP---NGVCVLVHPARsYICALVLTDEAKAMAFAKEHGIE-GEYPAILKDPE----FQKKATESLQET 645
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2786809754 554 AH------YEQIKKFTLLPQPFSMERGELTNTLKIKRSVLNKNYAVEIEKMYEE 601
Cdd:PTZ00216 646 ARaagrksFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFAD 699
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
36-485 |
9.82e-55 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 193.20 E-value: 9.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 36 VSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGE 115
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 116 QLqYDVAFRVMQLGSQLKRIIIFDREVKRDerdqTSIYFDDFLKLGEGHPHQAEVDKrisESGNgDLANILYTSGTTGDS 195
Cdd:cd05911 91 DG-LEKVKEAAKELGPKDKIIVLDDKPDGV----LSIEDLLSPTLGEEDEDLPPPLK---DGKD-DTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 196 KGVML-HHSCYEAAIPAHNERFPQLGDQDVIMNFLPFTHVFERAWTCWCLSMGCTLSInlrpadiqktikeirptaMcsv 274
Cdd:cd05911 162 KGVCLsHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVII------------------M--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 275 PRFWEKvyagvqekinettglkkkLMLDAIKvgrEHNLEYVYkglTPPPVLHMKYKFYEKTIYSLlkktigiENGRFFPT 354
Cdd:cd05911 221 PKFDSE------------------LFLDLIE---KYKITFLY---LVPPIAAALAKSPLLDKYDL-------SSLRVILS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 355 AGAAIPPAVQEFVLSVGINMVA--GYGLTESTATVACENDYDHVVGSVGRLMPHVQVKI-----------GENNEIMLRG 421
Cdd:cd05911 270 GGAPLSKELQELLAKRFPNATIkqGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIvdddgkdslgpNEPGEICVRG 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786809754 422 EGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE-HLFLTERIKDLFKTsNGKYIAPQAIEAKL 485
Cdd:cd05911 350 PQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDgYLYIVDRKKELIKY-KGFQVAPAELEAVL 413
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
9-482 |
1.94e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 190.40 E-value: 1.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDYKTetwipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:PRK06187 11 ILRHGARKHPDKEAVYFDGRRT------TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 P---FYatsSEAQVHYMVGDAEIRYIFVGEQLQYDVAfrvmQLGSQLK--RIIIFDREVKRDERDQTSIYFDDFLKLGEG 163
Cdd:PRK06187 85 PiniRL---KPEEIAYILNDAEDRVVLVDSEFVPLLA----AILPQLPtvRTVIVEGDGPAAPLAPEVGEYEELLAAASD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 164 HPHQAEVDKRisesgngDLANILYTSGTTGDSKGVML-HHSCYEAAIPAHneRFPQLGDQDVIMNFLPFTHVFerAWTcW 242
Cdd:PRK06187 158 TFDFPDIDEN-------DAAAMLYTSGTTGHPKGVVLsHRNLFLHSLAVC--AWLKLSRDDVYLVIVPMFHVH--AWG-L 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 243 C---LSMGCTLSINLR--PADIQKTIKEIRPTAMCSVPRFWEkvyagvqekinettglkkklMLDAIKVGREHNLeyvyk 317
Cdd:PRK06187 226 PylaLMAGAKQVIPRRfdPENLLDLIETERVTFFFAVPTIWQ--------------------MLLKAPRAYFVDF----- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 318 gltpppvlhmkykfyektiYSLLKKTIGiengrffptaGAAIPPA-VQEFVLSVGINMVAGYGLTESTATVACENDYDHV 396
Cdd:PRK06187 281 -------------------SSLRLVIYG----------GAALPPAlLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 397 VG------SVGRLMPHVQVKI------------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYI-KDEH 457
Cdd:PRK06187 332 PGqwtkrrSAGRPLPGVEARIvdddgdelppdgGEVGEIIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIdEDGY 410
|
490 500
....*....|....*....|....*
gi 2786809754 458 LFLTERIKDLFKtSNGKYIAPQAIE 482
Cdd:PRK06187 411 LYITDRIKDVII-SGGENIYPRELE 434
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
9-468 |
1.68e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 182.41 E-value: 1.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:PRK07656 10 LLARAARRFGDKEAYVFGDQR------LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PF---YaTSSEAqvHYMVGDAEIRYIFVGEQLQyDVAFRVMQLGSQLKRIIIFDREVKRDERDQTsIYFDDFLKLGEGHP 165
Cdd:PRK07656 84 PLntrY-TADEA--AYILARGDAKALFVLGLFL-GVDYSATTRLPALEHVVICETEEDDPHTEKM-KTFTDFLAAGDPAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 166 HQAEVDKRisesgngDLANILYTSGTTGDSKGVML-HHSCYEAA-----IPAHNErfpqlGDQDVIMNflPFTHVFerAW 239
Cdd:PRK07656 159 RAPEVDPD-------DVADILFTSGTTGRPKGAMLtHRQLLSNAadwaeYLGLTE-----GDRYLAAN--PFFHVF--GY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 240 T-CW--CLSMGCTLSINLR--PADIQKTIKEIRPTamcsvprfwekVYAGvqekinettglkkklmldaikvgrehnley 314
Cdd:PRK07656 223 KaGVnaPLMRGATILPLPVfdPDEVFRLIETERIT-----------VLPG------------------------------ 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 315 vykgltPPPVLHMKYKFYEKTIYSLlkKTIgiengRFFPTAGAAIPPA-VQEFVLSVGINMVA-GYGLTEStATVACEN- 391
Cdd:PRK07656 262 ------PPTMYNSLLQHPDRSAEDL--SSL-----RLAVTGAASMPVAlLERFESELGVDIVLtGYGLSEA-SGVTTFNr 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 392 ---DYDHVVGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE-H 457
Cdd:PRK07656 328 lddDRKTVAGTIGTAIAGVENKIvnelgeevpvGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEgY 407
|
490
....*....|.
gi 2786809754 458 LFLTERIKDLF 468
Cdd:PRK07656 408 LYIVDRKKDMF 418
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
181-483 |
4.92e-50 |
|
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: 176.32 E-value: 4.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCYEAAIpAHNERFPQLGDQDVIMNFLPFTHVFERAWTCWCLSMGCTLSI--NLRPAD 258
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAA-AALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLlpKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 259 IQKTIKEIRPTAMCSVPRFWEkvyagvqekinettglkkkLMLDAIKVgREHNLeyvykgltpppvlhmkykfyektiYS 338
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLA-------------------RLLKAPES-AGYDL------------------------SS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 339 LlkktigiengRFFPTAGAAIPPAVQE-FVLSVGINMVAGYGLTESTATVACENDYDHVV--GSVGRLMPHVQVKI---- 411
Cdd:cd04433 116 L----------RALVSGGAPLPPELLErFEEAPGIKLVNGYGLTETGGTVATGPPDDDARkpGSVGRPVPGVEVRIvdpd 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 ------GENNEIMLRGEGITHGYYKKEAATkAAFTEDGWFHTGDAGYIkDEH--LFLTERIKDLFKtSNGKYIAPQAIEA 483
Cdd:cd04433 186 ggelppGEIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRL-DEDgyLYIVGRLKDMIK-SGGENVYPAEVEA 262
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
6-467 |
3.37e-46 |
|
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: 169.28 E-value: 3.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 6 LSVLIQRQARKYGDRVVLRYRDYKTetwipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRA 85
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKL------TYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 86 VTVPFYATSSEAQVHYMVGDAEIRYIFVGeqlqydvafrvmqlgsqlkriiifdrevkrderdqtsIYFDDFLKLGEGHP 165
Cdd:cd05936 75 VVVPLNPLYTPRELEHILNDSGAKALIVA-------------------------------------VSFTDLLAAGAPLG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 166 HQAEVDKrisesgnGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGD-QDVIMNFLPFTHVFerAWTCWCL 244
Cdd:cd05936 118 ERVALTP-------EDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEgDDVVLAALPLFHVF--GLTVALL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 245 S---MGCTLSI--NLRPADIQKTIKEIRPTAMCSVPRfwekvyagvqekinettglkkklMLDAIkVGREHNLEYVYKGL 319
Cdd:cd05936 189 LplaLGATIVLipRFRPIGVLKEIRKHRVTIFPGVPT-----------------------MYIAL-LNAPEFKKRDFSSL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 320 tpppvlhmkykfyektiysllkktigiengRFFPTAGAAIPPAVQEFVLSV-GINMVAGYGLTEsTATVACENDYDHVV- 397
Cdd:cd05936 245 ------------------------------RLCISGGAPLPVEVAERFEELtGVPIVEGYGLTE-TSPVVAVNPLDGPRk 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 398 -GSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTeDGWFHTGDAGYI-KDEHLFLTERIK 465
Cdd:cd05936 294 pGSIGIPLPGTEVKIvdddgeelppGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMdEDGYFFIVDRKK 372
|
..
gi 2786809754 466 DL 467
Cdd:cd05936 373 DM 374
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
12-486 |
9.46e-42 |
|
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: 156.23 E-value: 9.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 12 RQARKYGDRVVLRYRDyktETWipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPfy 91
Cdd:cd17631 3 RRARRHPDRTALVFGG---RSL---TYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 92 atsseaqVHYMVGDAEIRYIfvgeqLQyDVAFRVMqlgsqlkriiifdrevkrderdqtsiyFDDflklgeghphqaevd 171
Cdd:cd17631 75 -------LNFRLTPPEVAYI-----LA-DSGAKVL---------------------------FDD--------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 172 krisesgngdLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGDqDVIMNFLPFTHVfeRAWTCWCLSM---GC 248
Cdd:cd17631 100 ----------LALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPD-DVLLVVAPLFHI--GGLGVFTLPTllrGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 249 TLSI--NLRPADIQKTIKEIRPTAMCSVPRFWEKVyagVQEKINETTGLKkklmldaikvgrehNLEYVYKGLTPPPVLh 326
Cdd:cd17631 167 TVVIlrKFDPETVLDLIERHRVTSFFLVPTMIQAL---LQHPRFATTDLS--------------SLRAVIYGGAPMPER- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 327 mkykfyektiysLLKktigiengrffptagaaippAVQEFvlsvGINMVAGYGLTEST--ATVACENDYDHVVGSVGRLM 404
Cdd:cd17631 229 ------------LLR--------------------ALQAR----GVKFVQGYGMTETSpgVTFLSPEDHRRKLGSAGRPV 272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 405 PHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYIKDE-HLFLTERIKDLFKtSNG 473
Cdd:cd17631 273 FFVEVRIvdpdgrevppGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDgYLYIVDRKKDMII-SGG 350
|
490
....*....|...
gi 2786809754 474 KYIAPQAIEAKLV 486
Cdd:cd17631 351 ENVYPAEVEDVLY 363
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
36-486 |
7.29e-41 |
|
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: 155.47 E-value: 7.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 36 VSWNQFAATVKTVSNALIELGIGIQENIAVFSqnkPECLYVDFGAFGVR---AVTVPFYATSSEAQVHYMVGDAEIRYIF 112
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLS---PNSIEFPVAFLAVLslgAVVTTANPLSTPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 113 VgeqlqydVAFRVMQLGSQLKRIIIFDREVKRderdqtSIYFDDFLKLGEGHPHQAEVDKRisesgnGDLANILYTSGTT 192
Cdd:cd05904 110 T-------TAELAEKLASLALPVVLLDSAEFD------SLSFSDLLFEADEAEPPVVVIKQ------DDVAALLYSSGTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 193 GDSKGVMLHHSCYEAAIPAHNERF-PQLGDQDVIMNFLPFTHVFERAWTCWC-LSMGCTLSInlrpadiqktikeirpta 270
Cdd:cd05904 171 GRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSSFALGlLRLGATVVV------------------ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 271 mcsVPRFwekvyagvqekinETTGlkkklMLDAIKvgrEHNLEYVYkgLTPPPVLHM-KYKFYEKtiYSLLK-KTIGien 348
Cdd:cd05904 233 ---MPRF-------------DLEE-----LLAAIE---RYKVTHLP--VVPPIVLALvKSPIVDK--YDLSSlRQIM--- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 349 grffpTAGAAIPPAVQEFVLSV--GINMVAGYGLTESTATVA-CENDYDHVV--GSVGRLMPHVQVKI-----------G 412
Cdd:cd05904 282 -----SGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVVAmCFAPEKDRAkyGSVGRLVPNVEAKIvdpetgeslppN 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786809754 413 ENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFKTsNGKYIAPQAIEAKLV 486
Cdd:cd05904 357 QTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIdEDGYLFIVDRLKELIKY-KGFQVAPAELEALLL 430
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
37-498 |
7.32e-39 |
|
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: 147.82 E-value: 7.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 37 SWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPfyatsseaqvhymvgdaeIRYIFVGEQ 116
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVP------------------INTALRGDE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 117 LQYDVAFRVMQLgsqlkrIIIfdrevkrderdqtsiyfddflklgeghphqaevdkrisesgngDLANILYTSGTTGDSK 196
Cdd:cd05934 67 LAYIIDHSGAQL------VVV-------------------------------------------DPASILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 197 GVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTHVFERAWTcWCLSMGCTLSINLRPAdiqktikeirptamCSVPR 276
Cdd:cd05934 98 GVVITHANLTFAGYYSARRFG-LGEDDVYLTVLPLFHINAQAVS-VLAALSVGATLVLLPR--------------FSASR 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 277 FWEKVyagvqekinettglkkklmldaikvgREHNleyvykgltpppvlhmkykfyeKTIYSLLKKTIGI---------- 346
Cdd:cd05934 162 FWSDV--------------------------RRYG----------------------ATVTNYLGAMLSYllaqppspdd 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 347 ENGRFFPTAGAAIPPA-VQEFVLSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKI----------GENN 415
Cdd:cd05934 194 RAHRLRAAYGAPNPPElHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIvdddgqelpaGEPG 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 416 EIMLRGE---GITHGYYKKEAATKAAFtEDGWFHTGDAGYIKDE-HLFLTERIKDLFKTSnGKYIAPQAIEAKLVVDRYI 491
Cdd:cd05934 274 ELVIRGLrgwGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADgFFYFVDRKKDMIRRR-GENISSAEVERAILRHPAV 351
|
....*..
gi 2786809754 492 DQISIIA 498
Cdd:cd05934 352 REAAVVA 358
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
10-601 |
2.70e-38 |
|
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: 148.73 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 10 IQRQARKYGDRVVLRYRDyKTETWIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAF--GVRAVT 87
Cdd:cd05921 1 LAHWARQAPDRTWLAERE-GNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMyaGVPAAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 88 V-PFYATSSE--AQVHYMVGDAEIRYIFVGEQLQYDVAfrvmqlgsqLKRIIIFDREV---KRDERDQTSIYFDDFLKLg 161
Cdd:cd05921 80 VsPAYSLMSQdlAKLKHLFELLKPGLVFAQDAAPFARA---------LAAIFPLGTPLvvsRNAVAGRGAISFAELAAT- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 162 eghPHQAEVDKRISESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGDQD-VIMNFLPFTHVF-ERAW 239
Cdd:cd05921 150 ---PPTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVDWLPWNHTFgGNHN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 240 TCWCLSMGCTLSINL---RPADIQKTI---KEIRPTAMCSVPRFWEKVyAGVQEKineTTGLKKKLMLDaikvgrehnle 313
Cdd:cd05921 227 FNLVLYNGGTLYIDDgkpMPGGFEETLrnlREISPTVYFNVPAGWEML-VAALEK---DEALRRRFFKR----------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 314 yvykgltpppvlhMKYKFYektiysllkktigiengrffptAGAAIPP----AVQEF-VLSVG--INMVAGYGLTES--T 384
Cdd:cd05921 292 -------------LKLMFY----------------------AGAGLSQdvwdRLQALaVATVGerIPMMAGLGATETapT 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 385 ATVaCENDYDHVvGSVGRLMPHVQVKIGENN---EIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDEH---- 457
Cdd:cd05921 337 ATF-THWPTERS-GLIGLPAPGTELKLVPSGgkyEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADPDdpak 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 458 -LFLTERIKDLFKTSNGKYIAPQAIEAKLV--VDRYIDQISIIADERKFVSALIIPEYKLVKEYAdkkGIHYGSMEDLLR 534
Cdd:cd05921 415 gLVFDGRVAEDFKLASGTWVSVGPLRARAVaaCAPLVHDAVVAGEDRAEVGALVFPDLLACRRLV---GLQEASDAEVLR 491
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786809754 535 KPEIIELFKERIDTLQQQFA-HYEQIKKFTLLPQPFSMERGELTNTLKI-KRSVLNKNyAVEIEKMYEE 601
Cdd:cd05921 492 HAKVRAAFRDRLAALNGEATgSSSRIARALLLDEPPSIDKGEITDKGYInQRAVLERR-AALVERLYAD 559
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
6-601 |
8.67e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 148.27 E-value: 8.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 6 LSVLIQRQARKYGDRVVLRYRDYKTETWIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRA 85
Cdd:PRK12582 51 IPHLLAKWAAEAPDRPWLAQREPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 86 VTVPF---YATSSE--AQVHYMVGDAEIRYIFVGEQLQYDVAFRVMQLGSqlKRIIIfdreVKRDERDQTSIYFDDFLkl 160
Cdd:PRK12582 131 PAAPVspaYSLMSHdhAKLKHLFDLVKPRVVFAQSGAPFARALAALDLLD--VTVVH----VTGPGEGIASIAFADLA-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 161 geGHPHQAEVDKRISESGNGDLANILYTSGTTGDSKGVMLHHS--CYEAAIPAHNERFPQLGDQDVIMNFLPFTHVFE-R 237
Cdd:PRK12582 203 --ATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRmmCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGgN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 238 AWTCWCLSMGCTLSIN---LRPADIQKTIK---EIRPTAMCSVPrfweKVYAGVQEKINETTGLKKKLMldaikvgreHN 311
Cdd:PRK12582 281 ANFNGLLWGGGTLYIDdgkPLPGMFEETIRnlrEISPTVYGNVP----AGYAMLAEAMEKDDALRRSFF---------KN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 312 LEYV-YKGLTPPPVLhmkykfYEKtIYSLLKKTIGiengrffptagaaippavQEFVLSvginmvAGYGLTEsTATVACE 390
Cdd:PRK12582 348 LRLMaYGGATLSDDL------YER-MQALAVRTTG------------------HRIPFY------TGYGATE-TAPTTTG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 391 NDYD-HVVGSVGRLMPHVQVK---IGENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDEH-----LFLT 461
Cdd:PRK12582 396 THWDtERVGLIGLPLPGVELKlapVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVDPDdpekgLIFD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 462 ERIKDLFKTSNGKYIAPQAIEAKLVV--DRYIDQISIIADERKFVSALIIPEYKLVKEYADKkgiHYGSMEDLLRKPEII 539
Cdd:PRK12582 476 GRVAEDFKLSTGTWVSVGTLRPDAVAacSPVIHDAVVAGQDRAFIGLLAWPNPAACRQLAGD---PDAAPEDVVKHPAVL 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786809754 540 ELFKERIDTLQQQFAHYE-QIKKFTLLPQPFSMERGELTNTLKI-KRSVLNKNYAVeIEKMYEE 601
Cdd:PRK12582 553 AILREGLSAHNAEAGGSSsRIARALLMTEPPSIDAGEITDKGYInQRAVLERRAAL-VERLYAE 615
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
11-601 |
1.75e-36 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 144.25 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 11 QRQARKYGDRVVLRYRDyKTETWIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAF--GVRAVTV 88
Cdd:PRK08180 46 VHWAQEAPDRVFLAERG-ADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMyaGVPYAPV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 -PFYATSSE--AQVHYMVGDAEIRYIFVGEQLQYDVAfrvmqlgsqLKRIIIFDREV---KRDERDQTSIYFDDFLKLGE 162
Cdd:PRK08180 125 sPAYSLVSQdfGKLRHVLELLTPGLVFADDGAAFARA---------LAAVVPADVEVvavRGAVPGRAATPFAALLATPP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 163 GhphqAEVDKRISESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGDQD-VIMNFLPFTHVF------ 235
Cdd:PRK08180 196 T----AAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPpVLVDWLPWNHTFggnhnl 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 236 ERAwtcwcLSMGCTLSI---NLRPADIQKTI---KEIRPTAMCSVPRFWEKVyagvqekineTTGLKKKLMLdaikvgRE 309
Cdd:PRK08180 272 GIV-----LYNGGTLYIddgKPTPGGFDETLrnlREISPTVYFNVPKGWEML----------VPALERDAAL------RR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 310 HNLEYVykgltpppvlhmKYKFYektiysllkktigiengrffptAGAAIPPAV----QEF-VLSVG--INMVAGYGLTE 382
Cdd:PRK08180 331 RFFSRL------------KLLFY----------------------AGAALSQDVwdrlDRVaEATCGerIRMMTGLGMTE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 383 sTATVACeNDYDHVVGS--VGRLMPHVQVKIGENN---EIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDEH 457
Cdd:PRK08180 377 -TAPSAT-FTTGPLSRAgnIGLPAPGCEVKLVPVGgklEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVDPA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 458 -----LFLTERIKDLFKTSNGKYIAPQAIEAKLV--VDRYIDQISIIADERKFVSALIIPEYKLVKEYADKKGIHygSME 530
Cdd:PRK08180 455 dpergLMFDGRIAEDFKLSSGTWVSVGPLRARAVsaGAPLVQDVVITGHDRDEIGLLVFPNLDACRRLAGLLADA--SLA 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786809754 531 DLLRKPEIIELFKERIDTLQQQfAH--YEQIKKFTLLPQPFSMERGELTNTLKI-KRSVLnKNYAVEIEKMYEE 601
Cdd:PRK08180 533 EVLAHPAVRAAFRERLARLNAQ-ATgsSTRVARALLLDEPPSLDAGEITDKGYInQRAVL-ARRAALVEALYAD 604
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
9-476 |
4.56e-36 |
|
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: 141.61 E-value: 4.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLrYRDYKTETWIpVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:cd12119 1 LLEHAARLHGDREIV-SRTHEGEVHR-YTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAfrvmQLGSQLKR----IIIFDREVKRDERDQTSIYFDDFLKLGEGH 164
Cdd:cd12119 79 TINPRLFPEQIAYIINHAEDRVVFVDRDFLPLLE----AIAPRLPTvehvVVMTDDAAMPEPAGVGVLAYEELLAAESPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 165 PHQAEVDKRisesgngDLANILYTSGTTGDSKGVML-HHSCYEAAIPAHNERFPQLGDQDVIMNFLPFTHVferawTCWC 243
Cdd:cd12119 155 YDWPDFDEN-------TAAAICYTSGTTGNPKGVVYsHRSLVLHAMAALLTDGLGLSESDVVLPVVPMFHV-----NAWG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 244 LSMGCTLS--------INLRPADIQKTIKEIRPTAMCSVPRFWekvyagvqekinettglkkkLMLdaikvgrehnLEYV 315
Cdd:cd12119 223 LPYAAAMVgaklvlpgPYLDPASLAELIEREGVTFAAGVPTVW--------------------QGL----------LDHL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 316 -YKGLTPPpvlhmkykfyektiySLLKKTIGiengrffptaGAAIPPAVQEFVLSVGINMVAGYGLTEsTATVACENDYD 394
Cdd:cd12119 273 eANGRDLS---------------SLRRVVIG----------GSAVPRSLIEAFEERGVRVIHAWGMTE-TSPLGTVARPP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 395 HVVG------------SVGRLMPHVQVKI-----------GEN-NEIMLRGEGITHGYYKKEAATkAAFTEDGWFHTGDA 450
Cdd:cd12119 327 SEHSnlsedeqlalraKQGRPVPGVELRIvdddgrelpwdGKAvGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDV 405
|
490 500
....*....|....*....|....*..
gi 2786809754 451 GYIKDE-HLFLTERIKDLFKtSNGKYI 476
Cdd:cd12119 406 ATIDEDgYLTITDRSKDVIK-SGGEWI 431
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
37-485 |
7.71e-32 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 128.34 E-value: 7.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 37 SWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGEQ 116
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 117 LqydvafrvmqlgsqlkriiifdrevkrDERDQTSIYFDDFLKlgeghphQAEVDKRISESGNGD-LANILYTSGTTGDS 195
Cdd:TIGR01923 81 L---------------------------EEKDFQADSLDRIEA-------AGRYETSLSASFNMDqIATLMFTSGTTGKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 196 KGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTHVFERAWTCWCLSMGCTLSINLRPADIQKTIKEIRPTAMCSVP 275
Cdd:TIGR01923 127 KAVPHTFRNHYASAVGSKENLG-FTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQLLEMIANERVTHISLVP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 276 rfwekvyagvqekinettglkkklmldaikvgrehnleyvykgltpppvlhmkykfyeKTIYSLLKKTIGIENGRFFPTA 355
Cdd:TIGR01923 206 ----------------------------------------------------------TQLNRLLDEGGHNENLRKILLG 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 356 GAAIPPAVQEFVLSVGINMVAGYGLTESTATV-ACENDYDHVVGSVGRLMPHVQVKI-----GENNEIMLRGEGITHGYY 429
Cdd:TIGR01923 228 GSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVtTATPEMLHARPDVGRPLAGREIKIkvdnkEGHGEIMVKGANLMKGYL 307
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786809754 430 KKEAATKAaFTEDGWFHTGDAGYIKDE-HLFLTERIKDLFkTSNGKYIAPQAIEAKL 485
Cdd:TIGR01923 308 YQGELTPA-FEQQGWFNTGDIGELDGEgFLYVLGRRDDLI-ISGGENIYPEEIETVL 362
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
30-485 |
1.68e-31 |
|
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: 128.20 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 30 TETWIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIR 109
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 110 YIFVGEQLQYDVAFRVMQLGSQLKRIIiFDREVKRDERDQTSIYFDDFLKLG---EGHPHqaevdkrisesgNGDLANIL 186
Cdd:cd05926 89 LVLTPKGELGPASRAASKLGLAILELA-LDVGVLIRAPSAESLSNLLADKKNaksEGVPL------------PDDLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 187 YTSGTTGDSKGVMLHHSCYEAAIpaHN-ERFPQLGDQDVIMNFLPFTHVfeRAWTCWCLSM---GCTLSINLR--PADIQ 260
Cdd:cd05926 156 HTSGTTGRPKGVPLTHRNLAASA--TNiTNTYKLTPDDRTLVVMPLFHV--HGLVASLLSTlaaGGSVVLPPRfsASTFW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 261 KTIKEIRPTAMCSVPrfwekvyagvqekinetTGLKkkLMLDaikvgREHNLEYvykglTPPPVLhmkykfyektiysll 340
Cdd:cd05926 232 PDVRDYNATWYTAVP-----------------TIHQ--ILLN-----RPEPNPE-----SPPPKL--------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 341 kktigiengRFFPTAGAAIPPAV-QEFVLSVGINMVAGYGLTESTATVACeNDYDHVV---GSVGRlmPH-VQVKI---- 411
Cdd:cd05926 268 ---------RFIRSCSASLPPAVlEALEATFGAPVLEAYGMTEAAHQMTS-NPLPPGPrkpGSVGK--PVgVEVRIlded 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 ------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIK-DEHLFLTERIKDLFKTSnGKYIAPQAIEAK 484
Cdd:cd05926 336 geilppGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDaDGYLFLTGRIKELINRG-GEKISPLEVDGV 414
|
.
gi 2786809754 485 L 485
Cdd:cd05926 415 L 415
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
9-470 |
1.44e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 125.82 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDyktETWipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGD---RSW---TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PfyatsseaqVHYMVGDAEIRYI--------FVGEQLQYDVAFRVMQLGSQLKriIIFDREVKRDERDQTSIYFDDFLKL 160
Cdd:PRK08316 90 P---------VNFMLTGEELAYIldhsgaraFLVDPALAPTAEAALALLPVDT--LILSLVLGGREAPGGWLDFADWAEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 161 GEGHPHQAEVDkrisesgNGDLANILYTSGTTGDSKGVMLHHSC----YEAAIPAHNerfpqLGDQDVIMNFLPF----- 231
Cdd:PRK08316 159 GSVAEPDVELA-------DDDLAQILYTSGTESLPKGAMLTHRAliaeYVSCIVAGD-----MSADDIPLHALPLyhcaq 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 232 THVFERAWtcwcLSMGCTLSINLRPA--DIQKTIKEIRPTAMCSVPRFWekvyagvqekinetTGLKKKLMLDaikvgrE 309
Cdd:PRK08316 227 LDVFLGPY----LYVGATNVILDAPDpeLILRTIEAERITSFFAPPTVW--------------ISLLRHPDFD------T 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 310 HNLEYVYKGltpppvlhmkykFYektiysllkktigiengrffptaGAAIPPA-----VQEFVLSVGI-NMvagYGLTE- 382
Cdd:PRK08316 283 RDLSSLRKG------------YY-----------------------GASIMPVevlkeLRERLPGLRFyNC---YGQTEi 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 383 -STATVACENDYDHVVGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAG 451
Cdd:PRK08316 325 aPLATVLGPEEHLRRPGSAGRPVLNVETRVvdddgndvapGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLG 403
|
490 500
....*....|....*....|.
gi 2786809754 452 YIkDEHLFLT--ERIKDLFKT 470
Cdd:PRK08316 404 VM-DEEGYITvvDRKKDMIKT 423
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
9-486 |
7.26e-30 |
|
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: 123.18 E-value: 7.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDyktetwIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:cd12118 9 FLERAAAVYPDRTSIVYGD------RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDvAFRVMQLGSqlkriiiFDREVKRDERDQTSIYfddflklgeghphqa 168
Cdd:cd12118 83 ALNTRLDAEEIAFILRHSEAKVLFVDREFEYE-DLLAEGDPD-------FEWIPPADEWDPIALN--------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 169 evdkrisesgngdlanilYTSGTTGDSKGVMLHH-SCYEAAI--PAHNErfpqLGDQDVIMNFLPFTHVfeRAWT-CWCL 244
Cdd:cd12118 140 ------------------YTSGTTGRPKGVVYHHrGAYLNALanILEWE----MKQHPVYLWTLPMFHC--NGWCfPWTV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 245 SMGCTLSINLR---PADIQKTIKEIRPTAMCSVPrfwekvyagvqekinettglkkkLMLDAIKVGREHNleyvyKGLTP 321
Cdd:cd12118 196 AAVGGTNVCLRkvdAKAIYDLIEKHKVTHFCGAP-----------------------TVLNMLANAPPSD-----ARPLP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 322 PPVLHMkykfyektiysllkktigiengrffpTAGAAIPPAVQEFVLSVGINMVAGYGLTEST--ATVACEND-YDHV-- 396
Cdd:cd12118 248 HRVHVM--------------------------TAGAPPPAAVLAKMEELGFDVTHVYGLTETYgpATVCAWKPeWDELpt 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 397 -----------VGSVG------------RLMPHVQVKIGEnneIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYI 453
Cdd:cd12118 302 eerarlkarqgVRYVGleevdvldpetmKPVPRDGKTIGE---IVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVI 377
|
490 500 510
....*....|....*....|....*....|....
gi 2786809754 454 K-DEHLFLTERIKDLFkTSNGKYIAPQAIEAKLV 486
Cdd:cd12118 378 HpDGYIEIKDRSKDII-ISGGENISSVEVEGVLY 410
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
12-467 |
3.66e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 121.84 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 12 RQARKYGDR--VVLRYRDYKtetWipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGA--FGVRAVT 87
Cdd:PRK08315 24 RTAARYPDReaLVYRDQGLR---W---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATakIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 88 V-PFYATSseaQVHYMVGDAEIRYIFVGEQLQyDVAFRVM------QLGSQ------------LKRIIIFDrevkrDERD 148
Cdd:PRK08315 98 InPAYRLS---ELEYALNQSGCKALIAADGFK-DSDYVAMlyelapELATCepgqlqsarlpeLRRVIFLG-----DEKH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 149 QTSIYFDDFLKLGeGHPHQAEVDKRISESGNGDLANILYTSGTTGDSKGVMLHHscyeaaipaHN---------ERFpQL 219
Cdd:PRK08315 169 PGMLNFDELLALG-RAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTH---------RNilnngyfigEAM-KL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 220 GDQDVIMNFLPFTHvferawtCW--------CLSMGCTLSINLR---PADIQKTIKEIRPTAMCSVPrfwekvyagvqek 288
Cdd:PRK08315 238 TEEDRLCIPVPLYH-------CFgmvlgnlaCVTHGATMVYPGEgfdPLATLAAVEEERCTALYGVP------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 289 inetTglkkklMLDAIkvgrehnleyvykgLTPPpvLHMKYKFyektiySLLKkTiGIengrffpTAGAAIPPAVQEFVL 368
Cdd:PRK08315 298 ----T------MFIAE--------------LDHP--DFARFDL------SSLR-T-GI-------MAGSPCPIEVMKRVI 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 369 SVgINM---VAGYGLTE----STATvACENDYDHVVGSVGRLMPHVQVKI-----------GENNEIMLRGEGITHGYYK 430
Cdd:PRK08315 337 DK-MHMsevTIAYGMTEtspvSTQT-RTDDPLEKRVTTVGRALPHLEVKIvdpetgetvprGEQGELCTRGYSVMKGYWN 414
|
490 500 510
....*....|....*....|....*....|....*....
gi 2786809754 431 KEAATKAAFTEDGWFHTGDAGyIKDEHLFL--TERIKDL 467
Cdd:PRK08315 415 DPEKTAEAIDADGWMHTGDLA-VMDEEGYVniVGRIKDM 452
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
9-482 |
9.34e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 120.65 E-value: 9.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDR--VVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAV 86
Cdd:PRK12583 23 AFDATVARFPDReaLVVRHQALR------YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 87 TVPFYATSSEAQVHYMVGDAEIRYIFVGEqlqydvAFR----VMQLGSQLKRIIIFDREVKRDERD---QTSIYFD---- 155
Cdd:PRK12583 97 LVNINPAYRASELEYALGQSGVRWVICAD------AFKtsdyHAMLQELLPGLAEGQPGALACERLpelRGVVSLApapp 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 156 -------DFLKLGEGHPHQAeVDKRISESGNGDLANILYTSGTTGDSKGVMLHHS--CYEAAIPAHNERfpqLGDQDVIM 226
Cdd:PRK12583 171 pgflawhELQARGETVSREA-LAERQASLDRDDPINIQYTSGTTGFPKGATLSHHniLNNGYFVAESLG---LTEHDRLC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 227 NFLPFTHVFERAW-TCWCLSMGCTL---SINLRPADIQKTIKEIRPTAMCSVPRFWekvyagvqekINETTglkkklmld 302
Cdd:PRK12583 247 VPVPLYHCFGMVLaNLGCMTVGACLvypNEAFDPLATLQAVEEERCTALYGVPTMF----------IAELD--------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 303 aikvgrehnleyvykgltpppvlHMKYKFYEktiYSLLKKTIgiengrffpTAGAAIPPAVQEFVLSvGINM---VAGYG 379
Cdd:PRK12583 308 -----------------------HPQRGNFD---LSSLRTGI---------MAGAPCPIEVMRRVMD-EMHMaevQIAYG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 380 LTES---TATVACENDYDHVVGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFH 446
Cdd:PRK12583 352 MTETspvSLQTTAADDLERRVETVGRTQPHLEVKVvdpdgatvprGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMH 431
|
490 500 510
....*....|....*....|....*....|....*..
gi 2786809754 447 TGDAGYIKDE-HLFLTERIKDLFkTSNGKYIAPQAIE 482
Cdd:PRK12583 432 TGDLATMDEQgYVRIVGRSKDMI-IRGGENIYPREIE 467
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
36-491 |
2.07e-28 |
|
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: 119.55 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 36 VSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGE 115
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 116 Q-LQydvafRVMQLGSQL---KRIIIFDreVKRDERDQTSIYfdDFLKlgEGHPHQAEVDKRISESGNGD--LANILYTS 189
Cdd:cd17642 125 KgLQ-----KVLNVQKKLkiiKTIIILD--SKEDYKGYQCLY--TFIT--QNLPPGFNEYDFKPPSFDRDeqVALIMNSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 190 GTTGDSKGVMLHHScyEAAIPAHNERFPQLGDQ----DVIMNFLPFTHVFerawtcwclsmGCTLSINlrpadiqktike 265
Cdd:cd17642 194 GSTGLPKGVQLTHK--NIVARFSHARDPIFGNQiipdTAILTVIPFHHGF-----------GMFTTLG------------ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 266 irpTAMCS-----VPRFWEKVYAGVQEKINETTGLkkklmldaikvgrehnleyvykgLTPPP-VLHMKYKFYEKTIYSL 339
Cdd:cd17642 249 ---YLICGfrvvlMYKFEEELFLRSLQDYKVQSAL-----------------------LVPTLfAFFAKSTLVDKYDLSN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 340 LKKtigIENGrffptaGAAIPPAVQEFVLS-VGINMV-AGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKI------ 411
Cdd:cd17642 303 LHE---IASG------GAPLSKEVGEAVAKrFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVvdldtg 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 -----GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFKTsNGKYIAPQAIEAKL 485
Cdd:cd17642 374 ktlgpNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLKSLIKY-KGYQVPPAELESIL 452
|
....*.
gi 2786809754 486 VVDRYI 491
Cdd:cd17642 453 LQHPKI 458
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
36-501 |
2.59e-28 |
|
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: 117.87 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 36 VSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGE 115
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 116 QlqydvaFRvmqlgsqlkriiifdrevkrderdqtsiyfddflklgeGHPHQAEVDkrisesgngDLANILYTSGTTGDS 195
Cdd:cd05903 82 R------FR--------------------------------------QFDPAAMPD---------AVALLLFTSGTTGEP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 196 KGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTHV--FERAWTCWCLsMGCT--LSINLRPADIQKTIKEIRPTAM 271
Cdd:cd05903 109 KGVMHSHNTLSASIRQYAERLG-LGPGDVFLVASPMAHQtgFVYGFTLPLL-LGAPvvLQDIWDPDKALALMREHGVTFM 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 272 CSVPRFwekvyagvqekinettglkkklMLDAIKVgrehnleyVYKGLTPPPVLhmkykfyektiysllkktigiengRF 351
Cdd:cd05903 187 MGATPF----------------------LTDLLNA--------VEEAGEPLSRL------------------------RT 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 352 FPTAGAAIPPAVQEFVLSVGINMVAG-YGLTE-STATVACE-NDYDHVVGSVGRLMPHVQVKI----------GENNEIM 418
Cdd:cd05903 213 FVCGGATVPRSLARRAAELLGAKVCSaYGSTEcPGAVTSITpAPEDRRLYTDGRPLPGVEIKVvddtgatlapGVEGELL 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 419 LRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYIKDE-HLFLTERIKDLFkTSNGKYIAPQAIEAKLVVDRYIDQISII 497
Cdd:cd05903 293 SRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDgYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVV 370
|
....*.
gi 2786809754 498 A--DER 501
Cdd:cd05903 371 AlpDER 376
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
6-466 |
2.03e-27 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 116.40 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 6 LSVLIQRQARKYGDRVVLRYrdykTETWIpvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRA 85
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVF----GGTRW--TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 86 VTVPFYATSSEAQVHYMVGDAEIRYIFVgeQLQYDVAFRVMQLGSQ-LKRIIIFDREVkrderdqtSIYFDDFLKLGEGH 164
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVV--EAALLAALEAADPGDLpLPAVWLLDAPA--------SVSVPAGWSTAPLP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 165 PHQAEVDKriSESGNGDLANILYTSGTTGDSKGVMLHHSCYeAAIPAHNERFPQLGDQDVIMNFLPFTHVFERAWTCWCL 244
Cdd:PRK06155 167 PLDAPAPA--AAVQPGDTAAILYTSGTTGPSKGVCCPHAQF-YWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 245 SMGCTLSINLRpadiqktikeirptamCSVPRFWEKVyagvqekinettglkkklmldaikvgREHNLEYVYkgltpppv 324
Cdd:PRK06155 244 LAGATYVLEPR----------------FSASGFWPAV--------------------------RRHGATVTY-------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 325 lhmkykfYEKTIYSLLKKTIGIENGRFFPTA---GAAIPPAV-QEFVLSVGINMVAGYGLTESTATVACENDYDHvVGSV 400
Cdd:PRK06155 274 -------LLGAMVSILLSQPARESDRAHRVRvalGPGVPAALhAAFRERFGVDLLDGYGSTETNFVIAVTHGSQR-PGSM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 401 GRLMPHVQVKI----------GENNEIMLRGE---GITHGYYKKEAATKAAFtEDGWFHTGDAGYIK-DEHLFLTERIKD 466
Cdd:PRK06155 346 GRLAPGFEARVvdehdqelpdGEPGELLLRADepfAFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDaDGWFRFVDRIKD 424
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
181-526 |
5.44e-27 |
|
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: 112.37 E-value: 5.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVML-HHSCYE-AAIPAHNERFPQlgdQDVIMNFLPFTHVFERAW-TCWCLSMGCTL---SINL 254
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLtHHNIVNnGYFIGERLGLTE---QDRLCIPVPLFHCFGSVLgVLACLTHGATMvfpSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 255 RPADIQKTIKEIRPTAMCSVPRfwekvyagvqekinettglkkklMLDAIkvgrehnleyvykgLTPPpvlhmkykfyEK 334
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPT-----------------------MFIAE--------------LEHP----------DF 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 335 TIYSLLKKTIGIengrffpTAGAAIPPAVQEFVLSVgINM---VAGYGLTESTATVAC---ENDYDHVVGSVGRLMPHVQ 408
Cdd:cd05917 113 DKFDLSSLRTGI-------MAGAPCPPELMKRVIEV-MNMkdvTIAYGMTETSPVSTQtrtDDSIEKRVNTVGRIMPHTE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 409 VKI-----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFkTSNGKYI 476
Cdd:cd05917 185 AKIvdpeggivppvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMdEDGYCRIVGRIKDMI-IRGGENI 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 477 APQAIEAKLVVDRYIDQISIIA--DER--KFVSALII--PEYKL----VKEYADKKGIHY 526
Cdd:cd05917 264 YPREIEEFLHTHPKVSDVQVVGvpDERygEEVCAWIRlkEGAELteedIKAYCKGKIAHY 323
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
181-501 |
1.55e-26 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 110.67 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHH--SCYEAAIPAHNERFPQlGDQDVIMNflPFTHVF-ERAWTCWCLSMGCTlsinlrpa 257
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHrqTLRAAAAWADCADLTE-DDRYLIIN--PFFHTFgYKAGIVACLLTGAT-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 258 diqktikeIRPTAMCSVPRFWEKVYagvQEKINETTGlkkklmldaikvgrehnleyvykgltPPPVLHmkykfyektiy 337
Cdd:cd17638 70 --------VVPVAVFDVDAILEAIE---RERITVLPG--------------------------PPTLFQ----------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 338 SLL----KKTIGIENGRFFPTAGAAIPPAVQEFVLS-VGINMVA-GYGLTESTATVACE--NDYDHVVGSVGRLMPHVQV 409
Cdd:cd17638 102 SLLdhpgRKKFDLSSLRAAVTGAATVPVELVRRMRSeLGFETVLtAYGLTEAGVATMCRpgDDAETVATTCGRACPGFEV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 410 KIGENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE-HLFLTERIKDLFkTSNGKYIAPQAIEAKLVVD 488
Cdd:cd17638 182 RIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERgYLRITDRLKDMY-IVGGFNVYPAEVEGALAEH 260
|
330
....*....|....*
gi 2786809754 489 RYIDQISII--ADER 501
Cdd:cd17638 261 PGVAQVAVIgvPDER 275
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
9-486 |
9.85e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 111.36 E-value: 9.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYR--DYKTETWipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAV 86
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEgeDGEERTL---TYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 87 TVP-FYATSSEAqVHYMVGDAEIRYIFVGEQLQY--------DVAFRVMQLGSQLKRIIIFDREVKRDERDQTsIYFDDF 157
Cdd:COG0365 91 HSPvFPGFGAEA-LADRIEDAEAKVLITADGGLRggkvidlkEKVDEALEELPSLEHVIVVGRTGADVPMEGD-LDWDEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 158 LKLGEGHPHQAEVDkriSEsgngDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGDQDVIMNFLPFthvfer 237
Cdd:COG0365 169 LAAASAEFEPEPTD---AD----DPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 238 AWT--CW-----CLSMGCTLSI------NLRPADIQKTIKEIRPTAMCSVPRFWekvyagvqekinettglkKKLMLDAI 304
Cdd:COG0365 236 GWAtgHSyivygPLLNGATVVLyegrpdFPDPGRLWELIEKYGVTVFFTAPTAI------------------RALMKAGD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 305 KVGREHNLEyvykgltpppvlhmkykfyektiySLlkKTIGiengrffpTAGAAIPPAVQEFVLS-VGINMVAGYGLTES 383
Cdd:COG0365 298 EPLKKYDLS------------------------SL--RLLG--------SAGEPLNPEVWEWWYEaVGVPIVDGWGQTET 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 384 TATVACENDYDHVV-GSVGRLMPHVQVKI----------GENNEIMLRGE--GITHGYYKKEAATKAAF--TEDGWFHTG 448
Cdd:COG0365 344 GGIFISNLPGLPVKpGSMGKPVPGYDVAVvdedgnpvppGEEGELVIKGPwpGMFRGYWNDPERYRETYfgRFPGWYRTG 423
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2786809754 449 DAGYIkDEH--LFLTERIKDLFKTSnGKYIAPQAIEAKLV 486
Cdd:COG0365 424 DGARR-DEDgyFWILGRSDDVINVS-GHRIGTAEIESALV 461
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
182-476 |
3.20e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 110.58 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 182 LANILYTSGTTGDSKGVML-HHSCYEAAIPahnerfpqLGDQDVIMNF--------LPFTHVFERAWTCWCLSMGCTLSI 252
Cdd:PTZ00342 306 ITSIVYTSGTSGKPKGVMLsNKNLYNTVVP--------LCKHSIFKKYnpkthlsyLPISHIYERVIAYLSFMLGGTINI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 253 -----NLRPADIQKTIKEIrptaMCSVPRFWEKVYAGVQEKINETTGLKKKLMLDAIKVGREHNleyvYKGLTpppvlhm 327
Cdd:PTZ00342 378 wskdiNYFSKDIYNSKGNI----LAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILSLRKSNN----NGGFS------- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 328 kyKFYEKT--IYSLLKKTIGiENGRFFPTAGAAIPPAV-QEFVLSVGINMVAGYGLTESTATVACENDYDHVVGSVG-RL 403
Cdd:PTZ00342 443 --KFLEGIthISSKIKDKVN-PNLEVILNGGGKLSPKIaEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGgPI 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 404 MPHVQVKIGE-----------NNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFKTS 471
Cdd:PTZ00342 520 SPNTKYKVRTwetykatdtlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQInKNGSLTFLDRSKGLVKLS 599
|
....*
gi 2786809754 472 NGKYI 476
Cdd:PTZ00342 600 QGEYI 604
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
6-485 |
3.24e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 109.59 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 6 LSVLIQRQARKYGDRVVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRA 85
Cdd:PRK06145 4 LSASIAFHARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 86 VTVPFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAFrvmqlgsqLKRIIIFDREVKRDERdqtsiyfddflKLGEGHP 165
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVAL--------ETPKIVIDAAAQADSR-----------RLAQGGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 166 HQAEVDKRISEsgngDLANILYTSGTTGDSKGVMLHHSCYeaaipaHNERFPQ-----LGDQDVIMNFLPFTHV--FERA 238
Cdd:PRK06145 139 EIPPQAAVAPT----DLVRLMYTSGTTDRPKGVMHSYGNL------HWKSIDHvialgLTASERLLVVGPLYHVgaFDLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 239 WTCwCLSMGCTLSI--NLRPADIQKTIKEIRPTAMCSVPrfwekvyagvqekinettglkkkLMLDAIkvgrehnleyvy 316
Cdd:PRK06145 209 GIA-VLWVGGTLRIhrEFDPEAVLAAIERHRLTCAWMAP-----------------------VMLSRV------------ 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 317 kgLTPPpvlhmkykfyEKTIYSLLKKTIGIENGRFFPTAgaaippAVQEFV-LSVGINMVAGYGLTESTA--TVACENDY 393
Cdd:PRK06145 253 --LTVP----------DRDRFDLDSLAWCIGGGEKTPES------RIRDFTrVFTRARYIDAYGLTETCSgdTLMEAGRE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 394 DHVVGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTeDGWFHTGDAGYIKDE-HLFLTE 462
Cdd:PRK06145 315 IEKIGSTGRALAHVEIRIadgagrwlppNMKGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEgFLYLTD 393
|
490 500
....*....|....*....|...
gi 2786809754 463 RIKDLFkTSNGKYIAPQAIEAKL 485
Cdd:PRK06145 394 RKKDMI-ISGGENIASSEVERVI 415
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
164-485 |
3.48e-25 |
|
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: 108.53 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 164 HPhQAEVDKRISESGNG---DLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFTHV---Fer 237
Cdd:cd05941 71 YP-LAELEYVITDSEPSlvlDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAW-RWTEDDVLLHVLPLHHVhglV-- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 238 awtcwcLSMGCTL----SINLRP---ADIQKTIKEIRP-TAMCSVPRFWEKVYAGVQEKINETTGLKKKLMldaikvgre 309
Cdd:cd05941 147 ------NALLCPLfagaSVEFLPkfdPKEVAISRLMPSiTVFMGVPTIYTRLLQYYEAHFTDPQFARAAAA--------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 310 hnleyvykgltpppvlhmkykfyektiysllkktigiENGRFFPTAGAAIPPAV-QEFVLSVGINMVAGYGLTESTATVA 388
Cdd:cd05941 212 -------------------------------------ERLRLMVSGSAALPVPTlEEWEAITGHTLLERYGMTEIGMALS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 389 CENDYDHVVGSVGRLMPHVQVKI-----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIK-DE 456
Cdd:cd05941 255 NPLDGERRPGTVGMPLPGVQARIvdeetgeplprGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDeDG 334
|
330 340
....*....|....*....|....*....
gi 2786809754 457 HLFLTERIKDLFKTSNGKYIAPQAIEAKL 485
Cdd:cd05941 335 YYWILGRSSVDIIKSGGYKVSALEIERVL 363
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
155-506 |
1.04e-24 |
|
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: 108.14 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 155 DDFLKLGEGHPHQAEVDKRISE------------SGNGDLANILYTSGTTGDSKGVMLHHS---CYEAAIPAHNERFPQl 219
Cdd:cd05906 130 AEFAGLETLSGLPGIRVLSIEElldtaadhdlpqSRPDDLALLMLTSGSTGFPKAVPLTHRnilARSAGKIQHNGLTPQ- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 220 gdqDVIMNFLPFTHVferawtcwclsmGCTLSINLRPadiqktikeirptamcsvprfwekVYAGVQEkinettglkkkl 299
Cdd:cd05906 209 ---DVFLNWVPLDHV------------GGLVELHLRA------------------------VYLGCQQ------------ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 300 mldaIKVGREHNLEyvykglTPPPVLHMKYKfYEKTI-------YSLLK--------KTIGIENGRFFPTAGAAIPPAVQ 364
Cdd:cd05906 238 ----VHVPTEEILA------DPLRWLDLIDR-YRVTItwapnfaFALLNdlleeiedGTWDLSSLRYLVNAGEAVVAKTI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 365 EFVLSV----GIN---MVAGYGLTESTATV-------ACENDYDHVVGSVGRLMPHVQVKI----------GENNEIMLR 420
Cdd:cd05906 307 RRLLRLlepyGLPpdaIRPAFGMTETCSGViysrsfpTYDHSQALEFVSLGRPIPGVSMRIvddegqllpeGEVGRLQVR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 421 GEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDEHLFLTERIKDLFkTSNGKYIAPQAIEAklvvdrYIDQISIIadE 500
Cdd:cd05906 387 GPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTKDTI-IVNGVNYYSHEIEA------AVEEVPGV--E 457
|
....*.
gi 2786809754 501 RKFVSA 506
Cdd:cd05906 458 PSFTAA 463
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
6-577 |
1.18e-23 |
|
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: 105.23 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 6 LSVLIQRQARKYGDRVVLRYR------DYKT-----------ETWIPVSWNQFAATVKTVSNALIELGIGiqENIAVFSQ 68
Cdd:cd17632 24 LAQIIATVMTGYADRPALGQRatelvtDPATgrttlrllprfETITYAELWERVGAVAAAHDPEQPVRPG--DFVAVLGF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 69 NKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVG-EQLqyDVAFRVMQLGSQLKRIIIFD-REVKRDE 146
Cdd:cd17632 102 TSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSaEHL--DLAVEAVLEGGTPPRLVVFDhRPEVDAH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 147 RDQTSIYFDDFLKLGEGHPHQAEVDKRI----------SESGNGDLANILYTSGTTGDSKGVMlhhscYEAAIPAH---- 212
Cdd:cd17632 180 RAALESARERLAAVGIPVTTLTLIAVRGrdlppaplfrPEPDDDPLALLIYTSGSTGTPKGAM-----YTERLVATfwlk 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 213 ----NERFPQLGdqdVIMNFLPFTHVFERAWTCWCLSMGCTLSINLRP--ADIQKTIKEIRPTAMCSVPRFWEKVYAGVQ 286
Cdd:cd17632 255 vssiQDIRPPAS---ITLNFMPMSHIAGRISLYGTLARGGTAYFAAASdmSTLFDDLALVRPTELFLVPRVCDMLFQRYQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 287 EKINETTGLKKKLMLDAIKVGREhnleyvykgltpppvlhmkykfyektiysLLKKTIGienGRFFP--TAGAAIPPAVQ 364
Cdd:cd17632 332 AELDRRSVAGADAETLAERVKAE-----------------------------LRERVLG---GRLLAavCGSAPLSAEMK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 365 EFVLSV-GINMVAGYGLTEsTATVACEN--------DYDHV-VGSVGRLM---PHVQvkigenNEIMLRGEGITHGYYKK 431
Cdd:cd17632 380 AFMESLlDLDLHDGYGSTE-AGAVILDGvivrppvlDYKLVdVPELGYFRtdrPHPR------GELLVKTDTLFPGYYKR 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 432 EAATKAAFTEDGWFHTGDA-GYIKDEHLFLTERIKDLFKTSNGKYIAPQAIEAKLVVDRYIDQISIIAD-ERKFVSALII 509
Cdd:cd17632 453 PEVTAEVFDEDGFYRTGDVmAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNsERAYLLAVVV 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786809754 510 PeyklvkeyadkkgihygsMEDLLRKPEIIELFKERIDTLQQ-----QFAHYEQIKKFTLLPQPFSMERGELT 577
Cdd:cd17632 533 P------------------TQDALAGEDTARLRAALAESLQRiareaGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
181-501 |
1.69e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 101.64 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTHV--FERAWTCwcLSMGCTLSINLRPAD 258
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG-FGGGDSWLLSLPLYHVggLAILVRS--LLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 259 IQKTIKEIRPTAMCSVPrfwekvyagvqekinetTGLKKklMLDAikvgrehnleyvykGLTPPPVLhmkykfyektiyS 338
Cdd:cd17630 78 LAEDLAPPGVTHVSLVP-----------------TQLQR--LLDS--------------GQGPAALK------------S 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 339 LLKKTIGiengrffptaGAAIPPAVQEFVLSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKIGENNEIM 418
Cdd:cd17630 113 LRAVLLG----------GAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVEDGEIW 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 419 LRGEGITHGYYKKEaaTKAAFTEDGWFHTGDAGYIKDE-HLFLTERIKDLFkTSNGKYIAPQAIEAKLVVDRYIDQISI- 496
Cdd:cd17630 183 VGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADgRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDAFVv 259
|
....*.
gi 2786809754 497 -IADER 501
Cdd:cd17630 260 gVPDEE 265
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
6-498 |
1.73e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 104.73 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 6 LSVLIQRQARKYGDRVVLRY--RDyktetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFG---A 80
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFlgKD--------ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGtllA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 81 FGVRAVTVPFYatsSEAQVHYMVGDAEIRYIfvgeqLQYDVAF-RV--MQLGSQLKRIII--------FDREVKRD--ER 147
Cdd:PRK06710 98 GGIVVQTNPLY---TERELEYQLHDSGAKVI-----LCLDLVFpRVtnVQSATKIEHVIVtriadflpFPKNLLYPfvQK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 148 DQTSIyfddFLKLGEGH------PHQAEVDKRISE--SGNGDLANILYTSGTTGDSKGVML-HHSCYEAAIPAHNERFPQ 218
Cdd:PRK06710 170 KQSNL----VVKVSESEtihlwnSVEKEVNTGVEVpcDPENDLALLQYTGGTTGFPKGVMLtHKNLVSNTLMGVQWLYNC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 219 LGDQDVIMNFLPFTHVFerawtcwclsmGCTLSINLrpaDIQKTIKeirptaMCSVPRFwekvyagvqekinettglKKK 298
Cdd:PRK06710 246 KEGEEVVLGVLPFFHVY-----------GMTAVMNL---SIMQGYK------MVLIPKF------------------DMK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 299 LMLDAIKvgrEHNLEyVYKGltPPPVlhmkykfYEKTIYSLLKKTIGIENGRFFPTAGAAIPPAVQE-FVLSVGINMVAG 377
Cdd:PRK06710 288 MVFEAIK---KHKVT-LFPG--APTI-------YIALLNSPLLKEYDISSIRACISGSAPLPVEVQEkFETVTGGKLVEG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 378 YGLTESTATVACENDYD-HVVGSVGRLMPHVQVKI-----------GENNEIMLRGEGITHGYYKKEAATkAAFTEDGWF 445
Cdd:PRK06710 355 YGLTESSPVTHSNFLWEkRVPGSIGVPWPDTEAMImsletgealppGEIGEIVVKGPQIMKGYWNKPEET-AAVLQDGWL 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2786809754 446 HTGDAGYIKDEHLF-LTERIKDLFKTSnGKYIAPQAIEAKLVVDRYIDQISIIA 498
Cdd:PRK06710 434 HTGDVGYMDEDGFFyVKDRKKDMIVAS-GFNVYPREVEEVLYEHEKVQEVVTIG 486
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-500 |
2.08e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 103.67 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 48 VSNALIELGIGIQENIAVFSQNKPECLYVDFGAF----GVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAF 123
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFTYIELSFAVAyaggRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 124 RVMQLGSQlkrIIIFDREVKRDERDQTsiyfddflklgEGHPHQAEvdkrisesgngDLANILYTSGTTGDSKGVMLHHS 203
Cdd:cd05922 86 ALPASPDP---GTVLDADGIRAARASA-----------PAHEVSHE-----------DLALLLYTSGSTGSPKLVRLSHQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 204 CYEAAIPAHNERFPQLGDqDVIMNFLPFTHvferawtCWCLSM-------GCTLSINLR---PADIQKTIKEIRPTAMCS 273
Cdd:cd05922 141 NLLANARSIAEYLGITAD-DRALTVLPLSY-------DYGLSVlnthllrGATLVLTNDgvlDDAFWEDLREHGATGLAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 274 VPRFWEkvyagvqekinettglkkklMLDAIkvgrehnleyvykGLTPPPVLHMkykfyektiysllkktigiengRFFP 353
Cdd:cd05922 213 VPSTYA--------------------MLTRL-------------GFDPAKLPSL----------------------RYLT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 354 TAGAAIPPA-VQEFV-LSVGINMVAGYGLTESTATVAC--ENDYDHVVGSVGRLMPHVQVKI----------GENNEIML 419
Cdd:cd05922 238 QAGGRLPQEtIARLReLLPGAQVYVMYGQTEATRRMTYlpPERILEKPGSIGLAIPGGEFEIldddgtptppGEPGEIVH 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 420 RGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE-HLFLTERIKDLFKTSnGKYIAPQAIEAKLVVDRYIDQISIIA 498
Cdd:cd05922 318 RGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDgFLFIVGRRDRMIKLF-GNRISPTEIEAAARSIGLIIEAAAVG 396
|
..
gi 2786809754 499 DE 500
Cdd:cd05922 397 LP 398
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
9-485 |
2.14e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 104.65 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRY-----RDYKTETWipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAfGV 83
Cdd:PRK07529 30 LLSRAAARHPDAPALSFlldadPLDRPETW---TYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG-EA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 84 RAVTVPFYATSSEAQVHYMVGDAEIRY-IFVGEQLQYDVAFRVMQL---GSQLKRIIIFD---------REVKRDERDQT 150
Cdd:PRK07529 106 AGIANPINPLLEPEQIAELLRAAGAKVlVTLGPFPGTDIWQKVAEVlaaLPELRTVVEVDlarylpgpkRLAVPLIRRKA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 151 SIYFDDFLKLGEGHPHQAEVDKRISESGngDLANILYTSGTTGDSKGVMLHHS--CYEAAIPAhneRFPQLGDQDVIMNF 228
Cdd:PRK07529 186 HARILDFDAELARQPGDRLFSGRPIGPD--DVAAYFHTGGTTGMPKLAQHTHGneVANAWLGA---LLLGLGPGDTVFCG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 229 LPFTHVFERAWTCW-CLSMGCTLSInLRPA---------DIQKTIKEIRPTAMCSVPrfweKVYAgvqekinettglkkk 298
Cdd:PRK07529 261 LPLFHVNALLVTGLaPLARGAHVVL-ATPQgyrgpgviaNFWKIVERYRINFLSGVP----TVYA--------------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 299 lMLDAIKVGReHNleyvykgltpppvlhmkykfyektIYSLlkktigiengRFFPTAGAAIPPAV-QEFVLSVGINMVAG 377
Cdd:PRK07529 321 -ALLQVPVDG-HD------------------------ISSL----------RYALCGAAPLPVEVfRRFEAATGVRIVEG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 378 YGLTESTATVACeNDYDHV--VGSVGRLMPHVQVKI---------------GENNEIMLRGEGITHGYYKkEAATKAAFT 440
Cdd:PRK07529 365 YGLTEATCVSSV-NPPDGErrIGSVGLRLPYQRVRVvilddagrylrdcavDEVGVLCIAGPNVFSGYLE-AAHNKGLWL 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2786809754 441 EDGWFHTGDAGYIkDEH--LFLTERIKDLFkTSNGKYIAPQAIEAKL 485
Cdd:PRK07529 443 EDGWLNTGDLGRI-DADgyFWLTGRAKDLI-IRGGHNIDPAAIEEAL 487
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
36-513 |
4.41e-23 |
|
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: 102.17 E-value: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 36 VSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGE 115
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 116 QLQydvafrvmqlgsqlkriiifdrevkrderdqtsiyfddflklgeghphqaevdkrisesgngDLANILYTSGTTGDS 195
Cdd:cd05935 82 ELD--------------------------------------------------------------DLALIPYTSGTTGLP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 196 KGVMLHHSCYEAAIpAHNERFPQLGDQDVIMNFLPFTHVferawtcwclsMGCTLSINLrpadiqktikeirptamcsvp 275
Cdd:cd05935 100 KGCMHTHFSAAANA-LQSAVWTGLTPSDVILACLPLFHV-----------TGFVGSLNT--------------------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 276 rfweKVYAGvqEKINETTGLKKKLMLDAIkvgREHNLEYVYKGLTPPPVLHMKYKFYEKTIYSLlkktigiengRFFPTA 355
Cdd:cd05935 147 ----AVYVG--GTYVLMARWDRETALELI---EKYKVTFWTNIPTMLVDLLATPEFKTRDLSSL----------KVLTGG 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 356 GAAIPPAVQEFVLSV-GINMVAGYGLTESTATV----------AC------ENDYDHVVGSVGRLMPhvqvkIGENNEIM 418
Cdd:cd05935 208 GAPMPPAVAEKLLKLtGLRFVEGYGLTETMSQThtnpplrpklQClgip*fGVDARVIDIETGRELP-----PNEVGEIV 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 419 LRGEGITHGYYKKEAATKAAFTEDG---WFHTGDAGYIKDE-HLFLTERIKDLFKTSnGKYIAPQAIEAKLVVDRYIDQI 494
Cdd:cd05935 283 VRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEgYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EV 361
|
490 500
....*....|....*....|....*
gi 2786809754 495 SIIA--DER--KFVSALII--PEYK 513
Cdd:cd05935 362 CVISvpDERvgEEVKAFIVlrPEYR 386
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
175-486 |
3.28e-22 |
|
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: 99.34 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 175 SESGNGDLANILYTSGTTGDSKGVML---HHScYEAAIPAHNerfpqLG--DQDVIMNFLPFTHVferawtcwclsmgCT 249
Cdd:cd05912 72 SDVKLDDIATIMYTSGTTGKPKGVQQtfgNHW-WSAIGSALN-----LGltEDDNWLCALPLFHI-------------SG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 250 LSINLRPAdiqktikeIRPTAMCSVPRFWEkvyagvqEKINEttglkkklmldAIKVGREHNLEYVYKGLTpppvlhmky 329
Cdd:cd05912 133 LSILMRSV--------IYGMTVYLVDKFDA-------EQVLH-----------LINSGKVTIISVVPTMLQ--------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 330 kfyektiySLLKKTIGI--ENGRFFPTAGAAIPPAVQEFVLSVGINMVAGYGLTESTATVACEN--DYDHVVGSVGRLMP 405
Cdd:cd05912 178 --------RLLEILGEGypNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSpeDALNKIGSAGKPLF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 406 HVQVKIGENN-------EIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYIKDE-HLFLTERIKDLFkTSNGKYIA 477
Cdd:cd05912 250 PVELKIEDDGqppyevgEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEgFLYVLDRRSDLI-ISGGENIY 327
|
....*....
gi 2786809754 478 PQAIEAKLV 486
Cdd:cd05912 328 PAEIEEVLL 336
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
181-543 |
3.70e-22 |
|
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: 100.10 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTHVFERAWTCWC-LSMGCTLSINLRPAD- 258
Cdd:cd05909 148 DPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD-PNPEDVVFGALPFFHSFGLTGCLWLpLLSGIKVVFHPNPLDy 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 259 --IQKTIKEIRPTAMCSVPRFwekvyagvqekinettglkkklmldaikvgrehnLEYVYKGLTPppvlhmkYKFYekti 336
Cdd:cd05909 227 kkIPELIYDKKATILLGTPTF----------------------------------LRGYARAAHP-------EDFS---- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 337 ySLlkktigiengRFFPTAGAAIPPAV-QEFVLSVGINMVAGYGLTESTATVACEN-DYDHVVGSVGRLMPHVQVKI--- 411
Cdd:cd05909 262 -SL----------RLVVAGAEKLKDTLrQEFQEKFGIRILEGYGTTECSPVISVNTpQSPNKEGTVGRPLPGMEVKIvsv 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 --------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYIKDE-HLFLTERIKDLFKTSnGKYIAPQAIE 482
Cdd:cd05909 331 etheevpiGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEgFLTITGRLSRFAKIA-GEMVSLEAIE 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786809754 483 AKLvvdryidqiSIIADERKFVSALIIPEYK--------LVKEYADKKgihygSMEDLLRKPEIIELFK 543
Cdd:cd05909 409 DIL---------SEILPEDNEVAVVSVPDGRkgekivllTTTTDTDPS-----SLNDILKNAGISNLAK 463
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
6-482 |
5.54e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 100.07 E-value: 5.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 6 LSVLIQRQARKYGDRVVLRYrdYKTETwipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRA 85
Cdd:PRK05605 34 LVDLYDNAVARFGDRPALDF--FGATT----TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 86 VTV---PFYaTSSEAQ--------------------VHYMVGDAEIRYIFVGEQLqyDVAFRVMQLGSQL--KRIiifdr 140
Cdd:PRK05605 108 VVVehnPLY-TAHELEhpfedhgarvaivwdkvaptVERLRRTTPLETIVSVNMI--AAMPLLQRLALRLpiPAL----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 141 evkRDERDQTS------IYFDDFLKLGEGHPHQAEVDKRISEsgnGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNE 214
Cdd:PRK05605 180 ---RKARAALTgpapgtVPWETLVDAAIGGDGSDVSHPRPTP---DDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 215 RFPQLGDQD-VIMNFLPFTHVFErawtcwcLSMGCTLSINL----------RPADIQKTIKEIRPTAMCSVPRFWEKVya 283
Cdd:PRK05605 254 WVPGLGDGPeRVLAALPMFHAYG-------LTLCLTLAVSIggelvllpapDIDLILDAMKKHPPTWLPGVPPLYEKI-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 284 gvqekinettglkkklmldaIKVGREHNLEyvykgltpppvLHmkykfyektiysllkktiGIENGrffpTAGA-AIPPA 362
Cdd:PRK05605 325 --------------------AEAAEERGVD-----------LS------------------GVRNA----FSGAmALPVS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 363 -VQEFVLSVGINMVAGYGLTEsTATVACENDY--DHVVGSVGRLMPHVQVKI------------GENNEIMLRGEGITHG 427
Cdd:PRK05605 352 tVELWEKLTGGLLVEGYGLTE-TSPIIVGNPMsdDRRPGYVGVPFPDTEVRIvdpedpdetmpdGEEGELLVRGPQVFKG 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2786809754 428 YYKKEAATKAAFtEDGWFHTGDAGyIKDEHLFLT--ERIKDLFKTSnGKYIAPQAIE 482
Cdd:PRK05605 431 YWNRPEETAKSF-LDGWFRTGDVV-VMEEDGFIRivDRIKELIITG-GFNVYPAEVE 484
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
6-485 |
6.34e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 99.73 E-value: 6.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 6 LSVLIQRQARKYGDRVVLRYRDyktETWipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRA 85
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGD---RSW---TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 86 VTVPFYATSSEAQVHYMVGDAEIRyIFVGEQLQYDVAFRVMQLGSQLKRIIIFDRevKRDERDqtsiyFDDFLKLGEGHP 165
Cdd:PRK07470 83 VWVPTNFRQTPDEVAYLAEASGAR-AMICHADFPEHAAAVRAASPDLTHVVAIGG--ARAGLD-----YEALVARHLGAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 166 HQ-AEVDKrisesgnGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHN-ERFPQLGDQDVIMNFLPFTH---------V 234
Cdd:PRK07470 155 VAnAAVDH-------DDPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLaDLMPGTTEQDASLVVAPLSHgagihqlcqV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 235 FERAWTCwclsmgCTLSINLRPADIQKTIKEIRPTAMCSVPrfwekvyagvqekinetTGLKkkLMLDAIKVGR-EH-NL 312
Cdd:PRK07470 228 ARGAATV------LLPSERFDPAEVWALVERHRVTNLFTVP-----------------TILK--MLVEHPAVDRyDHsSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 313 EYVykgltpppvlhmkykfyektIYsllkktigiengrffptAGAAIPPAVQEFVLSV-GINMVAGYGLTESTATVAC-- 389
Cdd:PRK07470 283 RYV--------------------IY-----------------AGAPMYRADQKRALAKlGKVLVQYFGLGEVTGNITVlp 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 390 -----ENDYDHV-VGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYI 453
Cdd:PRK07470 326 palhdAEDGPDArIGTCGFERTGMEVQIqddegrelppGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHL 404
|
490 500 510
....*....|....*....|....*....|...
gi 2786809754 454 KDE-HLFLTERIKDLFkTSNGKYIAPQAIEAKL 485
Cdd:PRK07470 405 DARgFLYITGRASDMY-ISGGSNVYPREIEEKL 436
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
6-482 |
8.58e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 98.78 E-value: 8.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 6 LSVLIQRQARKYGDRVVLRYRDyktETWipvSWNQFAATVKTVSNALI-ELGIGIQENIAVFSQNKPECLYVDFGAFGVR 84
Cdd:PRK06839 4 IAYWIEKRAYLHPDRIAIITEE---EEM---TYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 85 AVTVPFYATSSEAQVHYMVGDAEIRYIFVgeQLQYDVAFRVMQLGSQLKRIIifdREVKRDERDQTSIyfDDFLKLGEGH 164
Cdd:PRK06839 78 CIAVPLNIRLTENELIFQLKDSGTTVLFV--EKTFQNMALSMQKVSYVQRVI---SITSLKEIEDRKI--DNFVEKNESA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 165 PHQaevdkrisesgngdlanILYTSGTTGDSKGVMLHH-SCYEAAIpaHNERFPQLGDQDVIMNFLPFTHVFerawtcwc 243
Cdd:PRK06839 151 SFI-----------------ICYTSGTTGKPKGAVLTQeNMFWNAL--NNTFAIDLTMHDRSIVLLPLFHIG-------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 244 lsmgctlSINLrpadiqktikeirptamCSVPRFWEKVYAGVQEKINETtglkkklmlDAIKVGREHNLEYVYkGLtppP 323
Cdd:PRK06839 204 -------GIGL-----------------FAFPTLFAGGVIIVPRKFEPT---------KALSMIEKHKVTVVM-GV---P 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 324 VLHmkykfyEKTIYSLLKKTIGIENGRFFPTAGAAIP-PAVQEFVlSVGINMVAGYGLTESTATV--ACENDYDHVVGSV 400
Cdd:PRK06839 247 TIH------QALINCSKFETTNLQSVRWFYNGGAPCPeELMREFI-DRGFLFGQGFGMTETSPTVfmLSEEDARRKVGSI 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 401 GRLMPHV----------QVKIGENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYIKDE-HLFLTERIKDLFk 469
Cdd:PRK06839 320 GKPVLFCdyelidenknKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDgFVYIVGRKKEMI- 397
|
490
....*....|...
gi 2786809754 470 TSNGKYIAPQAIE 482
Cdd:PRK06839 398 ISGGENIYPLEVE 410
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
10-466 |
1.08e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 98.87 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 10 IQRQARKYGDRVVLRYRDyktetwIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVP 89
Cdd:PRK08162 24 LERAAEVYPDRPAVIHGD------RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 90 FYATSSEAQVHYMVGDAEIRYIFVGEQLQyDVAFRVMQLGSQLKRIIIF--DREVKRDERdQTSIYFDDFLKLG----EG 163
Cdd:PRK08162 98 LNTRLDAASIAFMLRHGEAKVLIVDTEFA-EVAREALALLPGPKPLVIDvdDPEYPGGRF-IGALDYEAFLASGdpdfAW 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 164 HPHQAEVDKrISesgngdlanILYTSGTTGDSKGVMLHH-SCYEAAIpaHNERFPQLGDQDVIMNFLPFTHvferawtC- 241
Cdd:PRK08162 176 TLPADEWDA-IA---------LNYTSGTTGNPKGVVYHHrGAYLNAL--SNILAWGMPKHPVYLWTLPMFH-------Cn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 242 -WCL--SMGCTLSIN--LR---PADIQKTIKEIRPTAMCSVPrfweKVYAGVqekINettglkkklMLDAIKVGREHnle 313
Cdd:PRK08162 237 gWCFpwTVAARAGTNvcLRkvdPKLIFDLIREHGVTHYCGAP----IVLSAL---IN---------APAEWRAGIDH--- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 314 yvykgltppPVLHMkykfyektiysllkktigiengrffpTAGAAIPPAVQEFVLSVGINMVAGYGLTES--TATVACEN 391
Cdd:PRK08162 298 ---------PVHAM--------------------------VAGAAPPAAVIAKMEEIGFDLTHVYGLTETygPATVCAWQ 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 392 D--------------------YdHVVGSVGRLMPHVQVKI---GEN-NEIMLRGEGITHGYYKKEAATKAAFtEDGWFHT 447
Cdd:PRK08162 343 PewdalplderaqlkarqgvrY-PLQEGVTVLDPDTMQPVpadGETiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHT 420
|
490 500
....*....|....*....|....*
gi 2786809754 448 GDA------GYIKdehlfLTERIKD 466
Cdd:PRK08162 421 GDLavlhpdGYIK-----IKDRSKD 440
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
14-513 |
2.94e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 97.72 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 14 ARKYGDRVVLRYrdYKTEtwipVSWNQFAATVKTVSNALI-ELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYA 92
Cdd:PRK08314 20 ARRYPDKTAIVF--YGRA----ISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 93 TSSEAQVHYMVGDAEIRYIFVGEQLqydvAFRVMQL--GSQLKRIIIFDRevkRDE-RDQTSIYFDDFLK---------- 159
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIVGSEL----APKVAPAvgNLRLRHVIVAQY---SDYlPAEPEIAVPAWLRaepplqalap 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 160 ---------LGEGH---PHQAEVDkrisesgngDLANILYTSGTTGDSKGVMLHHSCYEAAIpAHNERFPQLGDQDVIMN 227
Cdd:PRK08314 167 ggvvawkeaLAAGLappPHTAGPD---------DLAVLPYTSGTTGVPKGCMHTHRTVMANA-VGSVLWSNSTPESVVLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 228 FLPFTHVferawtcwcLSMGCTL--SINLRpadiqktikeirpTAMCSVPRfWEKVYAG-------VQEKINETTglkkk 298
Cdd:PRK08314 237 VLPLFHV---------TGMVHSMnaPIYAG-------------ATVVLMPR-WDREAAArlieryrVTHWTNIPT----- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 299 LMLDAikvgrehnleyvykgLTPPpvlhmkyKFYEKTIYSLLKKTIGiengrffptaGAAIPPAVQEFVLS-VGINMVAG 377
Cdd:PRK08314 289 MVVDF---------------LASP-------GLAERDLSSLRYIGGG----------GAAMPEAVAERLKElTGLDYVEG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 378 YGLTEsTATVACENDYDH---------VVGSVGRLMPHV---QVKIGENNEIMLRGEGITHGYYKKEAATKAAFTE-DG- 443
Cdd:PRK08314 337 YGLTE-TMAQTHSNPPDRpklqclgipTFGVDARVIDPEtleELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDGk 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786809754 444 -WFHTGDAGYIKDE-HLFLTERIKDLFKTSNGKyIAPQAIEAKLVVDRYIDQISIIA--DERK--FVSALII--PEYK 513
Cdd:PRK08314 416 rFFRTGDLGRMDEEgYFFITDRLKRMINASGFK-VWPAEVENLLYKHPAIQEACVIAtpDPRRgeTVKAVVVlrPEAR 492
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
9-486 |
6.27e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 96.18 E-value: 6.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRqARKYGDRVVLRYRDyKTETWIpvswnQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:PRK03640 8 LKQR-AFLTPDRTAIEFEE-KKVTFM-----ELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVgeqlqydvafrvmqlgsqlkriiifDREVKRDERDQTSIYFDDFLKLGEGHPH-Q 167
Cdd:PRK03640 81 LLNTRLSREELLWQLDDAEVKCLIT-------------------------DDDFEAKLIPGISVKFAELMNGPKEEAEiQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 168 AEVDKRisesgngDLANILYTSGTTGDSKGVML--HHSCYEAAIPAHNerfpqLG--DQDVIMNFLPFTHVferawtcwc 243
Cdd:PRK03640 136 EEFDLD-------EVATIMYTSGTTGKPKGVIQtyGNHWWSAVGSALN-----LGltEDDCWLAAVPIFHI--------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 244 lsmgCTLSINLR---------------PADIQKTIKEIRPTAMCSVPrfwekvyagvqekinetTGLKKklMLDAIKVGR 308
Cdd:PRK03640 195 ----SGLSILMRsviygmrvvlvekfdAEKINKLLQTGGVTIISVVS-----------------TMLQR--LLERLGEGT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 309 EHNleyvykgltpppvlhmkykfyektiysllkktigieNGRFFPTAGAAIPPAVQEFVLSVGINMVAGYGLTEST---A 385
Cdd:PRK03640 252 YPS------------------------------------SFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETAsqiV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 386 TVACEnDYDHVVGSVGRLMPHVQVKI---------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYIKDE 456
Cdd:PRK03640 296 TLSPE-DALTKLGSAGKPLFPCELKIekdgvvvppFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEE 373
|
490 500 510
....*....|....*....|....*....|.
gi 2786809754 457 -HLFLTERIKDLFkTSNGKYIAPQAIEAKLV 486
Cdd:PRK03640 374 gFLYVLDRRSDLI-ISGGENIYPAEIEEVLL 403
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
10-501 |
6.51e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 96.38 E-value: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 10 IQRQARKYGDRVVLRYRDYKTetwipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVP 89
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTT------TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 90 FYATSSEAQVHYMVGDAEIRYIFVGEQLQyDVAFRVMQLGSQLKRIIifdreVKRDERDQTSIYFDDFLKlgEGHPHQAE 169
Cdd:PRK07786 97 VNFRLTPPEIAFLVSDCGAHVVVTEAALA-PVATAVRDIVPLLSTVV-----VAGGSSDDSVLGYEDLLA--EAGPAHAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 170 VDkrISESGNgdlANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGDQDVimNFL--PFTHVFERAWTCWCLSMG 247
Cdd:PRK07786 169 VD--IPNDSP---ALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDV--GFVgvPLFHIAGIGSMLPGLLLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 248 CTLSIN----LRPADIQKTIKEIRPTAMCSVPRFWEKVYAGVQEKinettglkkklmldaikvGREHNLEYVYKGLTPPP 323
Cdd:PRK07786 242 APTVIYplgaFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQAR------------------PRDLALRVLSWGAAPAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 324 vlhmkykfyeKTIYSLLKKTigiengrfFPtaGAAIppavqefvlsvginmVAGYGLTEsTATVACENDYDHVV---GSV 400
Cdd:PRK07786 304 ----------DTLLRQMAAT--------FP--EAQI---------------LAAFGQTE-MSPVTCMLLGEDAIrklGSV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 401 GRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYIKDE-HLFLTERIKDLFk 469
Cdd:PRK07786 348 GKVIPTVAARVvdenmndvpvGEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEgYVWVVDRKKDMI- 425
|
490 500 510
....*....|....*....|....*....|....
gi 2786809754 470 TSNGKYIAPQAIEAKLVVDRYIDQISII--ADER 501
Cdd:PRK07786 426 ISGGENIYCAEVENVLASHPDIVEVAVIgrADEK 459
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
151-482 |
1.50e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 95.66 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 151 SIYFDDFLKLGEGHPHQAevdkriSESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGD--------- 221
Cdd:PRK12492 184 AVPFKQALRQGRGLSLKP------VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPdgqplmkeg 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 222 QDVIMNFLPFTHVFerAWTCWCLSMGCTLSINL---RPADIQKTIKEI---RPTAMCsvprfwekvyagvqekinettgl 295
Cdd:PRK12492 258 QEVMIAPLPLYHIY--AFTANCMCMMVSGNHNVlitNPRDIPGFIKELgkwRFSALL----------------------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 296 kkklmldaikvgrehnleyvykGLTPPPVLHMKYKFYEKTIYSLLKKTigiengrffPTAGAAIPPAVQEFVLSV-GINM 374
Cdd:PRK12492 313 ----------------------GLNTLFVALMDHPGFKDLDFSALKLT---------NSGGTALVKATAERWEQLtGCTI 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 375 VAGYGLTEsTATVACENDYDHV--VGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTED 442
Cdd:PRK12492 362 VEGYGLTE-TSPVASTNPYGELarLGTVGIPVPGTALKVidddgnelplGERGELCIKGPQVMKGYWQQPEATAEALDAE 440
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2786809754 443 GWFHTGDAGYI-KDEHLFLTERIKDLFKTSnGKYIAPQAIE 482
Cdd:PRK12492 441 GWFKTGDIAVIdPDGFVRIVDRKKDLIIVS-GFNVYPNEIE 480
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
14-497 |
3.67e-20 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 93.98 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 14 ARKYGDRVVLRYRDYKTETWiPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYAT 93
Cdd:PRK08008 17 ADVYGHKTALIFESSGGVVR-RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 94 SSEAQVHYMVGDAEIRYIFVGEQLqYDVAFRVMQLGSQLKRIIIFDREVkrDERDQTSIYFDDFLKLgeghpHQAEVDKR 173
Cdd:PRK08008 96 LLREESAWILQNSQASLLVTSAQF-YPMYRQIQQEDATPLRHICLTRVA--LPADDGVSSFTQLKAQ-----QPATLCYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 174 ISESGNgDLANILYTSGTTGDSKGVMLHHscyeaaipaHNERFP--------QLGDQDVIMNFLPFTHVferawTCWC-- 243
Cdd:PRK08008 168 PPLSTD-DTAEILFTSGTTSRPKGVVITH---------YNLRFAgyysawqcALRDDDVYLTVMPAFHI-----DCQCta 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 244 ----LSMGCTLSInlrpadIQKTikeirptamcSVPRFWEKV--Y-AGVQEKInetTGLKKKLMLDAIKVG-REHNLEYV 315
Cdd:PRK08008 233 amaaFSAGATFVL------LEKY----------SARAFWGQVckYrATITECI---PMMIRTLMVQPPSANdRQHCLREV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 316 YkgltpppvlhmkykFYektiysllkktigiengrffptagaaIPPAVQE---FVLSVGINMVAGYGLTEStatvacend 392
Cdd:PRK08008 294 M--------------FY--------------------------LNLSDQEkdaFEERFGVRLLTSYGMTET--------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 393 ydhVVG-------------SVGRLMPHVQVKI----------GENNEIMLRGE---GITHGYYKKEAATKAAFTEDGWFH 446
Cdd:PRK08008 325 ---IVGiigdrpgdkrrwpSIGRPGFCYEAEIrddhnrplpaGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEADGWLH 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2786809754 447 TGDAGYIKDEHLF-LTERIKDLFKTSnGKYIAPQAIEAKLVVDRYIDQISII 497
Cdd:PRK08008 402 TGDTGYVDEEGFFyFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVV 452
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
179-482 |
4.33e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 93.97 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 179 NGDLANILYTSGTTGDSKGVMLHHS--------CYEAAIPAHNERfpqlgdQDVIMNFLPFTHVFerawtcwCLSMGCTL 250
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRnmlanleqAKAAYGPLLHPG------KELVVTALPLYHIF-------ALTVNCLL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 251 SINL--------RPADIQKTIKEIRP---TAMcsvprfwekvyAGVQEKINETTglkkklmldaikvgreHNLEYvykgl 319
Cdd:PRK08974 272 FIELggqnllitNPRDIPGFVKELKKypfTAI-----------TGVNTLFNALL----------------NNEEF----- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 320 tpppvlhmkykfyEKTIYSLLKKTIGiengrffptAGAAIPPAVQE-FVLSVGINMVAGYGLTESTATVA-CENDYDHVV 397
Cdd:PRK08974 320 -------------QELDFSSLKLSVG---------GGMAVQQAVAErWVKLTGQYLLEGYGLTECSPLVSvNPYDLDYYS 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 398 GSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATkAAFTEDGWFHTGDAGYIKDEH-LFLTERIKD 466
Cdd:PRK08974 378 GSIGLPVPSTEIKLvdddgnevppGEPGELWVKGPQVMLGYWQRPEAT-DEVIKDGWLATGDIAVMDEEGfLRIVDRKKD 456
|
330
....*....|....*.
gi 2786809754 467 LFKTSnGKYIAPQAIE 482
Cdd:PRK08974 457 MILVS-GFNVYPNEIE 471
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
180-485 |
8.12e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 92.21 E-value: 8.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 180 GDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFT---HVFErawTCWCLSMGCTLSI---- 252
Cdd:cd05930 93 DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP-LTPGDRVLQFTSFSfdvSVWE---IFGALLAGATLVVlpee 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 253 -NLRPADIQKTIKEIRPTAMCSVPRFWekvyagvqekinettglkkKLMLDAIKVGREHNLEYVYkgltpppvlhmkykf 331
Cdd:cd05930 169 vRKDPEALADLLAEEGITVLHLTPSLL-------------------RLLLQELELAALPSLRLVL--------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 332 yektiysllkktigiengrffpTAGAAIPPAVQEFVLSVGINMVA--GYGLTESTATVAC-----ENDYDHVVgSVGRLM 404
Cdd:cd05930 215 ----------------------VGGEALPPDLVRRWRELLPGARLvnLYGPTEATVDATYyrvppDDEEDGRV-PIGRPI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 405 PHVQ----------VKIGENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFH------TGDAGYIK-DEHLFLTERIKDL 467
Cdd:cd05930 272 PNTRvyvldenlrpVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPgermyrTGDLVRWLpDGNLEFLGRIDDQ 351
|
330
....*....|....*...
gi 2786809754 468 FKTsNGKYIAPQAIEAKL 485
Cdd:cd05930 352 VKI-RGYRIELGEIEAAL 368
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
180-485 |
9.44e-20 |
|
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: 91.00 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 180 GDLANILYTSGTTGDSKGVMLHHS--CYEAAIPAHNERFpqlGDQDVIMNFLPFTHVFERAWTCWC-LSMGCTLSInLRP 256
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSneVYNAWMLALNSLF---DPDDVLLCGLPLFHVNGSVVTLLTpLASGAHVVL-AGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 257 A---------DIQKTIKEIRPTAMCSVPRfwekvyagvqekinettglkkklmldaikvgrehnleyVYKGLTPPPVlhm 327
Cdd:cd05944 78 AgyrnpglfdNFWKLVERYRITSLSTVPT--------------------------------------VYAALLQVPV--- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 328 kykfyEKTIYSLlkktigiengRFFPTAGAAIPPAV-QEFVLSVGINMVAGYGLTESTATVACE-NDYDHVVGSVGRLMP 405
Cdd:cd05944 117 -----NADISSL----------RFAMSGAAPLPVELrARFEDATGLPVVEGYGLTEATCLVAVNpPDGPKRPGSVGLRLP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 406 HVQVKI---------------GENNEIMLRGEGITHGYYKKEAAtKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFk 469
Cdd:cd05944 182 YARVRIkvldgvgrllrdcapDEVGEICVAGPGVFGGYLYTEGN-KNAFVADGWLNTGDLGRLdADGYLFITGRAKDLI- 259
|
330
....*....|....*.
gi 2786809754 470 TSNGKYIAPQAIEAKL 485
Cdd:cd05944 260 IRGGHNIDPALIEEAL 275
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
178-502 |
2.26e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 91.83 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 178 GNGDLANILYTSGTTGDSKGVMLHH----SCYEAAIPAHNERFPQLGDQDVIMNFLPFTHVFERA-WTCWCLSMGCTLSI 252
Cdd:PLN02574 196 KQDDVAAIMYSSGTTGASKGVVLTHrnliAMVELFVRFEASQYEYPGSDNVYLAALPMFHIYGLSlFVVGLLSLGSTIVV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 253 NLR--PADIQKTIKEIRPTAMCSVPrfwekvyagvqekinettglkkKLMLDAIKVGRehnleyvykgltppPVLHMKYK 330
Cdd:PLN02574 276 MRRfdASDMVKVIDRFKVTHFPVVP----------------------PILMALTKKAK--------------GVCGEVLK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 331 fyektiySLLKKTIGIEngrffPTAGAAIppavQEFVLSVG-INMVAGYGLTESTA--TVACENDYDHVVGSVGRLMPHV 407
Cdd:PLN02574 320 -------SLKQVSCGAA-----PLSGKFI----QDFVQTLPhVDFIQGYGMTESTAvgTRGFNTEKLSKYSSVGLLAPNM 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 408 QVKI-----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFKTsNGKY 475
Cdd:PLN02574 384 QAKVvdwstgcllppGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFdEDGYLYIVDRLKEIIKY-KGFQ 462
|
330 340
....*....|....*....|....*..
gi 2786809754 476 IAPQAIEAKLVVDRYIDQISIIADERK 502
Cdd:PLN02574 463 IAPADLEAVLISHPEIIDAAVTAVPDK 489
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
9-544 |
3.11e-19 |
|
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: 91.40 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDYKTETWIpVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:cd05970 22 VVDAMAKEYPDKLALVWCDDAGEERI-FTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFV--GEQLQYDVAFRVMQLGSQLKRIIIFDrevkrDERDQtsiyFDDFLKLGEGHPH 166
Cdd:cd05970 101 PATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGD-----PVPEG----WIDFRKLIKNASP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 167 QAEVDKRISESGNGDLANILYTSGTTGDSKGVmlhhscyeaaipAHNERFPqLGdqdvimnflpftHVFE-RAWTcwcls 245
Cdd:cd05970 172 DFERPTANSYPCGEDILLVYFSSGTTGMPKMV------------EHDFTYP-LG------------HIVTaKYWQ----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 246 mgctlsiNLRPADIQKTIKEIR-PTAMcsvprfWEKVY----AGVQEKINETTGLKKKLMLDAIKvgrehnlEYVYKGLT 320
Cdd:cd05970 222 -------NVREGGLHLTVADTGwGKAV------WGKIYgqwiAGAAVFVYDYDKFDPKALLEKLS-------KYGVTTFC 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 321 PPPVLhmkYKFYEK---TIYSLLKKtigiengRFFPTAGAAIPPAVQE-FVLSVGINMVAGYGLTESTATVACENDYDHV 396
Cdd:cd05970 282 APPTI---YRFLIRedlSRYDLSSL-------RYCTTAGEALNPEVFNtFKEKTGIKLMEGFGQTETTLTIATFPWMEPK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 397 VGSVGRLMPHVQV----------KIGENNEIMLRGE-----GITHGYYKKEAATKAAFtEDGWFHTGDAGYI-KDEHLFL 460
Cdd:cd05970 352 PGSMGKPAPGYEIdlidregrscEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMdEDGYLWF 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 461 TERIKDLFKTSnGKYIAPQAIEAKLVVDRYIDQISI--IADERK--FVSALII------PEYKLVKEYADkkgiHYGSME 530
Cdd:cd05970 431 VGRTDDLIKSS-GYRIGPFEVESALIQHPAVLECAVtgVPDPIRgqVVKATIVlakgyePSEELKKELQD----HVKKVT 505
|
570
....*....|....
gi 2786809754 531 DLLRKPEIIELFKE 544
Cdd:cd05970 506 APYKYPRIVEFVDE 519
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
181-482 |
1.87e-18 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 86.93 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGDQDVIMNFLPFTHVFERAWTCWCLSMGCTLSI---NLRPA 257
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTggeNTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 258 DIQKTIKEIRPTAMCSVPRFWEKVyagvqekINETTglkkklmlDAIKVGREHNLeyvykgltpppvlhmkykfyektiy 337
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKL-------VSELK--------SANATVPSLRL------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 338 sllkktigIENGRFFPtagaaIPPAVQEFVLSVGINMVAGYGLTESTATVACENDYDHV-VGSVGRLMPHVQVKI----- 411
Cdd:cd17635 122 --------IGYGGSRA-----IAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLaatdg 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786809754 412 -----GENNEIMLRGEGITHGYYKKEAATKAAFTeDGWFHTGDAGYI-KDEHLFLTERIKDLFkTSNGKYIAPQAIE 482
Cdd:cd17635 189 iagpsASFGTIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERrEDGFLFITGRSSESI-NCGGVKIAPDEVE 263
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
9-482 |
2.02e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 88.50 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDyktetwIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:PRK06188 17 LLVSALKRYPDRPALVLGD------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVGeqlqyDVAF--RVMQLGSQ---LKRIIIFDRevkrderdqtSIYFDDFLKLGEG 163
Cdd:PRK06188 91 ALHPLGSLDDHAYVLEDAGISTLIVD-----PAPFveRALALLARvpsLKHVLTLGP----------VPDGVDLLAAAAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 164 HPHQAEVDkrisESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAhnerfpQLGDQDVIMN--FL---PFTHVfERA 238
Cdd:PRK06188 156 FGPAPLVA----AALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQI------QLAEWEWPADprFLmctPLSHA-GGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 239 WTCWCLSMGCTLsINLR---PADIQKTIKEIRPTAMCSVPRFwekVYAgvqekinettglkkklMLDAIKVgREHN---L 312
Cdd:PRK06188 225 FFLPTLLRGGTV-IVLAkfdPAEVLRAIEEQRITATFLVPTM---IYA----------------LLDHPDL-RTRDlssL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 313 EYVYKGltpppvlhmkykfyektiysllkktigiengrffptaGAAIPPA-VQEFVLSVGINMVAGYGLTE--STATVAC 389
Cdd:PRK06188 284 ETVYYG-------------------------------------ASPMSPVrLAEAIERFGPIFAQYYGQTEapMVITYLR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 390 ENDYD----HVVGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYiKD 455
Cdd:PRK06188 327 KRDHDpddpKRLTSCGRPTPGLRVALldedgrevaqGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAR-ED 404
|
490 500
....*....|....*....|....*....
gi 2786809754 456 EH--LFLTERIKDLFkTSNGKYIAPQAIE 482
Cdd:PRK06188 405 EDgfYYIVDRKKDMI-VTGGFNVFPREVE 432
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
36-501 |
5.16e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 87.42 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 36 VSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGE 115
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 116 QLQ-YDVAFRVMQLGS---QLKRIIIFDREvkrderDQTSiyFDDFL--KLGEGHPHQAEVDKRiSESGNGDLANILYTS 189
Cdd:PRK13295 136 TFRgFDHAAMARRLRPelpALRHVVVVGGD------GADS--FEALLitPAWEQEPDAPAILAR-LRPGPDDVTQLIYTS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 190 GTTGDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFTHVFERAWtcwclsmGCTLSINLRPADIQKTIKEirPT 269
Cdd:PRK13295 207 GTTGEPKGVMHTANTLMANIVPYAERL-GLGADDVILMASPMAHQTGFMY-------GLMMPVMLGATAVLQDIWD--PA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 270 AMCSVPRfwekvyagvQEKINETTGLKKKL--MLDAIKvgrehnleyvykgLTPPPVlhmkykfyektiySLLKKtigie 347
Cdd:PRK13295 277 RAAELIR---------TEGVTFTMASTPFLtdLTRAVK-------------ESGRPV-------------SSLRT----- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 348 ngrfFPTAGAAIPPAVQEFVLSV-GINMVAGYGLTESTA-TVACENDYDHVVG-SVGRLMPHVQVKI----------GEN 414
Cdd:PRK13295 317 ----FLCAGAPIPGALVERARAAlGAKIVSAWGMTENGAvTLTKLDDPDERAStTDGCPLPGVEVRVvdadgaplpaGQI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 415 NEIMLRGEGITHGYYKKEAATKAAFteDGWFHTGDAGYIKDE-HLFLTERIKDLFkTSNGKYIAPQAIEAKLVVDRYIDQ 493
Cdd:PRK13295 393 GRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLARIDADgYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQ 469
|
490
....*....|
gi 2786809754 494 ISIIA--DER 501
Cdd:PRK13295 470 VAIVAypDER 479
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
12-483 |
5.47e-18 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 87.29 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 12 RQARKYGDRVVLRYRDYKTETWIPVSWNQFAATVKTVSNALIELGiGIQENIAVFSQNKPEclYVD--FGAFGVRAVTVP 89
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLD--FVAafLGCLYAGAIAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 90 FYA---TSSEAQVHYMVGDAEIRYIFVGEQLQYDVAFRVMQLGSQLKRIIIFDREVKRDERDQTSIyfddflklgeghPH 166
Cdd:cd05931 78 LPPptpGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPP------------PS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 167 QAEvdkrisesgnGDLANILYTSGTTGDSKGVMLHHscyeAAIpAHNER-----FpQLGDQDVIMNFLPFTH----VFer 237
Cdd:cd05931 146 PDP----------DDIAYLQYTSGSTGTPKGVVVTH----RNL-LANVRqirraY-GLDPGDVVVSWLPLYHdmglIG-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 238 awtCWCLSM--GCTLSInLRPAD-IQ------KTIKEIRPTAMcSVPRFwekVYAGVQEKINEttglKKKLMLDAikvgr 308
Cdd:cd05931 208 ---GLLTPLysGGPSVL-MSPAAfLRrplrwlRLISRYRATIS-AAPNF---AYDLCVRRVRD----EDLEGLDL----- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 309 eHNLEYVYKGLTP--PPVLHmkyKFYEktiysllkktigiengRFfptAGAAIPPAVqefvlsvginMVAGYGLTESTAT 386
Cdd:cd05931 271 -SSWRVALNGAEPvrPATLR---RFAE----------------AF---APFGFRPEA----------FRPSYGLAEATLF 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 387 VAC----------------------------ENDYDHVvgSVGRLMPHVQVKI-----------GENNEIMLRGEGITHG 427
Cdd:cd05931 318 VSGgppgtgpvvlrvdrdalagravavaaddPAARELV--SCGRPLPDQEVRIvdpetgrelpdGEVGEIWVRGPSVASG 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786809754 428 YYKKEAATKAAF------TEDGWFHTGDAGYIKDEHLFLTERIKDLFkTSNGKYIAPQAIEA 483
Cdd:cd05931 396 YWGRPEATAETFgalaatDEGGWLRTGDLGFLHDGELYITGRLKDLI-IVRGRNHYPQDIEA 456
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
56-485 |
6.72e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 86.78 E-value: 6.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 56 GIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIfVGEQlqydvafrvmqlGSQLKRI 135
Cdd:PRK09088 43 GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL-LGDD------------AVAAGRT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 136 IIFDREVKRDERDQtsiyfddfLKLGEGHPHQAEvdkRISEsgngdlanILYTSGTTGDSKGVMLHHSCYEAAipAHNer 215
Cdd:PRK09088 110 DVEDLAAFIASADA--------LEPADTPSIPPE---RVSL--------ILFTSGTSGQPKGVMLSERNLQQT--AHN-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 216 FPQLGDQDVIMNFL---PFTHVFerawtcwclsmgcTLSINLRPADIQKTIKEI-------RPTAMCSVPRFWEKVYAGV 285
Cdd:PRK09088 167 FGVLGRVDAHSSFLcdaPMFHII-------------GLITSVRPVLAVGGSILVsngfepkRTLGRLGDPALGITHYFCV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 286 QEkinettglkkklMLDAIkvgREHnleyvyKGLTPPPVLHMKYKFyektiysllkktigiengrffpTAGAAIPPAVQE 365
Cdd:PRK09088 234 PQ------------MAQAF---RAQ------PGFDAAALRHLTALF----------------------TGGAPHAAEDIL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 366 FVLSVGINMVAGYGLTESTATVACENDYDHV---VGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKE 432
Cdd:PRK09088 271 GWLDDGIPMVDGFGMSEAGTVFGMSVDCDVIrakAGAAGIPTPTVQTRVvddqgndcpaGVPGELLLRGPNLSPGYWRRP 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2786809754 433 AATKAAFTEDGWFHTGD-AGYIKDEHLFLTERIKDLFkTSNGKYIAPQAIEAKL 485
Cdd:PRK09088 351 QATARAFTGDGWFRTGDiARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVL 403
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
145-482 |
8.31e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 86.85 E-value: 8.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 145 DERDQTSIYFDDFLKLGEGH---PHQAEVDkrisesgngDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGD 221
Cdd:PRK08751 179 EYRINGAIRFREALALGRKHsmpTLQIEPD---------DIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 222 ----QDVIMNFLPFTHVFerAWTCWCLSM----GCTLSINlRPADIQKTIKEIRPTamcsvpRFweKVYAGVQEKINett 293
Cdd:PRK08751 250 leegCEVVITALPLYHIF--ALTANGLVFmkigGCNHLIS-NPRDMPGFVKELKKT------RF--TAFTGVNTLFN--- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 294 glkkklmldaikvgrehnleyvykGLTPPPvlhmkykFYEKTIYSLLKKTIGiengrffptAGAAIPPAVQEFVLSV-GI 372
Cdd:PRK08751 316 ------------------------GLLNTP-------GFDQIDFSSLKMTLG---------GGMAVQRSVAERWKQVtGL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 373 NMVAGYGLTEsTATVACEN--DYDHVVGSVGRLMPHVQV----------KIGENNEIMLRGEGITHGYYKKEAATKAAFT 440
Cdd:PRK08751 356 TLVEAYGLTE-TSPAACINplTLKEYNGSIGLPIPSTDAcikddagtvlAIGEIGELCIKGPQVMKGYWKRPEETAKVMD 434
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2786809754 441 EDGWFHTGDAGYIKDE-HLFLTERIKDLFKTSnGKYIAPQAIE 482
Cdd:PRK08751 435 ADGWLHTGDIARMDEQgFVYIVDRKKDMILVS-GFNVYPNEIE 476
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
5-486 |
1.20e-17 |
|
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: 86.27 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 5 FLSVLIQRQARKYGDRVVLrYRDYKTetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVR 84
Cdd:cd05959 5 AATLVDLNLNEGRGDKTAF-IDDAGS-----LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 85 AVTVPFYATSSEAQVHYMVGDAEIRYIFVGEQLqYDVAFRVMQLGSQLKRIIIfdreVKRDERDQtsiyfDDFLKLGEGH 164
Cdd:cd05959 79 IVPVPVNTLLTPDDYAYYLEDSRARVVVVSGEL-APVLAAALTKSEHTLVVLI----VSGGAGPE-----AGALLLAELV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 165 PHQAEVDKRISESGNgDLANILYTSGTTGDSKGVM-LHHSCYEAAIpAHNERFPQLGDQDVIMNF--LPFTHVFERAWTC 241
Cdd:cd05959 149 AAEAEQLKPAATHAD-DPAFWLYSSGSTGRPKGVVhLHADIYWTAE-LYARNVLGIREDDVCFSAakLFFAYGLGNSLTF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 242 wCLSMGCT---LSINLRPADIQKTIKEIRPTAMCSVPRFwekvyagvqekinettglkkklmldaikvgrehnleyvYKG 318
Cdd:cd05959 227 -PLSVGATtvlMPERPTPAAVFKRIRRYRPTVFFGVPTL--------------------------------------YAA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 319 LTPPPVLhmkykfyEKTIYSLLkktigiengRFFPTAGAAIPPAV-QEFVLSVGINMVAGYGLTEsTATVACENDYDHV- 396
Cdd:cd05959 268 MLAAPNL-------PSRDLSSL---------RLCVSAGEALPAEVgERWKARFGLDILDGIGSTE-MLHIFLSNRPGRVr 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 397 VGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAgYIKDEHLFLT--ERI 464
Cdd:cd05959 331 YGTTGKPVPGYEVELrdedggdvadGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDK-YVRDDDGFYTyaGRA 408
|
490 500
....*....|....*....|..
gi 2786809754 465 KDLFKTSnGKYIAPQAIEAKLV 486
Cdd:cd05959 409 DDMLKVS-GIWVSPFEVESALV 429
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1-508 |
1.35e-17 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 86.08 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 1 MSSSFLSVLIQRQARKygDRVVLRYRDykTETWipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGA 80
Cdd:PRK07514 1 MNNNLFDALRAAFADR--DAPFIETPD--GLRY---TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 81 FGVRAVTVPFYATSSEAQVHYMVGDAEIRyIFVGEQLQYD----VAFR-----VMQLGsqlkriiifdrevkrDERDQTs 151
Cdd:PRK07514 74 LRAGAVFLPLNTAYTLAELDYFIGDAEPA-LVVCDPANFAwlskIAAAagaphVETLD---------------ADGTGS- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 152 iyfddFLKLGEGHPHQAEVDKRisesGNGDLANILYTSGTTGDSKGVMLHHS-CYEAAIPAHNE-RFpqlGDQDVIMNFL 229
Cdd:PRK07514 137 -----LLEAAAAAPDDFETVPR----GADDLAAILYTSGTTGRSKGAMLSHGnLLSNALTLVDYwRF---TPDDVLIHAL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 230 PFTHV---FerawtcwcLSMGCTL----SINLRPA-DIQKTIKEI-RPTAMCSVPRFWEKvyagvqekinettglkkklM 300
Cdd:PRK07514 205 PIFHThglF--------VATNVALlagaSMIFLPKfDPDAVLALMpRATVMMGVPTFYTR-------------------L 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 301 LDAikvgrehnleyvyKGLTPPPVLHMkykfyektiysllkktigiengRFFpTAGAA--IPPAVQEFVLSVGINMVAGY 378
Cdd:PRK07514 258 LQE-------------PRLTREAAAHM----------------------RLF-ISGSAplLAETHREFQERTGHAILERY 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 379 GLTESTATVAceNDYD--HVVGSVGRLMPHVQVKI-----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWF 445
Cdd:PRK07514 302 GMTETNMNTS--NPYDgeRRAGTVGFPLPGVSLRVtdpetgaelppGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFF 379
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786809754 446 HTGDAGYIKDE-HLFLTERIKDLFkTSNGKYIAPQAIEAklvvdrYIDQISIIADerkfvSALI 508
Cdd:PRK07514 380 ITGDLGKIDERgYVHIVGRGKDLI-ISGGYNVYPKEVEG------EIDELPGVVE-----SAVI 431
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
151-482 |
1.69e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 85.97 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 151 SIYFDDFLKLGEGHPHQaEVDkriseSGNGDLANILYTSGTTGDSKGVMLHHSCYEA------AIPAHNerfpqLGD-QD 223
Cdd:PRK05677 184 AVKFNDALAKGAGQPVT-EAN-----PQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlqcrALMGSN-----LNEgCE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 224 VIMNFLPFTHVFerAWTCWCLSMGCTLSINL---RPADIQKTIKEIRPTamcsvpRFwekvyagvqekinetTGLkkkLM 300
Cdd:PRK05677 253 ILIAPLPLYHIY--AFTFHCMAMMLIGNHNIlisNPRDLPAMVKELGKW------KF---------------SGF---VG 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 301 LDAIKVGREHNLEYvykgltpppvlhmkykfyEKTIYSLLKKTIgiengrffpTAGAAIPPAVQEFVLSV-GINMVAGYG 379
Cdd:PRK05677 307 LNTLFVALCNNEAF------------------RKLDFSALKLTL---------SGGMALQLATAERWKEVtGCAICEGYG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 380 LTEsTATVACENDYDHV-VGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTG 448
Cdd:PRK05677 360 MTE-TSPVVSVNPSQAIqVGTIGIPVPSTLCKVidddgnelplGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTG 438
|
330 340 350
....*....|....*....|....*....|....*
gi 2786809754 449 DAGYIK-DEHLFLTERIKDLFKTSnGKYIAPQAIE 482
Cdd:PRK05677 439 DIALIQeDGYMRIVDRKKDMILVS-GFNVYPNELE 472
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
181-461 |
2.79e-17 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 86.13 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTHVFERAWTCW---CLSMGCTLSINlrPA 257
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFN-LRNDDVILSSLPFFHSFGLTVTLWlplLEGIKVVYHPD--PT 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 258 D---IQKTIKEIRPTAMCSVPRFWeKVYAGVQeKInettglkKKLMLDaikvgrehNLEYVYKGLtpppvlhmkykfyEK 334
Cdd:PRK08633 860 DalgIAKLVAKHRATILLGTPTFL-RLYLRNK-KL-------HPLMFA--------SLRLVVAGA-------------EK 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 335 tiyslLKKTIGIEngrffptagaaippavqeFVLSVGINMVAGYGLTESTATVAC------ENDY----DHVVGSVGRLM 404
Cdd:PRK08633 910 -----LKPEVADA------------------FEEKFGIRILEGYGATETSPVASVnlpdvlAADFkrqtGSKEGSVGMPL 966
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2786809754 405 PHVQVKI-----------GENNEIMLRGEGITHGYYKKEAATKAAFTE---DGWFHTGDAGYIkDEHLFLT 461
Cdd:PRK08633 967 PGVAVRIvdpetfeelppGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGHL-DEDGFLT 1036
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
181-497 |
3.30e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 85.03 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCYEAAIPAhnERF---PQLGDQDVIMNFLPFTHVFERAWTCwclsmgctlsinlrpa 257
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANLCS--SLFsvgPEMIGQVVTLGLIPFFHIYGITGIC---------------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 258 diqktikeirptamCSVPRFWEKVYAgvqekineTTGLKKKLMLDAIKVGrehnlEYVYKGLTPPPVLHM-KYKFYEKTI 336
Cdd:PLN02330 247 --------------CATLRNKGKVVV--------MSRFELRTFLNALITQ-----EVSFAPIVPPIILNLvKNPIVEEFD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 337 YSLLKKtigiengRFFPTAGAAIPPAV-----QEFVlsvGINMVAGYGLTESTATVACENDYDHVVG-----SVGRLMPH 406
Cdd:PLN02330 300 LSKLKL-------QAIMTAAAPLAPELltafeAKFP---GVQVQEAYGLTEHSCITLTHGDPEKGHGiakknSVGFILPN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 407 VQVK---------IGENN--EIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE-HLFLTERIKDLFKTsNGK 474
Cdd:PLN02330 370 LEVKfidpdtgrsLPKNTpgELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDgDIFIVDRIKELIKY-KGF 448
|
330 340
....*....|....*....|...
gi 2786809754 475 YIAPQAIEAKLVVDRYIDQISII 497
Cdd:PLN02330 449 QVAPAELEAILLTHPSVEDAAVV 471
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
182-482 |
1.21e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 82.92 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 182 LANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFTHvferawtcwclSMGcTLSINLRPAdIQK 261
Cdd:cd05908 108 LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST-EWKTKDRILSWMPLTH-----------DMG-LIAFHLAPL-IAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 262 TIKEIRPTAMCSV-PRFWekVYAGVQEKINETT--GLKKKLMLDAIKVGREHN-----LEYVYKGLTP--PPVLHM---- 327
Cdd:cd05908 174 MNQYLMPTRLFIRrPILW--LKKASEHKATIVSspNFGYKYFLKTLKPEKANDwdlssIRMILNGAEPidYELCHEfldh 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 328 --KYKFYEKTIYSLLkktigienGRFFPTAGAAIPPAVQEFVLSVGINmvAGYGLTESTATVACENDYDHVVGSVGRLMP 405
Cdd:cd05908 252 msKYGLKRNAILPVY--------GLAEASVGASLPKAQSPFKTITLGR--RHVTHGEPEPEVDKKDSECLTFVEVGKPID 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 406 HVQVKI-GENNEIM---------LRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDEHLFLTERIKDLFKTsNGKY 475
Cdd:cd05908 322 ETDIRIcDEDNKILpdgyighiqIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRNGRLVITGREKDIIFV-NGQN 400
|
....*..
gi 2786809754 476 IAPQAIE 482
Cdd:cd05908 401 VYPHDIE 407
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
178-482 |
2.20e-16 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 82.38 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 178 GNGDLANILYTSGTTGDSKGVMLHHSCYEAAI--------PAHNERfPQLgDQDVIMNFLPFTHVFerAWT-CWCLSM-- 246
Cdd:PRK07059 202 GPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEKK-PRP-DQLNFVCALPLYHIF--ALTvCGLLGMrt 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 247 -GCTLSINlRPADIQKTIKEIRPTAMCSVPrfwekvyagvqekinettglkkklmldaikvgrehNLEYVYKGLtpppvl 325
Cdd:PRK07059 278 gGRNILIP-NPRDIPGFIKELKKYQVHIFP-----------------------------------AVNTLYNAL------ 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 326 hMKYKFYEKTIYSLLKKTIGiengrffptAGAAIPPAVQEFVLSV-GINMVAGYGLTEsTATVACEN--DYDHVVGSVGR 402
Cdd:PRK07059 316 -LNNPDFDKLDFSKLIVANG---------GGMAVQRPVAERWLEMtGCPITEGYGLSE-TSPVATCNpvDATEFSGTIGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 403 LMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIkDEHLF--LTERIKDLFKT 470
Cdd:PRK07059 385 PLPSTEVSIrdddgndlplGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVM-DERGYtkIVDRKKDMILV 463
|
330
....*....|..
gi 2786809754 471 SnGKYIAPQAIE 482
Cdd:PRK07059 464 S-GFNVYPNEIE 474
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
44-486 |
2.84e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 81.95 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 44 TVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV---PFYaTSSEAQVHYMVGDAEI-----RYIFVGE 115
Cdd:PLN02246 59 LSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTtanPFY-TPAEIAKQAKASGAKLiitqsCYVDKLK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 116 QLQYDVAFRVMQLgsqlkriiifdrevkrDERDQTSIYFDDFLKLGEGHPHQAEVDKRisesgngDLANILYTSGTTGDS 195
Cdd:PLN02246 138 GLAEDDGVTVVTI----------------DDPPEGCLHFSELTQADENELPEVEISPD-------DVVALPYSSGTTGLP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 196 KGVMLHH----SCYEAAIPAHNERFpQLGDQDVIMNFLPFTHVFerawtcwclSMGCTLSINLRPAdiqktikeirpTAM 271
Cdd:PLN02246 195 KGVMLTHkglvTSVAQQVDGENPNL-YFHSDDVILCVLPMFHIY---------SLNSVLLCGLRVG-----------AAI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 272 CSVPRFwekvyagvqekinETTglkkkLMLDAIkvgREHNLEYVykGLTPPPVLHM-KYKFYEKTIYSLLK------KTI 344
Cdd:PLN02246 254 LIMPKF-------------EIG-----ALLELI---QRHKVTIA--PFVPPIVLAIaKSPVVEKYDLSSIRmvlsgaAPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 345 GIENGRFFptaGAAIPPAVqefvlsvginMVAGYGLTESTATVA-C----ENDYDHVVGSVGRLMPHVQVKI-------- 411
Cdd:PLN02246 311 GKELEDAF---RAKLPNAV----------LGQGYGMTEAGPVLAmClafaKEPFPVKSGSCGTVVRNAELKIvdpetgas 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786809754 412 -GEN--NEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFKTsNGKYIAPQAIEAKLV 486
Cdd:PLN02246 378 lPRNqpGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIdDDDELFIVDRLKELIKY-KGFQVAPAELEALLI 455
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1-482 |
5.94e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 80.91 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 1 MSSSFL-SVLIQRQARKYGD------RV---VLRYrdyktetwipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNK 70
Cdd:PRK07008 6 MDMPLLiSSLIAHAARHAGDteivsrRVegdIHRY-----------TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 71 PECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFvgeqlqYDVAFR--VMQLGSQLKRIIIFDREVKRDERD 148
Cdd:PRK07008 75 YRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVL------FDLTFLplVDALAPQCPNVKGWVAMTDAAHLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 149 QTSIYFDDFLKLGEGHPHQAE---VDKRISESgngdlanILYTSGTTGDSKGVMLHHS-----CYEAAIP-AHNerfpqL 219
Cdd:PRK07008 149 AGSTPLLCYETLVGAQDGDYDwprFDENQASS-------LCYTSGTTGNPKGALYSHRstvlhAYGAALPdAMG-----L 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 220 GDQDVIMNFLPFTHVfeRAWTC--WCLSMGCTLSI---NLRPADIQKTIKEIRPTAMCSVPRFWEKVYAGVQEkinetTG 294
Cdd:PRK07008 217 SARDAVLPVVPMFHV--NAWGLpySAPLTGAKLVLpgpDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMRE-----AG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 295 LKkklmldaikvgrehnleyvykgltpppvlhmkykfyektiYSLLKKTIgiengrffpTAGAAIPPA-VQEFVLSVGIN 373
Cdd:PRK07008 290 LR----------------------------------------FSTLRRTV---------IGGSACPPAmIRTFEDEYGVE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 374 MVAGYGLTE-STATVACENDYDH-------------------------VVGSVGRLMPHVQVKIGEnneIMLRGEGITHG 427
Cdd:PRK07008 321 VIHAWGMTEmSPLGTLCKLKWKHsqlpldeqrkllekqgrviygvdmkIVGDDGRELPWDGKAFGD---LQVRGPWVIDR 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2786809754 428 YYKKEAATkaafTEDGWFHTGDAGYI-KDEHLFLTERIKDLFKtSNGKYIAPQAIE 482
Cdd:PRK07008 398 YFRGDASP----LVDGWFPTGDVATIdADGFMQITDRSKDVIK-SGGEWISSIDIE 448
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
9-482 |
1.27e-15 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 79.80 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDR-VVLRyrdyKTETWIP-VSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAV 86
Cdd:PRK06018 15 IIDHAARIHGNReVVTR----SVEGPIVrTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 87 TVPFYATSSEAQVHYMVGDAEIRYIFVgeqlqyDVAFR--VMQLGSQL---KRIIIF-DREVKRDERDQTSIYFDDFLKL 160
Cdd:PRK06018 91 CHTVNPRLFPEQIAWIINHAEDRVVIT------DLTFVpiLEKIADKLpsvERYVVLtDAAHMPQTTLKNAVAYEEWIAE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 161 GEGHPHQAEVDKRISesgngdlANILYTSGTTGDSKGVML-HHSCYEAAIPAHNERFPQLGDQDVIMNFLPFTHVfeRAW 239
Cdd:PRK06018 165 ADGDFAWKTFDENTA-------AGMCYTSGTTGDPKGVLYsHRSNVLHALMANNGDALGTSAADTMLPVVPLFHA--NSW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 240 --TCWCLSMGCTLSI---NLRPADIQKTIKEIRPTAMCSVPRFWekvyagvqekinettglkkkLMLdaikvgrehnLEY 314
Cdd:PRK06018 236 giAFSAPSMGTKLVMpgaKLDGASVYELLDTEKVTFTAGVPTVW--------------------LML----------LQY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 315 VYK-GLTPPpvlHMKykfyektiysllKKTIGiengrffptaGAAIPPAVQEFVLSVGINMVAGYGLTESTAtvacendy 393
Cdd:PRK06018 286 MEKeGLKLP---HLK------------MVVCG----------GSAMPRSMIKAFEDMGVEVRHAWGMTEMSP-------- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 394 dhvVGSVGRLMPH----------------------VQVKI--GENNEI----------MLRGEGITHGYYKKEAATkaaF 439
Cdd:PRK06018 333 ---LGTLAALKPPfsklpgdarldvlqkqgyppfgVEMKItdDAGKELpwdgktfgrlKVRGPAVAAAYYRVDGEI---L 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2786809754 440 TEDGWFHTGDAGYIkDEHLFL--TERIKDLFKtSNGKYIAPQAIE 482
Cdd:PRK06018 407 DDDGFFDTGDVATI-DAYGYMriTDRSKDVIK-SGGEWISSIDLE 449
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
85-485 |
3.17e-15 |
|
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: 78.08 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 85 AVTVPFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAFRVmqlgsqlKRIIIFDrevkrderdqtsiyfDDFLKLGEGH 164
Cdd:TIGR01733 50 AAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGLV-------LPVILLD---------------PLELAALDDA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 165 PHQAEVDkriSESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTH---VFErawTC 241
Cdd:TIGR01733 108 PAPPPPD---APSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG-LDPDDRVLQFASLSFdasVEE---IF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 242 WCLSMGCTL------SINLRPADIQKTIKEIRPTAMCSVPRFWEkvyagvqekinettglkkklMLDAIKVGREHNLEYV 315
Cdd:TIGR01733 181 GALLAGATLvvppedEERDDAALLAALIAEHPVTVLNLTPSLLA--------------------LLAAALPPALASLRLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 316 YkgltpppvlhmkykfyektiysllkktigiengrffpTAGAAIPPAVQEFVLSV--GINMVAGYGLTEsTATVACENDY 393
Cdd:TIGR01733 241 I-------------------------------------LGGEALTPALVDRWRARgpGARLINLYGPTE-TTVWSTATLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 394 DHVVGS------VGRLMPHVQ----------VKIGENNEIMLRGEGITHGYYKKEAATKAAFTEDG--------WFHTGD 449
Cdd:TIGR01733 283 DPDDAPrespvpIGRPLANTRlyvldddlrpVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPfaggdgarLYRTGD 362
|
410 420 430
....*....|....*....|....*....|....*..
gi 2786809754 450 -AGYIKDEHLFLTERIKDLFKTsNGKYIAPQAIEAKL 485
Cdd:TIGR01733 363 lVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAAL 398
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
356-485 |
3.71e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 77.99 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 356 GAAIPPAVQEFVLSVGINMVAGYGLTESTATVaCENDYDHVVGsVGRLMPHVQVKIgENNEIMLRGEGITHGYYKKEAAT 435
Cdd:PRK09029 249 GAAIPVELTEQAEQQGIRCWCGYGLTEMASTV-CAKRADGLAG-VGSPLPGREVKL-VDGEIWLRGASLALGYWRQGQLV 325
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2786809754 436 KAAfTEDGWFHTGDAGYIKDEHLFLTERIKDLFkTSNGKYIAPQAIEAKL 485
Cdd:PRK09029 326 PLV-NDEGWFATRDRGEWQNGELTILGRLDNLF-FSGGEGIQPEEIERVI 373
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
181-455 |
1.21e-13 |
|
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: 73.44 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFT---HVFErAWTCWCLsmGCTLSINLR-- 255
Cdd:cd05945 98 DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFP-LGPGDVFLNQAPFSfdlSVMD-LYPALAS--GATLVPVPRda 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 256 ---PADIQKTIKEIRPTAMCSVPRFWEKVyagvqekinettglkkkLMLDAIKVGREHNLEYVYKGLTPPPVlhmkykfy 332
Cdd:cd05945 174 tadPKQLFRFLAEHGITVWVSTPSFAAMC-----------------LLSPTFTPESLPSLRHFLFCGEVLPH-------- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 333 eKTIYSLLKKtigiengrfFPtaGAAIppavqefvlsvgINmvaGYGLTEstATVACE---------NDYDHVvgSVGRL 403
Cdd:cd05945 229 -KTARALQQR---------FP--DARI------------YN---TYGPTE--ATVAVTyievtpevlDGYDRL--PIGYA 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786809754 404 MPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTED---GWFHTGDAGYIKD 455
Cdd:cd05945 278 KPGAKLVIldedgrpvppGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEA 342
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
181-544 |
1.88e-13 |
|
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: 72.75 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCYEAAIPahNERFPQ-LGDQDVIMNflpfthVFERAWTCWCLS-------MGCTlsi 252
Cdd:cd05972 82 DPALIYFTSGTTGLPKGVLHTHSYPLGHIP--TAAYWLgLRPDDIHWN------IADPGWAKGAWSsffgpwlLGAT--- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 253 nlrpadiqktikeirpTAMCSVPRFWEKVYAGVQEKINETTglkkklmldaikvgrehnleyvykgLTPPPvlhmkykfy 332
Cdd:cd05972 151 ----------------VFVYEGPRFDAERILELLERYGVTS-------------------------FCGPP--------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 333 ekTIYSLLKKtIGIENGRF-----FPTAGAAIPPAVQE-FVLSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPH 406
Cdd:cd05972 181 --TAYRMLIK-QDLSSYKFshlrlVVSAGEPLNPEVIEwWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 407 VQVKI----------GENNEIMLRGE--GITHGYYKKEAATKAAFTEDgWFHTGDAGYiKDE--HLFLTERIKDLFKTSn 472
Cdd:cd05972 258 YDVAIidddgrelppGEEGDIAIKLPppGLFLGYVGDPEKTEASIRGD-YYLTGDRAY-RDEdgYFWFVGRADDIIKSS- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 473 GKYIAPQAIEAKLVVDRYIDQISIIA---DER-KFVSALII------PEYKLVKEYADKKGIHYGSMEdllrKPEIIELF 542
Cdd:cd05972 335 GYRIGPFEVESALLEHPAVAEAAVVGspdPVRgEVVKAFVVltsgyePSEELAEELQGHVKKVLAPYK----YPREIEFV 410
|
..
gi 2786809754 543 KE 544
Cdd:cd05972 411 EE 412
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
356-501 |
2.61e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 71.61 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 356 GAAIPPAVQEFVLSVGINMVAGYGLTESTAtvACEndYDhvvgsvGRLMPHVQVKIgENNEIMLRGEGITHGYykKEAAT 435
Cdd:PRK07824 160 GGPAPAPVLDAAAAAGINVVRTYGMSETSG--GCV--YD------GVPLDGVRVRV-EDGRIALGGPTLAKGY--RNPVD 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786809754 436 KAAFTEDGWFHTGDAGYIKDEHLFLTERIKDLFKTSnGKYIAPQAIEAKLVVDRYIDQISI--IADER 501
Cdd:PRK07824 227 PDPFAEPGWFRTDDLGALDDGVLTVLGRADDAISTG-GLTVLPQVVEAALATHPAVADCAVfgLPDDR 293
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
37-498 |
5.68e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 71.59 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 37 SWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGEQ 116
Cdd:PLN03102 41 TWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 117 LQyDVAFRVMQL----GSQLKRIIIFDREVKRDERDQTS-IYFDDFLKLGEGHPHQAEVDKRISESGngDLANILYTSGT 191
Cdd:PLN03102 121 FE-PLAREVLHLlsseDSNLNLPVIFIHEIDFPKRPSSEeLDYECLIQRGEPTPSLVARMFRIQDEH--DPISLNYTSGT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 192 TGDSKGVML-HHSCYEAAIPAHNERfpQLGDQDVIMNFLPFTHVfeRAWT-CWCLSMGCTLSINLR---PADIQKTIKEI 266
Cdd:PLN03102 198 TADPKGVVIsHRGAYLSTLSAIIGW--EMGTCPVYLWTLPMFHC--NGWTfTWGTAARGGTSVCMRhvtAPEIYKNIEMH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 267 RPTAMCSVPRFWEKVYAGvqekinettglkkklmlDAIKVGREHNLEYVYKGLTPPPVlhmkykfyektiySLLKKtigi 346
Cdd:PLN03102 274 NVTHMCCVPTVFNILLKG-----------------NSLDLSPRSGPVHVLTGGSPPPA-------------ALVKK---- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 347 engrffptagaaippavqefVLSVGINMVAGYGLTESTATVA-CE--NDYDhvvgsvgRLMPHVQVKIGENN-------- 415
Cdd:PLN03102 320 --------------------VQRLGFQVMHAYGLTEATGPVLfCEwqDEWN-------RLPENQQMELKARQgvsilgla 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 416 ---------------------EIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYIK-DEHLFLTERIKDLFkTSNG 473
Cdd:PLN03102 373 dvdvknketqesvprdgktmgEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHpDGHVEIKDRSKDII-ISGG 450
|
490 500
....*....|....*....|....*
gi 2786809754 474 KYIAPQAIEAKLVVDRYIDQISIIA 498
Cdd:PLN03102 451 ENISSVEVENVLYKYPKVLETAVVA 475
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
52-485 |
1.11e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 70.84 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 52 LIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGEQLqYDVAFRVmqlgsq 131
Cdd:PRK06178 75 LRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL-APVVEQV------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 132 lkriiifdrevkrdeRDQTSIY------FDDFLKLGEGHPHQAEVDK-RISESGNGDL---------------------A 183
Cdd:PRK06178 148 ---------------RAETSLRhvivtsLADVLPAEPTLPLPDSLRApRLAAAGAIDLlpalractapvplpppaldalA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 184 NILYTSGTTGDSKGVMLHHS--CYEAAipAHNERFPQLGDQDVIMNFLP-FTHVFERAWTCWCLSMGCTLSINLRpADIQ 260
Cdd:PRK06178 213 ALNYTGGTTGMPKGCEHTQRdmVYTAA--AAYAVAVVGGEDSVFLSFLPeFWIAGENFGLLFPLFSGATLVLLAR-WDAV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 261 ktikeirpTAMCSVPRFwekvyagvqeKINETTGLKKKL--MLDAIKVGrEHNLeyvyKGLTPPPVLhmkykfyektiyS 338
Cdd:PRK06178 290 --------AFMAAVERY----------RVTRTVMLVDNAveLMDHPRFA-EYDL----SSLRQVRVV------------S 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 339 LLKKTIGIENGRFFPTAGAAIppavqefvlsvginMVAGYGLTES----TATVACENDyDHVVGS----VGRLMPHVQVK 410
Cdd:PRK06178 335 FVKKLNPDYRQRWRALTGSVL--------------AEAAWGMTEThtcdTFTAGFQDD-DFDLLSqpvfVGLPVPGTEFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 411 I-----------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYIkDEHLFL--TERIKDLFKTsNGKYIA 477
Cdd:PRK06178 400 IcdfetgellplGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKI-DEQGFLhyLGRRKEMLKV-NGMSVF 476
|
....*...
gi 2786809754 478 PQAIEAKL 485
Cdd:PRK06178 477 PSEVEALL 484
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
322-497 |
1.84e-12 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 68.84 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 322 PPVLHMKYKFYEKTIYSL--LKKTIGIENgrffptagaaiPPAVQEFVLSVGINMVAGYGLTEsTATVACENDYDHVVGS 399
Cdd:cd17637 96 PPILSNLLDAAEKSGVDLssLRHVLGLDA-----------PETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 400 VGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFtEDGWFHTGDAGYIKDE-HLFLTERI--KD 466
Cdd:cd17637 164 AGRPGPLVRVRIvddndrpvpaGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDgYLWYAGRKpeKE 242
|
170 180 190
....*....|....*....|....*....|.
gi 2786809754 467 LFKTSnGKYIAPQAIEAKLVVDRYIDQISII 497
Cdd:cd17637 243 LIKPG-GENVYPAEVEKVILEHPAIAEVCVI 272
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
34-485 |
1.86e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 69.77 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 34 IPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYifv 113
Cdd:PRK06164 34 RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 114 geqLQYDVAFRVMQLGSQLKRIiifDREVKRDER-----DQTSIYFDDFLKLGE----GHPHQAEVDKRISESGNGDLAN 184
Cdd:PRK06164 111 ---LVVWPGFKGIDFAAILAAV---PPDALPPLRaiavvDDAADATPAPAPGARvqlfALPDPAPPAAAGERAADPDAGA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 185 ILYT-SGTTGDSKGVMlhHScyEAAIPAHNERFPQ---LGDQDVIMNFLPFTHVFERAWTCWCLSMGCTLsINLRPADIQ 260
Cdd:PRK06164 185 LLFTtSGTTSGPKLVL--HR--QATLLRHARAIARaygYDPGAVLLAALPFCGVFGFSTLLGALAGGAPL-VCEPVFDAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 261 KTIKEIRptamcsvprfwekvyagvQEKINETTGLKKklMLDAIkvgreHNLEYVykgltPPPVLHMKYkfyektiysll 340
Cdd:PRK06164 260 RTARALR------------------RHRVTHTFGNDE--MLRRI-----LDTAGE-----RADFPSARL----------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 341 kktIGIenGRFFPTAGAAIPPAVQEFVLSVGInmvagYGLTESTATVAC---ENDYDHVVGSVGRLM-PHVQVKI----- 411
Cdd:PRK06164 299 ---FGF--ASFAPALGELAALARARGVPLTGL-----YGSSEVQALVALqpaTDPVSVRIEGGGRPAsPEARVRArdpqd 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 ------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDEHLFLTE-RIKDLFKTSnGKYIAPQAIEAK 484
Cdd:PRK06164 369 gallpdGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQtRMGDSLRLG-GFLVNPAEIEHA 447
|
.
gi 2786809754 485 L 485
Cdd:PRK06164 448 L 448
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
9-449 |
2.11e-12 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 70.27 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDyktETWipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPEcLYVdfGAFGV---RA 85
Cdd:COG1020 481 LFEAQAARTPDAVAVVFGD---QSL---TYAELNARANRLAHHLRALGVGPGDLVGVCLERSLE-MVV--ALLAVlkaGA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 86 VTVPFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAfrvmqlGSQLKRIIIfdrevkrderDQTSIyfddflklgeghp 165
Cdd:COG1020 552 AYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLP------ELGVPVLAL----------DALAL------------- 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 166 HQAEVDKRISESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFTH---VFErawTCW 242
Cdd:COG1020 603 AAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYG-LGPGDRVLQFASLSFdasVWE---IFG 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 243 CLSMGCTLSI----NLR-PADIQKTIKEIRPTAMCSVPRFWEkvyagvqekinettglkkkLMLDAIkvgrehnleyvyk 317
Cdd:COG1020 679 ALLSGATLVLappeARRdPAALAELLARHRVTVLNLTPSLLR-------------------ALLDAA------------- 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 318 gltPPPVLHMKYKFyektiysllkktigiengrffpTAGAAIPPA-VQEFV-LSVGINMVAGYGLTESTATVAC----EN 391
Cdd:COG1020 727 ---PEALPSLRLVL----------------------VGGEALPPElVRRWRaRLPGARLVNLYGPTETTVDSTYyevtPP 781
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2786809754 392 DYDHVVGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAF-----TEDG--WFHTGD 449
Cdd:COG1020 782 DADGGSVPIGRPIANTRVYVldahlqpvpvGVPGELYIGGAGLARGYLNRPELTAERFvadpfGFPGarLYRTGD 856
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
131-467 |
1.91e-11 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 66.69 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 131 QLKRIIIFDREVKRDERDQTSIYFDDFLKLGEGhphqaevdkrISESGNgDLANILYTSGTTGDSKGVMLHHSCYEAAIP 210
Cdd:PRK06087 149 QLQQIVGVDKLAPATSSLSLSQIIADYEPLTTA----------ITTHGD-ELAAVLFTSGTEGLPKGVMLTHNNILASER 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 211 AHNERFpQLGDQDVIMNFLPFTHV--FERAWTCWCLSMGCT-LSINLRPADIQKTIKEIRPTamCSVprfwekvyagvqe 287
Cdd:PRK06087 218 AYCARL-NLTWQDVFMMPAPLGHAtgFLHGVTAPFLIGARSvLLDIFTPDACLALLEQQRCT--CML------------- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 288 kinettglkkklmldaikvgrehnleyvykGLTPppvlhmkykFyektIYSLLK----KTIGIENGRFFPTAGAAIPPAV 363
Cdd:PRK06087 282 ------------------------------GATP---------F----IYDLLNllekQPADLSALRFFLCGGTTIPKKV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 364 QEFVLSVGINMVAGYGLTEST--ATVACENDYDHVVGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKK 431
Cdd:PRK06087 319 ARECQQRGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVvdearktlppGCEGEEASRGPNVFMGYLDE 398
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2786809754 432 EAATKAAFTEDGWFHTGD------AGYIKdehlfLTERIKDL 467
Cdd:PRK06087 399 PELTARALDEEGWYYSGDlcrmdeAGYIK-----ITGRKKDI 435
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
9-501 |
2.73e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 66.41 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPeCLYVdfGAFGV----- 83
Cdd:PLN02479 25 FLERAAVVHPTRKSVVHGSVR------YTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIP-AMYE--AHFGVpmaga 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 84 ---------RAVTVPFYATSSEAQVhYMVgDAEirYIFVGEQlqydvAFRVM--QLGSQLKR---IIIFDREVK----RD 145
Cdd:PLN02479 96 vvncvnirlNAPTIAFLLEHSKSEV-VMV-DQE--FFTLAEE-----ALKILaeKKKSSFKPpllIVIGDPTCDpkslQY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 146 ERDQTSIYFDDFLKlgEGHPhqaEVDKRISESGNGDLAnILYTSGTTGDSKGVMLHH-SCYEAAIPahNERFPQLGDQDV 224
Cdd:PLN02479 167 ALGKGAIEYEKFLE--TGDP---EFAWKPPADEWQSIA-LGYTSGTTASPKGVVLHHrGAYLMALS--NALIWGMNEGAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 225 IMNFLPFTHVFERAWTcWCLSMGCTLSINLRpadiQKTIKEIRP-------TAMCSVPRFWEK-VYAGVQEKInettglk 296
Cdd:PLN02479 239 YLWTLPMFHCNGWCFT-WTLAALCGTNICLR----QVTAKAIYSaianygvTHFCAAPVVLNTiVNAPKSETI------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 297 kklmldaikvgrehnleyvykgLTPPPVLHMKykfyektiysllkktigiengrffpTAGAAIPPAVQEFVLSVGINMVA 376
Cdd:PLN02479 307 ----------------------LPLPRVVHVM-------------------------TAGAAPPPSVLFAMSEKGFRVTH 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 377 GYGLTES--TATV-ACENDYDHV----------------VGSVG------RLMPHVQVKIGENNEIMLRGEGITHGYYKK 431
Cdd:PLN02479 340 TYGLSETygPSTVcAWKPEWDSLppeeqarlnarqgvryIGLEGldvvdtKTMKPVPADGKTMGEIVMRGNMVMKGYLKN 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786809754 432 EAATKAAFtEDGWFHTGDAGyIK--DEHLFLTERIKDLFkTSNGKYIAPQAIEAKLVVDRYIDQISIIA--DER 501
Cdd:PLN02479 420 PKANEEAF-ANGWFHSGDLG-VKhpDGYIEIKDRSKDII-ISGGENISSLEVENVVYTHPAVLEASVVArpDER 490
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
357-485 |
2.88e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 65.78 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 357 AAIPPAVQE-FVLSVGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKIGENN------------EIMLRGEG 423
Cdd:PRK07787 251 AALPVPVFDrLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDggpvphdgetvgELQVRGPT 330
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2786809754 424 ITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE--HLFLTERIKDLFKtSNGKYIAPQAIEAKL 485
Cdd:PRK07787 331 LFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDgmHRIVGRESTDLIK-SGGYRIGAGEIETAL 393
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
396-482 |
4.44e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 65.80 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 396 VVGSVGRLMPHVQVkigenNEIMLRGEGITHGYYKKEAATKAaFTEDGWFHTGDAGYIKDEHLFLTERIKDLFkTSNGKY 475
Cdd:PRK09192 398 IRNEAGMPLPERVV-----GHICVRGPSLMSGYFRDEESQDV-LAADGWLDTGDLGYLLDGYLYITGRAKDLI-IINGRN 470
|
....*..
gi 2786809754 476 IAPQAIE 482
Cdd:PRK09192 471 IWPQDIE 477
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
9-500 |
7.94e-11 |
|
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: 64.66 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQT------LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAFRvmqlgsqlkriiifdREVKRDERDQTSIYFDDFLKlgegHPHQA 168
Cdd:cd17655 76 PIDPDYPEERIQYILEDSGADILLTQSHLQPPIAFI---------------GLIDLLDEDTIYHEESENLE----PVSKS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 169 evdkrisesgnGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGDQDVIMnFLPF------THVFErawtcw 242
Cdd:cd17655 137 -----------DDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVAL-FASIsfdasvTEIFA------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 243 CLSMGCTLSINLRPA--DIQKTIKEIRptamcsvprfwekvyagvQEKINETTGLKKKL-MLDAIKVGREHNL-EYVYKG 318
Cdd:cd17655 199 SLLSGNTLYIVRKETvlDGQALTQYIR------------------QNRITIIDLTPAHLkLLDAADDSEGLSLkHLIVGG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 319 LTPPPVLhmkykfyEKTIYSLLKKTIGIENgRFFPT---AGAAIPPAVQEFVLSVGINMvagygltestaTVACENDYDH 395
Cdd:cd17655 261 EALSTEL-------AKKIIELFGTNPTITN-AYGPTettVDASIYQYEPETDQQVSVPI-----------GKPLGNTRIY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 396 VVGSVGRLMPhvqvkIGENNEIMLRGEGITHGYYKKEAATKAAFTEDGW------FHTGD-AGYIKDEHLFLTERIKDLF 468
Cdd:cd17655 322 ILDQYGRPQP-----VGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDlARWLPDGNIEFLGRIDHQV 396
|
490 500 510
....*....|....*....|....*....|..
gi 2786809754 469 KTsNGKYIAPQAIEAKLVVDRYIDQISIIADE 500
Cdd:cd17655 397 KI-RGYRIELGEIEARLLQHPDIKEAVVIARK 427
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
350-510 |
1.37e-10 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 64.14 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 350 RFFPTAGAAIPPAV-QEFVLSVGINMVAGYGLTESTATVA--------CENDYDHVVGSVGRlMPHVQVKI--------- 411
Cdd:PRK05852 298 RFIRSCSAPLTAETaQALQTEFAAPVVCAFGMTEATHQVTttqiegigQTENPVVSTGLVGR-STGAQIRIvgsdglplp 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 -GENNEIMLRGEGITHGYYKKEAATKAAFTeDGWFHTGDAGYIK-DEHLFLTERIKDLFKTSnGKYIAPQAIEAKLVVDR 489
Cdd:PRK05852 377 aGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSaAGDLSIRGRIKELINRG-GEKISPERVEGVLASHP 454
|
170 180
....*....|....*....|....*
gi 2786809754 490 YIDQISIIADERKF----VSALIIP 510
Cdd:PRK05852 455 NVMEAAVFGVPDQLygeaVAAVIVP 479
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
181-512 |
1.41e-10 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 63.61 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVML-HHSCYEAAIPAHNERFPQLGDQDVIMNFLPFTHVFERAWTCWClsMGCTLsiNLRPAdi 259
Cdd:cd17644 107 NLAYVIYTSGSTGKPKGVMIeHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLL--SGATL--VLRPE-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 260 qktikEIRPtamcSVPRFWEKVYagvQEKINettglkkklMLDaikvgrehnleyvykglTPPPVLHMkykfyekTIYSL 339
Cdd:cd17644 181 -----EMRS----SLEDFVQYIQ---QWQLT---------VLS-----------------LPPAYWHL-------LVLEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 340 LKKTIGIENG-RFFPTAGAAIPPA-VQEFVLSVG--INMVAGYGLTESTATVACEN---DYDHVVGSV--GRLMPHVQ-- 408
Cdd:cd17644 216 LLSTIDLPSSlRLVIVGGEAVQPElVRQWQKNVGnfIQLINVYGPTEATIAATVCRltqLTERNITSVpiGRPIANTQvy 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 409 --------VKIGENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFH--------TGD-AGYIKDEHLFLTERIKDLFKTs 471
Cdd:cd17644 296 ildenlqpVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDlARYLPDGNIEYLGRIDNQVKI- 374
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2786809754 472 NGKYIAPQAIEAKLVVDRYIDQISIIADE----RKFVSALIIPEY 512
Cdd:cd17644 375 RGFRIELGEIEAVLSQHNDVKTAVVIVREdqpgNKRLVAYIVPHY 419
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
181-584 |
1.74e-10 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 63.66 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCY------EAAIPAHNErfpqlgdQDVIMNFLPFTHVferAWTCWCLSM----GCTL 250
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSALivqslaKIAIVGYGE-------DDVYLHTAPLCHI---GGLSSALAMlmvgACHV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 251 SI-NLRPADIQKTIKEIRPTAMCSVPrfwekvyagvqekinettglkkKLMLDAIKVGRE----HNLEYVYKGLTPPPVL 325
Cdd:PLN02860 243 LLpKFDAKAALQAIKQHNVTSMITVP----------------------AMMADLISLTRKsmtwKVFPSVRKILNGGGSL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 326 HMKykfyektiysLLKKTIgiengRFFPTAgaaippavqefvlsvgiNMVAGYGLTES-------------------TAT 386
Cdd:PLN02860 301 SSR----------LLPDAK-----KLFPNA-----------------KLFSAYGMTEAcssltfmtlhdptlespkqTLQ 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 387 VACENDYDHV---VGS-VGRLMPHVQVKIGENN-----EIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE- 456
Cdd:PLN02860 349 TVNQTKSSSVhqpQGVcVGKPAPHVELKIGLDEssrvgRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAg 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 457 HLFLTERIKDLFKTSnGKYIAPQAIEAKLVVDRYIDQISIIA--DER--KFVSALIIPEYKLVkeYADKKGIHYGsmEDL 532
Cdd:PLN02860 429 NLWLIGRSNDRIKTG-GENVYPEEVEAVLSQHPGVASVVVVGvpDSRltEMVVACVRLRDGWI--WSDNEKENAK--KNL 503
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2786809754 533 LRKPEIIelfkeRIDTLQQQFAHYEQIKKFTLLPQPFSmergeLTNTLKIKR 584
Cdd:PLN02860 504 TLSSETL-----RHHCREKNLSRFKIPKLFVQWRKPFP-----LTTTGKIRR 545
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
180-514 |
1.81e-10 |
|
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: 63.26 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 180 GDLANILYTSGTTGDSKGVMLHHSCYEAAIPA-----HNERFPQLGDQDVIMNFLPFTHVFERAWTCWCLSMGCTLSINL 254
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAwrreyELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 255 RPADIQKTIKEIRPTAMCSVPrfweKVYAGVQEKINEttglkKKLMLDAIK---VGREHNLEYVYKGLTPPPVLHMK--- 328
Cdd:cd17650 173 DPAALYDLILKSRITLMESTP----ALIRPVMAYVYR-----NGLDLSAMRlliVGSDGCKAQDFKTLAARFGQGMRiin 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 329 -YKFYEKTIYSLLKKT--IGIENGRFFPTaGAAIPpavqefvlsvgiNMvAGYGLTESTATVAcendydhvVGSVGRLMp 405
Cdd:cd17650 244 sYGVTEATIDSTYYEEgrDPLGDSANVPI-GRPLP------------NT-AMYVLDERLQPQP--------VGVAGELY- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 406 hvqvkIGenneimlrGEGITHGYYKKEAATKAAFTEDGW------FHTGD-AGYIKDEHLFLTERIKDLFKTsNGKYIAP 478
Cdd:cd17650 301 -----IG--------GAGVARGYLNRPELTAERFVENPFapgermYRTGDlARWRADGNVELLGRVDHQVKI-RGFRIEL 366
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2786809754 479 QAIEAKLVVDRYIDQISIIADE----RKFVSALIIPEYKL 514
Cdd:cd17650 367 GEIESQLARHPAIDEAVVAVREdkggEARLCAYVVAAATL 406
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
9-501 |
2.23e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 62.99 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRS------LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRyifvgeqlqydvafrvmqlgsqlkrIIIFDREVK-RDERDQTSIYFDDFLKLGEGHPHQ 167
Cdd:cd12117 76 PLDPELPAERLAFMLADAGAK-------------------------VLLTDRSLAgRAGGLEVAVVIDEALDAGPAGNPA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 168 AEVDKrisesgnGDLANILYTSGTTGDSKGVMLHHscyeAAIP--AHNERFPQLGDQDVIMNFLP-----FThvFErAWT 240
Cdd:cd12117 131 VPVSP-------DDLAYVMYTSGSTGRPKGVAVTH----RGVVrlVKNTNYVTLGPDDRVLQTSPlafdaST--FE-IWG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 241 cwCLSMGCTLSIN-----LRPADIQKTIKEIRPTAMcsvprfWekvyagvqekinETTGLKKKLMldaikvgrEHNLEyV 315
Cdd:cd12117 197 --ALLNGARLVLApkgtlLDPDALGALIAEEGVTVL------W------------LTAALFNQLA--------DEDPE-C 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 316 YKGLtpppvlhmkykfyektiysllkktigiengRFFPTAGAAIPPAVQEFVLSV--GINMVAGYGLTESTaTVAC---- 389
Cdd:cd12117 248 FAGL------------------------------RELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTENT-TFTTshvv 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 390 ENDYD----------------HVVGSVGRLMPhvqvkIGENNEIMLRGEGITHGYYKKEAATKAAFTEDGW------FHT 447
Cdd:cd12117 297 TELDEvagsipigrpiantrvYVLDEDGRPVP-----PGVPGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRT 371
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2786809754 448 GD-AGYIKDEHLFLTERIKDLFKTsNGKYIAPQAIEAKLVVDRYIDQISIIADER 501
Cdd:cd12117 372 GDlARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALRAHPGVREAVVVVRED 425
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
182-485 |
2.31e-10 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 63.16 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 182 LANILYTSGTTGDSKGVMLHHscyeAAIPAHNE---RFPQLGDQDVIMNFLPFThvFERAWTCWCLSMGCTLSINLRPAD 258
Cdd:cd17649 96 LAYVIYTSGSTGTPKGVAVSH----GPLAAHCQataERYGLTPGDRELQFASFN--FDGAHEQLLPPLICGACVVLRPDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 259 IQKTIKEIRptamcsvprfwEKVYAGVQEKINETTGLKKKLMLDAIKVGREhnleyvykglTPPPVlhmkykfyektiys 338
Cdd:cd17649 170 LWASADELA-----------EMVRELGVTVLDLPPAYLQQLAEEADRTGDG----------RPPSL-------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 339 llkktigiengRFFPTAGAAIPPAVQEFVLSVGINMVAGYGLTESTATVA---CENDYDHVVGSV--GRLMPHVQVKI-- 411
Cdd:cd17649 215 -----------RLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLvwkCEAGAARAGASMpiGRPLGGRSAYIld 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 --------GENNEIMLRGEGITHGYYKKEAATKAAFTEDG-------WFHTGD-AGYIKDEHLFLTERIKDLFKTsNGKY 475
Cdd:cd17649 284 adlnpvpvGVTGELYIGGEGLARGYLGRPELTAERFVPDPfgapgsrLYRTGDlARWRDDGVIEYLGRVDHQVKI-RGFR 362
|
330
....*....|
gi 2786809754 476 IAPQAIEAKL 485
Cdd:cd17649 363 IELGEIEAAL 372
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-442 |
2.76e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.82 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:PRK12316 4556 LVAERARMTPDAVAVVFDEEK------LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVGEQLQydvafRVMQLGSQLKRIIIfDREvkrderdqtsiyfDDFlklgEGHPHQA 168
Cdd:PRK12316 4630 PLDPEYPRERLAYMMEDSGAALLLTQSHLL-----QRLPIPDGLASLAL-DRD-------------EDW----EGFPAHD 4686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 169 EVDKRISEsgngDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFThvFERAWTCWCLSMGC 248
Cdd:PRK12316 4687 PAVRLHPD----NLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERY-ELTPDDRVLQFMSFS--FDGSHEGLYHPLIN 4759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 249 TLSINLRPA---DIQKTIKEI---RPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLMLDAIKVGrehNLEYVYKGLtPP 322
Cdd:PRK12316 4760 GASVVIRDDslwDPERLYAEIhehRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQA---SYDLAWRAL-KP 4835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 323 PVLHMKYKFYEKTIYSLLKKTigiengRFFPTAGAAIPPavqefvLSVGINMVAGYGLTESTATVAcendydhvVGSVGr 402
Cdd:PRK12316 4836 VYLFNGYGPTETTVTVLLWKA------RDGDACGAAYMP------IGTPLGNRSGYVLDGQLNPLP--------VGVAG- 4894
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2786809754 403 lmphvqvkigennEIMLRGEGITHGYYKKEAATKAAFTED 442
Cdd:PRK12316 4895 -------------ELYLGGEGVARGYLERPALTAERFVPD 4921
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
36-510 |
5.59e-10 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 61.76 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 36 VSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGe 115
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIA- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 116 qlqydVAFRVMQLGSQLK-RIIIFDREVkrDERDQTSiyFDDFLKLGEGHPHQAevdkrisesgngdlANILYTSGTTGD 194
Cdd:cd05923 108 -----VDAQVMDAIFQSGvRVLALSDLV--GLGEPES--AGPLIEDPPREPEQP--------------AFVFYTSGTTGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 195 SKGVMLHHSCYE--AAIPAHNE--RFpqlGDQDVIMNFLPFTHVFE-RAWTCWCLSMGCTLSI--NLRPADIQKTIKEIR 267
Cdd:cd05923 165 PKGAVIPQRAAEsrVLFMSTQAglRH---GRHNVVLGLMPLYHVIGfFAVLVAALALDGTYVVveEFDPADALKLIEQER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 268 PTAMCSVPRFWEKV-----YAGVQEKINETTGLKKKLMLDAIkvgrehnLEYVYKGLTPPPVlhmkykfyekTIYSllkk 342
Cdd:cd05923 242 VTSLFATPTHLDALaaaaeFAGLKLSSLRHVTFAGATMPDAV-------LERVNQHLPGEKV----------NIYG---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 343 TIGIENGRFFPTAGAaippavqefvlsvGINMVAGYgltestatvacendYDHV-VGSVGRlMPHVQVKIGENNEIM--L 419
Cdd:cd05923 301 TTEAMNSLYMRDART-------------GTEMRPGF--------------FSEVrIVRIGG-SPDEALANGEEGELIvaA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 420 RGEGITHGYYKKEAATkAAFTEDGWFHTGDAGYIKDE-HLFLTERIKDLFkTSNGKYIAPQAIEAKLVVDRYIDQISII- 497
Cdd:cd05923 353 AADAAFTGYLNQPEAT-AKKLQDGWYRTGDVGYVDPSgDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIg 430
|
490
....*....|....*.
gi 2786809754 498 -ADER--KFVSALIIP 510
Cdd:cd05923 431 vADERwgQSVTACVVP 446
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
6-468 |
8.44e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 61.43 E-value: 8.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 6 LSVLIQRQARKYGDRVVLRYRDYKTetwipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVrA 85
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALLFEDQSI------SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKL-G 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 86 VTVPFYATSSEAQV--HyMVGDAEIRYIFVGEqlqyDVAFRVMQLGSQLK---RIIIFDREVKRDERDqtsiyFDDFLKL 160
Cdd:PRK08279 112 AVVALLNTQQRGAVlaH-SLNLVDAKHLIVGE----ELVEAFEEARADLArppRLWVAGGDTLDDPEG-----YEDLAAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 161 GEGHP-HQAEVDKRISesgNGDLANILYTSGTTGDSK-GVMLHHSCYEA-AIPAHNERfpqLGDQDVIMNFLPFTH---- 233
Cdd:PRK08279 182 AAGAPtTNPASRSGVT---AKDTAFYIYTSGTTGLPKaAVMSHMRWLKAmGGFGGLLR---LTPDDVLYCCLPLYHntgg 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 234 -VferawtCWC--LSMGCTLSINLRpadiqktikeirptamCSVPRFWEKVyagVQEK------INEttgLKKKLMLDAI 304
Cdd:PRK08279 256 tV------AWSsvLAAGATLALRRK----------------FSASRFWDDV---RRYRatafqyIGE---LCRYLLNQPP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 305 KVG-REHNLEYVY-KGLTPppvlhmkykfyekTIYSLLKKTIGIengrffptagaaipPAVQEFvlsvginmvagYGLTE 382
Cdd:PRK08279 308 KPTdRDHRLRLMIgNGLRP-------------DIWDEFQQRFGI--------------PRILEF-----------YAASE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 383 stATVACENdYDHVVGSVGRL-----MPHVQVKIGENNEIMLR--------------GEGITH--------GYYKKEAAT 435
Cdd:PRK08279 350 --GNVGFIN-VFNFDGTVGRVplwlaHPYAIVKYDVDTGEPVRdadgrcikvkpgevGLLIGRitdrgpfdGYTDPEASE 426
|
490 500 510
....*....|....*....|....*....|....*....
gi 2786809754 436 KA----AFTE-DGWFHTGD-AGYIKDEHLFLTERIKDLF 468
Cdd:PRK08279 427 KKilrdVFKKgDAWFNTGDlMRDDGFGHAQFVDRLGDTF 465
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
185-486 |
1.21e-09 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 60.85 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 185 ILYTSGTTGDSKGVMLHHSCyeAAIPAHNERFPQLGD----QDVIMNFLPFTHVFERAWTCWCLSMGCTLSI--NLRPAD 258
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPG--GPPDNDTLMAAALGFgpgaDSVYLSPAPLYHAAPFRWSMTALFMGGTLVLmeKFDPEE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 259 IQKTIKEIRPTAMCSVP----RFWeKVYAGVQEKINETTgLKKklmldAIKVGrehnleyvykGLTPPPVlhmkykfyek 334
Cdd:cd05929 208 FLRLIERYRVTFAQFVPtmfvRLL-KLPEAVRNAYDLSS-LKR-----VIHAA----------APCPPWV---------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 335 tiysllkKTIGIENGrffptagaaiPPAVQEFvlsvginmvagYGLTESTATVAC--ENDYDHVvGSVGRLMPHVqVKI- 411
Cdd:cd05929 261 -------KEQWIDWG----------GPIIWEY-----------YGGTEGQGLTIIngEEWLTHP-GSVGRAVLGK-VHIl 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 ---------GENNEIMLRGeGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLTERIKDLFkTSNGKYIAPQAI 481
Cdd:cd05929 311 dedgnevppGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWSTLGDVGYLdEDGYLYLTDRRSDMI-ISGGVNIYPQEI 388
|
....*
gi 2786809754 482 EAKLV 486
Cdd:cd05929 389 ENALI 393
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
180-482 |
1.85e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.95 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 180 GDLANILYTSGTTGDSKGVMLHHSCYEAaipahNERFPQ------LGDQDVIMNFLPFTH-----------VFERAwTCW 242
Cdd:PRK05691 166 DDIAFLQYTSGSTALPKGVQVSHGNLVA-----NEQLIRhgfgidLNPDDVIVSWLPLYHdmgliggllqpIFSGV-PCV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 243 CLSMGCTLSinlRPADIQKTIKEIRPTaMCSVPRFwekVYAGVQEKINETTglKKKLMLDAIKVGrehnleyvYKGlTPP 322
Cdd:PRK05691 240 LMSPAYFLE---RPLRWLEAISEYGGT-ISGGPDF---AYRLCSERVSESA--LERLDLSRWRVA--------YSG-SEP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 323 PVLHMKYKFYEKTiysllkKTIGIENGRFFPTAGAAippavqEFVLSVGiNMVAGYGLT------ESTATVACENDYDHV 396
Cdd:PRK05691 302 IRQDSLERFAEKF------AACGFDPDSFFASYGLA------EATLFVS-GGRRGQGIPaleldaEALARNRAEPGTGSV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 397 VGSVGRLMPHVQVKI---------GENN--EIMLRGEGITHGYYKKEAATKAAFTE-DG--WFHTGDAGYIKDEHLFLTE 462
Cdd:PRK05691 369 LMSCGRSQPGHAVLIvdpqslevlGDNRvgEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFLRDGELFVTG 448
|
330 340
....*....|....*....|
gi 2786809754 463 RIKDLFkTSNGKYIAPQAIE 482
Cdd:PRK05691 449 RLKDML-IVRGHNLYPQDIE 467
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
350-498 |
1.99e-09 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 60.17 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 350 RFFPTAGAAIPPAVQEFVLS-VGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKI----------GENNEIM 418
Cdd:cd05919 211 RLCVSAGEALPRGLGERWMEhFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLvdeeghtippGEEGDLL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 419 LRGEGITHGYYKKEAATKAAFtEDGWFHTGDAgYIKDEHLFLTE--RIKDLFKTSnGKYIAPQAIEAKLVVDRYIDQISI 496
Cdd:cd05919 291 VRGPSAAVGYWNNPEKSRATF-NGGWYRTGDK-FCRDADGWYTHagRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAV 367
|
..
gi 2786809754 497 IA 498
Cdd:cd05919 368 VA 369
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
394-482 |
4.00e-09 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 59.39 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 394 DHVVGSVGRLM-PHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE-HLFLT 461
Cdd:COG1021 349 EVILTTQGRPIsPDDEVRIvdedgnpvppGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDgYLVVE 428
|
90 100
....*....|....*....|...
gi 2786809754 462 ERIKDLFktsN--GKYIAPQAIE 482
Cdd:COG1021 429 GRAKDQI---NrgGEKIAAEEVE 448
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
378-485 |
5.05e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 58.94 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 378 YGLTESTATVACEN-DYDHVVGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFH 446
Cdd:PRK12406 303 YGSTESGAVTFATSeDALSHPGTVGKAAPGAELRFvdedgrplpqGEIGEIYSRIAGNPDFTYHNKPEKRAEIDRGGFIT 382
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2786809754 447 TGDAGYI-KDEHLFLTERIKDLFkTSNGKYIAPQAIEAKL 485
Cdd:PRK12406 383 SGDVGYLdADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVL 421
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
167-456 |
5.11e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 58.63 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 167 QAEVDKRISESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERF-PQLGDQDvIMNFLPFThVFERAwtcwcls 245
Cdd:cd05910 72 EAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYgIRPGEVD-LATFPLFA-LFGPA------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 246 MGCTLSI----NLRPAD-----IQKTIKEIRPTAMCSVPRFWEKVyagvqekinettglkkklmldaIKVGREHnleyvy 316
Cdd:cd05910 143 LGLTSVIpdmdPTRPARadpqkLVGAIRQYGVSIVFGSPALLERV----------------------ARYCAQH------ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 317 kGLTPPPVlhmkykfyeKTIYSllkktigiengrffptAGAAIPPAVQEFV---LSVGINMVAGYGLTE----------- 382
Cdd:cd05910 195 -GITLPSL---------RRVLS----------------AGAPVPIALAARLrkmLSDEAEILTPYGATEalpvssigsre 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 383 --STATVACENdydHVVGSVGRLMPHVQVKI-------------------GENNEIMLRGEGITHGYYKKEAATKAAFTE 441
Cdd:cd05910 249 llATTTAATSG---GAGTCVGRPIPGVRVRIieiddepiaewddtlelprGEIGEITVTGPTVTPTYVNRPVATALAKID 325
|
330
....*....|....*....
gi 2786809754 442 DG----WFHTGDAGYIKDE 456
Cdd:cd05910 326 DNsegfWHRMGDLGYLDDE 344
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
18-203 |
8.01e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 58.36 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 18 GDRVVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPEclYVD--FGAFGVRAVTVP--FYAT 93
Cdd:PRK07798 17 PDRVALVCGDRR------LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIE--YVEamLGAFKARAVPVNvnYRYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 94 SSEaqVHYMVGDAEIRYIFVGEQLQYDVAfRVMQLGSQLKRIIIFDREVKRDERDqTSIYFDDFLKLGEGHPHQAEvdkr 173
Cdd:PRK07798 89 EDE--LRYLLDDSDAVALVYEREFAPRVA-EVLPRLPKLRTLVVVEDGSGNDLLP-GAVDYEDALAAGSPERDFGE---- 160
|
170 180 190
....*....|....*....|....*....|
gi 2786809754 174 isesGNGDLANILYTSGTTGDSKGVMLHHS 203
Cdd:PRK07798 161 ----RSPDDLYLLYTGGTTGMPKGVMWRQE 186
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
174-457 |
8.68e-09 |
|
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: 58.09 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 174 ISESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFThvFeraWTCW-----CLSMGC 248
Cdd:cd17653 99 LTTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARL-DVGPGSRVAQVLSIA--F---DACIgeifsTLCNGG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 249 TLSINLRPADIQKTIKEIrpTAMCSVPRFwekvyagvqekinettglkkklmLDAIKVGREHNLEYVY-KGLTPPPVLHM 327
Cdd:cd17653 173 TLVLADPSDPFAHVARTV--DALMSTPSI-----------------------LSTLSPQDFPNLKTIFlGGEAVPPSLLD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 328 KYKFyektiysllkktigiengrffptagaaippavqefvlsvGINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHV 407
Cdd:cd17653 228 RWSP---------------------------------------GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNS 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786809754 408 QVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFH------TGDAGYIKDEH 457
Cdd:cd17653 269 TCYIldadlqpvpeGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDG 334
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
372-501 |
1.03e-08 |
|
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: 57.03 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 372 INMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKI-----GENNEIMLRGEGITHGYYKKEAatkaaFTEDGWFH 446
Cdd:cd17633 137 ANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIrnadgGEIGKIFVKSEMVFSGYVRGGF-----SNPDGWMS 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2786809754 447 TGDAGYIKDE-HLFLTERIKDLFkTSNGKYIAPQAIEAKLVVDRYIDQISIIA--DER 501
Cdd:cd17633 212 VGDIGYVDEEgYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVGipDAR 268
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
181-449 |
1.62e-08 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 57.17 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFT---HVFErAWTCW----CLsmgCTLSIN 253
Cdd:cd05918 107 DAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG-LTSESRVLQFASYTfdvSILE-IFTTLaaggCL---CIPSEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 254 LRPADIQKTIKEIRPTAMcsvprfwekvyagvqekinettglkkklmldaikvgrehnleyvykGLTPppvlhmkykfye 333
Cdd:cd05918 182 DRLNDLAGFINRLRVTWA----------------------------------------------FLTP------------ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 334 kTIYSLLK-------KTIGiengrffpTAGAAIPPAVQEfVLSVGINMVAGYGLTEST-ATVACENDYD----------- 394
Cdd:cd05918 204 -SVARLLDpedvpslRTLV--------LGGEALTQSDVD-TWADRVRLINAYGPAECTiAATVSPVVPStdprnigrplg 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2786809754 395 ---HVV--GSVGRLMPhvqvkIGENNEIMLRGEGITHGYYKKEAATKAAFTED-GW------------FHTGD 449
Cdd:cd05918 274 atcWVVdpDNHDRLVP-----IGAVGELLIEGPILARGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGD 341
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
398-486 |
2.44e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 56.84 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 398 GSVGRLMpHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIKDE-HLFLTERIKD 466
Cdd:PRK08276 315 GSVGKAV-LGEVRIldedgnelppGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDgYLYLTDRKSD 393
|
90 100
....*....|....*....|
gi 2786809754 467 LFkTSNGKYIAPQAIEAKLV 486
Cdd:PRK08276 394 MI-ISGGVNIYPQEIENLLV 412
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
160-486 |
2.69e-08 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 56.33 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 160 LGEGHPHQAEVDKRISESGngDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGDQDVIMNFLPFTHVFER-- 237
Cdd:cd05958 79 LDKARITVALCAHALTASD--DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLgg 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 238 -AWTCWCLSMGCTLSINLRPADIQKTIKEIRPTAMCSVPrfwekvyagvqekinetTGLKKKLmldAIKVGREHNLeyvy 316
Cdd:cd05958 157 vLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAP-----------------TAYRAML---AHPDAAGPDL---- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 317 kgltpppvlhmkykfyektiySLLKKTIgiengrffpTAGAAIPPAVQE-FVLSVGINMVAGYGLTESTAtVACENDYDH 395
Cdd:cd05958 213 ---------------------SSLRKCV---------SAGEALPAALHRaWKEATGIPIIDGIGSTEMFH-IFISARPGD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 396 V-VGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATkaaFTEDGWFHTGDAGYIKDEHLF-LTER 463
Cdd:cd05958 262 ArPGATGKPVPGYEAKVvddegnpvpdGTIGRLAVRGPTGCRYLADKRQRT---YVQGGWNITGDTYSRDPDGYFrHQGR 338
|
330 340
....*....|....*....|...
gi 2786809754 464 IKDLFKtSNGKYIAPQAIEAKLV 486
Cdd:cd05958 339 SDDMIV-SGGYNIAPPEVEDVLL 360
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
350-486 |
2.90e-08 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 56.57 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 350 RFFPTAGAAIPPavqefVLSVGINMVagYGLTESTATVACENDYDHVV-GSVGRLM-PHVQVKI----------GENNEI 417
Cdd:cd05920 266 RLSPALARRVPP-----VLGCTLQQV--FGMAEGLLNYTRLDDPDEVIiHTQGRPMsPDDEIRVvdeegnpvppGEEGEL 338
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 418 MLRGEGITHGYYKKEAATKAAFTEDGWFHTGD-AGYIKDEHLFLTERIKDLFkTSNGKYIAPQAIEAKLV 486
Cdd:cd05920 339 LTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDlVRRTPDGYLVVEGRIKDQI-NRGGEKIAAEEVENLLL 407
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
16-486 |
5.55e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 55.56 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 16 KYGDRVvlrYRDYKTETWI-----PVSWNQFAATVKTVSNALI-ELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVP 89
Cdd:PRK05620 17 EYGSTV---HGDTTVTTWGgaeqeQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 90 FYATSSEAQVHYMVGDAEIRYIFVGEQLQydvafrvMQLGSQLK-----RIIIFdreVKRDERDQTSIYFDDFLKLgegH 164
Cdd:PRK05620 94 LNKQLMNDQIVHIINHAEDEVIVADPRLA-------EQLGEILKecpcvRAVVF---IGPSDADSAAAHMPEGIKV---Y 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 165 PHQAEVDKRISESGNGDL-----ANILYTSGTTGDSKGVML-HHSCYEAAIpahnerfpQLGDQD--VIMN---FL---P 230
Cdd:PRK05620 161 SYEALLDGRSTVYDWPELdettaAAICYSTGTTGAPKGVVYsHRSLYLQSL--------SLRTTDslAVTHgesFLccvP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 231 FTHVFErawtcWCLSMGCTLS--------INLRPADIQKTIKEIRPTAMCSVPRFWekvyagVQekinettglkkkLMld 302
Cdd:PRK05620 233 IYHVLS-----WGVPLAAFMSgtplvfpgPDLSAPTLAKIIATAMPRVAHGVPTLW------IQ------------LM-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 303 aikvgrehnleyVYKGLTPPPVLHMKykfyekTIYSllkktigiengrffptAGAAIPPAV-----QEFvlsvGINMVAG 377
Cdd:PRK05620 288 ------------VHYLKNPPERMSLQ------EIYV----------------GGSAVPPILikaweERY----GVDVVHV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 378 YGLTEST---------ATVACENDYDHVVgSVGRLMPHVQVKIGENNEIM-----------LRGEGITHGYYKKEAATKA 437
Cdd:PRK05620 330 WGMTETSpvgtvarppSGVSGEARWAYRV-SQGRFPASLEYRIVNDGQVMestdrnegeiqVRGNWVTASYYHSPTEEGG 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786809754 438 A----------------FTEDGWFHTGDAGYI-KDEHLFLTERIKDLFKtSNGKYIAPQAIEAKLV 486
Cdd:PRK05620 409 GaastfrgedvedandrFTADGWLRTGDVGSVtRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIM 473
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
176-482 |
6.70e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 55.39 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 176 ESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPQLGDQDVIMNFLPFTHvferawtcwclSMGCT--LSIN 253
Cdd:PRK07768 148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFH-----------DMGMVgfLTVP 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 254 L-RPADIQKtikeIRPTAMCSVPRFWEKvyagvqekinettglkkklMLDAikvgrehnleyvYKG-LTPPPvlhmkyKF 331
Cdd:PRK07768 217 MyFGAELVK----VTPMDFLRDPLLWAE-------------------LISK------------YRGtMTAAP------NF 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 332 yektIYSLLKKTI--GIENGRF------FPTAGA-AIPPAVQEFVLSVGIN-------MVAGYGLTESTATVA------- 388
Cdd:PRK07768 256 ----AYALLARRLrrQAKPGAFdlsslrFALNGAePIDPADVEDLLDAGARfglrpeaILPAYGMAEATLAVSfspcgag 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 389 ---CENDYDHV----------------VGSVGRLMPHVQVKIGENN----------EIMLRGEGITHGYyKKEAATKAAF 439
Cdd:PRK07768 332 lvvDEVDADLLaalrravpatkgntrrLATLGPPLPGLEVRVVDEDgqvlpprgvgVIELRGESVTPGY-LTMDGFIPAQ 410
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2786809754 440 TEDGWFHTGDAGYIKDE-HLFLTERIKDLFKTSnGKYIAPQAIE 482
Cdd:PRK07768 411 DADGWLDTGDLGYLTEEgEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
355-486 |
8.04e-08 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 54.88 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 355 AGAAIPPAVQEFVLSV-GINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKI-------GENNEIML-----RG 421
Cdd:cd05974 208 AGEPLNPEVIEQVRRAwGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALldpdgapATEGEVALdlgdtRP 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2786809754 422 EGITHGYYKKEAATKAAFtEDGWFHTGDAGYiKDEHLFLT--ERIKDLFKTSNGKyIAPQAIEAKLV 486
Cdd:cd05974 288 VGLMKGYAGDPDKTAHAM-RGGYYRTGDIAM-RDEDGYLTyvGRADDVFKSSDYR-ISPFELESVLI 351
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
31-557 |
1.11e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 54.63 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 31 ETWIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAF--GVRAVTVPFYATSSEAQvhYMVGDAEI 108
Cdd:PRK13390 20 ETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALrsGLYITAINHHLTAPEAD--YIVGDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 109 RYIFVGEQLQYDVAfrvmQLGSQLKRIIIFDREVkrderdqtsiyfDDFlklGEGHPHQAEVDKRISESGNGdlANILYT 188
Cdd:PRK13390 98 RVLVASAALDGLAA----KVGADLPLRLSFGGEI------------DGF---GSFEAALAGAGPRLTEQPCG--AVMLYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 189 SGTTGDSKGV---MLHHSCYEAAIP--AHNERFPQLGDQDVIMNFLPFTHVFERAWTCWCLSMGCTLSINLR--PADIQK 261
Cdd:PRK13390 157 SGTTGFPKGIqpdLPGRDVDAPGDPivAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRfdAQATLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 262 TIKEIRPTAMCSVPRFWEKVYagvqeKINETTGLKKKLmldaikvgreHNLEYVYKGLTPPP--VLHMKYKFYEKTIYSL 339
Cdd:PRK13390 237 HVERYRITVTQMVPTMFVRLL-----KLDADVRTRYDV----------SSLRAVIHAAAPCPvdVKHAMIDWLGPIVYEY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 340 LKKT-----IGIENGRFFPTAGaaippavqefvlSVGINMVAGYGLtestatvaCENDydhvvgsvGRLMPhvqvkIGEN 414
Cdd:PRK13390 302 YSSTeahgmTFIDSPDWLAHPG------------SVGRSVLGDLHI--------CDDD--------GNELP-----AGRI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 415 NEIMLRGEGITHGYYKKEAATKAAF--TEDGWFHTGDAGYIKDE-HLFLTERiKDLFKTSNGKYIAPQAIEAKLVVDRYI 491
Cdd:PRK13390 349 GTVYFERDRLPFRYLNDPEKTAAAQhpAHPFWTTVGDLGSVDEDgYLYLADR-KSFMIISGGVNIYPQETENALTMHPAV 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786809754 492 DQISIIAderkfvsaliIPEYKLVKEYadKKGIHygsMEDLLRKPEiiELFKERIDTLQQQFAHYE 557
Cdd:PRK13390 428 HDVAVIG----------VPDPEMGEQV--KAVIQ---LVEGIRGSD--ELARELIDYTRSRIAHYK 476
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
18-449 |
1.24e-07 |
|
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: 54.22 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 18 GDRVVLRYRDyktetwIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEA 97
Cdd:cd12116 1 PDATAVRDDD------RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 98 QVHYMVGDAEIRyifvgeqlqydvafrvmqlgsqlkrIIIFDRevkrDERDQTSIYFDDFLKLGEGHPHQAEVdKRISES 177
Cdd:cd12116 75 RLRYILEDAEPA-------------------------LVLTDD----ALPDRLPAGLPVLLLALAAAAAAPAA-PRTPVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 178 GNgDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERfPQLGDQDVIMNFLPFT---HVFERAWTCWClsmGCTLSInl 254
Cdd:cd12116 125 PD-DLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRER-LGLGPGDRLLAVTTYAfdiSLLELLLPLLA---GARVVI-- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 255 RPADIQK-------TIKEIRPTAMCSVPRFWekvyagvqekinettglkkKLMLDAIKVGREhnleyvykGLTpppvlhm 327
Cdd:cd12116 198 APRETQRdpealarLIEAHSITVMQATPATW-------------------RMLLDAGWQGRA--------GLT------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 328 kykfyektiysLLkktigiengrffpTAGAAIPPAVQEFVLSVG---INMvagYGLTEST--ATVACENDYD-------- 394
Cdd:cd12116 244 -----------AL-------------CGGEALPPDLAARLLSRVgslWNL---YGPTETTiwSTAARVTAAAgpipigrp 296
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2786809754 395 ------HVVGSVGRLMPhvqvkIGENNEIMLRGEGITHGYYKKEAATKAAFTEDG-------WFHTGD 449
Cdd:cd12116 297 lantqvYVLDAALRPVP-----PGVPGELYIGGDGVAQGYLGRPALTAERFVPDPfagpgsrLYRTGD 359
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
36-226 |
1.61e-07 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 54.20 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 36 VSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRyifvge 115
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGAR------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 116 qlqydvaFRVMQLGSQLKRIIIFDREVKRDERDQTSiyfDDFLKlgeghphqaevdkriSESGNGDLANILYTSGTTGDS 195
Cdd:cd12114 87 -------LVLTDGPDAQLDVAVFDVLILDLDALAAP---APPPP---------------VDVAPDDLAYVIFTSGSTGTP 141
|
170 180 190
....*....|....*....|....*....|....
gi 2786809754 196 KGVMLHHscyEAA---IPAHNERFpQLGDQDVIM 226
Cdd:cd12114 142 KGVMISH---RAAlntILDINRRF-AVGPDDRVL 171
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
345-451 |
2.62e-07 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 52.69 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 345 GIENGRFFPTAGAAIPPAVQEFVLSVGinmvaGYGLTESTAtVACENDY-DHVVGSVGRLMPHVQVKI----------GE 413
Cdd:cd17636 115 SLRSSPAAPEWNDMATVDTSPWGRKPG-----GYGQTEVMG-LATFAALgGGAIGGAGRPSPLVQVRIldedgrevpdGE 188
|
90 100 110
....*....|....*....|....*....|....*...
gi 2786809754 414 NNEIMLRGEGITHGYYKKEAATkAAFTEDGWFHTGDAG 451
Cdd:cd17636 189 VGEIVARGPTVMAGYWNRPEVN-ARRTRGGWHHTNDLG 225
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
180-511 |
4.53e-07 |
|
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: 52.56 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 180 GDLANILYTSGTTGDSKGVMLHHscyeaaipaHNerfpqlgdqdvIMNFLpfthvferAWTCWCLSMGctlsinlrPADI 259
Cdd:cd17645 104 DDLAYVIYTSGSTGLPKGVMIEH---------HN-----------LVNLC--------EWHRPYFGVT--------PADK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 260 QKTIKEIRPTAmcSVPRFWEKVYAGVQEKInettgLKKKLMLDAIKVGREHNLEYVYKGLTPPPVLHmkyKFYEKTIYSL 339
Cdd:cd17645 148 SLVYASFSFDA--SAWEIFPHLTAGAALHV-----VPSERRLDLDALNDYFNQEGITISFLPTGAAE---QFMQLDNQSL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 340 lkktigiengRFFPTAGAAIPPAVQEfvlsvGINMVAGYGLTESTATV-ACENDYDHVVGSVGRLMPHVQVKI------- 411
Cdd:cd17645 218 ----------RVLLTGGDKLKKIERK-----GYKLVNNYGPTENTVVAtSFEIDKPYANIPIGKPIDNTRVYIldealql 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 ---GENNEIMLRGEGITHGYYKKEAATKAAFTEDGW------FHTGD-AGYIKDEHLFLTERIKDLFKTsNGKYIAPQAI 481
Cdd:cd17645 283 qpiGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDlAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEI 361
|
330 340 350
....*....|....*....|....*....|....
gi 2786809754 482 EAKLVVDRYIDQISIIA----DERKFVSALIIPE 511
Cdd:cd17645 362 EPFLMNHPLIELAAVLAkedaDGRKYLVAYVTAP 395
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
378-464 |
5.10e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 52.59 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 378 YGLTEstATVACE---------NDYDHVvgSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAA 438
Cdd:PRK04813 293 YGPTE--ATVAVTsieitdemlDQYKRL--PIGYAKPDSPLLIideegtklpdGEQGEIVISGPSVSKGYLNNPEKTAEA 368
|
90 100
....*....|....*....|....*....
gi 2786809754 439 F-TEDGW--FHTGDAGYIKDEHLFLTERI 464
Cdd:PRK04813 369 FfTFDGQpaYHTGDAGYLEDGLLFYQGRI 397
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
174-486 |
5.49e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 52.51 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 174 ISESGNGDLANILYTSGTTGDSKGVMLHHscyeAAIPAHNE---RFPQLGDQDVIMNFLPFTHVFE-RAWTCWCLSMG-- 247
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTH----ANLLANQRaclKFFSPKEDDVMMSFLPPFHAYGfNSCTLFPLLSGvp 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 248 CTLSIN-LRPADIQKTIKEIRPTAMCSVPRFWEKVYagvqekineTTGLKKKLMLDAikvgrehnLEYVYKGLTPppvlh 326
Cdd:PRK06334 253 VVFAYNpLYPKKIVEMIDEAKVTFLGSTPVFFDYIL---------KTAKKQESCLPS--------LRFVVIGGDA----- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 327 MKYKFYEKTIysllkktigiengRFFPTagaaippavqefvlsvgINMVAGYGLTESTATVACEND----YDHVVGSVGR 402
Cdd:PRK06334 311 FKDSLYQEAL-------------KTFPH-----------------IQLRQGYGTTECSPVITINTVnspkHESCVGMPIR 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 403 LM--------PHVQVKIGENNEIMLRGEGITHGYYkkEAATKAAFTE---DGWFHTGDAGYIkDEH--LFLTERIKDLFK 469
Cdd:PRK06334 361 GMdvlivseeTKVPVSSGETGLVLTRGTSLFSGYL--GEDFGQGFVElggETWYVTGDLGYV-DRHgeLFLKGRLSRFVK 437
|
330
....*....|....*..
gi 2786809754 470 TSnGKYIAPQAIEAKLV 486
Cdd:PRK06334 438 IG-AEMVSLEALESILM 453
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
18-202 |
5.50e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 52.59 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 18 GDRVVLRYRDYKTETwiPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPEcLYVD-FGAFGVRAVTVPFYATSSE 96
Cdd:PRK04319 58 KDKVALRYLDASRKE--KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPE-LYFAlLGALKNGAIVGPLFEAFME 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 97 AQVHYMVGDAEIRYIFVGEQLQYDVAFRVMqlgSQLKRIIIFDREVKRDERDQtsiyfdDFLKLGEGHPHQAEVDKRISE 176
Cdd:PRK04319 135 EAVRDRLEDSEAKVLITTPALLERKPADDL---PSLKHVLLVGEDVEEGPGTL------DFNALMEQASDEFDIEWTDRE 205
|
170 180
....*....|....*....|....*.
gi 2786809754 177 sgngDLANILYTSGTTGDSKGVMLHH 202
Cdd:PRK04319 206 ----DGAILHYTSGSTGKPKGVLHVH 227
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
412-520 |
5.66e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 52.42 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 GENNEIMLRGEGITHGYYKKEAATKAAF----------------TEDG-WFHTGDAGYIKDEHLFLTERIKDLFkTSNGK 474
Cdd:PRK07769 416 GQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegaPDDAlWVRTGDYGVYFDGELYITGRVKDLV-IIDGR 494
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2786809754 475 YIAPQAIEaklvvdrYIDQISIIADERKFVSALIIPEYKLVKEYAD 520
Cdd:PRK07769 495 NHYPQDLE-------YTAQEATKALRTGYVAAFSVPANQLPQVVFD 533
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
181-475 |
5.77e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 52.59 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFP-QLGDQDVIMnFLPFThVFERAwtcwcLSMGCTL-SINL-RPA 257
Cdd:PRK09274 175 DMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGiEPGEIDLPT-FPLFA-LFGPA-----LGMTSVIpDMDPtRPA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 258 --DIQKTIKEIRP---TAMCSVPRFWEKVyagvqekinettglkkklmldaikvGREhnleyvykgltpppvlhmkykfy 332
Cdd:PRK09274 248 tvDPAKLFAAIERygvTNLFGSPALLERL-------------------------GRY----------------------- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 333 ektiysllkktiGIENGRFFPT------AGAAIPPAVQE-F--VLSVGINMVAGYGLTES------------TATVA--- 388
Cdd:PRK09274 280 ------------GEANGIKLPSlrrvisAGAPVPIAVIErFraMLPPDAEILTPYGATEAlpissiesreilFATRAatd 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 389 -----CendydhvvgsVGRLMPHVQVKI-------------------GENNEIMLRGEGITHGYYKKEAATKAAFTEDG- 443
Cdd:PRK09274 348 ngagiC----------VGRPVDGVEVRIiaisdapipewddalrlatGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGq 417
|
330 340 350
....*....|....*....|....*....|....*.
gi 2786809754 444 ---WFHTGDAGYIKDE-HLFLTERIKDLFKTSNGKY 475
Cdd:PRK09274 418 gdvWHRMGDLGYLDAQgRLWFCGRKAHRVETAGGTL 453
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
168-460 |
7.60e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 51.99 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 168 AEVDKRISESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFTH---VFerawTCWCL 244
Cdd:PRK07867 140 RDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRF-GLGPDDVCYVSMPLFHsnaVM----AGWAV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 245 SMGCTLSINLRpadiqktikeirptAMCSVPRFWEKVyagvqEKINETTglkkklmldAIKVGREhnLEYVykgLTPPPV 324
Cdd:PRK07867 215 ALAAGASIALR--------------RKFSASGFLPDV-----RRYGATY---------ANYVGKP--LSYV---LATPER 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 325 -------LHMKYkfyektiysllkktiGIEngrffptagaAIPPAVQEFVLSVGINMVAGYGLTEstATVACENDYDHVV 397
Cdd:PRK07867 262 pddadnpLRIVY---------------GNE----------GAPGDIARFARRFGCVVVDGFGSTE--GGVAITRTPDTPP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 398 GSVGRLMPHVQV------------------------KIGEnnEIMLRGEGITHGYYKKEAATkAAFTEDGWFHTGDAGYi 453
Cdd:PRK07867 315 GALGPLPPGVAIvdpdtgtecppaedadgrllnadeAIGE--LVNTAGPGGFEGYYNDPEAD-AERMRGGVYWSGDLAY- 390
|
....*..
gi 2786809754 454 KDEHLFL 460
Cdd:PRK07867 391 RDADGYA 397
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
50-497 |
8.23e-07 |
|
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: 51.73 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 50 NALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGEQLqYDvafrvmqlg 129
Cdd:cd05969 15 NVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL-YE--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 130 sqlkriiifdrevKRDERDQTSIyfddflklgeghphqaevdkrisesgngdlaniLYTSGTTGDSKGVMLHHSCYEAAI 209
Cdd:cd05969 85 -------------RTDPEDPTLL---------------------------------HYTSGTTGTPKGVLHVHDAMIFYY 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 210 PAHNERFpQLGDQDVimnflpFTHVFERAW---------TCWClsMGCTLSINLRPADIQK---TIKEIRPTAMCSVPrf 277
Cdd:cd05969 119 FTGKYVL-DLHPDDI------YWCTADPGWvtgtvygiwAPWL--NGVTNVVYEGRFDAESwygIIERVKVTVWYTAP-- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 278 wekvyagvqekinetTGLKKkLMLDAIKVGREHNLEYVykgltpppvlhmkykfyektiysllkktigiengRFFPTAGA 357
Cdd:cd05969 188 ---------------TAIRM-LMKEGDELARKYDLSSL----------------------------------RFIHSVGE 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 358 AIPPAVQEFVLSV-GINMVAGYGLTEsTATVACEN--DYDHVVGSVGRLMPHVQVKI----------GENNEIMLRGE-- 422
Cdd:cd05969 218 PLNPEAIRWGMEVfGVPIHDTWWQTE-TGSIMIANypCMPIKPGSMGKPLPGVKAAVvdengnelppGTKGILALKPGwp 296
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786809754 423 GITHGYYKKEAATKAAFTeDGWFHTGDAGYIKDEHLF-LTERIKDLFKTSnGKYIAPQAIEAKLVVDRYIDQISII 497
Cdd:cd05969 297 SMFRGIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFwFVGRADDIIKTS-GHRVGPFEVESALMEHPAVAEAGVI 370
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
371-454 |
1.25e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 51.89 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 371 GINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVK------IGENNEIMLRGEGITHGYYKKEAATKAAFTEDGW 444
Cdd:PRK06814 932 GIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRlepvpgIDEGGRLFVRGPNVMLGYLRAENPGVLEPPADGW 1011
|
90
....*....|....*.
gi 2786809754 445 FHTGD------AGYIK 454
Cdd:PRK06814 1012 YDTGDivtideEGFIT 1027
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
181-486 |
1.27e-06 |
|
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: 51.15 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 181 DLANILYTSGTTGDSKGVMLHHSCYeAAIPAHNERFPQLGDQDVIMNFLPFTHVFErAWTCW-CLSMGCTLSInlRPADI 259
Cdd:cd17643 94 DLAYVIYTSGSTGRPKGVVVSHANV-LALFAATQRWFGFNEDDVWTLFHSYAFDFS-VWEIWgALLHGGRLVV--VPYEV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 260 QKTikeirptamcsvPR-FWEKVYAGVQEKINETTGLKKKLMLDAIKVGREH-NLEYVYKGltpppvlhmkykfyektiy 337
Cdd:cd17643 170 ARS------------PEdFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPlALRYVIFG------------------- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 338 sllkktigiengrffptaGAAIPPAV-----QEFVLSVG--INMvagYGLTESTATV----ACENDYDHVVGSV-GRLMP 405
Cdd:cd17643 219 ------------------GEALEAAMlrpwaGRFGLDRPqlVNM---YGITETTVHVtfrpLDAADLPAAAASPiGRPLP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 406 HVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGW-------FHTGD-AGYIKDEHLFLTERIKDL 467
Cdd:cd17643 278 GLRVYVldadgrpvppGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDlARRLPDGELEYLGRADEQ 357
|
330
....*....|....*....
gi 2786809754 468 FKTsNGKYIAPQAIEAKLV 486
Cdd:cd17643 358 VKI-RGFRIELGEIEAALA 375
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-511 |
1.41e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.88 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDyktetwIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:PRK12316 516 LFEEQVERTPEAPALAFGE------ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYV 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAeiryifvgeqlqyDVAFRVMQlgSQLKRIIIFDREVKRDERDQTSIYFddflklgEGHPHQA 168
Cdd:PRK12316 590 PLDPEYPAERLAYMLEDS-------------GVQLLLSQ--SHLGRKLPLAAGVQVLDLDRPAAWL-------EGYSEEN 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 169 EVDKRISEsgngDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFT---HVFERAWTcwcLS 245
Cdd:PRK12316 648 PGTELNPE----NLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAY-GLGVGDTVLQKTPFSfdvSVWEFFWP---LM 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 246 MGCTLSI-----NLRPADIQKTIKEIRPTAMCSVPRfwekvyagvqekinettglkkklMLDAIkvgrehnleyvykgLT 320
Cdd:PRK12316 720 SGARLVVaapgdHRDPAKLVELINREGVDTLHFVPS-----------------------MLQAF--------------LQ 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 321 PPPVlhmkykfyeKTIYSLlkktigiengRFFPTAGAAIPPAVQEFV---LSVG--INMvagYGLTESTATVACENDYDH 395
Cdd:PRK12316 763 DEDV---------ASCTSL----------RRIVCSGEALPADAQEQVfakLPQAglYNL---YGPTEAAIDVTHWTCVEE 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 396 VVGSV--GRLMPHVQ----------VKIGENNEIMLRGEGITHGYYKKEAATKAAFTEDGW------FHTGD-AGYIKDE 456
Cdd:PRK12316 821 GGDSVpiGRPIANLAcyildanlepVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTGDlARYRADG 900
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2786809754 457 HLFLTERIKDLFKTsNGKYIAPQAIEAKLVVDRYIDQISIIADERKFVSALIIPE 511
Cdd:PRK12316 901 VIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLE 954
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-511 |
3.10e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.73 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:PRK12316 3062 LFEEQVERTPDAVALAFGEQR------LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYV 3135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAFRVMQLgsqlkriiifdrEVKRDERDqtsiyfddflkLGEGHPHqa 168
Cdd:PRK12316 3136 PLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVL------------DLDRGDEN-----------YAEANPA-- 3190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 169 evdkriSESGNGDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFTHVFERAWTCWCLSMGC 248
Cdd:PRK12316 3191 ------IRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAY-GLGVGDRVLQFTTFSFDVFVEELFWPLMSGA 3263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 249 T--LSINLRPADIQKTIKEIRPTAMCSVPRFWEKVYAGVQEKINETTGLKKKLMLdaikvgrehnleyvykgltpppvlh 326
Cdd:PRK12316 3264 RvvLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVC------------------------- 3318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 327 mkykfyektiysllkktigiengrffptAGAAIPPAVQEFVLSvGINMVAGYGLTESTATVACENDYDHVVGS--VGRLM 404
Cdd:PRK12316 3319 ----------------------------GGEALPADLQQQVFA-GLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPI 3369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 405 PHVQ----------VKIGENNEIMLRGEGITHGYYKKEAATKAAFTEDGW------FHTGD-AGYIKDEHLFLTERIKDL 467
Cdd:PRK12316 3370 ANRAcyildgslepVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDlARYRADGVIEYIGRVDHQ 3449
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2786809754 468 FKTsNGKYIAPQAIEAKLVVDRYIDQISIIADERKFVSALIIPE 511
Cdd:PRK12316 3450 VKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPE 3492
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-452 |
4.59e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.96 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 2 SSSFLSVLIQRQARKYGDRVVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAF 81
Cdd:PRK12316 2001 RGPGVHQRIAEQAARAPEAIAVVFGDQH------LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVL 2074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 82 GVRAVTVPFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDvafrvMQLGSQLKRIIiFDREVKRDERDQTsiyfddflklg 161
Cdd:PRK12316 2075 KAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLER-----LPLPAGVARLP-LDRDAEWADYPDT----------- 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 162 egHPhQAEVDKRisesgngDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFThvFERA-WT 240
Cdd:PRK12316 2138 --AP-AVQLAGE-------NLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFS--FDGAhEQ 2204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 241 C-WCLSMGCTLSInlRPADI---QKTIKEIRP---TAMCSVPRFWEKVyagvqekinettglkkklmldAIKVGREHNle 313
Cdd:PRK12316 2205 WfHPLLNGARVLI--RDDELwdpEQLYDEMERhgvTILDFPPVYLQQL---------------------AEHAERDGR-- 2259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 314 yvykgltPPPVlhmkykfyektiysllkktigiengRFFPTAGAAIPPAVQEFVLSV--GINMVAGYGLTESTATV---- 387
Cdd:PRK12316 2260 -------PPAV-------------------------RVYCFGGEAVPAASLRLAWEAlrPVYLFNGYGPTEAVVTPllwk 2307
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786809754 388 -----ACENDYDHVVGSVGRLMPHV------QVKIGENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGY 452
Cdd:PRK12316 2308 crpqdPCGAAYVPIGRALGNRRAYIldadlnLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLY 2383
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
180-485 |
4.73e-06 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 49.17 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 180 GDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFThvFERAWTCWCLSMGCTLSINLRPADi 259
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAF-DVGPGSRVLQFASPS--FDASVWELLMALLAGATLVLAPAE- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 260 qktikEIRPTAmcsvprfwekvyagvqekinettglkkklmlDAIKVGREHNLEYVykgLTPPPVLhmkykfyektiySL 339
Cdd:cd17652 169 -----ELLPGE-------------------------------PLADLLREHRITHV---TLPPAAL------------AA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 340 LKKTiGIENGRFFPTAGAAIPPA-VQEFvlSVGINMVAGYGLTEST--ATVA-CENDYDHVvgSVGRLMPHVQVKI---- 411
Cdd:cd17652 198 LPPD-DLPDLRTLVVAGEACPAElVDRW--APGRRMINAYGPTETTvcATMAgPLPGGGVP--PIGRPVPGTRVYVldar 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 ------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGW-------FHTGD-AGYIKDEHLFLTERIKDLFKTsNGKYIA 477
Cdd:cd17652 273 lrpvppGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDlARWRADGQLEFLGRADDQVKI-RGFRIE 351
|
....*...
gi 2786809754 478 PQAIEAKL 485
Cdd:cd17652 352 LGEVEAAL 359
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
9-485 |
5.23e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 49.77 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:PRK12467 517 LIEAQARQHPERPALVFGEQV------LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYV 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVGEqlqydvafrvmqlgSQLKRIIIFDrevkrderDQTSIYFDDFLKLGEGHP-HQ 167
Cdd:PRK12467 591 PLDPEYPQDRLAYMLDDSGVRLLLTQS--------------HLLAQLPVPA--------GLRSLCLDEPADLLCGYSgHN 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 168 AEVdkrisESGNGDLANILYTSGTTGDSKGVMLHHSC---YEAAIpahnERFPQLGDQDVIMNFLPFTHVFERAWTCWCL 244
Cdd:PRK12467 649 PEV-----ALDPDNLAYVIYTSGSTGQPKGVAISHGAlanYVCVI----AERLQLAADDSMLMVSTFAFDLGVTELFGAL 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 245 SMGCTLSI-----NLRPADIQKTIKEIRPTAMCSVPRFWekvyagvqekinettglkkKLMLDAIKVGREHNLEYVYKGl 319
Cdd:PRK12467 720 ASGATLHLlppdcARDAEAFAALMADQGVTVLKIVPSHL-------------------QALLQASRVALPRPQRALVCG- 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 320 tpppvlhmkykfyektiysllkktigiengrffptaGAAIPPA--VQEFVLSVGINMVAGYGLTESTATVA----CENDY 393
Cdd:PRK12467 780 ------------------------------------GEALQVDllARVRALGPGARLINHYGPTETTVGVStyelSDEER 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 394 DHVVGSVGRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGW-------FHTGD-AGYIKD 455
Cdd:PRK12467 824 DFGNVPIGQPLANLGLYIldhylnpvpvGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYRTGDlARYRAD 903
|
490 500 510
....*....|....*....|....*....|
gi 2786809754 456 EHLFLTERIKDLFKTsNGKYIAPQAIEAKL 485
Cdd:PRK12467 904 GVIEYLGRMDHQVKI-RGFRIELGEIEARL 932
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
180-511 |
7.18e-06 |
|
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: 48.88 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 180 GDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFPqLGDQDVIMNFLPFThvFERA-WTCW-CLSMGCTLSinLRPA 257
Cdd:cd17651 136 DDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASS-LGPGARTLQFAGLG--FDVSvQEIFsTLCAGATLV--LPPE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 258 diqktikEIRPtamcSVPRFWEKVyagvqekinettglkkklmldaikvgREHNLEYVYkglTPPPVLHmkykfyektiy 337
Cdd:cd17651 211 -------EVRT----DPPALAAWL--------------------------DEQRISRVF---LPTVALR----------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 338 SLLkktigiENGRFFPTAGAA------------IPPAVQEFVLSV-GINMVAGYGLTESTATVACENDYDHV----VGSV 400
Cdd:cd17651 240 ALA------EHGRPLGVRLAAlrylltggeqlvLTEDLREFCAGLpGLRLHNHYGPTETHVVTALSLPGDPAawpaPPPI 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 401 GRLMPHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGW------FHTGD-AGYIKDEHLFLTER 463
Cdd:cd17651 314 GRPIDNTRVYVldaalrpvppGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDlARWLPDGELEFLGR 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2786809754 464 IKDLFKTsNGKYIAPQAIEAKLVVDRYIDQISIIADER----KFVSALIIPE 511
Cdd:cd17651 394 ADDQVKI-RGFRIELGEIEAALARHPGVREAVVLAREDrpgeKRLVAYVVGD 444
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
371-461 |
2.17e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 47.40 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 371 GINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVK------IGENNEIMLRGEGITHGYYKKE---------AAT 435
Cdd:PRK08043 504 GLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARllsvpgIEQGGRLQLKGPNIMNGYLRVEkpgvlevptAEN 583
|
90 100
....*....|....*....|....*.
gi 2786809754 436 KAAFTEDGWFHTGDAGYIkDEHLFLT 461
Cdd:PRK08043 584 ARGEMERGWYDTGDIVRF-DEQGFVQ 608
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
416-483 |
2.37e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 47.24 E-value: 2.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786809754 416 EIMLRGEGITHGYYKKEAATKAAF----------TEDG-WFHTGDAGYIKDEHLFLTERIKDLFkTSNGKYIAPQAIEA 483
Cdd:PRK05850 399 EIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFISEGELFIVGRIKDLL-IVDGRNHYPDDIEA 476
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
412-511 |
2.72e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 47.04 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 412 GENNEIMLRGEGITHGYY----------------KKEAATKAAFTEDG--WFHTGDAGYIKDEHLFLTERIKDLFkTSNG 473
Cdd:PRK12476 427 GEVGEIWLHGDNIGRGYWgrpeetertfgaklqsRLAEGSHADGAADDgtWLRTGDLGVYLDGELYITGRIADLI-VIDG 505
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2786809754 474 KYIAPQAIEAKL-----VVDR-YIDQISIIADERKFVsaLIIPE 511
Cdd:PRK12476 506 RNHYPQDIEATVaeaspMVRRgYVTAFTVPAEDNERL--VIVAE 547
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
354-535 |
8.22e-05 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 45.79 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 354 TAGAAIPPAVQEFVLSV--GINMVAGYGLTESTATVACENDYDHVVGSVGRLMPHVQVKI----------GENNEIMLRG 421
Cdd:PRK06060 267 SAGEALELGLAERLMEFfgGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVvapdgttagpGVEGDLWVRG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 422 EGITHGYYKKeaaTKAAFTEDGWFHTGDAGYIKDEHLFLTERIKDLFKTSNGKYIAPQAIEAKLVVDRYIDQISIIAdER 501
Cdd:PRK06060 347 PAIAKGYWNR---PDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVA-VR 422
|
170 180 190
....*....|....*....|....*....|....
gi 2786809754 502 KFVSALIIPEYkLVKeyADKKGIHYGSMEDLLRK 535
Cdd:PRK06060 423 ESTGASTLQAF-LVA--TSGATIDGSVMRDLHRG 453
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
9-202 |
1.36e-04 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 44.79 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRY--RDYKTETWipvSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAV 86
Cdd:cd05968 66 LLDKWLADTRTRPALRWegEDGTSRTL---TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 87 TVPFYATSSEAQVHYMVGDAEIRYIFVGEQLQ--------YDVAFRVMQLGSQLKRIIIfDREVKRDERDQTS--IYFDD 156
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQDAEAKALITADGFTrrgrevnlKEEADKACAQCPTVEKVVV-VRHLGNDFTPAKGrdLSYDE 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2786809754 157 FLklgEGHPHQAEvdkrisESGNGDLANILYTSGTTGDSKGVMLHH 202
Cdd:cd05968 222 EK---ETAGDGAE------RTESEDPLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
9-275 |
1.83e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 44.77 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVVLRYRDYKtetwipVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:PRK12467 1579 LIEDQAAATPEAVALVFGEQE------LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYV 1652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVGEQLQYDVAfrvmqLGSQLkRIIIFDREvkrderdqtsiyfDDFLklgEGHPhqa 168
Cdd:PRK12467 1653 PLDPEYPRERLAYMIEDSGIELLLTQSHLQARLP-----LPDGL-RSLVLDQE-------------DDWL---EGYS--- 1707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 169 EVDKRISESGNgDLANILYTSGTTGDSKGVMLHHSCYEAAIPAHNERFpQLGDQDVIMNFLPFTHVFERAWTCWCLSMGC 248
Cdd:PRK12467 1708 DSNPAVNLAPQ-NLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAY-QLSAADVVLQFTSFAFDVSVWELFWPLINGA 1785
|
250 260 270
....*....|....*....|....*....|..
gi 2786809754 249 TL-----SINLRPADIQKTIKEIRPTAMCSVP 275
Cdd:PRK12467 1786 RLviappGAHRDPEQLIQLIERQQVTTLHFVP 1817
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
350-482 |
1.97e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 44.37 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 350 RFFPTAGAAIPpavqefvlsvginmvaGYGLTESTATVAC---------------ENDYDHVVGSVGRLMPHVQVKIG-- 412
Cdd:PRK05851 298 PFGFDAGAAAP----------------SYGLAESTCAVTVpvpgiglrvdevttdDGSGARRHAVLGNPIPGMEVRISpg 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786809754 413 ---------ENNEIMLRGEGITHGYYKKeaatkAAFTEDGWFHTGDAGYIKDEHLFLTERIKDLFkTSNGKYIAPQAIE 482
Cdd:PRK05851 362 dgaagvagrEIGEIEIRGASMMSGYLGQ-----APIDPDDWFPTGDLGYLVDGGLVVCGRAKELI-TVAGRNIFPTEIE 434
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
9-485 |
2.16e-04 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 43.96 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 9 LIQRQARKYGDRVvlrYRDyktetwIPVSWNQFAATVKTVSNALIELGIGIQENIAVFSQNKPECLYVDFGAFGVRAVTV 88
Cdd:cd05915 7 LFGRKEVVSRLHT---GEV------HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 89 PFYATSSEAQVHYMVGDAEIRYIFVGEQLqYDVAFRVMQLGSQlkriiIFDREVKRDERDQtsiyFDDFLKlgEGHPHQa 168
Cdd:cd05915 78 TANPRLSPKEIAYILNHAEDKVLLFDPNL-LPLVEAIRGELKT-----VQHFVVMDEKAPE----GYLAYE--EALGEE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 169 evdKRISESGNGDLANILYTSGTTGDSKGVML-HHSCY--EAAIPAHNERFPQlgDQDVIMNFLPFTHVfeRAWT-CWCL 244
Cdd:cd05915 145 ---ADPVRVPERAACGMAYTTGTTGLPKGVVYsHRALVlhSLAASLVDGTALS--EKDVVLPVVPMFHV--NAWClPYAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 245 SMGCTLSINLRPADIQKTIKEirptamcSVPRFWEKVYAGVQEKINETTGLKkklmlDAIKVGREHNLEYVYKGLTPPPV 324
Cdd:cd05915 218 TLVGAKQVLPGPRLDPASLVE-------LFDGEGVTFTAGVPTVWLALADYL-----ESTGHRLKTLRRLVVGGSAAPRS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 325 LhMKykfyektiyslLKKTigienGRFfptagaaippavqEFVLSVGINMVAGYGLT------------ESTATVACEND 392
Cdd:cd05915 286 L-IA-----------RFER-----MGV-------------EVRQGYGLTETSPVVVQnfvkshleslseEEKLTLKAKTG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 393 YDHVVGSVGRLMPhVQVKIGENNE----IMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYIK-DEHLFLTERIKDL 467
Cdd:cd05915 336 LPIPLVRLRVADE-EGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDeEGYVEIKDRLKDL 414
|
490
....*....|....*...
gi 2786809754 468 FkTSNGKYIAPQAIEAKL 485
Cdd:cd05915 415 I-KSGGEWISSVDLENAL 431
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
378-510 |
2.34e-04 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 43.83 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 378 YGLTESTATVACENDYDHVVG--SVGRLMPHVQVKIGENN--EIMLRGEGITHGYYkkeaatKAAFTEDGWFHTGDAGYI 453
Cdd:PRK07445 261 YGMTETASQIATLKPDDFLAGnnSSGQVLPHAQITIPANQtgNITIQAQSLALGYY------PQILDSQGIFETDDLGYL 334
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2786809754 454 -KDEHLFLTERIKDLFkTSNGKYIAPQAIEAKLVVDRYIDQISII--ADER--KFVSALIIP 510
Cdd:PRK07445 335 dAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATGLVQDVCVLglPDPHwgEVVTAIYVP 395
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
180-250 |
4.26e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.54 E-value: 4.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2786809754 180 GDLANILYTSGTTGDSKGVMLHHScyeaaipAHNERFP------QLGDQDVIMNFLPFThvFE-RAWTC-WCLSMGCTL 250
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHA-------ALAERLQwmqatyALDDSDVLMQKAPIS--FDvSVWECfWPLITGCRL 1342
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
394-514 |
5.84e-03 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 39.59 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786809754 394 DHVVGSVGRLM-PHVQVKI----------GENNEIMLRGEGITHGYYKKEAATKAAFTEDGWFHTGDAGYI-KDEHLFLT 461
Cdd:PRK10946 349 ERIFTTQGRPMsPDDEVWVadadgnplpqGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIdPDGYITVV 428
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2786809754 462 ERIKDLFkTSNGKYIA-----------PQAIEAKLV--VDRYIDQIS---IIADE-------RKFVSALIIPEYKL 514
Cdd:PRK10946 429 GREKDQI-NRGGEKIAaeeienlllrhPAVIHAALVsmEDELMGEKScafLVVKEplkavqlRRFLREQGIAEFKL 503
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
175-202 |
6.13e-03 |
|
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: 39.38 E-value: 6.13e-03
10 20
....*....|....*....|....*...
gi 2786809754 175 SESGNGDLANILYTSGTTGDSKGVMLHH 202
Cdd:cd17656 123 YINNSDDLLYIIYTSGTTGKPKGVQLEH 150
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
181-202 |
7.17e-03 |
|
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: 39.31 E-value: 7.17e-03
|
| |
