|
Name |
Accession |
Description |
Interval |
E-value |
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
54-471 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 603.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 54 QPGSYPALSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTgKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERD 133
Cdd:TIGR02188 3 NLEQYKELYEESIEDPDKFWAKLARELLDWFKPFTKVLDWSFPP-FYKWFVGGELNVSYNCVDRHLEARPDKVAIIWEGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 134 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARI------------------------- 188
Cdd:TIGR02188 82 EPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIgaihsvvfggfsaealadrindaga 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 --------------------------------------------------------------------------------
Cdd:TIGR02188 162 klvitadeglrggkviplkaivdealekcpvsvehvlvvrrtgnpvvpwvegrdvwwhdlmakasaycepepmdsedplf 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 189 ------------GAVHT--------------------------------------------------VIFAGFSAESLAG 206
Cdd:TIGR02188 242 ilytsgstgkpkGVLHTtggyllyaamtmkyvfdikdgdifwctadvgwitghsyivygplangattVMFEGVPTYPDPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 207 RIND-----------------------------------------VGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGG 245
Cdd:TIGR02188 322 RFWEiiekhkvtifytaptairalmrlgdewvkkhdlsslrllgsVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 246 ICIAPRPSeeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYF 325
Cdd:TIGR02188 402 IMITPLPG--ATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 326 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQ 405
Cdd:TIGR02188 480 TGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRK 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 406 ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEILS 471
Cdd:TIGR02188 560 ELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELIE 625
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
57-462 |
0e+00 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 597.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 57 SYPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEPG 136
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKE-LDWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 137 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDV----- 211
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAqcklv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 212 ---------GEPIN------------------------------------------------CEA--------------- 219
Cdd:cd05966 161 itadggyrgGKVIPlkeivdealekcpsvekvlvvkrtggevpmtegrdlwwhdlmakqspeCEPewmdsedplfilyts 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 220 -----------------------------------------------------------------------------WE- 221
Cdd:cd05966 241 gstgkpkgvvhttggyllyaattfkyvfdyhpddiywctadigwitghsyivygplangattvmfegtptypdpgryWDi 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 222 -------------------------------------------------WL--HRVVGDSRCTLVDTWWQTETGGICIAP 250
Cdd:cd05966 321 vekhkvtifytaptairalmkfgdewvkkhdlsslrvlgsvgepinpeaWMwyYEVIGKERCPIVDTWWQTETGGIMITP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 251 RPSEegAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGA 330
Cdd:cd05966 401 LPGA--TPLKPGSATRPFFGIEPAILDEEGNEVEG-EVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 331 YRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSM 410
Cdd:cd05966 478 RRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKH 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 578835624 411 VATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAqELGDTTTLED 462
Cdd:cd05966 558 VRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEE-ELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
58-477 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 522.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 58 YPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDfsTGKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEPGT 137
Cdd:PRK00174 19 YKALYQESVEDPEGFWAEQAKR-LDWFKPFDTVLDWN--APFIKWFEDGELNVSYNCLDRHLKTRGDKVAIIWEGDDPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDV------ 211
Cdd:PRK00174 96 SRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAgaklvi 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 212 -------------------------------------GEPIN-------------------CEAwEWL------------ 223
Cdd:PRK00174 176 tadegvrggkpiplkanvdealancpsvekvivvrrtGGDVDwvegrdlwwhelvagasdeCEP-EPMdaedplfilyts 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 --------------------------------------------------------------------------------
Cdd:PRK00174 255 gstgkpkgvlhttggylvyaamtmkyvfdykdgdvywctadvgwvtghsyivygplangattlmfegvpnypdpgrfwev 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 224 ---HRV--------------------------------------------------VGDSRCTLVDTWWQTETGGICIAP 250
Cdd:PRK00174 335 idkHKVtifytaptairalmkegdehpkkydlsslrllgsvgepinpeawewyykvVGGERCPIVDTWWQTETGGIMITP 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 251 RPseeGA-EILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDG 329
Cdd:PRK00174 415 LP---GAtPLKPGSATRPLPGIQPAVVDEEGNPLEG-GEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDG 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 330 AYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKS 409
Cdd:PRK00174 491 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRN 570
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578835624 410 MVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAqELGDTTTLEDPSIIAEILSVYQKCK 477
Cdd:PRK00174 571 WVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-ILGDTSTLADPSVVEKLIEARQNRK 637
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
102-469 |
2.12e-145 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 427.99 E-value: 2.12e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 102 WFLGGQLNVSVNCLDQHVRKSPESVALIWErDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAA 181
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHAEGRGDKVALIWE-GEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 182 MLACARIGAVHTVIFAGFSAESLAGRIND-------------------------------------------VGEPINCE 218
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDaeakvlitadgglrggkvidlkekvdealeelpslehvivvgrTGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 219 AWEWLHRVVGDSR------------------------------------------------------------------- 231
Cdd:COG0365 161 GDLDWDELLAAASaefepeptdaddplfilytsgttgkpkgvvhthggylvhaattakyvldlkpgdvfwctadigwatg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 --------------------------------------------------------------------------------
Cdd:COG0365 241 hsyivygpllngatvvlyegrpdfpdpgrlweliekygvtvfftaptairalmkagdeplkkydlsslrllgsageplnp 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 232 -----------CTLVDTWWQTETGGICIAPRPseeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPG 300
Cdd:COG0365 321 evwewwyeavgVPIVDGWGQTETGGIFISNLP---GLPVKPGSMGKPVPGYDVAVVDEDGNPVPP-GEEGELVIKGPWPG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 301 MARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPH 380
Cdd:COG0365 397 MFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 381 DIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItsEAQELGDTTTL 460
Cdd:COG0365 477 EIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA--EGRPLGDTSTL 554
|
....*....
gi 578835624 461 EDPSIIAEI 469
Cdd:COG0365 555 EDPEALDEI 563
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
55-472 |
1.45e-104 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 326.08 E-value: 1.45e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 55 PGSYPALSAQAAREPAAFWGPLArDTLVWDTPYHTVWDC----DFSTG--KIGWFLGGQLNVSVNCLDQHVRK-SPESVA 127
Cdd:PLN02654 29 PQQYMEMYKRSVDDPAGFWSDIA-SQFYWKQKWEGDEVCsenlDVRKGpiSIEWFKGGKTNICYNCLDRNVEAgNGDKIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 128 LIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYM------PVSPLAV---------------------- 179
Cdd:PLN02654 108 IYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLpmlmelPIAMLACarigavhsvvfagfsaeslaqr 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 180 -----------------------------AAMLACAR------------------------------------------- 187
Cdd:PLN02654 188 ivdckpkvvitcnavkrgpktinlkdivdAALDESAKngvsvgicltyenqlamkredtkwqegrdvwwqdvvpnyptkc 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 188 -----------------------IGAVHT--------------------------------------------------V 194
Cdd:PLN02654 268 evewvdaedplfllytsgstgkpKGVLHTtggymvytattfkyafdykptdvywctadcgwitghsyvtygpmlngatvL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 195 IFAGFSAESLAGRIND-----------------------------------------VGEPINCEAWEWLHRVVGDSRCT 233
Cdd:PLN02654 348 VFEGAPNYPDSGRCWDivdkykvtifytaptlvrslmrdgdeyvtrhsrkslrvlgsVGEPINPSAWRWFFNVVGDSRCP 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 234 LVDTWWQTETGGICIAPRPseeGAEIL-PAMAMRPFFGIVPVLMDEKGSVVEGSnVSGALCISQAWPGMARTIYGDHQRF 312
Cdd:PLN02654 428 ISDTWWQTETGGFMITPLP---GAWPQkPGSATFPFFGVQPVIVDEKGKEIEGE-CSGYLCVKKSWPGAFRTLYGDHERY 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 313 VDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIV 392
Cdd:PLN02654 504 ETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVT 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 393 VKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEILSV 472
Cdd:PLN02654 584 LVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTSTLADPGVVDQLIAL 663
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
58-469 |
4.99e-96 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 302.31 E-value: 4.99e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 58 YPALSAQAAREPAAFWGPLARdTLVWDTPYHTVWDCDfSTGKIGWFLGGQLNVSVNCLDQHVRKS-PESVALIWERDEPG 136
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQAR-LIDWFKPPEKILDNS-NPPFTRWFVGGRLNTCYNALDRHVEAGrGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 137 TEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDV----- 211
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAkpkli 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 212 ---------GEPI--------------------------NCEA----------WEWLHR--------------------- 225
Cdd:cd05967 159 vtascgiepGKVVpykplldkalelsghkphhvlvlnrpQVPAdltkpgrdldWSELLAkaepvdcvpvaatdplyilyt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 226 ---------VVGDSRCTLV---------------DTWW------------------------------------------ 239
Cdd:cd05967 239 sgttgkpkgVVRDNGGHAValnwsmrniygikpgDVWWaasdvgwvvghsyivygpllhgattvlyegkpvgtpdpgafw 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 240 ----------------------------------------------------------------------QTETGG---- 245
Cdd:cd05967 319 rviekyqvnalftaptairairkedpdgkyikkydlsslrtlflagerldpptlewaentlgvpvidhwwQTETGWpita 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 246 --ICIAPRPSEEGAEILPAMAMRpffgiVPVLmDEKGSVVeGSNVSGALCISQAW-PGMARTIYGDHQRFVDAYFKAYPG 322
Cdd:cd05967 399 npVGLEPLPIKAGSPGKPVPGYQ-----VQVL-DEDGEPV-GPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 323 YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSD 401
Cdd:cd05967 472 YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKiTAE 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItsEAQELGDTTTLEDPSIIAEI 469
Cdd:cd05967 552 ELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA--DGEDYTIPSTIEDPSVLDEI 617
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
64-439 |
3.62e-95 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 299.49 E-value: 3.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 64 QAAREPAAFWGPLARDtLVWDTPYHTVWDCDFSTGK--IGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEpGTEVR- 140
Cdd:cd17634 7 QSINDPDTFWGEAGKI-LDWITPYQKVKNTSFAPGApsIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDD-TSQSRt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAML--------------------ACARI------------ 188
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLacarigavhsvifggfapeaVAGRIidsssrllitad 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 --------------------------------------------------------------------------------
Cdd:cd17634 165 ggvragrsvplkknvddalnpnvtsvehvivlkrtgsdidwqegrdlwwrdliakaspehqpeamnaedplfilytsgtt 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 189 ----GAVH--------------------------------------------------TVIFAGFSAESLAGRINDV--- 211
Cdd:cd17634 245 gkpkGVLHttggylvyaattmkyvfdygpgdiywctadvgwvtghsyllygplacgatTLLYEGVPNWPTPARMWQVvdk 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 212 --------------------------------------GEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPs 253
Cdd:cd17634 325 hgvnilytaptairalmaagddaiegtdrsslrilgsvGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLP- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 254 eeGAEILPA-MAMRPFFGIVPVLMDEKGSVVEGSNVsGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYR 332
Cdd:cd17634 404 --GAIELKAgSATRPVFGVQPAVVDNEGHPQPGGTE-GNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 333 TEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVA 412
Cdd:cd17634 481 DEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVR 560
|
570 580
....*....|....*....|....*..
gi 578835624 413 TKIAKYAVPDEILVVKRLPKTRSGKVM 439
Cdd:cd17634 561 KEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
57-469 |
1.81e-79 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 259.50 E-value: 1.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 57 SYPALSAQAAREPAAFWGPLARdtLV-WDTPYHTVwdCDFSTGKIG-WFLGGQLNVSVNCLDQHVRKSPESVALIWERDE 134
Cdd:PRK10524 3 SYSEFYQRSIDDPEAFWAEQAR--RIdWQTPFTQV--LDYSNPPFArWFVGGRTNLCHNAVDRHLAKRPEQLALIAVSTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 135 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRIND---- 210
Cdd:PRK10524 79 TDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDakpv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 211 --------------------VGEPIN------------------------------------CEA---WEWLHR------ 225
Cdd:PRK10524 159 livsadagsrggkvvpykplLDEAIAlaqhkprhvllvdrglapmarvagrdvdyatlraqhLGArvpVEWLESnepsyi 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 226 ------------------------------------------------VVGDS----------RCTLV----------DT 237
Cdd:PRK10524 239 lytsgttgkpkgvqrdtggyavalatsmdtifggkagetffcasdigwVVGHSyivyapllagMATIMyeglptrpdaGI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 238 WW--------------------------------------------------------------------QTETGGICIA 249
Cdd:PRK10524 319 WWrivekykvnrmfsaptairvlkkqdpallrkhdlsslralflagepldeptaswisealgvpvidnywQTETGWPILA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 250 PRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAW-PGMARTIYGDHQRFVDAYFKAY-PGYYFTG 327
Cdd:PRK10524 399 IARGVEDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 328 DGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD-----V 402
Cdd:PRK10524 479 DWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADrearlA 558
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 403 VVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIitSEAQELGDTTTLEDPSIIAEI 469
Cdd:PRK10524 559 LEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAI--AEGRDPGDLTTIEDPAALQQI 623
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
56-463 |
8.78e-78 |
|
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: 254.72 E-value: 8.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 56 GSYPALSAQAAREPAAFWGPLARDTLVW--DTPYHTVwdcDFSTGK--IGWFLGGQLNVSVNCLDQHVRKSPESVALIWE 131
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGIEwyEPPYQTL---DLSGGKpwAAWFVGGRMNIVEQLLDKWLADTRTRPALRWE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 132 rDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARI----------------------- 188
Cdd:cd05968 84 -GEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIggivvpifsgfgkeaaatrlqda 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 --------------------------------------------------------------------------------
Cdd:cd05968 163 eakalitadgftrrgrevnlkeeadkacaqcptvekvvvvrhlgndftpakgrdlsydeeketagdgaertesedplmii 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 189 ----------GAVHT-------------------------------------VIFA------------------------ 197
Cdd:cd05968 243 ytsgttgkpkGTVHVhagfplkaaqdmyfqfdlkpgdlltwftdlgwmmgpwLIFGglilgatmvlydgapdhpkadrlw 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 198 -----------GFSA---ESLAGR---------------INDVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTE-TGGI- 246
Cdd:cd05968 323 rmvedheithlGLSPtliRALKPRgdapvnahdlsslrvLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEiSGGIl 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 247 -CIAPRPseegaeILPAMAMRPFFGIVPVLMDEKGSVVEGSnvSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYF 325
Cdd:cd05968 403 gNVLIKP------IKPSSFNGPVPGMKADVLDESGKPARPE--VGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 326 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQ 405
Cdd:cd05968 475 HGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAE 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 578835624 406 ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEaqELGDTTTLEDP 463
Cdd:cd05968 555 ELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
102-462 |
1.02e-65 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 221.69 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 102 WFLGGQLNVSVNCLDQHVrKSP--ESVALIWERdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAV 179
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHA-DGGrkDKVALRYLD--ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 180 AAMLACARIGAVHTVIFAGFSAESLAGRIND------------------------------------------------- 210
Cdd:PRK04319 113 FALLGALKNGAIVGPLFEAFMEEAVRDRLEDseakvlittpallerkpaddlpslkhvllvgedveegpgtldfnalmeq 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 --------------------------------------------------------------------------------
Cdd:PRK04319 193 asdefdiewtdredgailhytsgstgkpkgvlhvhnamlqhyqtgkyvldlheddvywctadpgwvtgtsygifapwlng 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 211 ----------------------------------------------------------VGEPINCEAWEWLHRVVGdsrC 232
Cdd:PRK04319 273 atnvidggrfsperwyriledykvtvwytaptairmlmgagddlvkkydlsslrhilsVGEPLNPEVVRWGMKVFG---L 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 233 TLVDTWWQTETGGICIAPRPSEEgaeILPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPGMARTIYGDHQRF 312
Cdd:PRK04319 350 PIHDNWWMTETGGIMIANYPAMD---IKPGSMGKPLPGIEAAIVDDQGNELP-PNRMGNLAIKKGWPSMMRGIWNNPEKY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 313 vDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIV 392
Cdd:PRK04319 426 -ESYFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVA 502
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578835624 393 VKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRkiitseAQEL----GDTTTLED 462
Cdd:PRK04319 503 LRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK------AWELglpeGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
208-446 |
8.56e-64 |
|
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: 213.13 E-value: 8.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 208 INDVGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPseeGAEILPAMAMRPFFGIVPVLMDEKGSVVEgSN 287
Cdd:cd05969 212 IHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIANYP---CMPIKPGSMGKPLPGVKAAVVDENGNELP-PG 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 288 VSGALCISQAWPGMARTIYGDHQRFvDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH 367
Cdd:cd05969 285 TKGILALKPGWPSMFRGIWNDEERY-KNSFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEH 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578835624 368 PAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 446
Cdd:cd05969 362 PAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
142-445 |
7.30e-55 |
|
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: 189.47 E-value: 7.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 142 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRIND----------- 210
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAagakaivtdae 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 --------------------------------------------------------------------------------
Cdd:cd05972 82 dpaliyftsgttglpkgvlhthsyplghiptaaywlglrpddihwniadpgwakgawssffgpwllgatvfvyegprfda 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 211 -------------------------------------------VGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGgIC 247
Cdd:cd05972 162 erilellerygvtsfcgpptayrmlikqdlssykfshlrlvvsAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-LT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 248 IAPRPseeGAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAWPGMARTiYGDHQRFVDAYFKAypGYYFTG 327
Cdd:cd05972 238 VGNFP---DMPVKPGSMGRPTPGYDVAIIDDDGREL-PPGEEGDIAIKLPPPGLFLG-YVGDPEKTEASIRG--DYYLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 328 DGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQEL 407
Cdd:cd05972 311 DRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEEL 390
|
410 420 430
....*....|....*....|....*....|....*...
gi 578835624 408 KSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd05972 391 QGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
115-453 |
2.41e-54 |
|
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: 188.48 E-value: 2.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:COG0318 5 LRRAAARHPDRPALVFG------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 195 IFAGFSAESLAGRINDV-----------------GEP-----------INCEAWEWLHRVVGDSR--------------- 231
Cdd:COG0318 79 LNPRLTAEELAYILEDSgaralvtalilytsgttGRPkgvmlthrnllANAAAIAAALGLTPGDVvlvalplfhvfgltv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 232 ---------CTLV-------DTWW-------------------------------------------------------- 239
Cdd:COG0318 159 gllapllagATLVllprfdpERVLelierervtvlfgvptmlarllrhpefarydlsslrlvvsggaplppellerfeer 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 240 ----------QTETGGICIAPRpsEEGAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD- 308
Cdd:COG0318 239 fgvrivegygLTETSPVVTVNP--EDPGERRPGSVGRPLPGVEVRIVDEDGREL-PPGEVGEIVVRG--PNVMKGYWNDp 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 309 ---HQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 385
Cdd:COG0318 314 eatAEAFRD-------GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGE 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578835624 386 AAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 453
Cdd:COG0318 387 RVVAFVVLRP---GAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
139-439 |
3.66e-45 |
|
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: 160.91 E-value: 3.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 139 VRITYRELLettCRLANTLKRHGVHRGDRVAIYMPVSPLA-VAAMLACARIGAVHtVIFAGFSAESLAGRIND------- 210
Cdd:cd04433 18 VVLSHRNLL---AAAAALAASGGLTEGDVFLSTLPLFHIGgLFGLLGALLAGGTV-VLLPKFDPEAALELIERekvtill 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 211 ----------------------------VGEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGICIAPRPSEEgaEILPA 262
Cdd:cd04433 94 gvptllarllkapesagydlsslralvsGGAPLPPELLERFEEAPG---IKLVNGYGLTETGGTVATGPPDDD--ARKPG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 263 MAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPGMARTIYGDHQRFVDayfkaYPGYYFTGDGAYRTEGGYYQITG 342
Cdd:cd04433 169 SVGRPVPGVEVRIVDPDGGELPP-GEIGELVVRGPSVMKGYWNNPEATAAVD-----EDGWYRTGDLGRLDEDGYLYIVG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 343 RMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPD 422
Cdd:cd04433 243 RLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA---DLDAEELRAHVRERLAPYKVPR 319
|
330
....*....|....*..
gi 578835624 423 EILVVKRLPKTRSGKVM 439
Cdd:cd04433 320 RVVFVDALPRTASGKID 336
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-444 |
2.05e-35 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 136.79 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 136 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRIND----- 210
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNsgasa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 211 ------------------VGEPINC-EAwewlHRVV-----------------GDSRCTLVDTWWQTETGGICIA----- 249
Cdd:cd05971 82 lvtdgsddpaliiytsgtTGPPKGAlHA----HRVLlghlpgvqfpfnlfprdGDLYWTPADWAWIGGLLDVLLPslyfg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 250 -------PRPSEEGAEI------------LPAMAMRPF-----------------------------------FGI---- 271
Cdd:cd05971 158 vpvlahrMTKFDPKAALdlmsrygvttafLPPTALKMMrqqgeqlkhaqvklraiatggeslgeellgwareqFGVevne 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 272 -------------VPVLMDEK----GSVVEGSNVS--------------GALCISQAWPGMARTiYGDHQRFVDAYFKAy 320
Cdd:cd05971 238 fygqtecnlvignCSALFPIKpgsmGKPIPGHRVAivddngtplppgevGEIAVELPDPVAFLG-YWNNPSATEKKMAG- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 321 pGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDS 400
Cdd:cd05971 316 -DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPS 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 578835624 401 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:cd05971 395 DALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
107-444 |
8.96e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 136.47 E-value: 8.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 107 QLNVSvNCLDQHVRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACA 186
Cdd:PRK06187 5 PLTIG-RILRHGARKHPDKEAVYFDGR------RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 187 RIGAV-HTV-IFagFSAESLAGRINDvgepinCEAwewlhRV--VGDS----------RCTLVDTWWQTETGGICIAPRP 252
Cdd:PRK06187 78 KIGAVlHPInIR--LKPEEIAYILND------AED-----RVvlVDSEfvpllaailpQLPTVRTVIVEGDGPAAPLAPE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 253 SEEGAEILPA------------------------------------------MAMRPFFG---------IVP-------- 273
Cdd:PRK06187 145 VGEYEELLAAasdtfdfpdidendaaamlytsgttghpkgvvlshrnlflhsLAVCAWLKlsrddvylvIVPmfhvhawg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 274 ------------VLMDE--KGSVV---EGSNVSGALCISQAWPGMAR--------------------------------- 303
Cdd:PRK06187 225 lpylalmagakqVIPRRfdPENLLdliETERVTFFFAVPTIWQMLLKaprayfvdfsslrlviyggaalppallrefkek 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 304 ------TIYG--------------DHQ-------------------RFVD-------------------------AYFKA 319
Cdd:PRK06187 305 fgidlvQGYGmtetspvvsvlppeDQLpgqwtkrrsagrplpgveaRIVDddgdelppdggevgeiivrgpwlmqGYWNR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 320 --------YPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 391
Cdd:PRK06187 385 peataetiDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVV 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 578835624 392 VVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK06187 465 VLKP---GATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
115-440 |
1.09e-34 |
|
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: 134.66 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV--- 191
Cdd:cd17631 1 LRRRARRHPDRTALVFG------GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVfvp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 192 ---------------------------------------------------------------------------HT--- 193
Cdd:cd17631 75 lnfrltppevayiladsgakvlfddlallmytsgttgrpkgamlthrnllwnavnalaaldlgpddvllvvaplfHIggl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 194 --------------VIFAGFSAESL-----AGRINDVGEP-------INCEAW-------------------EWLHRVVG 228
Cdd:cd17631 155 gvftlptllrggtvVILRKFDPETVldlieRHRVTSFFLVptmiqalLQHPRFattdlsslraviyggapmpERLLRALQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 229 DSRCTLVDTWWQTETG-GICIAPRpseEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQawPGMARTIYG 307
Cdd:cd17631 235 ARGVKFVQGYGMTETSpGVTFLSP---EDHRRKLGSAGRPVFFVEVRIVDPDGREVPP-GEVGEIVVRG--PHVMAGYWN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 308 DHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAA 387
Cdd:cd17631 309 RPEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAV 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 578835624 388 FAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 440
Cdd:cd17631 386 VAVVVPRPGA---ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
212-444 |
7.01e-34 |
|
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: 134.16 E-value: 7.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 212 GEPINCEAWEWLHRVVGDSrctLVDTWWQTETGgICIAPRPseeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNvSGA 291
Cdd:cd05970 310 GEALNPEVFNTFKEKTGIK---LMEGFGQTETT-LTIATFP---WMEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 292 LCI--SQAWP-GMARTIYGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP 368
Cdd:cd05970 382 IVIrtSKGKPvGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHP 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 369 AVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:cd05970 459 AVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
211-445 |
1.39e-33 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 132.97 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 211 VGEPINCEAWE-WLHRVVGDsrctLVDTWWQTETGGICIAPRpseeGAEILPAMAMRPFFGIVPVLMDEKGSVV-EGSNV 288
Cdd:cd05928 299 GGEPLNPEVLEkWKAQTGLD----IYEGYGQTETGLICANFK----GMKIKPGSMGKASPPYDVQIIDDNGNVLpPGTEG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 289 SGALCISQAWPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP 368
Cdd:cd05928 371 DIGIRVKPIRPFGLFSGYVDNPEKTAATIRG--DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHP 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578835624 369 AVPESAVIGYPHDIKGEAAFAFIVVKD--SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd05928 449 AVVESAVVSSPDPIRGEVVKAFVVLAPqfLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
140-444 |
7.62e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 123.56 E-value: 7.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV---------------------------- 191
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVlvpintalrgdelayiidhsgaqlvvvd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 192 -HTVIF-----------------AGFSAESLAgRINDVGE--------P---INCEAWEWLHRVVGDSRCTLVDT----- 237
Cdd:cd05934 83 pASILYtsgttgppkgvvithanLTFAGYYSA-RRFGLGEddvyltvlPlfhINAQAVSVLAALSVGATLVLLPRfsasr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 238 WWQ---------TETGGICIA------PRPSEE--------GAEILPAMAmRPF---FGiVPVL----MDEKGSVVEGSN 287
Cdd:cd05934 162 FWSdvrrygatvTNYLGAMLSyllaqpPSPDDRahrlraayGAPNPPELH-EEFeerFG-VRLLegygMTETIVGVIGPR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 288 VS--GALCISQAWPGMARTIYGDHQRFV---------------DAYFKAY---P---------GYYFTGDGAYRTEGGYY 338
Cdd:cd05934 240 DEprRPGSIGRPAPGYEVRIVDDDGQELpagepgelvirglrgWGFFKGYynmPeataeamrnGWFHTGDLGYRDADGFF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 339 QITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSdvvVQELKSMVATKIAKY 418
Cdd:cd05934 320 YFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLD---PEELFAFCEGQLAYF 396
|
410 420
....*....|....*....|....*.
gi 578835624 419 AVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:cd05934 397 KVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
148-445 |
6.47e-30 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 121.09 E-value: 6.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 148 ETTCRlanTLKRHGVHRgdrvaiyMPVSPLAVAAMLAcarigavhtvifAGFSAESLAG----RINDVGEPINCEAWEWL 223
Cdd:cd05973 168 ESTWR---VIERLGVTN-------LAGSPTAYRLLMA------------AGAEVPARPKgrlrRVSSAGEPLTPEVIRWF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 224 HRVVGdsrCTLVDTWWQTETGgICIA-----PRPSEEGAEILPAMAMRpffgiVPVLMDEKGSVVEGsnVSGALCISQA- 297
Cdd:cd05973 226 DAALG---VPIHDHYGQTELG-MVLAnhhalEHPVHAGSAGRAMPGWR-----VAVLDDDGDELGPG--EPGRLAIDIAn 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 298 WPGMArtiYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 377
Cdd:cd05973 295 SPLMW---FRGYQLPDTPAIDG--GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIG 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578835624 378 YPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd05973 370 VPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
123-443 |
4.97e-29 |
|
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: 118.78 E-value: 4.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 123 PESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV----------- 191
Cdd:cd05930 1 PDAVAVVDGDQ------SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAyvpldpsypae 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 --------------------------------------------------------------------------------
Cdd:cd05930 75 rlayiledsgaklvltdpddlayviytsgstgkpkgvmvehrglvnlllwmqeaypltpgdrvlqftsfsfdvsvweifg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 192 -----HTVIFAGFSAE----------------------SLAGRINDVGEPINCEAWEWLhrVVG---------------D 229
Cdd:cd05930 155 allagATLVVLPEEVRkdpealadllaeegitvlhltpSLLRLLLQELELAALPSLRLV--LVGgealppdlvrrwrelL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 230 SRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAwpGMARTIYGDH 309
Cdd:cd05930 233 PGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPV-PPGVPGELYIGGA--GLARGYLNRP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 310 ----QRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 385
Cdd:cd05930 310 eltaERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEK 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 578835624 386 AAFAFIVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd05930 390 RLVAYVV---PDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
115-444 |
1.37e-28 |
|
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: 118.05 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 115 LDQHVRKSPESVALIWerdepgTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV--- 191
Cdd:cd05936 5 LEEAARRFPDKTALIF------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 192 ---------------HTVIFAGFSAESLAGRI--------------NDV----------GEP-----------INCEA-W 220
Cdd:cd05936 79 lnplytprelehilnDSGAKALIVAVSFTDLLaagaplgervaltpEDVavlqytsgttGVPkgamlthrnlvANALQiK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 221 EWL-HRVVGDSR--CTL--VDTWWQTETGGICIA--------PRP---------SEEGAEILPA-----MAM-------- 265
Cdd:cd05936 159 AWLeDLLEGDDVvlAALplFHVFGLTVALLLPLAlgativliPRFrpigvlkeiRKHRVTIFPGvptmyIALlnapefkk 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 266 RPFFGI---------VPVLMDEK------GSVVEG---SNVSGALC------------ISQAWPGMARTIYGDHQRFVDA 315
Cdd:cd05936 239 RDFSSLrlcisggapLPVEVAERfeeltgVPIVEGyglTETSPVVAvnpldgprkpgsIGIPLPGTEVKIVDDDGEELPP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 316 Y------------FKAY---P---------GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP 371
Cdd:cd05936 319 GevgelwvrgpqvMKGYwnrPeetaeafvdGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578835624 372 ESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:cd05936 399 EAAVVGVPDPYSGEAVKAFVVLKE---GASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
238-445 |
3.79e-28 |
|
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: 116.96 E-value: 3.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 238 WWQTETGGICIAPRP-------SEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVS-GALCISQAWpgMARTIYGDH 309
Cdd:cd12119 311 WGMTETSPLGTVARPpsehsnlSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWDGKAvGELQVRGPW--VTKSYYKND 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 310 QR----FVDAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGE 385
Cdd:cd12119 389 EEsealTEDGWLR-------TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGE 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 386 AAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd12119 462 RPLAVVVLKE---GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
269-445 |
3.30e-27 |
|
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: 114.33 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 269 FGIVPVLMDEKGSVVEgSNVSGALCISQawPGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVI 348
Cdd:cd05926 325 VGVEVRILDEDGEILP-PGVVGEICLRG--PNVTRGYLNNPEANAEAAFKD--GWFRTGDLGYLDADGYLFLTGRIKELI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 349 NISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVK 428
Cdd:cd05926 400 NRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLR---EGASVTEEELRAFCRKHLAAFKVPKKVYFVD 476
|
170
....*....|....*..
gi 578835624 429 RLPKTRSGKVMRRLLRK 445
Cdd:cd05926 477 ELPKTATGKIQRRKVAE 493
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
322-445 |
4.57e-27 |
|
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: 113.15 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRM-DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAfiVVKDSAGDS 400
Cdd:cd05941 320 GWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVA--VVVLRAGAA 397
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578835624 401 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd05941 398 ALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
115-351 |
6.09e-26 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 109.32 E-value: 6.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 115 LDQHVRKSPESVALiwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:pfam00501 1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 195 IFAGFSAESLAGRINDV--------------------------------------------------------------- 211
Cdd:pfam00501 76 LNPRLPAEELAYILEDSgakvlitddalkleellealgklevvklvlvldrdpvlkeeplpeeakpadvppppppppdpd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 212 ------------GEP-----------INCEAWEW---------------------------------------------- 222
Cdd:pfam00501 156 dlayiiytsgttGKPkgvmlthrnlvANVLSIKRvrprgfglgpddrvlstlplfhdfglslgllgpllagatvvlppgf 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 223 -------LHRVVGDSRCT---------------------------------------------------LVDTWWQTETG 244
Cdd:pfam00501 236 paldpaaLLELIERYKVTvlygvptllnmlleagapkrallsslrlvlsggaplppelarrfrelfggaLVNGYGLTETT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 245 GICIAPRPSEEGAEILPAmAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAYFKayPGYY 324
Cdd:pfam00501 316 GVVTTPLPLDEDLRSLGS-VGRPLPGTEVKIVDDETGEPVPPGEPGELCVRG--PGVMKGYLNDPELTAEAFDE--DGWY 390
|
410 420
....*....|....*....|....*..
gi 578835624 325 FTGDGAYRTEGGYYQITGRMDDVINIS 351
Cdd:pfam00501 391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
212-444 |
6.65e-26 |
|
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: 110.54 E-value: 6.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 212 GEPINCEAWE-WLHRVVgdsrCTLVDTWWQTETGGICIAPRPSEegaeILPAMAMRPFFGIVPVLMDEKGSVVEGSnVSG 290
Cdd:cd05959 289 GEALPAEVGErWKARFG----LDILDGIGSTEMLHIFLSNRPGR----VRYGTTGKPVPGYEVELRDEDGGDVADG-EPG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 291 ALCISQawPGMArTIYGdHQRfvDAYFKAYPGYYF-TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPA 369
Cdd:cd05959 360 ELYVRG--PSSA-TMYW-NNR--DKTRDTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPA 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578835624 370 VPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:cd05959 434 VLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
359-437 |
2.04e-25 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 99.16 E-value: 2.04e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578835624 359 EIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 437
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP---GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
56-447 |
4.35e-25 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 108.51 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 56 GSYPALSAQAAREPAAFWgplardTLVWD---TPYHTVWDCDFSTGKI----GWFLGGQLNVSVNCLdQHvRKSPESVAL 128
Cdd:cd05943 17 ADYAALHRWSVDDPGAFW------AAVWDfsgVRGSKPYDVVVVSGRImpgaRWFPGARLNYAENLL-RH-ADADDPAAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 129 IweRDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRI 208
Cdd:cd05943 89 Y--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 209 ---------------------------------------------------NDVGEPINCEAWEWL-------------- 223
Cdd:cd05943 167 gqiepkvlfavdaytyngkrhdvrekvaelvkglpsllavvvvpytvaagqPDLSKIAKALTLEDFlatgaagelefepl 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 224 -----------------------------------HRVVGDSR--------------------------CTLV------- 235
Cdd:cd05943 247 pfdhplyilyssgttglpkcivhgaggtllqhlkeHILHCDLRpgdrlfyyttcgwmmwnwlvsglavgATIVlydgspf 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 236 ---------------------------------------------------------------------DTWWQTETGG- 245
Cdd:cd05943 327 ypdtnalwdladeegitvfgtsakyldalekaglkpaethdlsslrtilstgsplkpesfdyvydhikpDVLLASISGGt 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 246 -IC--------IAP-RPSEEGAEILpAMAMRPFfgivpvlmDEKGSVVEGsnVSGALCISQAWPGMARTIYGDH--QRFV 313
Cdd:cd05943 407 dIIscfvggnpLLPvYRGEIQCRGL-GMAVEAF--------DEEGKPVWG--EKGELVCTKPFPSMPVGFWNDPdgSRYR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 314 DAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVV 393
Cdd:cd05943 476 AAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKL 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 578835624 394 KDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKII 447
Cdd:cd05943 556 REGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKII 609
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
322-448 |
6.97e-25 |
|
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: 107.54 E-value: 6.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsd 401
Cdd:COG1021 409 GFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEP---- 484
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 578835624 402 VVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 448
Cdd:COG1021 485 LTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
267-475 |
8.04e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 107.91 E-value: 8.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 267 PFFGIVPVLMDEKGSVVeGSNVSGALCISQAWP-GMARTIYGDHQRFvDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMD 345
Cdd:PTZ00237 438 PSIFIKPSILSEDGKEL-NVNEIGEVAFKLPMPpSFATTFYKNDEKF-KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 346 DVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKS----MVATKIAKYAVP 421
Cdd:PTZ00237 516 DQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNeinnIITQDIESLAVL 595
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578835624 422 DEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTtlEDPSIIAEILSVYQK 475
Cdd:PTZ00237 596 RKIIIVNQLPKTKTGKIPRQIISKFLNDSNYQLPDNV--NDSEIFYKIKELYMK 647
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
322-444 |
2.38e-24 |
|
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: 105.25 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 401
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGP 396
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:cd05958 397 VLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
230-439 |
3.81e-24 |
|
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: 104.99 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 230 SRCTLVDTWWQTETGGICIAPRPSEEGAE----ILPAMAMRpffgivpvLMDEKGSVVEGSNVSGALCIS--QAWPG--- 300
Cdd:cd05911 287 PNATIKQGYGMTETGGILTVNPDGDDKPGsvgrLLPNVEAK--------IVDDDGKDSLGPNEPGEICVRgpQVMKGyyn 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 301 ----MARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI 376
Cdd:cd05911 359 npeaTKETFDED-------------GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVI 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578835624 377 GYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKY-AVPDEILVVKRLPKTRSGKVM 439
Cdd:cd05911 426 GIPDEVSGELPRAYVVRKPGEKLTE---KEVKDYVAKKVASYkQLRGGVVFVDEIPKSASGKIL 486
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
141-444 |
4.84e-24 |
|
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: 104.08 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRIND---------- 210
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDcearlvvtsa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 211 ------------VGEP-----------INCEAW--EWLHRVVGDSRCTLV----------DTWWQTETGGICI--APRPS 253
Cdd:cd05919 91 ddiayllyssgtTGPPkgvmhahrdplLFADAMarEALGLTPGDRVFSSAkmffgyglgnSLWFPLAVGASAVlnPGWPT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 254 EEGAEILPAmAMRP--FFGiVPVL---MDEKGSVVEGSNVSGALCIS----------QAW-------------------- 298
Cdd:cd05919 171 AERVLATLA-RFRPtvLYG-VPTFyanLLDSCAGSPDALRSLRLCVSagealprglgERWmehfggpildgigatevghi 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 299 -----PGMARtiYGDHQRFVDAY---------------------------FKAY------------PGYYFTGDGAYRTE 334
Cdd:cd05919 249 flsnrPGAWR--LGSTGRPVPGYeirlvdeeghtippgeegdllvrgpsaAVGYwnnpeksratfnGGWYRTGDKFCRDA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 335 GGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATK 414
Cdd:cd05919 327 DGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLER 406
|
410 420 430
....*....|....*....|....*....|
gi 578835624 415 IAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:cd05919 407 LSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
54-208 |
1.65e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 104.05 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 54 QPGSYPALSAQAAREPAAFWGPLARDTLVWDTPYHTVwdcdFSTGKI--GWFLGGQLNVSVNCLDQHVrKSP---ESVAL 128
Cdd:PTZ00237 6 DPFDYENDSNYANSNPESFWDEVAKKYVHWDKMYDKV----YSGDEIypDWFKGGELNTCYNVLDIHV-KNPlkrDQDAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 129 IWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRI 208
Cdd:PTZ00237 81 IYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRI 160
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
238-445 |
2.13e-23 |
|
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: 102.46 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 238 WWQTETGGICIAPRPSEEGAeilpAMAM--RPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMartIYGDHQRfVDA 315
Cdd:cd05903 240 YGSTECPGAVTSITPAPEDR----RLYTdgRPLPGVEIKVVDDTGATL-APGVEGELLSRG--PSV---FLGYLDR-PDL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 316 YFKAYP-GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVK 394
Cdd:cd05903 309 TADAAPeGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTK 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578835624 395 DSAG-DSDVVVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd05903 389 SGALlTFDELVAYLD---RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
56-443 |
9.04e-23 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 101.80 E-value: 9.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 56 GSYPALSAQAAREPAAFWgplardTLVWD-------TPYHTVWDcdfSTGKIG--WFLGGQLNVSVNCLDQHvrkSPESV 126
Cdd:PRK03584 34 DDYAALWRWSVEDLEAFW------QSVWDffgvigsTPYTVVLA---GRRMPGarWFPGARLNYAENLLRHR---RDDRP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 127 ALIWeRDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV----------HTVI- 195
Cdd:PRK03584 102 AIIF-RGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIwsscspdfgvQGVLd 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 196 -----------------FAG--FS--------AESL-----------AGRINDVGEPINCEAWEWLHRVVGDSRCTLVDT 237
Cdd:PRK03584 181 rfgqiepkvliavdgyrYGGkaFDrrakvaelRAALpslehvvvvpyLGPAAAAAALPGALLWEDFLAPAEAAELEFEPV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 238 ------------------------------------------------WWQTETG-------------GICI-------- 248
Cdd:PRK03584 261 pfdhplwilyssgttglpkcivhghggillehlkelglhcdlgpgdrfFWYTTCGwmmwnwlvsgllvGATLvlydgspf 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 249 APRPS-------EEG----------------AEILPA-----MAMR-------P-------------------------- 267
Cdd:PRK03584 341 YPDPNvlwdlaaEEGvtvfgtsakyldacekAGLVPGethdlSALRtigstgsPlppegfdwvyehvkadvwlasisggt 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 268 -----FFGIVPVL------------------MDEKGSVVEGsnVSGALCISQAWPGMArtIY----GDHQRFVDAYFKAY 320
Cdd:PRK03584 421 dicscFVGGNPLLpvyrgeiqcrglgmaveaWDEDGRPVVG--EVGELVCTKPFPSMP--LGfwndPDGSRYRDAYFDTF 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 321 PGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDS 400
Cdd:PRK03584 497 PGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLD 576
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 578835624 401 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVM----RRLL 443
Cdd:PRK03584 577 DALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
322-445 |
1.81e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 100.36 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsd 401
Cdd:PRK07656 392 GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAE--- 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:PRK07656 469 LTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
276-444 |
2.66e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 97.73 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 276 MDEKGSVVEGSNVSGALCISQAwpGMARTIYGDHQRFVDAYFKAypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRL 355
Cdd:cd05917 188 VDPEGGIVPPVGVPGELCIRGY--SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENI 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 356 GTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRS 435
Cdd:cd05917 264 YPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGA---ELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVS 340
|
....*....
gi 578835624 436 GKVMRRLLR 444
Cdd:cd05917 341 GKIQKFKLR 349
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
322-453 |
1.11e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 97.70 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsD 401
Cdd:PRK08316 395 GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGA---T 471
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 453
Cdd:PRK08316 472 VTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGAFTD 523
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
140-443 |
1.43e-21 |
|
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: 96.78 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV---------------------------- 191
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVvvpinpmlkereleyilndsgakvavvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 192 -----------------------HTVIFAGFSAESLA---------------------GRINDVGEPINCEA-------W 220
Cdd:cd05935 81 selddlalipytsgttglpkgcmHTHFSAAANALQSAvwtgltpsdvilaclplfhvtGFVGSLNTAVYVGGtyvlmarW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 221 --EWLHRVVGDSRCTLvdtWWQTETGGICIAPRPSEE-------------GAEILPAMAMR------------------- 266
Cdd:cd05935 161 drETALELIEKYKVTF---WTNIPTMLVDLLATPEFKtrdlsslkvltggGAPMPPAVAEKllkltglrfvegygltetm 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 267 ------------------PFFGIVPVLMDEKGSVVEGSNVSGALCISQawPGMARTIYGDHQRFVDAYFKAYPGYYF-TG 327
Cdd:cd05935 238 sqthtnpplrpklqclgiP*FGVDARVIDIETGRELPPNEVGEIVVRG--PQIFKGYWNRPEETEESFIEIKGRRFFrTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 328 DGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsAGDSDVVVQEL 407
Cdd:cd05935 316 DLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP-EYRGKVTEEDI 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 578835624 408 KSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd05935 395 IEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
233-444 |
1.50e-21 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 97.45 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 233 TLVDTWWQTETGGICIAPRPSEEgaEILPAMAmRPFFGIVPVLMDEKGSVVEgSNVSGALCIsQAWPGmaRTIYGDHQRF 312
Cdd:PRK08008 314 RLLTSYGMTETIVGIIGDRPGDK--RRWPSIG-RPGFCYEAEIRDDHNRPLP-AGEIGEICI-KGVPG--KTIFKEYYLD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 313 VDAYFKAYP--GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAF 390
Cdd:PRK08008 387 PKATAKVLEadGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAF 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578835624 391 IVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK08008 467 VVLNEGE---TLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
322-448 |
5.79e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 95.41 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdsagDSD 401
Cdd:PRK03640 360 GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK-----SGE 434
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 448
Cdd:PRK03640 435 VTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
322-443 |
5.90e-21 |
|
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: 95.47 E-value: 5.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 401
Cdd:cd05920 364 GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAA 443
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 578835624 402 VVVQELKSMvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd05920 444 QLRRFLRER---GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
321-445 |
1.63e-20 |
|
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: 92.39 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 321 PGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDS 400
Cdd:cd17630 204 DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV-----GRG 278
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578835624 401 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd17630 279 PADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
123-443 |
2.31e-20 |
|
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: 93.53 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd17643 1 PEAVAVVDE------DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 203 SLAGRIND------VGEPIN------------------------------CEA----------------------WE-W- 222
Cdd:cd17643 75 RIAFILADsgpsllLTDPDDlayviytsgstgrpkgvvvshanvlalfaaTQRwfgfneddvwtlfhsyafdfsvWEiWg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 223 ---------------------LHRVVGDSRCTLVDtwwQTETG------GICIAPRPSEE------GAEILPAMAMRPFF 269
Cdd:cd17643 155 allhggrlvvvpyevarspedFARLLRDEGVTVLN---QTPSAfyqlveAADRDGRDPLAlryvifGGEALEAAMLRPWA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 270 GIVPV----------------------------------------------LMDEKGSVVEGSnVSGALCISQawPGMAR 303
Cdd:cd17643 232 GRFGLdrpqlvnmygitettvhvtfrpldaadlpaaaaspigrplpglrvyVLDADGRPVPPG-VVGELYVSG--AGVAR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 304 TIYG----DHQRFVDAYFKAyPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIG 377
Cdd:cd17643 309 GYLGrpelTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIV 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 378 YpHDIKGEAAFAFIVVKDSAgdSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd17643 388 R-EDEPGDTRLVAYVVADDG--AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
322-445 |
2.53e-20 |
|
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: 92.79 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSD 401
Cdd:cd05912 293 GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV-----SERP 367
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd05912 368 ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
322-462 |
4.62e-20 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 92.89 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSagDSD 401
Cdd:PRK06087 410 GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAP--HHS 487
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578835624 402 VVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItseAQELGDTTTLED 462
Cdd:PRK06087 488 LTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDI---MRRLTQDVCEEI 546
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
322-444 |
5.62e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 92.36 E-value: 5.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMD-DVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDS 400
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV-----GAD 424
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578835624 401 DVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK07787 425 DVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
322-444 |
6.12e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 92.81 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 401
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEE 511
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578835624 402 vvvqELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK08974 512 ----ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
212-445 |
2.00e-19 |
|
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: 90.32 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 212 GEPINCEAWEWLHRVVGdsrCTLVDTWWQTETGGIcIAPRPseeGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVsgA 291
Cdd:cd05974 209 GEPLNPEVIEQVRRAWG---LTIRDGYGQTETTAL-VGNSP---GQPVKAGSMGRPLPGYRVALLDPDGAPATEGEV--A 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 292 LCISQAWP-GMARTIYGDHQRFVDAYfkaYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV 370
Cdd:cd05974 280 LDLGDTRPvGLMKGYAGDPDKTAHAM---RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAV 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578835624 371 PESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEiLVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd05974 357 AEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRR-LEFAELPKTISGKIRRVELRR 430
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
322-445 |
2.14e-19 |
|
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: 90.82 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsD 401
Cdd:cd12118 367 GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGA---K 443
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd12118 444 VTEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
116-443 |
2.88e-19 |
|
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: 90.34 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 116 DQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd12117 4 EEQAARTPDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 196 FAGFSAESLAGRINDVG-----------------EPINCEAWEWLHRVVGDSRCT------------------------- 233
Cdd:cd12117 78 DPELPAERLAFMLADAGakvlltdrslagragglEVAVVIDEALDAGPAGNPAVPvspddlayvmytsgstgrpkgvavt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 234 ------LV-DTWWQTETGGICIA-------------------------------PRPSEE-------------------- 255
Cdd:cd12117 158 hrgvvrLVkNTNYVTLGPDDRVLqtsplafdastfeiwgallngarlvlapkgtLLDPDAlgaliaeegvtvlwltaalf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 256 -------------------GAEILPAMAMR---------------------------------PFFGIVPV--------- 274
Cdd:cd12117 238 nqladedpecfaglrelltGGEVVSPPHVRrvlaacpglrlvngygptenttfttshvvteldEVAGSIPIgrpiantrv 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 275 -LMDEKGSVVEgSNVSGALCISQAwpGMARTIYGD----HQRFVDAYFKayPG--YYFTGDGAYRTEGGYYQITGRMDDV 347
Cdd:cd12117 318 yVLDEDGRPVP-PGVPGELYVGGD--GLALGYLNRpaltAERFVADPFG--PGerLYRTGDLARWLPDGRLEFLGRIDDQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 348 INISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVV 427
Cdd:cd12117 393 VKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV-----AEGALDAAELRAFLRERLPAYMVPAAFVVL 467
|
490
....*....|....*.
gi 578835624 428 KRLPKTRSGKVMRRLL 443
Cdd:cd12117 468 DELPLTANGKVDRRAL 483
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
261-446 |
3.48e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 90.37 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 261 PAMAMRPFFGIVPVLMDEKGSVVEGsNVSGALCISQAWPgMARTIYGDHQRFVDayfkaypGYYFTGDGAYRTEGGYYQI 340
Cdd:PRK07788 375 PGTVGRPPKGVTVKILDENGNEVPR-GVVGRIFVGNGFP-FEGYTDGRDKQIID-------GLLSSGDVGYFDEDGLLFV 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 341 TGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKIAKYAV 420
Cdd:PRK07788 446 DGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAP---GAALDEDAIKDYVRDNLARYKV 522
|
170 180
....*....|....*....|....*.
gi 578835624 421 PDEILVVKRLPKTRSGKVMRRLLRKI 446
Cdd:PRK07788 523 PRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
115-451 |
4.08e-19 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 90.11 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 115 LDQHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV--- 191
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVlnp 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 192 -------HTV----------------IFAGFSAESLAGRI---------------------------------------- 208
Cdd:PRK13295 110 lmpifreRELsfmlkhaeskvlvvpkTFRGFDHAAMARRLrpelpalrhvvvvggdgadsfeallitpaweqepdapail 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 209 -------NDV----------GEP--------------INCEawEWLHRVVGD-------------------------SRC 232
Cdd:PRK13295 190 arlrpgpDDVtqliytsgttGEPkgvmhtantlmaniVPYA--ERLGLGADDvilmaspmahqtgfmyglmmpvmlgATA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 233 TLVDTW--------WQTE---------------TGGICIAPRPSEE-------GAEILPAMA--MRPFFG--IVPVL-MD 277
Cdd:PRK13295 268 VLQDIWdparaaelIRTEgvtftmastpfltdlTRAVKESGRPVSSlrtflcaGAPIPGALVerARAALGakIVSAWgMT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 278 EKGSVVEG---------SNVSGAlcisqAWPGMA-RTIYGDHQR----------------FVdAYFK-------AYPGYY 324
Cdd:PRK13295 348 ENGAVTLTklddpderaSTTDGC-----PLPGVEvRVVDADGAPlpagqigrlqvrgcsnFG-GYLKrpqlngtDADGWF 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 325 FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DSDVV 403
Cdd:PRK13295 422 DTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSlDFEEM 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 578835624 404 VQELKSmvaTKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEA 451
Cdd:PRK13295 502 VEFLKA---QKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGED 546
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
322-444 |
4.99e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 89.69 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsd 401
Cdd:PRK07059 435 GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA---- 510
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK07059 511 LTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
322-444 |
7.30e-19 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 89.43 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKdsaGDSD 401
Cdd:PRK13382 416 GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLK---PGAS 492
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK13382 493 ATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
136-443 |
1.01e-18 |
|
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: 88.29 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 136 GTEVrITYRELLETTCRLANTLKRHGVHrgdrvaIYMPVSPLAVAAMLACARigavhtvifAGFSAESLagRINDVGEPI 215
Cdd:cd17650 161 GTLV-ICPDEVKLDPAALYDLILKSRIT------LMESTPALIRPVMAYVYR---------NGLDLSAM--RLLIVGSDG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 216 NCEAW-EWLHRVVGdSRCTLVDTWWQTETggiCIAPRPSEEGAEILPAMAM----RPFFGIVPVLMDEKGSVVEgSNVSG 290
Cdd:cd17650 223 CKAQDfKTLAARFG-QGMRIINSYGVTEA---TIDSTYYEEGRDPLGDSANvpigRPLPNTAMYVLDERLQPQP-VGVAG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 291 ALCISQAwpGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIAD 366
Cdd:cd17650 298 ELYIGGA--GVARGYLNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLAR 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 367 HPAVPESAVIgYPHDIKGEAAFAFIVVKDSAGDSdvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd17650 376 HPAIDEAVVA-VREDKGGEARLCAYVVAAATLNT----AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
322-449 |
1.15e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 88.38 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsD 401
Cdd:PRK06839 371 GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSS---V 447
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITS 449
Cdd:PRK06839 448 LIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
144-443 |
2.00e-18 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 87.30 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 144 RELLETTCRLANTLKRHGVHrgdrVAIYMPvSPLAVAAM---LACARIGAVHTVIFAGfsaeslagrindvgEPINCEAW 220
Cdd:cd05945 171 RDATADPKQLFRFLAEHGIT----VWVSTP-SFAAMCLLsptFTPESLPSLRHFLFCG--------------EVLPHKTA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 221 EWLHRVVGDSRctLVDTWWQTETGGICIAPRPSEE---GAEILPAMamRPFFGIVPVLMDEKGSVVEGsNVSGALCISQa 297
Cdd:cd05945 232 RALQQRFPDAR--IYNTYGPTEATVAVTYIEVTPEvldGYDRLPIG--YAKPGAKLVILDEDGRPVPP-GEKGELVISG- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 298 wPGMARTiYGDHQRFVDAYFKAYPGY--YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 375
Cdd:cd05945 306 -PSVSKG-YLNNPEKTAAAFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV 383
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578835624 376 IGYPHDIKGEAAFAFIVVKDsaGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd05945 384 VPKYKGEKVTELIAFVVPKP--GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
322-446 |
2.21e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 87.96 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsd 401
Cdd:PRK12492 441 GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPG---- 516
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 446
Cdd:PRK12492 517 LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
117-444 |
2.36e-18 |
|
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: 87.40 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 117 QHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:cd17651 3 RQAARTPDAPALVAE------GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 197 AGFSAESLAGRINDVG------------------EPINCEAWE------------------------------------- 221
Cdd:cd17651 77 PAYPAERLAFMLADAGpvlvlthpalagelavelVAVTLLDQPgaaagadaepdpaldaddlayviytsgstgrpkgvvm 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 222 ----------WLHRV--VGDSRCTL--------VDTW--WQTETGGICIAPRPSEE------------------------ 255
Cdd:cd17651 157 phrslanlvaWQARAssLGPGARTLqfaglgfdVSVQeiFSTLCAGATLVLPPEEVrtdppalaawldeqrisrvflptv 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 256 ------------------------GAEILPAM-AMRPFF----------------------GIVPVLMDEK------GSV 282
Cdd:cd17651 237 alralaehgrplgvrlaalrylltGGEQLVLTeDLREFCaglpglrlhnhygptethvvtaLSLPGDPAAWpapppiGRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 283 VEGS--------------NVSGALCIsqAWPGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRM 344
Cdd:cd17651 317 IDNTrvyvldaalrpvppGVPGELYI--GGAGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 345 DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEI 424
Cdd:cd17651 395 DDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV---GDPEAPVDAAELRAALATHLPEYMVPSAF 471
|
490 500
....*....|....*....|
gi 578835624 425 LVVKRLPKTRSGKVMRRLLR 444
Cdd:cd17651 472 VLLDALPLTPNGKLDRRALP 491
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
322-452 |
2.51e-18 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 87.74 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagdsd 401
Cdd:PRK10946 409 GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE------ 482
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 402 vvvqELKSMVATK------IAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 452
Cdd:PRK10946 483 ----PLKAVQLRRflreqgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRAS 535
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
322-452 |
2.80e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 87.17 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsD 401
Cdd:PRK09088 361 GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGA---P 437
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 452
Cdd:PRK09088 438 LDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
238-445 |
3.35e-18 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 87.11 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 238 WWQTET---GGICIAPRPSEE--GAEILPAMAM--RPFFGIVPVLMDEKG-SVVEGSNVSGALCISQawPGMARTIYGDH 309
Cdd:PRK06018 325 WGMTEMsplGTLAALKPPFSKlpGDARLDVLQKqgYPPFGVEMKITDDAGkELPWDGKTFGRLKVRG--PAVAAAYYRVD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 310 QRFVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFA 389
Cdd:PRK06018 403 GEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLL 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 390 FIVVKDsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:PRK06018 478 IVQLKP---GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
322-440 |
6.18e-18 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 84.38 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSd 401
Cdd:cd17633 208 GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS-----GDK- 281
|
90 100 110
....*....|....*....|....*....|....*....
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 440
Cdd:cd17633 282 LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
323-443 |
9.63e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 85.78 E-value: 9.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 323 YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSdV 402
Cdd:PRK08314 417 FFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGK-T 495
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 578835624 403 VVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:PRK08314 496 TEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
322-444 |
1.68e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 85.04 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSD 401
Cdd:PRK06188 393 GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRP---GAA 469
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK06188 470 VDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
177-443 |
2.28e-17 |
|
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: 84.48 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 177 LAVAAMLACARIGAVHTVIFAGFS-AESLAGRINdvgepiNCEAWEwlhrvvgdsrctLVDTWWQTETGGICIAPRPSEE 255
Cdd:cd05923 255 LAAAAEFAGLKLSSLRHVTFAGATmPDAVLERVN------QHLPGE------------KVNIYGTTEAMNSLYMRDARTG 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 256 GAeilpamaMRPFFG----IVPVL--MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDayfkaypGYYFTGDG 329
Cdd:cd05923 317 TE-------MRPGFFsevrIVRIGgsPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKKLQD-------GWYRTGDV 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 330 AYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKs 409
Cdd:cd05923 383 GYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCR- 461
|
250 260 270
....*....|....*....|....*....|....
gi 578835624 410 mvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd05923 462 --ASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
322-444 |
2.69e-17 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 84.16 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVInISG-HRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-D 399
Cdd:PRK07514 377 GFFITGDLGKIDERGYVHIVGRGKDLI-ISGgYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAAlD 455
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578835624 400 SDVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK07514 456 EAAILAALKG----RLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
266-440 |
3.09e-17 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 82.69 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 266 RPFFGIVPVLMDEKG-SVVEGSNvsGALCISQAWpgMARTIYGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRM 344
Cdd:cd17635 174 RPYPGVDVYLAATDGiAGPSASF--GTIWIKSPA--NMLGYWNNPERTAEVLID---GWVNTGDLGERREDGFLFITGRS 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 345 DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEI 424
Cdd:cd17635 247 SESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA--SAELDENAIRALKHTIRRELEPYARPSTI 324
|
170
....*....|....*.
gi 578835624 425 LVVKRLPKTRSGKVMR 440
Cdd:cd17635 325 VIVTDIPRTQSGKVKR 340
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
233-446 |
3.47e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 84.04 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 233 TLVDTWWQTETGGICIAPRPSEEgaeilPAMAMRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAWPG-MARTIYGDHQR 311
Cdd:PRK06155 319 DLLDGYGSTETNFVIAVTHGSQR-----PGSMGRLAPGFEARVVDEHDQELP-DGEPGELLLRADEPFaFATGYFGMPEK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 312 FVDAYFKAYpgyYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 391
Cdd:PRK06155 393 TVEAWRNLW---FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAV 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 392 VVKD-SAGDSDVVVQELKSMvatkIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 446
Cdd:PRK06155 470 VLRDgTALEPVALVRHCEPR----LAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
296-444 |
9.87e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 82.83 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 296 QAWPGMArtiYGD-HQR---FVDAYFK--AYP---GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIAD 366
Cdd:PRK07008 377 LPWDGKA---FGDlQVRgpwVIDRYFRgdASPlvdGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVA 453
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578835624 367 HPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK07008 454 HPAVAEAACIACAHPKWDERPLLVVVKRPGA---EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
326-445 |
1.09e-16 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 82.58 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 326 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDIKGEaafAFIVVKDSAGDSDv 402
Cdd:TIGR02262 388 SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVAdedGLIKPK---AFVVLRPGQTALE- 463
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578835624 403 vvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:TIGR02262 464 --TELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
175-453 |
1.13e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.47 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 175 SPLAVAAMLACARIGAVHTVI--------FAGFSAESLAGRINDVGEPInceAWEWLHRVVGD-SRCTLVDTWWQTE-TG 244
Cdd:PRK12316 734 DPAKLVELINREGVDTLHFVPsmlqaflqDEDVASCTSLRRIVCSGEAL---PADAQEQVFAKlPQAGLYNLYGPTEaAI 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 245 GICIAPRPSEEGAEILPAmamRPFFGIVPVLMDEKGSVVEgSNVSGALCISQAwpGMARTIYG----DHQRFVDAYFKAY 320
Cdd:PRK12316 811 DVTHWTCVEEGGDSVPIG---RPIANLACYILDANLEPVP-VGVLGELYLAGR--GLARGYHGrpglTAERFVPSPFVAG 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 321 PGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGyphdIKGEAAFAFIVVKDSAGDs 400
Cdd:PRK12316 885 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESEGGD- 959
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 578835624 401 dvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 453
Cdd:PRK12316 960 --WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQ 1010
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
288-443 |
1.72e-16 |
|
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: 81.75 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 288 VSGALCISQAwpGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDA 363
Cdd:cd17656 326 IVGELYISGA--SVARGYLNRqeltAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 364 IADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvqeLKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd17656 404 LLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQ-----LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
322-444 |
1.88e-16 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 81.85 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsd 401
Cdd:PRK08751 437 GWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPA---- 512
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK08751 513 LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
322-444 |
2.04e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 81.73 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsd 401
Cdd:PRK05677 433 GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGET--- 509
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK05677 510 LTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
260-445 |
2.54e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 81.54 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 260 LPAMAMRpffgIVPVlmDEKGSVVEGSNVS--GALCISQA--WPGMARtiyGDHQRfvDAYFkaYPGYYFTGDGAYRTEG 335
Cdd:PRK07529 392 LPYQRVR----VVIL--DDAGRYLRDCAVDevGVLCIAGPnvFSGYLE---AAHNK--GLWL--EDGWLNTGDLGRIDAD 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 336 GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATKI 415
Cdd:PRK07529 459 GYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKP---GASATEAELLAFARDHI 535
|
170 180 190
....*....|....*....|....*....|.
gi 578835624 416 A-KYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:PRK07529 536 AeRAAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
317-448 |
3.09e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 80.81 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 317 FKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDS 396
Cdd:PRK07445 319 ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 578835624 397 AGDsdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 448
Cdd:PRK07445 399 SIS----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
322-455 |
3.32e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 81.04 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 401
Cdd:PLN02479 430 GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSD 509
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 402 --VVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLLRkiitSEAQELG 455
Cdd:PLN02479 510 eaALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR----AKAKEMG 560
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
56-480 |
5.67e-16 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 80.69 E-value: 5.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 56 GSYPALSAQAAREPAAFWGPLARDT-LVWDTPYHTVWDCDFSTGKIgWFLGGQLNVSVNCLdqhvRKSPESVALIWeRDE 134
Cdd:TIGR01217 35 GGYDALHRWSVDELDTFWKAVWEWFdVRFSTPCARVVDDRTMPGAQ-WFPGARLNYAENLL----RAAGTEPALLY-VDE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 135 PGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDVgEP 214
Cdd:TIGR01217 109 THEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQI-EP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 215 ---INCEAWEW--------------------LHRVV-----GDSR----------------------------------- 231
Cdd:TIGR01217 188 kllFTVDGYRYngkehdrrdkvaevrkelptLRAVVhipylGPREteapkidgaldledftaaaqaaelvfeqlpfdhpl 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 232 ---------------------------------CTLVDT---WWQTETG---------------------GICIAPRPS- 253
Cdd:TIGR01217 268 wilfssgttglpkcivhsaggtlvqhlkehglhCDLGPGdrlFYYTTTGwmmwnwlvsglatgatlvlydGSPGFPATNv 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 254 ------EEGAEILPAMA----------MRP-------------------------------------------------F 268
Cdd:TIGR01217 348 lwdiaeRTGATLFGTSAkyvmacrkagVHParthdlsalqcvastgsplppdgfrwvydeikadvwlasisggtdicscF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 269 FGIVPVL------------------MDEKGSVVEGSnvSGALCISQAWPGMARTIYGDHQ--RFVDAYFKAYPGYYFTGD 328
Cdd:TIGR01217 428 AGANPTLpvhigeiqapglgtavqsWDPEGKPVTGE--VGELVCTNPMPSMPIRFWNDPDgsKYRDAYFDTYPGVWRHGD 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 329 GAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELK 408
Cdd:TIGR01217 506 WITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIK 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578835624 409 SMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSeaqelgdtTTLEDPSIIA--EILSVYQKCKDKQ 480
Cdd:TIGR01217 586 RTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQG--------TPVDNPGAIDnpELLDLYEELAELR 651
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
275-444 |
5.88e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 80.32 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 275 LMDEKGSVVEgSNVSGALCISQawPGMARTIYGDHQRFVDAYFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHR 354
Cdd:PRK06145 332 IADGAGRWLP-PNMKGEICMRG--PKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGEN 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 355 LGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTR 434
Cdd:PRK06145 406 IASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGA---TLTLEALDRHCRQRLASFKVPRQLKVRDELPRNP 482
|
170
....*....|
gi 578835624 435 SGKVMRRLLR 444
Cdd:PRK06145 483 SGKVLKRVLR 492
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
326-444 |
5.93e-16 |
|
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: 79.79 E-value: 5.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 326 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPhDIKGEAAFAFIVVKDSAGDSDVVVq 405
Cdd:cd05922 345 TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKIDPKDVLR- 422
|
90 100 110
....*....|....*....|....*....|....*....
gi 578835624 406 elksMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:cd05922 423 ----SLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
322-445 |
6.30e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 80.21 E-value: 6.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsaGDSD 401
Cdd:PRK07786 399 GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN--DDAA 476
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:PRK07786 477 LTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
58-114 |
6.43e-16 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 71.73 E-value: 6.43e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 58 YPALSAQAAREPAAFWGPLARDtLVWDTPYHTVWDCDFStGKIGWFLGGQLNVSVNC 114
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKE-LDWFKPFDKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
326-444 |
1.03e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 79.56 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 326 TGDGAYRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 401
Cdd:PRK08276 373 VGDVGYLDEDGYLYLTDRKSDMI-ISG---GVniypQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGD 448
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK08276 449 ALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
231-444 |
1.05e-15 |
|
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: 78.95 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 231 RCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAM-RPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMARTIYG-- 307
Cdd:cd17649 236 PVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIgRPLGGRSAYILDADLNPVP-VGVTGELYI--GGEGLARGYLGrp 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 308 --DHQRFV-DAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIkG 384
Cdd:cd17649 313 elTAERFVpDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-G 391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 385 EAAFAFIVVKDSAGDSDvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:cd17649 392 KQLVAYVVLRAAAAQPE-LRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
327-452 |
1.18e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 79.05 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 327 GDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAfiVVKDSAGdsdvvVQE 406
Cdd:PRK07638 366 RDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVA--IIKGSAT-----KQQ 438
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 578835624 407 LKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 452
Cdd:PRK07638 439 LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEK 484
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
325-443 |
1.18e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 78.54 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 325 FTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAfIVVKDSAGDSDvvv 404
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA-KVISHEEIDPV--- 369
|
90 100 110
....*....|....*....|....*....|....*....
gi 578835624 405 qELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:PRK08308 370 -QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
322-445 |
1.36e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 78.93 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgdsD 401
Cdd:PRK07470 394 GWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGA---P 470
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:PRK07470 471 VDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
266-443 |
1.52e-15 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 78.51 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 266 RPFFGIVPVLMDEKGSVVeGSNVSGALCISQAwpGMARTIYGD----HQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQIT 341
Cdd:cd12115 272 RPLANTQAYVLDRALQPV-PLGVPGELYIGGA--GVARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFL 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 342 GRMDDVINISGHRLGTAEIEDAIADHPAVPEsAVIGYPHDIKGEAAF-AFIVVKDSAGdsdVVVQELKSMVATKIAKYAV 420
Cdd:cd12115 349 GRADNQVKVRGFRIELGEIEAALRSIPGVRE-AVVVAIGDAAGERRLvAYIVAEPGAA---GLVEDLRRHLGTRLPAYMV 424
|
170 180
....*....|....*....|...
gi 578835624 421 PDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd12115 425 PSRFVRLDALPLTPNGKIDRSAL 447
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
322-440 |
2.23e-15 |
|
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: 77.16 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAG-DS 400
Cdd:cd17638 215 GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTlTE 294
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 578835624 401 DVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMR 440
Cdd:cd17638 295 EDVIAWCRE----RLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
322-459 |
2.90e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 78.15 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSD 401
Cdd:PRK06710 431 GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE---GTE 507
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLrkiITSEAQELGDTTT 459
Cdd:PRK06710 508 CSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL---IEEEKRKNEDEQT 562
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
232-445 |
3.21e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 77.80 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 232 CTLVDTWWQTEtGGICIAPRPSEegaeilPAMAMRPFFGIVPVLMDEKGS-----------VVEGSNVSGALcISQAWPG 300
Cdd:PRK07867 291 CVVVDGFGSTE-GGVAITRTPDT------PPGALGPLPPGVAIVDPDTGTecppaedadgrLLNADEAIGEL-VNTAGPG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 301 MARTIY----GDHQRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI 376
Cdd:PRK07867 363 GFEGYYndpeADAERMRG-------GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVY 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 377 GYPHDIKGEAAFAFIVVKDSAG-DSDVVVQELKSmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:PRK07867 436 AVPDPVVGDQVMAALVLAPGAKfDPDAFAEFLAA--QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
287-449 |
5.46e-15 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 77.33 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 287 NVSGALCI-SQAwpgMARTIYGDHQ---RFVDAyfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED 362
Cdd:PLN02330 386 NTPGELCVrSQC---VMQGYYNNKEetdRTIDE-----DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEA 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 363 AIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRL 442
Cdd:PLN02330 458 ILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESE---EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRL 534
|
....*..
gi 578835624 443 LRKIITS 449
Cdd:PLN02330 535 LKEKMLS 541
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
322-438 |
7.11e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 77.00 E-value: 7.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGD-GAYrTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDS 400
Cdd:PRK06178 442 GWLHTGDiGKI-DEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKP---GA 517
|
90 100 110
....*....|....*....|....*....|....*...
gi 578835624 401 DVVVQELKSMVATKIAKYAVPdEILVVKRLPKTRSGKV 438
Cdd:PRK06178 518 DLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKV 554
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
57-452 |
8.50e-15 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 77.04 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 57 SYPALSAQAAREPAAFWgPLARDTL--VWDTPYHTVWDCDFSTGKIG-WFLGGQLNVSVNCLDQHVRKSPESVALIWeRD 133
Cdd:PLN03052 121 SFSEFQRFSVENPEVYW-SIVLDELslVFSVPPRCILDTSDESNPGGqWLPGAVLNVAECCLTPKPSKTDDSIAIIW-RD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 134 EPGTEV---RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRIN- 209
Cdd:PLN03052 199 EGSDDLpvnRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKi 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 210 ---------DV--------------------------------------------------------------------- 211
Cdd:PLN03052 279 skakaiftqDVivrggksiplysrvveakapkaivlpadgksvrvklregdmswddflaranglrrpdeykaveqpveaf 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 212 ----------GEP----------INCEAWEWLHRVV--GDSRCtlvdtwWQTETG--------------GICIA-----P 250
Cdd:PLN03052 359 tnilfssgttGEPkaipwtqltpLRAAADAWAHLDIrkGDIVC------WPTNLGwmmgpwlvyasllnGATLAlyngsP 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 251 RPSEEG-----AEI-----LPAM----------------AMRPF------------------FGIVPVLMDEKGSVVEGS 286
Cdd:PLN03052 433 LGRGFAkfvqdAKVtmlgtVPSIvktwkntncmagldwsSIRCFgstgeassvddylwlmsrAGYKPIIEYCGGTELGGG 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 287 NVSGALCISQAW-----PGMARTIY----------------------------------GDHQrfvDAYFKAYPGYYFT- 326
Cdd:PLN03052 513 FVTGSLLQPQAFaafstPAMGCKLFilddsgnpypddapctgelalfplmfgasstllnADHY---KVYFKGMPVFNGKi 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 327 ----GDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAI-ADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 401
Cdd:PLN03052 590 lrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGPEQLVIAAVLKDPPGSN 669
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 578835624 402 VVVQELKSMVATKIAKYAVP----DEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 452
Cdd:PLN03052 670 PDLNELKKIFNSAIQKKLNPlfkvSAVVIVPSFPRTASNKVMRRVLRQQLAQELS 724
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
305-445 |
9.62e-15 |
|
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: 75.59 E-value: 9.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 305 IYGDHQRFVDAYfkayPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKG 384
Cdd:cd05944 220 LYTEGNKNAFVA----DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAG 295
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578835624 385 EAAFAFIVVKDSAgdsDVVVQELKSMVATKIA-KYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd05944 296 ELPVAYVQLKPGA---VVEEEELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
322-451 |
1.19e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 76.14 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVInISG-HRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGds 400
Cdd:PRK08162 416 GWFHTGDLAVLHPDGYIKIKDRSKDII-ISGgENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGAS-- 492
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 578835624 401 dVVVQELKSMVATKIAKYAVPDEIlVVKRLPKTRSGKVMRRLLRKIITSEA 451
Cdd:PRK08162 493 -ATEEEIIAHCREHLAGFKVPKAV-VFGELPKTSTGKIQKFVLREQAKSLK 541
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
320-453 |
1.35e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 76.19 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 320 YPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAgd 399
Cdd:PRK05605 443 LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGA-- 520
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 578835624 400 sDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 453
Cdd:PRK05605 521 -ALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEKLGA 573
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
261-443 |
1.40e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 75.80 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 261 PAMAMRPFFGIVPVLMDEKGSVVeGSNVSGALCISQAWPGmartiygdhQRFVDAYFKAY-PGYYFTGDGAYRTEGGYYQ 339
Cdd:PRK13383 344 PETVGKPVAGCPVRILDRNNRPV-GPRVTGRIFVGGELAG---------TRYTDGGGKAVvDGMTSTGDMGYLDNAGRLF 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 340 ITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSagdSDVVVQELKSMVATKIAKYA 419
Cdd:PRK13383 414 IVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG---SGVDAAQLRDYLKDRVSRFE 490
|
170 180
....*....|....*....|....
gi 578835624 420 VPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:PRK13383 491 QPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
115-443 |
1.46e-14 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 75.77 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 115 LDQHVRKSPESVALIWERdepgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV--- 191
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 192 -----------HTVIFAG----FSAESLAGRINDVGEPINCEAWEWLHR--------VVGDSRCTLVDT----------- 237
Cdd:cd17646 78 ldpgypadrlaYMLADAGpavvLTTADLAARLPAGGDVALLGDEALAAPpatpplvpPRPDNLAYVIYTsgstgrpkgvm 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 238 -----------WWQTE-----------------------------TGGICIAPRPSEE---------------------- 255
Cdd:cd17646 158 vthagivnrllWMQDEyplgpgdrvlqktplsfdvsvwelfwplvAGARLVVARPGGHrdpaylaalirehgvttchfvp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 256 -----------------------GAEILPAMAMRPFF-------------------------------GIVPV------- 274
Cdd:cd17646 238 smlrvflaepaagscaslrrvfcSGEALPPELAARFLalpgaelhnlygpteaaidvthwpvrgpaetPSVPIgrpvpnt 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 275 ---LMDEKGSVVEgSNVSGALCIsqAWPGMARTIYG----DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDV 347
Cdd:cd17646 318 rlyVLDDALRPVP-VGVPGELYL--GGVQLARGYLGrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 348 INISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVV 427
Cdd:cd17646 395 VKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVP--AAGAAGPDTAALRAHLAERLPEYMVPAAFVVL 472
|
490
....*....|....*.
gi 578835624 428 KRLPKTRSGKVMRRLL 443
Cdd:cd17646 473 DALPLTANGKLDRAAL 488
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
319-450 |
1.94e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 74.70 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 319 AYPGYYFTGD-GAYrtEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVkdsA 397
Cdd:PRK07824 231 AEPGWFRTDDlGAL--DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG---D 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578835624 398 GDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSE 450
Cdd:PRK07824 306 GGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAGE 358
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
322-448 |
2.95e-14 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 74.88 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 401
Cdd:PLN02574 430 GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQ 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 578835624 402 vvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIIT 448
Cdd:PLN02574 510 ---EAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLT 553
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
322-440 |
3.59e-14 |
|
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: 74.41 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSD 401
Cdd:TIGR01923 320 GWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIV-----SESD 394
|
90 100 110
....*....|....*....|....*....|....*....
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 440
Cdd:TIGR01923 395 ISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILR 433
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
288-443 |
3.79e-14 |
|
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: 74.21 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 288 VSGALCIsqAWPGMARTiYGDH-----QRFVDAYFKAyPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEI 360
Cdd:cd17652 280 VPGELYI--AGAGLARG-YLNRpgltaERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 361 EDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 440
Cdd:cd17652 356 EAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPT---AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
...
gi 578835624 441 RLL 443
Cdd:cd17652 433 RAL 435
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
117-449 |
4.60e-14 |
|
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: 74.12 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 117 QHVRKSPESVAL-IWERDepgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 196 FAGFSAESLAGRINDVGEPI----------------------------------NCEAWEWLHRVVGDSRC--------- 232
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVvltsspsdaayviftsgstgkpkgvviehralstSALAHGRALGLTSESRVlqfasytfd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 233 -TLVDTWWQTETGG-ICIaprPSEEG----------------AEILPAMA--MRPffGIVP-----VLMDEK-------- 279
Cdd:cd05918 160 vSILEIFTTLAAGGcLCI---PSEEDrlndlagfinrlrvtwAFLTPSVArlLDP--EDVPslrtlVLGGEAltqsdvdt 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 280 ----------------------GSVVEGSNVS---------------------------GALCISQawPGMARTIYGDHQ 310
Cdd:cd05918 235 wadrvrlinaygpaectiaatvSPVVPSTDPRnigrplgatcwvvdpdnhdrlvpigavGELLIEG--PILARGYLNDPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 311 R----FV-DAYFKAYPGY------YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY- 378
Cdd:cd05918 313 KtaaaFIeDPAWLKQEGSgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVv 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 379 -PHDIKGEAAF-AFIVVKDSAGDSD--------------VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRL 442
Cdd:cd05918 393 kPKDGSSSPQLvAFVVLDGSSSGSGdgdslflepsdefrALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRA 472
|
....*..
gi 578835624 443 LRKIITS 449
Cdd:cd05918 473 LRELAES 479
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
322-446 |
5.48e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 74.04 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDsagDSD 401
Cdd:PRK12583 428 GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHP---GHA 504
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 446
Cdd:PRK12583 505 ASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
308-444 |
6.04e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 73.89 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 308 DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAA 387
Cdd:PRK13390 365 DPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQV 444
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 388 FAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK13390 445 KAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
279-444 |
7.06e-14 |
|
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: 73.57 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 279 KGSVveGSNVSGALCI-----SQAWPGMARTIYgdhqrFVDAYFKAYPGYYF-------------TGDGAYRTEGGYYQI 340
Cdd:cd05929 296 PGSV--GRAVLGKVHIldedgNEVPPGEIGEVY-----FANGPGFEYTNDPEktaaarneggwstLGDVGYLDEDGYLYL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 341 TGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAV 420
Cdd:cd05929 369 TDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKC 448
|
170 180
....*....|....*....|....
gi 578835624 421 PDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:cd05929 449 PRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
115-212 |
8.59e-14 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 73.60 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 115 LDQHVRKSPESVALIWERDepGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:COG1022 17 LRRRAARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90
....*....|....*...
gi 578835624 195 IFAGFSAESLAGRINDVG 212
Cdd:COG1022 95 IYPTSSAEEVAYILNDSG 112
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
267-446 |
9.28e-14 |
|
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: 73.33 E-value: 9.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 267 PFFGIVPVLMDEKGSVveGSNVSGALCISQawPGMARTIYGDHQRFVDAYFKayPGYYFTGDGAYRTEGGYYQITGRMDD 346
Cdd:cd17642 361 PFFYAKVVDLDTGKTL--GPNERGELCVKG--PMIMKGYVNNPEATKALIDK--DGWLHSGDIAYYDEDGHFFIVDRLKS 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 347 VINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFivvkdsagdsdVVVQELKSMVATKIAKYaVPDEILV 426
Cdd:cd17642 435 LIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAV-----------VVLEAGKTMTEKEVMDY-VASQVST 502
|
170 180 190
....*....|....*....|....*....|
gi 578835624 427 VKRL----------PKTRSGKVMRRLLRKI 446
Cdd:cd17642 503 AKRLrggvkfvdevPKGLTGKIDRRKIREI 532
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
234-474 |
9.84e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.22 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 234 LVDTWWQTETGGICIAPRPSEEGAEILPAMamRPFFGIVPVLMDEKGSVVEGSNVsGALCIsqAWPGMARtiyGDHQR-- 311
Cdd:PRK12316 3337 LYNLYGPTEATITVTHWQCVEEGKDAVPIG--RPIANRACYILDGSLEPVPVGAL-GELYL--GGEGLAR---GYHNRpg 3408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 312 -----FVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgyphDIKGEA 386
Cdd:PRK12316 3409 ltaerFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQ 3484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 387 AFAFIVVKDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE--LGDTTTLED-- 462
Cdd:PRK12316 3485 LVAYVVPEDEAGD---LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQdyVAPVNELERrl 3561
|
250
....*....|..
gi 578835624 463 PSIIAEILSVYQ 474
Cdd:PRK12316 3562 AAIWADVLKLEQ 3573
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
322-457 |
2.18e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 72.15 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVI-----NISGhRlgtaEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDs 396
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMIirggeNIYP-R----EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRP- 500
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578835624 397 agDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIItseAQELGDT 457
Cdd:PRK08315 501 --GATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM---IEELGLQ 556
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
223-474 |
2.23e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.07 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 223 LHRVVGDSRCTLVDTWWQTETGGICiaprpseeGAEILPAMamRPFFGIVPVLMDEKGSV----VEGSNVSGALCISQAW 298
Cdd:PRK12316 4838 LFNGYGPTETTVTVLLWKARDGDAC--------GAAYMPIG--TPLGNRSGYVLDGQLNPlpvgVAGELYLGGEGVARGY 4907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 299 ---PGMARtiygdhQRFVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 374
Cdd:PRK12316 4908 lerPALTA------ERFVPDPFGAPGGrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 375 VIGYPHDIkGEAAFAFIVVKDSA-GDSDVV----VQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITS 449
Cdd:PRK12316 4982 VIAQEGAV-GKQLVGYVVPQDPAlADADEAqaelRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDAS 5060
|
250 260
....*....|....*....|....*....
gi 578835624 450 EAQE--LGDTTTLED--PSIIAEILSVYQ 474
Cdd:PRK12316 5061 LLQQayVAPRSELEQqvAAIWAEVLQLER 5089
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
266-444 |
2.61e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 72.03 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 266 RPFFGIVPVLMDekgsvvegsnvSGALCIsqawPGMARTIYGDHQR-FVdaYFK----------AYPGYYFTGDGAYRTE 334
Cdd:PRK13391 332 RAMFGDLHILDD-----------DGAELP----PGEPGTIWFEGGRpFE--YLNdpaktaearhPDGTWSTVGDIGYVDE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 335 GGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATK 414
Cdd:PRK13391 395 DGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQR 474
|
170 180 190
....*....|....*....|....*....|
gi 578835624 415 IAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK13391 475 LSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
288-443 |
2.81e-13 |
|
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: 71.53 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 288 VSGALCISQAwpGMARTIYGDHQRFVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIA 365
Cdd:cd12114 325 VPGELWIGGR--GVALGYLGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQ 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578835624 366 DHPAVPESAVIGYPHDikGEAAFAFIVVKDSAGDSDvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd12114 403 AHPGVARAVVVVLGDP--GGKRLAAFVVPDNDGTPI-APDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
115-191 |
3.99e-13 |
|
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: 72.20 E-value: 3.99e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:COG1020 482 FEAQAARTPDAVAVVFG------DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA 552
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
275-443 |
4.32e-13 |
|
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: 71.20 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 275 LMDEKGSVV-EGsnVSGALCISQAwpGMARTiYGDH-----QRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVI 348
Cdd:cd17655 322 ILDQYGRPQpVG--VAGELYIGGE--GVARG-YLNRpeltaEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 349 NISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdsaGDSDVVVQELKSMVATKIAKYAVPDEILVVK 428
Cdd:cd17655 397 KIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-----SEKELPVAQLREFLARELPDYMIPSYFIKLD 471
|
170
....*....|....*
gi 578835624 429 RLPKTRSGKVMRRLL 443
Cdd:cd17655 472 EIPLTPNGKVDRKAL 486
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
322-445 |
4.39e-13 |
|
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: 71.31 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSD 401
Cdd:cd05915 389 GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPE 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 578835624 402 VVVQELKSMVATkiaKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd05915 469 ELNEHLLKAGFA---KWQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
326-443 |
4.49e-13 |
|
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: 71.11 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 326 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKdsaGDSDVVVQ 405
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRK---PGSSLTED 467
|
90 100 110
....*....|....*....|....*....|....*...
gi 578835624 406 ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd05904 468 EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
275-472 |
4.65e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.12 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 275 LMDEKGSVVEGSNVsGALCIsqAWPGMARTIYGDHQR----FVDAYFKAyPG--YYFTGDGAYRTEGGYYQITGRMDDVI 348
Cdd:PRK05691 4053 LLDEALELVPLGAV-GELCV--AGTGVGRGYVGDPLRtalaFVPHPFGA-PGerLYRTGDLARRRSDGVLEYVGRIDHQV 4128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 349 NISGHRLGTAEIEDAIADHPAVPESAViGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVK 428
Cdd:PRK05691 4129 KIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLD 4207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578835624 429 RLPKTRSGKVMRRLLRKIITSEAQE---LGDTTTLED--PSIIAEILSV 472
Cdd:PRK05691 4208 RLPLNANGKLDRKALPALDIGQLQSqayLAPRNELEQtlATIWADVLKV 4256
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
322-441 |
4.90e-13 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 71.07 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsd 401
Cdd:PRK05852 408 GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAP--- 484
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 578835624 402 VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRR 441
Cdd:PRK05852 485 PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
116-445 |
5.90e-13 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 70.42 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 116 DQHVRKSPESVALiwerdePGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGA----- 190
Cdd:cd17653 4 ERIAAAHPDAVAV------ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAayvpl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 191 -----------------------------------------------------VHTVIFAGFSAESLAGRIN-------- 209
Cdd:cd17653 78 daklpsariqailrtsgatlllttdspddlayiiftsgstgipkgvmvphrgvLNYVSQPPARLDVGPGSRVaqvlsiaf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 210 --DVGEPINC-------------EAWEWLHRVVGDSRCT----------------------------LVDTWWqtetGGI 246
Cdd:cd17653 158 daCIGEIFSTlcnggtlvladpsDPFAHVARTVDALMSTpsilstlspqdfpnlktiflggeavppsLLDRWS----PGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 247 CI--APRPSEegAEILPAMA-MRPffgIVPV------------LMDE-KGSVVEGsnVSGALCISQawPGMARTIYGDHQ 310
Cdd:cd17653 234 RLynAYGPTE--CTISSTMTeLLP---GQPVtigkpipnstcyILDAdLQPVPEG--VVGEICISG--VQVARGYLGNPA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 311 RFVDAY--FKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED-AIADHPAVPESAVIgyphdIKGE 385
Cdd:cd17653 305 LTASKFvpDPFWPGsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAI-----VVNG 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 386 AAFAFIVvkdsagDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd17653 380 RLVAFVT------PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
288-443 |
1.65e-12 |
|
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: 69.24 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 288 VSGALCIsqAWPGMARTIYGD----HQRFVDAYFkAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIE 361
Cdd:cd12116 316 VPGELYI--GGDGVAQGYLGRpaltAERFVPDPF-AGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 362 DAIADHPAVPESAVIGYPHDIKGEAAfAFIVVKD-SAGDSDvvvqELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 440
Cdd:cd12116 393 AALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAgAAPDAA----ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDR 467
|
...
gi 578835624 441 RLL 443
Cdd:cd12116 468 KAL 470
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
223-453 |
1.88e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 70.19 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 223 LHRVVGDSRCTLVDTWWQTETGGICIAPRpseegaeiLPAMamRPFFGIVPVLMDEKGSVVEgSNVSGALCIsqAWPGMA 302
Cdd:PRK12467 3380 LTNGYGPTEAVVTVTLWKCGGDAVCEAPY--------APIG--RPVAGRSIYVLDGQLNPVP-VGVAGELYI--GGVGLA 3446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 303 RtiyGDHQ-------RFVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESA 374
Cdd:PRK12467 3447 R---GYHQrpsltaeRFVADPFSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAV 3523
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578835624 375 VIGYPHDiKGEAAFAFIVVKDSAGDsdvVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE 453
Cdd:PRK12467 3524 VLARDGA-GGKQLVAYVVPADPQGD---WRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSRE 3598
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
288-469 |
4.87e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 68.65 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 288 VSGALCISQAwpGMARtiyGDHQR-------FVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAE 359
Cdd:PRK12467 853 VVGELYIGGA--GLAR---GYHRRpaltaerFVPDPFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGE 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 360 IEDAIADHPAVPESAVIGYPHDiKGEAAFAFIVVKDSAGDSD--VVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 437
Cdd:PRK12467 928 IEARLLAQPGVREAVVLAQPGD-AGLQLVAYLVPAAVADGAEhqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGK 1006
|
170 180 190
....*....|....*....|....*....|..
gi 578835624 438 VMRRLLRKIITSEAQELGDTTTLEDPSIIAEI 469
Cdd:PRK12467 1007 LDRKALPKPDASAVQATFVAPQTELEKRLAAI 1038
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
231-444 |
6.50e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 67.74 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 231 RCTLVDTWWQTETGGICIAPRPSEEGAeilpamAMRPFFGIV-----------PVLMDEKGSVVEGSNVSGALcISQAWP 299
Cdd:PRK13388 288 GCQVEDGYGSSEGAVIVVREPGTPPGS------IGRGAPGVAiynpetltecaVARFDAHGALLNADEAIGEL-VNTAGA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 300 GMARTIYGDH----QRFVDayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 375
Cdd:PRK13388 361 GFFEGYYNNPeataERMRH-------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAV 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578835624 376 IGYPHDIKGEAAFAFIVVKDsagDSDVVVQELKSMVATK--IAKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK13388 434 YAVPDERVGDQVMAALVLRD---GATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
152-474 |
8.89e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.06 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 152 RLANTLKRHGVHRGDRVAIYMpvSPLAVAAMLACARIgAVHTVIFAGfsaeslagrindvgEPINCEAWEWLHRVVGDSR 231
Cdd:PRK12316 2227 QLYDEMERHGVTILDFPPVYL--QQLAEHAERDGRPP-AVRVYCFGG--------------EAVPAASLRLAWEALRPVY 2289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 232 ctLVDTWWQTETggiCIAPRPSEEGAEILPAMAMRPffgIVPVLMDEKGSVVEGS------NVSGALCISQAwpGMARTI 305
Cdd:PRK12316 2290 --LFNGYGPTEA---VVTPLLWKCRPQDPCGAAYVP---IGRALGNRRAYILDADlnllapGMAGELYLGGE--GLARGY 2359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 306 YG----DHQRFVDAYFKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGypH 380
Cdd:PRK12316 2360 LNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA--Q 2437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 381 DIKGEAAFAFIVVKDSAGDSDvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQE--LGDTT 458
Cdd:PRK12316 2438 DGASGKQLVAYVVPDDAAEDL--LAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQayVAPQE 2515
|
330
....*....|....*...
gi 578835624 459 TLED--PSIIAEILSVYQ 474
Cdd:PRK12316 2516 GLEQrlAAIWQAVLKVEQ 2533
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
315-446 |
9.30e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 67.35 E-value: 9.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 315 AYFKAYP-GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVV 393
Cdd:PLN03102 412 ATSEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVL 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 394 KDS----AGDSDVVVQELKSMVA---TKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKI 446
Cdd:PLN03102 492 EKGettkEDRVDKLVTRERDLIEycrENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
195-445 |
9.65e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 67.12 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 195 IFAGFSAESlagrindvgePINCEAWEWLHRVvgdsrcTLVDTWWQTETGGICIAPRPSEeGAEILPAMAMRPFFGIVPV 274
Cdd:PRK05620 303 IYVGGSAVP----------PILIKAWEERYGV------DVVHVWGMTETSPVGTVARPPS-GVSGEARWAYRVSQGRFPA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 275 LMDEK----GSVVEGSN-------VSGALCI-------SQAWPGMARTIYGDHQRFVDAYFKAyPGYYFTGDGAYRTEGG 336
Cdd:PRK05620 366 SLEYRivndGQVMESTDrnegeiqVRGNWVTasyyhspTEEGGGAASTFRGEDVEDANDRFTA-DGWLRTGDVGSVTRDG 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 337 YYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIA 416
Cdd:PRK05620 445 FLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLP 524
|
250 260
....*....|....*....|....*....
gi 578835624 417 KYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:PRK05620 525 NWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
272-443 |
1.74e-11 |
|
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: 66.04 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 272 VPVLMDEKGSVVEGSNVSGALCIsqAWPGMARTIYG----DHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDV 347
Cdd:cd17645 271 TRVYILDEALQLQPIGVAGELCI--AGEGLARGYLNrpelTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 348 INISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKdsagdSDVVVQELKSMVATKIAKYAVPDEILVV 427
Cdd:cd17645 349 VKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP-----EEIPHEELREWLKNDLPDYMIPTYFVHL 423
|
170
....*....|....*.
gi 578835624 428 KRLPKTRSGKVMRRLL 443
Cdd:cd17645 424 KALPLTANGKVDRKAL 439
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
310-452 |
1.88e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.11 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 310 QRFVDAYFkAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgyPHD-IKGEA 386
Cdd:PRK12467 1941 ERFVADPF-GTVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVI--AQDgANGKQ 2017
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578835624 387 AFAFIVVKDSAGDSDVVVQ-----ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 452
Cdd:PRK12467 2018 LVAYVVPTDPGLVDDDEAQvalraILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQ 2088
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
247-443 |
2.78e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.35 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 247 CIAPRPSEEGAEILP---AMAMRpffgiVPVLMDEKGSVVEgSNVSGALCISQAwpGMARtiyGDHQR-------FVDAY 316
Cdd:PRK05691 2493 CLAPEQLEEGAASVPigrVVGAR-----VAYILDADLALVP-QGATGELYVGGA--GLAQ---GYHDRpgltaerFVADP 2561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 317 FKAYPG-YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGypHDIKGEAAFAFIVVKD 395
Cdd:PRK05691 2562 FAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA--LDTPSGKQLAGYLVSA 2639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578835624 396 SAGDSDVVVQEL----KSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:PRK05691 2640 VAGQDDEAQAALrealKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
115-191 |
4.09e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 65.28 E-value: 4.09e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 115 LDQHVRKSPESVALIWERDepgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQ------SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
322-444 |
4.69e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 64.76 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAfAFIVVKDSAGDSD 401
Cdd:PRK06164 406 GYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPTDGASPDE 484
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 578835624 402 vvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSG---KVMRRLLR 444
Cdd:PRK06164 485 ---AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
175-375 |
5.67e-11 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 64.21 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 175 SPLAVAAMLACARIGAVHTVIFAGfsaeslagrindvgEPINCEAWEWLHRVVGDSRctLVDTWWQTETGGICIA---PR 251
Cdd:TIGR01733 221 SLLALLAAALPPALASLRLVILGG--------------EALTPALVDRWRARGPGAR--LINLYGPTETTVWSTAtlvDP 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 252 PSEEGAEILPAMamRPFFGIVPVLMDEKGSVVeGSNVSGALCISQawPGMARTIYGD----HQRFVDAYFKAYPGY--YF 325
Cdd:TIGR01733 285 DDAPRESPVPIG--RPLANTRLYVLDDDLRPV-PVGVVGELYIGG--PGVARGYLNRpeltAERFVPDPFAGGDGArlYR 359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578835624 326 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAV 375
Cdd:TIGR01733 360 TGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
310-443 |
1.25e-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: 63.22 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 310 QRFVDAYFKAYPG--YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAA 387
Cdd:cd17644 332 EKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRL 411
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 388 FAFIVVKDSAGDSdvvVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd17644 412 VAYIVPHYEESPS---TVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
323-437 |
1.84e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 62.40 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 323 YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDv 402
Cdd:cd05924 246 YAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGVDL- 324
|
90 100 110
....*....|....*....|....*....|....*
gi 578835624 403 vvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 437
Cdd:cd05924 325 --EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
123-192 |
2.14e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 62.98 E-value: 2.14e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 123 PESVALIWeRDEpgtevRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVH 192
Cdd:PRK07798 17 PDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVP 80
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
237-440 |
3.16e-10 |
|
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: 61.52 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 237 TWW----QTETGG-ICIAP---RPSEEGAEIlPAMAMRpffgIV-----PVLMDEKGSVVegsnVSGALCISQAWPGMAR 303
Cdd:cd17637 138 TFWslygQTETSGlVTLSPyreRPGSAGRPG-PLVRVR----IVddndrPVPAGETGEIV----VRGPLVFQGYWNLPEL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 304 TIYGdhqrfvdayFKAypGYYFTGDGAYRTEGGYYQITGRM--DDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPhD 381
Cdd:cd17637 209 TAYT---------FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP-D 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 382 IK-GEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMR 440
Cdd:cd17637 277 PKwGEGIKAVCVLKPGAT---LTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
212-452 |
3.74e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 62.14 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 212 GEPINCEAWEWLHRVVGDSRcTLVDTWWQTETGGICIAPRPSEEGAeilPAMAMRPFFGIVPVLMDEKG-SVVEGSNVSG 290
Cdd:PLN03051 245 GEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYISSTLLQPQA---PGAFSTASLGTRFVLLNDNGvPYPDDQPCVG 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 291 ALCISQAWPGMA-RTIYGDHQRfvdAYFKAYPGYYFT-------GDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED 362
Cdd:PLN03051 321 EVALAPPMLGASdRLLNADHDK---VYYKGMPMYGSKgmplrrhGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIER 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 363 AI-ADHPAVPESAVIGYPhDIKGEAAFAFIVVKDS-------AGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTR 434
Cdd:PLN03051 398 ACdRAVAGIAETAAVGVA-PPDGGPELLVIFLVLGeekkgfdQARPEALQKKFQEAIQTNLNPLFKVSRVKIVPELPRNA 476
|
250
....*....|....*...
gi 578835624 435 SGKVMRRLLRKIITSEAQ 452
Cdd:PLN03051 477 SNKLLRRVLRDQLKKELS 494
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
115-190 |
6.63e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 61.30 E-value: 6.63e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 115 LDQHVRKSPESVALIwerDEPGTevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGA 190
Cdd:PRK06164 16 LDAHARARPDAVALI---DEDRP---LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGA 85
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
324-438 |
7.77e-10 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 60.99 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 324 YFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES------------AVIGY--PHDIKGEAAFA 389
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSYivPRFDKPDDESF 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 578835624 390 FIVVKDSAGDSDVVV----------QELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 438
Cdd:cd17647 454 AQEDVPKEVSTDPIVkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
336-444 |
9.36e-10 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 61.20 E-value: 9.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 336 GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKI 415
Cdd:PRK06060 379 GWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRL 458
|
90 100
....*....|....*....|....*....
gi 578835624 416 AKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK06060 459 SAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
266-443 |
1.56e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.95 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 266 RPFFGIVPVLMDEKGSVVEGSnVSGALCISQAwpGMARTIYG----DHQRFV-DAYFKAYPGYYFTGDGAYRTEGGYYQI 340
Cdd:PRK05691 1447 RPLGNVLCRVLDAELNLLPPG-VAGELCIGGA--GLARGYLGrpalTAERFVpDPLGEDGARLYRTGDRARWNADGALEY 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 341 TGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIgyphdIKGEAAFAFIVVKDSAGDS-DVVVQELKSMVATKIAKYA 419
Cdd:PRK05691 1524 LGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQLVGYYTGEAGqEAEAERLKAALAAELPEYM 1598
|
170 180
....*....|....*....|....
gi 578835624 420 VPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:PRK05691 1599 VPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
285-445 |
2.15e-09 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 59.61 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 285 GSNVSGALCI--SQAWPG-------MARTIYGDhqrfvdayfkaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRL 355
Cdd:PLN02246 379 PRNQPGEICIrgPQIMKGylndpeaTANTIDKD-------------GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQV 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 356 GTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVvkdSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRS 435
Cdd:PLN02246 446 APAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV---RSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPS 522
|
170
....*....|
gi 578835624 436 GKVMRRLLRK 445
Cdd:PLN02246 523 GKILRKDLRA 532
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
310-442 |
2.46e-09 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 59.34 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 310 QRFVDAYFKA--------YPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVI-GYPH 380
Cdd:cd17648 310 ERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVaKEDA 389
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 381 DIKGEAAFAFIV---VKDSAGDSDvvvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV-MRRL 442
Cdd:cd17648 390 SQAQSRIQKYLVgyyLPEPGHVPE---SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLdVRAL 452
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
142-195 |
3.70e-09 |
|
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: 58.43 E-value: 3.70e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 578835624 142 TYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL 55
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
115-191 |
4.78e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 58.67 E-value: 4.78e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 115 LDQHVRKSPESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK08315 22 LDRTAARYPDREALV----YRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
317-438 |
7.35e-09 |
|
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: 57.73 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 317 FKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADH-PAVPESAVIGYPHDIKGEAAFAFIVvkD 395
Cdd:cd05909 364 FAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT--T 441
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 578835624 396 SAGDSDVVVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKV 438
Cdd:cd05909 442 TDTDPSSLNDILK---NAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
322-445 |
7.85e-09 |
|
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: 58.02 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIAD-HPAVPESAVigyphdikgeAAFA---------FI 391
Cdd:cd05931 417 GWLRTGDLGFLHDGELY-ITGRLKDLIIVRGRNHYPQDIEATAEEaHPALRPGCV----------AAFSvpddgeerlVV 485
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 578835624 392 VVKDSAGDSDVVVQELKSMVATKIAK-YAV-PDEILVVKR--LPKTRSGKVMRRLLRK 445
Cdd:cd05931 486 VAEVERGADPADLAAIAAAIRAAVAReHGVaPADVVLVRPgsIPRTSSGKIQRRACRA 543
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
324-438 |
1.19e-08 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 57.77 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 324 YFTGD-GAYrTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPES------------AVIGY--PHDiKGEAAF 388
Cdd:TIGR03443 680 YRTGDlGRY-LPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENvtlvrrdkdeepTLVSYivPQD-KSDELE 757
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 389 AFIVVKDSAGDSDVVVQ----------ELKSMVATKIAKYAVPDEILVVKRLPKTRSGKV 438
Cdd:TIGR03443 758 EFKSEVDDEESSDPVVKglikyrklikDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKV 817
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
117-191 |
1.41e-08 |
|
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: 57.25 E-value: 1.41e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578835624 117 QHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVhRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAI 74
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
323-437 |
1.58e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 56.82 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 323 YYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDv 402
Cdd:PRK07798 409 YAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL- 487
|
90 100 110
....*....|....*....|....*....|....*
gi 578835624 403 vvQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 437
Cdd:PRK07798 488 --AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
321-449 |
1.88e-08 |
|
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: 56.73 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 321 PGYY---------FTGDGAYRT------EGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVP--ESAVIG-YPHDI 382
Cdd:cd05908 352 PGYYnnpeatakvFTDDGWLKTgdlgfiRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVElgRVVACGvNNSNT 431
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 383 KGEAAFAFIVVKDSAGDSDVVVQELKSMVaTKIAKYAVpDEILVVKRLPKTRSGKVMRRLLRKIITS 449
Cdd:cd05908 432 RNEEIFCFIEHRKSEDDFYPLGKKIKKHL-NKRGGWQI-NEVLPIRRIPKTTSGKVKRYELAQRYQS 496
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
322-444 |
2.77e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 56.25 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVInISGhrlGT----AEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSA 397
Cdd:PRK12406 379 GFITSGDVGYLDADGYLFLCDRKRDMV-ISG---GVniypAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGA 454
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 578835624 398 G-DSDVVVQELKSMVAtkiaKYAVPDEILVVKRLPKTRSGKVMRRLLR 444
Cdd:PRK12406 455 TlDEADIRAQLKARLA----GYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
140-205 |
3.66e-08 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 55.44 E-value: 3.66e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLA 205
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLA 68
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
141-212 |
4.59e-08 |
|
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: 55.29 E-value: 4.59e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578835624 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDVG 212
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSE 77
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
241-443 |
7.82e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 54.63 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 241 TETG--GICIaPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAW---PGMARTIYGDHQRFVDA 315
Cdd:PRK05857 320 SETGctALCL-PTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPSASFGTLWiksPANMLGYWNNPERTAEV 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 316 YFKaypGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGeaAFAFIVVKD 395
Cdd:PRK05857 399 LID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG--ALVGLAVVA 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578835624 396 SAGDSDVVVQELKSMVATKIAK----YAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:PRK05857 474 SAELDESAARALKHTIAARFRResepMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
322-449 |
1.03e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 54.23 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAV-PESAV-IGYPHDIKGEaAFAfIVVKDSAGD 399
Cdd:PRK07768 414 GWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrPGNAVaVRLDAGHSRE-GFA-VAVESNAFE 491
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 578835624 400 SDVVVQELKSMVATKIAKyAV---PDEILVVK--RLPKTRSGKVMRRLLRKIITS 449
Cdd:PRK07768 492 DPAEVRRIRHQVAHEVVA-EVgvrPRNVVVLGpgSIPKTPSGKLRRANAAELVTP 545
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
115-205 |
1.05e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 54.39 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 115 LDQHVRKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK12583 24 FDATVARFPDREALVVRHQA----LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90
....*....|.
gi 578835624 195 IFAGFSAESLA 205
Cdd:PRK12583 100 INPAYRASELE 110
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
326-454 |
3.45e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 52.49 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 326 TGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD---------- 395
Cdd:PLN02860 418 TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDgwiwsdneke 497
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578835624 396 SAGDSDVVVQE-LKSMVATK-IAKYAVPDEILV-VKRLPKTRSGKVMRRLLRKIITSEAQEL 454
Cdd:PLN02860 498 NAKKNLTLSSEtLRHHCREKnLSRFKIPKLFVQwRKPFPLTTTGKIRRDEVRREVLSHLQSL 559
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
314-443 |
7.53e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 51.43 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 314 DAYFKAYPGY--YFTGDGAYrTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFI 391
Cdd:PRK04813 366 AEAFFTFDGQpaYHTGDAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYV 444
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578835624 392 VVKDSAGDSDV-VVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:PRK04813 445 VPKEEDFEREFeLTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
314-445 |
7.89e-07 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 51.28 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 314 DAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDikGEAAFAF 390
Cdd:cd05937 337 DIYFR-------TGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvpgHD--GRAGCAA 407
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 391 IVVKDSAGD-SDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd05937 408 ITLEESSAVpTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
358-438 |
1.12e-06 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 50.38 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 358 AEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGdsdVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGK 437
Cdd:cd17636 253 AEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAS---VTEAELIEHCRARIASYKKPKSVEFADALPRTAGGA 329
|
.
gi 578835624 438 V 438
Cdd:cd17636 330 D 330
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
115-191 |
1.17e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 51.20 E-value: 1.17e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 115 LDQHVRKSPESVALIWERDEpgtevrITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQ------FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAA 534
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
324-438 |
1.58e-06 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. 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: 341309 [Multi-domain] Cd Length: 449 Bit Score: 50.55 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 324 YFTGDGAYRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYphdiKGEAAFAFIVVKDSagdSDVV 403
Cdd:cd17654 341 RATGDFVTVKDGELF-FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLS----DQQRLIAFIVGESS---SSRI 412
|
90 100 110
....*....|....*....|....*....|....*
gi 578835624 404 VQELksmVATKIAKYAVPDEILVVKRLPKTRSGKV 438
Cdd:cd17654 413 HKEL---QLTLLSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
115-191 |
4.64e-06 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 49.11 E-value: 4.64e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 115 LDQHVRKSPESVALIWERDEpgteVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADR----IAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV 94
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
322-454 |
5.15e-06 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 49.15 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIadHPAVPES----AVIGYPHDIKGEAafafIVV--KD 395
Cdd:PRK08633 1019 GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL--AKALGGEevvfAVTAVPDEKKGEK----LVVlhTC 1092
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 578835624 396 SAGDSDVVVQELKsmvATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIitseAQEL 454
Cdd:PRK08633 1093 GAEDVEELKRAIK---ESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL----ALAL 1144
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
322-443 |
6.01e-06 |
|
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: 48.59 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINI-SGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKG----EAAFAFIVVKDS 396
Cdd:cd05914 336 GWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVAlayiDPDFLDVKALKQ 415
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 578835624 397 AGDSDVVVQELKSMVATKIAKYA-VPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:cd05914 416 RNIIDAIKWEVRDKVNQKVPNYKkISKVKIVKEEFEKTPKGKIKRFLY 463
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
260-446 |
6.20e-06 |
|
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: 48.82 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 260 LPAMAMRPFFGivpvlMDEKGSVVEGSNVSGALCISQAWPGMA--RTIYGDHQRFVDAYFKAYP---------------- 321
Cdd:cd05906 318 LPPDAIRPAFG-----MTETCSGVIYSRSFPTYDHSQALEFVSlgRPIPGVSMRIVDDEGQLLPegevgrlqvrgpvvtk 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYY---------FTGDGAYRT------EGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKG-- 384
Cdd:cd05906 393 GYYnnpeanaeaFTEDGWFRTgdlgflDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPGae 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578835624 385 --EAAFAFIVVKDSAGDSDVVVQELKSMVATKIAkyAVPDEILVVKR--LPKTRSGKVMRRLLRKI 446
Cdd:cd05906 473 teELAIFFVPEYDLQDALSETLRAIRSVVSREVG--VSPAYLIPLPKeeIPKTSLGKIQRSKLKAA 536
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
123-205 |
6.69e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 48.40 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:PRK08162 32 PDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAA 105
|
...
gi 578835624 203 SLA 205
Cdd:PRK08162 106 SIA 108
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
140-209 |
7.15e-06 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 48.19 E-value: 7.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 140 RITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRIN 209
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCIT 72
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
321-441 |
8.49e-06 |
|
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: 47.98 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 321 PGYYFTGDGAYRTEGGYYQITGRMDDVI-NISGHRLGTAEIEDAIADHPAVPESAVIG--YPH-----DIKGEAAFAFIV 392
Cdd:cd05907 306 DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGdgRPFlvaliVPDPEALEAWAE 385
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578835624 393 VKDSAGDSDV-------VVQELKSMV---------ATKIAKYAVPDEILVVKRLPKTRSGKVMRR 441
Cdd:cd05907 386 EHGIAYTDVAelaanpaVRAEIEAAVeaanarlsrYEQIKKFLLLPEPFTIENGELTPTLKLKRP 450
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
138-210 |
9.05e-06 |
|
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: 47.82 E-value: 9.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578835624 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRIND 210
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNH 77
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
142-193 |
1.21e-05 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 47.67 E-value: 1.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 578835624 142 TYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHT 193
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTT 103
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
115-212 |
1.35e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 48.24 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 115 LDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTV 194
Cdd:PRK05691 1137 LNEQARQTPERIALVWD------GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90
....*....|....*...
gi 578835624 195 IFAGFSAESLAGRINDVG 212
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSG 1228
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
125-205 |
1.39e-05 |
|
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: 47.45 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 125 SVALIWERDEpgtevrITYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAES 203
Cdd:cd17632 58 TLRLLPRFET------ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQ 131
|
..
gi 578835624 204 LA 205
Cdd:cd17632 132 LA 133
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
311-443 |
1.74e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 47.73 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 311 RFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHP----AVPESAVIGYPHDIKGEA 386
Cdd:PRK10252 826 RFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQAAATGGDA 905
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 387 A--FAFIVVKDSAG-DSDVvvqeLKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLL 443
Cdd:PRK10252 906 RqlVGYLVSQSGLPlDTSA----LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
134-193 |
2.81e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 46.53 E-value: 2.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578835624 134 EPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIY--MPV--SPLAVAAMLACARIGAVHT 193
Cdd:PRK07768 23 EPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLagAPVeiAPTAQGLWMRGASLTMLHQ 86
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
113-191 |
2.85e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 46.57 E-value: 2.85e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578835624 113 NCLDQHVRKSPESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWG------DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV 83
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
360-470 |
3.68e-05 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 45.91 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 360 IEDAIADHPAVPESAVIGYPHDIKGEAAFAFIvvkdsAGDSDVVVQELKSMVATKIAKYAvPDEILVVKRLPKTRSGKVM 439
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
90 100 110
....*....|....*....|....*....|..
gi 578835624 440 RRLLRKIITSEAQELGD-TTTLEDPSIIAEIL 470
Cdd:PRK09188 319 DDILRLIAMNQIDELDDlLREPEIRGLVEAIA 350
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
314-445 |
4.58e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 46.02 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 314 DAYFKaypgyyfTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYP---HDikGEAAFAF 390
Cdd:PRK08279 438 DAWFN-------TGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEvpgTD--GRAGMAA 508
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 578835624 391 IVVKDSAgdsDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:PRK08279 509 IVLADGA---EFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
245-445 |
4.62e-05 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 45.88 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 245 GICIAPRPSEEGA---EILPAMAMRPFFGIVpvlmDEKGSvvegsnvsgalcisqawpgmartiygdHQRFVDAYFKAYP 321
Cdd:cd05939 300 GLCIPCQPGEPGLlvgKIIQNDPLRRFDGYV----NEGAT---------------------------NKKIARDVFKKGD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGY--PHdIKGEAAFAFIVVKDSAGD 399
Cdd:cd05939 349 SAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVevPG-VEGRAGMAAIVDPERKVD 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578835624 400 SDVVVQELKSmvatKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRK 445
Cdd:cd05939 428 LDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
321-442 |
8.58e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.14 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 321 PGYYF-TGDGAYRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDiKGEAAFAFIVVKDSAG- 398
Cdd:PRK05851 394 PDDWFpTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTG-EGSARPGLVIAAEFRGp 471
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 578835624 399 DSDVVVQELKSMVATKIAkyAVPDEILVVK--RLPKTRSGKvMRRL 442
Cdd:PRK05851 472 DEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGK-LRRL 514
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
140-189 |
9.73e-05 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 44.97 E-value: 9.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 578835624 140 RITYRELLETTCRLANTLKRH-GVHRGDRVAIYMPVSPLAVAAMLACARIG 189
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLG 55
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
141-183 |
1.28e-04 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 44.63 E-value: 1.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 578835624 141 ITYRELLETTCRLANTLKRHGVHRGDRVAIYMP---VSPLAVAAML 183
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPnvlQYPVAIAAVL 94
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
117-215 |
1.42e-04 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 44.23 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 117 QHVRKSPESVALiweRDEPGTEvRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIF 196
Cdd:PRK05857 22 EQARQQPEAIAL---RRCDGTS-ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97
|
90
....*....|....*....
gi 578835624 197 AGFSAESLAgRINDVGEPI 215
Cdd:PRK05857 98 GNLPIAAIE-RFCQITDPA 115
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
139-184 |
1.52e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 44.18 E-value: 1.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 578835624 139 VRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLA 184
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG 102
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
123-212 |
2.98e-04 |
|
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: 43.16 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 123 PESVALIWErdepgtEVRITYRELLETTCRLANTLKRHGVHRGD-RVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSA 201
Cdd:cd17648 1 PDRVAVVYG------DKRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPD 74
|
90
....*....|.
gi 578835624 202 ESLAGRINDVG 212
Cdd:cd17648 75 ERIQFILEDTG 85
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
142-195 |
3.79e-04 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 42.80 E-value: 3.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 578835624 142 TYRELLETTCRLANTLK-RHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFI 61
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
321-452 |
4.34e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.78 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 321 PGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIED-AIADHPAVPESAVIgYPHDIKGEAAFAFivVKDSAGD 399
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAI-KSDASKGEALVLF--TTDSELT 666
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 578835624 400 SDVVVQELKSmvaTKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQ 452
Cdd:PRK08043 667 REKLQQYARE---HGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQ 716
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
123-212 |
5.59e-04 |
|
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: 42.22 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 123 PESVALIwerdEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAE 202
Cdd:cd05904 19 PSRPALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90
....*....|
gi 578835624 203 SLAGRINDVG 212
Cdd:cd05904 95 EIAKQVKDSG 104
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
322-377 |
8.03e-04 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 42.01 E-value: 8.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGhrlGT----AEIEDAIADHPAVPESAVIG 377
Cdd:COG1022 443 GWLHTGDIGELDEDGFLRITGRKKDLIVTSG---GKnvapQPIENALKASPLIEQAVVVG 499
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
322-453 |
9.54e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 41.87 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 322 GYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAafaFIVVKDSAgdsD 401
Cdd:PRK06814 1010 GWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGER---IILLTTAS---D 1083
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578835624 402 VVVQELKSMVATK-IAKYAVPDEILVVKRLPKTRSGKV----MRRLLRKIITSEAQE 453
Cdd:PRK06814 1084 ATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIdyvaVTKLAEEAAAKPEAA 1140
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
241-477 |
1.86e-03 |
|
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: 40.81 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 241 TETGGICIAPRPSEegaeILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALcisqawpgMARtiyGDHqrFVDAYFK-- 318
Cdd:cd17640 247 TETSPVVSARRLKC----NVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIV--------WVR---GPQ--VMKGYYKnp 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 319 -------AYPGYYFTGDGAYRTEGGYYQITGRMDDVINIS-GHRLGTAEIEDAIADHPAVPESAVIGypHDIKgeAAFAF 390
Cdd:cd17640 310 eatskvlDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG--QDQK--RLGAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 391 IVvkdsaGDSDVVVQELKSmVATKIAKyaVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEIL 470
Cdd:cd17640 386 IV-----PNFEELEKWAKE-SGVKLAN--DRSQLLASKKVLKLYKNEIKDEISNRPGFKSFEQIAPFALLEEPFIENGEM 457
|
....*..
gi 578835624 471 SVYQKCK 477
Cdd:cd17640 458 TQTMKIK 464
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
138-212 |
2.23e-03 |
|
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: 40.42 E-value: 2.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578835624 138 EVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDVG 212
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSE 77
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
322-377 |
2.70e-03 |
|
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: 40.14 E-value: 2.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578835624 322 GYY---------FTGDGAYRT-------EGGYYQITGRMDDVINIS-GHRLGTAEIEDAIADHPAVPESAVIG 377
Cdd:cd05932 355 GYYkdpeataeaFTADGFLRTgdkgeldADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
112-191 |
3.35e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.15 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 112 VNCLDQHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHrGDRVAIYMPVSPLAVAAMLACARIGAV 191
Cdd:PRK05691 12 VQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAGVI 90
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
108-195 |
3.78e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 39.80 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 108 LNVSVNCLDQHVRKSPESVALIWER--DEP-GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLA 184
Cdd:PLN02430 41 ITTAWDIFSKSVEKYPDNKMLGWRRivDGKvGPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEA 120
|
90
....*....|.
gi 578835624 185 CarigAVHTVI 195
Cdd:PLN02430 121 C----AAHSLI 127
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
136-185 |
4.40e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 39.44 E-value: 4.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 578835624 136 GTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLAC 185
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC 122
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
120-195 |
5.06e-03 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 39.50 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 120 RKSPESVALI----WERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVI 195
Cdd:PRK09274 17 QERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
326-453 |
5.63e-03 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 39.22 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578835624 326 TGDGAYRTEGGYYqITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYphDIKGEAAFAFIVVKDSAGDSDVVVQ 405
Cdd:PRK09192 443 TGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAAF--SIAQENGEKIVLLVQCRISDEERRG 519
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 578835624 406 ELKSMVATKI-AKYAVP-DEILVVKR-LPKTRSGKVMRRLLRKIITSEAQE 453
Cdd:PRK09192 520 QLIHALAALVrSEFGVEaAVELVPPHsLPRTSSGKLSRAKAKKRYLSGAFA 570
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
114-184 |
8.17e-03 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 38.71 E-value: 8.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578835624 114 CLDQHVRKSPESVALIwERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSP----LAVAAMLA 184
Cdd:PRK08180 44 RLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIehalLALAAMYA 117
|
|
| |
