|
Name |
Accession |
Description |
Interval |
E-value |
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
61-572 |
0e+00 |
|
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: 974.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 61 YKRHFAASVADPERFWGKAAEQISWYKPWTKTLENRHSSSTSWFVEGMLNMCYNAIDRHIESGKGDKVAIIYDSPVTDTK 140
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPPFTRWFVGGRLNTCYNALDRHVEAGRGDQIALIYDSPVTGTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 141 ATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVT 220
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 221 ASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQDCVPVLSEHPLYILYTSG 300
Cdd:cd05967 161 ASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQVPADLTKPGRDLDWSELLAKAEPVDCVPVAATDPLYILYTSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 301 TTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVGTPDAGAYFRV 380
Cdd:cd05967 241 TTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVGTPDPGAFWRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 381 LAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPITASC 460
Cdd:cd05967 321 IEKYQVNALFTAPTAIRAIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 461 IGLGNsKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAG 540
Cdd:cd05967 401 VGLEP-LPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAG 479
|
490 500 510
....*....|....*....|....*....|..
gi 1191882765 541 YMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05967 480 YKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE 511
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
103-572 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 584.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 103 WFVEGMLNMCYNAIDRHIEsGKGDKVAIIYDSpVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMY 182
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHAE-GRGDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 183 TMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRiGQHKPDKVLIYNRPNmetV 262
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALE-ELPSLEHVIVVGRTG---A 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 263 PLASGRDLDWDEEMAKAQSQ-DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDL 341
Cdd:COG0365 156 DVPMEGDLDWDELLAAASAEfEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 342 GWVVGHSYICYGPLIHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLF 421
Cdd:COG0365 236 GWATGHSYIVYGPLLNGATVVLYEGRPD-FPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGD--EPLKKYDLSSLRLLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 422 VAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPITASCIGlgnskTPP-PGQAGKSVPGYNVMILDDNMQKLKARCLGN 500
Cdd:COG0365 313 SAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPG-----LPVkPGSMGKPVPGYDVAVVDEDGNPVPPGEEGE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 501 IVVKLPLpPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:COG0365 388 LVIKGPW-PGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIES 458
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
61-572 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 567.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 61 YKRHFAASVADPERFWGKAAEQISWYKPWTKTLENRHSSSTSWFVEGMLNMCYNAIDRHIESgKGDKVAIIYDSPVTDTK 140
Cdd:PRK10524 4 YSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSNPPFARWFVGGRTNLCHNAVDRHLAK-RPEQLALIAVSTETDEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 141 ATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVT 220
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 221 ASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRpNMETVPLASGRDLDWDEEMAKAQSQDcVPVL---SEHPLYILY 297
Cdd:PRK10524 163 ADAGSRGGKVVPYKPLLDEAIALAQHKPRHVLLVDR-GLAPMARVAGRDVDYATLRAQHLGAR-VPVEwleSNEPSYILY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 298 TSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVgTPDAGAY 377
Cdd:PRK10524 241 TSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPT-RPDAGIW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 378 FRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPIT 457
Cdd:PRK10524 320 WRIVEKYKVNRMFSAPTAIRVLKKQDP--ALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGWPIL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 458 ASCIGLGnSKTPPPGQAGKSVPGYNVMILDDNM-QKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKF-PGYYD 535
Cdd:PRK10524 398 AIARGVE-DRPTRLGSPGVPMYGYNVKLLNEVTgEPCGPNEKGVLVIEGPLPPGCMQTVWGDDDRFVKTYWSLFgRQVYS 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 1191882765 536 TMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK10524 477 TFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEE 513
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
60-571 |
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: 536.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 60 EYKRHFAASVADPERFWGKAAEQISWYKPWTKTLENRHSS-STSWFVEGMLNMCYNAIDRHIESgKGDKVAIIYDSPVTD 138
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSKGPpFIKWFEGGKLNISYNCLDRHLKE-RGDKVAIIWEGDEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 139 TKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVV 218
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 219 VTASFGIEPGRKVEYMPILEEAMRIGqHKPDKVLIYNRPNmETVPLASGRDLDWDEEMAKaQSQDC--VPVLSEHPLYIL 296
Cdd:cd05966 161 ITADGGYRGGKVIPLKEIVDEALEKC-PSVEKVLVVKRTG-GEVPMTEGRDLWWHDLMAK-QSPECepEWMDSEDPLFIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 297 YTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVgTPDAGA 376
Cdd:cd05966 238 YTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPT-YPDPGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 377 YFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKV---FRVPVLDHWWQTETG 453
Cdd:cd05966 317 YWDIVEKHKVTIFYTAPTAIRALMKF--GDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVigkERCPIVDTWWQTETG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 454 SPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLpPGAFSGLWKNQEAFKHLYFEKFPGY 533
Cdd:cd05966 395 GIMITPLPGATPLK---PGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPW-PGMARTIYGDHERYEDTYFSKFPGY 470
|
490 500 510
....*....|....*....|....*....|....*...
gi 1191882765 534 YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05966 471 YFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVE 508
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
56-571 |
1.33e-180 |
|
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: 523.35 E-value: 1.33e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 56 SSCGEYKRHFAASVADPERFWGK-AAEQISWYKPWTKTLENRHSSSTSWFVEGMLNMCYNAIDRHIESgKGDKVAIIYDS 134
Cdd:TIGR02188 2 ANLEQYKELYEESIEDPDKFWAKlARELLDWFKPFTKVLDWSFPPFYKWFVGGELNVSYNCVDRHLEA-RPDKVAIIWEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 135 PVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAK 214
Cdd:TIGR02188 81 DEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 215 PKVVVTASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLDWDEEMAKaQSQDCVP--VLSEHP 292
Cdd:TIGR02188 161 AKLVITADEGLRGGKVIPLKAIVDEALEKCPVSVEHVLVVRRTGNPVVPWVEGRDVWWHDLMAK-ASAYCEPepMDSEDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 293 LYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVgTP 372
Cdd:TIGR02188 240 LFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPT-YP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 373 DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF---RVPVLDHWWQ 449
Cdd:TIGR02188 319 DPGRFWEIIEKHKVTIFYTAPTAIRALMRL--GDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVgkeRCPIVDTWWQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 450 TETGSPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNI-VVKLPLpPGAFSGLWKNQEAFKHLYFE 528
Cdd:TIGR02188 397 TETGGIMITPLPGATPTK---PGSATLPFFGIEPAVVDEEGNPVEGPGEGGYlVIKQPW-PGMLRTIYGDHERFVDTYFS 472
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1191882765 529 KFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:TIGR02188 473 PFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIE 515
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
60-571 |
2.45e-180 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 523.16 E-value: 2.45e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 60 EYKRHFAASVADPERFWGKAAEQISWYKPWTKTLENRHSSSTsWFVEGMLNMCYNAIDRHIESGkGDKVAIIY--DSPVT 137
Cdd:PRK00174 18 QYKALYQESVEDPEGFWAEQAKRLDWFKPFDTVLDWNAPFIK-WFEDGELNVSYNCLDRHLKTR-GDKVAIIWegDDPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 138 DTKatITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKV 217
Cdd:PRK00174 96 SRK--ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 218 VVTASFGIEPGRKVEYMPILEEAMRIGqHKPDKVLIYNRPNmETVPLASGRDLDWDEEMAKaQSQDC--VPVLSEHPLYI 295
Cdd:PRK00174 174 VITADEGVRGGKPIPLKANVDEALANC-PSVEKVIVVRRTG-GDVDWVEGRDLWWHELVAG-ASDECepEPMDAEDPLFI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 296 LYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVgTPDAG 375
Cdd:PRK00174 251 LYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPN-YPDPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 376 AYFRVLAEHGVAALFTAPTAIRA-IRQqdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF---RVPVLDHWWQTE 451
Cdd:PRK00174 330 RFWEVIDKHKVTIFYTAPTAIRAlMKE---GDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVggeRCPIVDTWWQTE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 452 TGSPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLpPGAFSGLWKNQEAFKHLYFEKFP 531
Cdd:PRK00174 407 TGGIMITPLPGATPLK---PGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPW-PGMMRTIYGDHERFVKTYFSTFK 482
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1191882765 532 GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK00174 483 GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIE 522
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
61-571 |
6.04e-179 |
|
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: 517.90 E-value: 6.04e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 61 YKRHFAASVADPERFWGKAAEQISWYKPWTK---TLENRHSSSTSWFVEGMLNMCYNAIDRHIESGkGDKVAIIYDSPVT 137
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKvknTSFAPGAPSIKWFEDATLNLAANALDRHLREN-GDRTAIIYEGDDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 138 DTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKV 217
Cdd:cd17634 80 SQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 218 VVTASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRPNMEtVPLASGRDLDWDEEMAKAQSQ-DCVPVLSEHPLYIL 296
Cdd:cd17634 160 LITADGGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGSD-IDWQEGRDLWWRDLIAKASPEhQPEAMNAEDPLFIL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 297 YTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVGtPDAGA 376
Cdd:cd17634 239 YTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNW-PTPAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 377 YFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGkqYSLTRFKTLFVAGERCDVETLEWSKKVF---RVPVLDHWWQTETG 453
Cdd:cd17634 318 MWQVVDKHGVNILYTAPTAIRALMAAGDDAIEG--TDRSSLRILGSVGEPINPEAYEWYWKKIgkeKCPVVDTWWQTETG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 454 SPITASCIGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEaFKHLYFEKFPGY 533
Cdd:cd17634 396 GFMITPLPGAIELKA---GSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHER-FEQTYFSTFKGM 471
|
490 500 510
....*....|....*....|....*....|....*...
gi 1191882765 534 YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17634 472 YFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIE 509
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
52-571 |
1.83e-118 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 365.37 E-value: 1.83e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 52 RVLSSSCGEYKRHFAASVADPERFWGKAAEQISWYKPW------TKTLENRHSS-STSWFVEGMLNMCYNAIDRHIESGK 124
Cdd:PLN02654 23 QALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWegdevcSENLDVRKGPiSIEWFKGGKTNICYNCLDRNVEAGN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:PLN02654 103 GDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVTASfGIEPGRKVEYMPILEEAMRIGQHKP----DKVLIY-NRPNM--ETVPLASGRDLDWdeema 277
Cdd:PLN02654 183 SLAQRIVDCKPKVVITCN-AVKRGPKTINLKDIVDAALDESAKNgvsvGICLTYeNQLAMkrEDTKWQEGRDVWW----- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 278 kaqsQDCVP----------VLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGH 347
Cdd:PLN02654 257 ----QDVVPnyptkcevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGH 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 348 SYICYGPLIHGNTTVLYEGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERC 427
Cdd:PLN02654 333 SYVTYGPMLNGATVLVFEGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRD--GDEYVTRHSRKSLRVLGSVGEPI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 428 DVETLEWSKKVF---RVPVLDHWWQTETGSPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVK 504
Cdd:PLN02654 410 NPSAWRWFFNVVgdsRCPISDTWWQTETGGFMITPLPGAWPQK---PGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVK 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 505 LPLpPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PLN02654 487 KSW-PGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVE 552
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
61-571 |
4.97e-101 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 319.38 E-value: 4.97e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 61 YKRHFAASVADPERFWGKAAEQiswYKPWTKTLENRHSSST---SWFVEGMLNMCYNAIDRHIESG-KGDKVAIIYDSPV 136
Cdd:PTZ00237 10 YENDSNYANSNPESFWDEVAKK---YVHWDKMYDKVYSGDEiypDWFKGGELNTCYNVLDIHVKNPlKRDQDALIYECPY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 137 TDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPK 216
Cdd:PTZ00237 87 LKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 217 VVVTASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNR------------PNMETVPlasgRDLDWDEEMAKAQSQ-- 282
Cdd:PTZ00237 167 LIITTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRnditsesdlkkiETIPTIP----NTLSWYDEIKKIKENnq 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 283 ----DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHG 358
Cdd:PTZ00237 243 spfyEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSLG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 359 NTTVLYEGKPVGTPDAGAYF-RVLAEHGVAALFTAPTAIRAIRQQDPGAA-LGKQYSLTRFKTLFVAGERCDVETLEWSK 436
Cdd:PTZ00237 322 NTFVMFEGGIIKNKHIEDDLwNTIEKHKVTHTLTLPKTIRYLIKTDPEATiIRSKYDLSNLKEIWCGGEVIEESIPEYIE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 437 KVFRVPVLDHWWQTETGspiTASCIGLGNSKTpPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLW 516
Cdd:PTZ00237 402 NKLKIKSSRGYGQTEIG---ITYLYCYGHINI-PYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPPSFATTFY 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 517 KNQEAFKHLyFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PTZ00237 478 KNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIE 531
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
102-565 |
2.21e-94 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 299.89 E-value: 2.21e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 102 SWFVEGMLNMCYNAIDRHIESGKGDKVAIIYDSPvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAM 181
Cdd:PRK04319 35 SWLETGKVNIAYEAIDRHADGGRKDKVALRYLDA--SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 182 YTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTasfgiepgrkveympileeAMRIGQHKPDKVLiynrPNMET 261
Cdd:PRK04319 113 FALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT-------------------TPALLERKPADDL----PSLKH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 262 VPL------ASGRDLDWDEEMAKAQSQ-DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGgyAVMLNWtMSSIYG--LKPG 332
Cdd:PRK04319 170 VLLvgedveEGPGTLDFNALMEQASDEfDIEWTDREDGAILHYTSGSTGKPKGVLHVHN--AMLQHY-QTGKYVldLHED 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 333 EVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQY 412
Cdd:PRK04319 247 DVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGR----FSPERWYRILEDYKVTVWYTAPTAIRMLMGA--GDDLVKKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 413 SLTRFKtlFVA--GERCDVETLEWSKKVFRVPVLDHWWQTETGspitasCIGLGNSKTPP--PGQAGKSVPGYNVMILDD 488
Cdd:PRK04319 321 DLSSLR--HILsvGEPLNPEVVRWGMKVFGLPIHDNWWMTETG------GIMIANYPAMDikPGSMGKPLPGIEAAIVDD 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 489 NMQKLKARCLGNIVVKLPLpPGAFSGLWKNQEAFKHlYFEkfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRI 565
Cdd:PRK04319 393 QGNELPPNRMGNLAIKKGW-PSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERV 465
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
123-561 |
6.70e-88 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 278.04 E-value: 6.70e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 123 GKGDKVAIIYDSPVTdtkatITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFA 202
Cdd:pfam00501 7 RTPDKTALEVGEGRR-----LTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 203 SKELSSRIDHAKPKVVVTASFGIepgrkveyMPILEEAMRIGQHKPDKVLIYNrpnmetVPLASGRDLDWDEEMAKAQSQ 282
Cdd:pfam00501 82 AEELAYILEDSGAKVLITDDALK--------LEELLEALGKLEVVKLVLVLDR------DPVLKEEPLPEEAKPADVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 283 DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGG--YAVMLNWTMS-SIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGN 359
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNlvANVLSIKRVRpRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 360 TTVLYEGKPvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalGKQYSLTRFKTLFVAGERCDVETLEWSKKVF 439
Cdd:pfam00501 228 TVVLPPGFP--ALDPAALLELIERYKVTVLYGVPTLLNMLLEAGA----PKRALLSSLRLVLSGGAPLPPELARRFRELF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 440 RVPVLDHWWQTETGSPITasCIGLGNSKTPPPGQAGKSVPGYNVMILDDN-MQKLKARCLGNIVVKlplPPGAFSGLWKN 518
Cdd:pfam00501 302 GGALVNGYGLTETTGVVT--TPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR---GPGVMKGYLND 376
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1191882765 519 QEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVA 561
Cdd:pfam00501 377 PELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
59-571 |
5.20e-83 |
|
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: 271.29 E-value: 5.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 59 GEYKRHFAASVADPERFWGKAAEQ--ISWYKPWTKTLE-NRHSSSTSWFVEGMLNMCYNAIDRHIESGKgDKVAIIYDSP 135
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDvgIEWYEPPYQTLDlSGGKPWAAWFVGGRMNIVEQLLDKWLADTR-TRPALRWEGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 136 VTDTKaTITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 215
Cdd:cd05968 86 DGTSR-TLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 216 KVVVTASFGIEPGRKVEYMPILEEAMRigqHKP--DKVLIYNRPNMEtVPLASGRDLDWDEEMAKAQSQdCVPVLSEHPL 293
Cdd:cd05968 165 KALITADGFTRRGREVNLKEEADKACA---QCPtvEKVVVVRHLGND-FTPAKGRDLSYDEEKETAGDG-AERTESEDPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 294 YILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGhSYICYGPLIHGNTTVLYEGKPvGTPD 373
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAP-DHPK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 374 AGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF---RVPVLDHWWQT 450
Cdd:cd05968 318 ADRLWRMVEDHEITHLGLSPTLIRALKPR--GDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVgkgRNPIINYSGGT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 451 ETGSPItascigLGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKARcLGNIVVKLPLpPGAFSGLWKNQEAFKHLYFE 528
Cdd:cd05968 396 EISGGI------LGNVLIKPikPSSFNGPVPGMKADVLDESGKPARPE-VGELVLLAPW-PGMTRGFWRDEDRYLETYWS 467
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1191882765 529 KFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05968 468 RFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIE 510
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
144-572 |
2.11e-78 |
|
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: 253.80 E-value: 2.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASf 223
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 224 giepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdcvpvlsEHPLYILYTSGTTG 303
Cdd:cd05972 81 ------------------------------------------------------------------EDPALIYFTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 304 LPKGVVRPTG-GYAVMLnwTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVgtpDAGAYFRVLA 382
Cdd:cd05972 95 LPKGVLHTHSyPLGHIP--TAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF---DAERILELLE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 383 EHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGspitascIG 462
Cdd:cd05972 170 RYGVTSFCGPPTAYRMLIKQDL-----SSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETG-------LT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 463 LGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAG 540
Cdd:cd05972 238 VGNFPDMPvkPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLP-PPGLFLGYVGDPEKTEASIRG---DYYLTGDRA 313
|
410 420 430
....*....|....*....|....*....|..
gi 1191882765 541 YMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05972 314 YRDEDGYFWFVGRADDIIKSSGYRIGPFEVES 345
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
144-571 |
6.35e-74 |
|
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: 242.41 E-value: 6.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAsf 223
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 224 giepgrkveympilEEamrigqhkpdkvlIYNRPNMETvplasgrdldwdeemakaqsqdcvpvlsehPLYILYTSGTTG 303
Cdd:cd05969 80 --------------EE-------------LYERTDPED------------------------------PTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 304 LPKGVVRPTGgyAVMLNW-TMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPvgtpDAGAYFRVLA 382
Cdd:cd05969 103 TPKGVLHVHD--AMIFYYfTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF----DAESWYGIIE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 383 EHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPITASCIG 462
Cdd:cd05969 177 RVKVTVWYTAPTAIRMLMKE--GDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 463 LgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlPLPPGAFSGLWKNQEAFKhLYFEKfpGYYDTMDAGYM 542
Cdd:cd05969 255 M----PIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALK-PGWPSMFRGIWNDEERYK-NSFID--GWYLTGDLAYR 326
|
410 420
....*....|....*....|....*....
gi 1191882765 543 DEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05969 327 DEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
125-572 |
3.87e-66 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 221.99 E-value: 3.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:COG0318 13 PDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVTAsfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdc 284
Cdd:COG0318 87 ELAYILEDSGARALVTA--------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 285 vpvlsehplYILYTSGTTGLPKGVVRPTGgyAVMLN-WTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVL 363
Cdd:COG0318 104 ---------LILYTSGTTGRPKGVMLTHR--NLLANaAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 364 YEGkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPV 443
Cdd:COG0318 173 LPR-----FDPERVLELIERERVTVLFGVPTMLARLLRH-PEFA---RYDLSSLRLVVSGGAPLPPELLERFEERFGVRI 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 444 LDHWWQTETGSPITascIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFK 523
Cdd:COG0318 244 VEGYGLTETSPVVT---VNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR---GPNVMKGYWNDPEATA 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1191882765 524 hlyfEKFP-GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:COG0318 318 ----EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEE 363
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
291-572 |
1.86e-58 |
|
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: 198.28 E-value: 1.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 291 HPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVvGHSYICYGPLIHGNTTVLYEGkpvg 370
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAA-LAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 371 tPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQT 450
Cdd:cd04433 75 -FDPEAALELIEREKVTILLGVPTLLARLLKAPESAG----YDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 451 ETGSPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPpgaFSGLWKNQEAFkhlYFEKF 530
Cdd:cd04433 150 ETGGTVATGPPDDDARK---PGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV---MKGYWNNPEAT---AAVDE 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1191882765 531 PGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd04433 221 DGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEA 262
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
143-571 |
2.02e-51 |
|
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: 182.33 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 143 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTas 222
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 fgiepgrkveympilEEAMRigqHKpdkvliynrpnmetvplasgrdldwdeemakaqsqdcvpvLSEHPLYILYTSGTT 302
Cdd:cd05973 79 ---------------DAANR---HK----------------------------------------LDSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 303 GLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKpvGTPDagAYFRVLA 382
Cdd:cd05973 101 GLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG--FSVE--STWRVIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 383 EHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTlfvAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPItasCIG 462
Cdd:cd05973 176 RLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSS---AGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVL---ANH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 463 LGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPP-GAFSGLW-KNQEAFKHlyfekfpGYYDTMDAG 540
Cdd:cd05973 250 HALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPlMWFRGYQlPDTPAIDG-------GYYLTGDTV 322
|
410 420 430
....*....|....*....|....*....|.
gi 1191882765 541 YMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05973 323 EFDPDGSFSFIGRADDVITMSGYRIGPFDVE 353
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
144-572 |
4.87e-51 |
|
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: 181.48 E-value: 4.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTasf 223
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 224 giepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwDEemakaqsqdcvpvlSEHPLYILYTSGTTG 303
Cdd:cd05971 85 -------------------------------------------------DG--------------SDDPALIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 304 LPKGVVRptgGYAVML----NWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVgtpDAGAYFR 379
Cdd:cd05971 102 PPKGALH---AHRVLLghlpGVQFPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF---DPKAALD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 380 VLAEHGVAALFTAPTAIRAIRQQdpgaalGKQYSLT--RFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSpIT 457
Cdd:cd05971 176 LMSRYGVTTAFLPPTALKMMRQQ------GEQLKHAqvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNL-VI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 458 ASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEAFKhlyfEKFPG-YYDT 536
Cdd:cd05971 249 GNCSALFPIK---PGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELP-DPVAFLGYWNNPSATE----KKMAGdWLLT 320
|
410 420 430
....*....|....*....|....*....|....*.
gi 1191882765 537 MDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05971 321 GDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEE 356
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
68-565 |
1.28e-47 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 176.14 E-value: 1.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 68 SVADPERFWGKAAE--QISWYKPWTKTLENRHSSSTSWFVEGMLNMCYNAIdRHiesGKGDKVAIIYDSPvTDTKATITY 145
Cdd:PRK03584 43 SVEDLEAFWQSVWDffGVIGSTPYTVVLAGRRMPGARWFPGARLNYAENLL-RH---RRDDRPAIIFRGE-DGPRRELSW 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 146 KEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA---S 222
Cdd:PRK03584 118 AELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVdgyR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 FGiepGRKVEYMPILEEamrIGQHKPD--KVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQ--DCVPVLSEHPLYILYT 298
Cdd:PRK03584 198 YG---GKAFDRRAKVAE---LRAALPSleHVVVVPYLGPAAAAAALPGALLWEDFLAPAEAAelEFEPVPFDHPLWILYS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 299 SGTTGLPKGVVRPTGG------YAVMLNWtmssiyGLKPGEVWWAASDLGWV-----VGhsyicyGPLIhGNTTVLYEGK 367
Cdd:PRK03584 272 SGTTGLPKCIVHGHGGillehlKELGLHC------DLGPGDRFFWYTTCGWMmwnwlVS------GLLV-GATLVLYDGS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 368 PvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWskkVFRVPVLDHW 447
Cdd:PRK03584 339 P-FYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKA--GLVPGETHDLSALRTIGSTGSPLPPEGFDW---VYEHVKADVW 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 448 WQTETGSPITASCIGLGNSKTPP-PGQAGKSVPGYNVMILDDNMQKLKARcLGNIVVKLPLP--PgafSGLW--KNQEAF 522
Cdd:PRK03584 413 LASISGGTDICSCFVGGNPLLPVyRGEIQCRGLGMAVEAWDEDGRPVVGE-VGELVCTKPFPsmP---LGFWndPDGSRY 488
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1191882765 523 KHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRI 565
Cdd:PRK03584 489 RDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRI 531
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
68-565 |
2.00e-44 |
|
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: 167.06 E-value: 2.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 68 SVADPERFWGKAAE--QISWYKPWTKTLEN-RHSSSTSWFVEGMLNMCYNAIdRHIESGkgDKVAIIYDSpvTDTKATIT 144
Cdd:cd05943 26 SVDDPGAFWAAVWDfsGVRGSKPYDVVVVSgRIMPGARWFPGARLNYAENLL-RHADAD--DPAAIYAAE--DGERTEVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 145 YKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFG 224
Cdd:cd05943 101 WAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 225 IEPGRKVEYMP-ILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQ--DCVPVLSEHPLYILYTSGT 301
Cdd:cd05943 181 TYNGKRHDVREkVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDFLATGAAGelEFEPLPFDHPLYILYSSGT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 302 TGLPKGVVRPTGGY------AVMLNWtmssiyGLKPGEVWWAASDLGWVVGHSYIcyGPLIHGNTTVLYEGKPvGTPDAG 375
Cdd:cd05943 261 TGLPKCIVHGAGGTllqhlkEHILHC------DLRPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGSP-FYPDTN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 376 AYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW-SKKVFRvpvlDHWWQTETGS 454
Cdd:cd05943 332 ALWDLADEEGITVFGTSAKYLDALEKA--GLKPAETHDLSSLRTILSTGSPLKPESFDYvYDHIKP----DVLLASISGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 455 PITASCIGLGNSKTPP-PGQAGKSVPGYNVMILDDNMQKLKARcLGNIVVKLPLP--PGAFsglWKNQEA--FKHLYFEK 529
Cdd:cd05943 406 TDIISCFVGGNPLLPVyRGEIQCRGLGMAVEAFDEEGKPVWGE-KGELVCTKPFPsmPVGF---WNDPDGsrYRAAYFAK 481
|
490 500 510
....*....|....*....|....*....|....*.
gi 1191882765 530 FPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRI 565
Cdd:cd05943 482 YPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRI 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
125-572 |
1.46e-42 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 158.16 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:cd17631 9 PDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVtasfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdc 284
Cdd:cd17631 83 EVAYILADSGAKVLF----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 285 vpvlsEHPLYILYTSGTTGLPKGVVRPTGG-YAVMLNWTMSsiYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVL 363
Cdd:cd17631 98 -----DDLALLMYTSGTTGRPKGAMLTHRNlLWNAVNALAA--LDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVI 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 364 YEGkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkQYSLTRFKTLFVAGERCDVETLE-WskKVFRVP 442
Cdd:cd17631 171 LRK-----FDPETVLDLIERHRVTSFFLVPTMIQALLQH-PRFA---TTDLSSLRAVIYGGAPMPERLLRaL--QARGVK 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 443 VLDHWWQTETGSPITAsciglgnskTPP------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLW 516
Cdd:cd17631 240 FVQGYGMTETSPGVTF---------LSPedhrrkLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR---GPHVMAGYW 307
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 517 KNQEA----FKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd17631 308 NRPEAtaaaFRD-------GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVED 360
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
138-572 |
5.15e-42 |
|
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: 157.76 E-value: 5.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 138 DTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKV 217
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 218 VVTASFGIE----------PGRKVEYMPILEEAMrigqhkpdkvliynrPNMETVPLASGRDLDWDEEMAKAQSQDcvpv 287
Cdd:cd05911 86 IFTDPDGLEkvkeaakelgPKDKIIVLDDKPDGV---------------LSIEDLLSPTLGEEDEDLPPPLKDGKD---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 288 lseHPLYILYTSGTTGLPKGVVRPtggYAVMLNWTMSSIYGLK----PGEVWWAASDLGWVVG-HSYICYgpLIHGNTTV 362
Cdd:cd05911 147 ---DTAAILYSSGTTGLPKGVCLS---HRNLIANLSQVQTFLYgndgSNDVILGFLPLYHIYGlFTTLAS--LLNGATVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 363 LYEGkpvgtPDAGAYFRVLAEHGVAALFTAPtAIRAIRQQDPgaaLGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVP 442
Cdd:cd05911 219 IMPK-----FDSELFLDLIEKYKITFLYLVP-PIAAALAKSP---LLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 443 VLDHWW-QTETGSPITASCIGlgnskTPPPGQAGKSVPGYNVMILDDN-MQKLKARCLGNIVVKLPLppgAFSGLWKNQE 520
Cdd:cd05911 290 TIKQGYgMTETGGILTVNPDG-----DDKPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQ---VMKGYYNNPE 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 521 AFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05911 362 ATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEA 411
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
125-572 |
6.29e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 158.04 E-value: 6.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAiiydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI-HSL-IFggFA 202
Cdd:PRK06187 20 PDKEA------VYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVlHPInIR--LK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 203 SKELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLAsgrdLDWDEEMAKAQSQ 282
Cdd:PRK06187 92 PEEIAYILNDAEDRVVLVDS---------EFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEV----GEYEELLAAASDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 283 DCVPVLSEHPLY-ILYTSGTTGLPKGVVRptgGYAVMLNWTMSSIYGLKpgevwWAASDLGWVV---GHSY---ICYGPL 355
Cdd:PRK06187 159 FDFPDIDENDAAaMLYTSGTTGHPKGVVL---SHRNLFLHSLAVCAWLK-----LSRDDVYLVIvpmFHVHawgLPYLAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 356 IHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETLEWS 435
Cdd:PRK06187 231 MAGAKQVI-----PRRFDPENLLDLIETERVTFFFAVPTIWQMLLK----APRAYFVDFSSLRLVIYGGAALPPALLREF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 436 KKVFRVPVLDHWWQTETGSPITASciglgnsktPPPGQ----------AGKSVPGYNVMILDDNMQKLKARC--LGNIVV 503
Cdd:PRK06187 302 KEKFGIDLVQGYGMTETSPVVSVL---------PPEDQlpgqwtkrrsAGRPLPGVEARIVDDDGDELPPDGgeVGEIIV 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 504 KlplPPGAFSGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK06187 373 R---GPWLMQGYWNRPEATA----ETIDgGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELED 435
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
110-571 |
1.23e-41 |
|
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: 157.66 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 110 NMCYNAIDRHIESgKGDKVAIIYDSPVTDTKaTITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACAR 189
Cdd:cd05970 17 NFAYDVVDAMAKE-YPDKLALVWCDDAGEER-IFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 190 IGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRkveympiLEEAMRIGQHKPDKVLIYNrpnmetvPLASGRd 269
Cdd:cd05970 95 LGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEE-------IEKAAPECPSKPKLVWVGD-------PVPEGW- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 270 LDWDEEMAKA-----QSQDCVPVLSEHPLYILYTSGTTGLPKGV----VRPTGGYAVMLNWtmssiYGLKPGEVWWAASD 340
Cdd:cd05970 160 IDFRKLIKNAspdfeRPTANSYPCGEDILLVYFSSGTTGMPKMVehdfTYPLGHIVTAKYW-----QNVREGGLHLTVAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 341 LGWVVGHSYICYGPLIHGNTTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTL 420
Cdd:cd05970 235 TGWGKAVWGKIYGQWIAGAAVFVYDYDKF---DPKALLEKLSKYGVTTFCAPPTIYRFLIREDL-----SRYDLSSLRYC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 421 FVAGERCDVETLEWSKKVFRVPVLDHWWQTETgspitASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGN 500
Cdd:cd05970 307 TTAGEALNPEVFNTFKEKTGIKLMEGFGQTET-----TLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGE 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191882765 501 IVVKLP--LPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05970 382 IVIRTSkgKPVGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVE 451
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
144-571 |
2.05e-37 |
|
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: 143.17 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVK-HGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAS 222
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 fgiepgrkveymPILEEAMRIGQhkpdkvLIYNRPNMETVPLASGRDLDWDEemakaqsqdcVPVLSEHPLYILYTSGTT 302
Cdd:TIGR01733 81 ------------ALASRLAGLVL------PVILLDPLELAALDDAPAPPPPD----------APSGPDDLAYVIYTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 303 GLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLYEGKPVGtPDAGAYFRVLA 382
Cdd:TIGR01733 133 GRPKGVVVTHRSLVNLLAW-LARRYGLDPDDRVLQFASLSFDASVEEI-FGALLAGATLVVPPEDEER-DDAALLAALIA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 383 EHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERCDVETLE-WSKKVFRVPVLDHWWQTETgsPITASCI 461
Cdd:TIGR01733 210 EHPVTVLNLTPSLLALLAAALPPA-------LASLRLVILGGEALTPALVDrWRARGPGARLINLYGPTET--TVWSTAT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 462 GLGNSKTPPPGQA--GKSVPGYNVMILDDNMQKLKARCLGNIVVklpLPPGAFSGLW----KNQEAFKHLYFEKFPGY-- 533
Cdd:TIGR01733 281 LVDPDDAPRESPVpiGRPLANTRLYVLDDDLRPVPVGVVGELYI---GGPGVARGYLnrpeLTAERFVPDPFAGGDGArl 357
|
410 420 430
....*....|....*....|....*....|....*...
gi 1191882765 534 YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:TIGR01733 358 YRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
144-571 |
4.65e-35 |
|
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: 138.75 E-value: 4.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKH-GVSKGDTVVIYMPMIPQAMYTMLACARIGAIhsLIFGG--FASKELSSRIDHAKPKVVVT 220
Cdd:cd05928 43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLV--FIPGTiqLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 221 ASfgiepgrkvEYMPILEEamrigqhkpdkvLIYNRPNMETVPLAS--GRD--LDWDEEMAKA-QSQDCVPVLSEHPLYI 295
Cdd:cd05928 121 SD---------ELAPEVDS------------VASECPSLKTKLLVSekSRDgwLNFKELLNEAsTEHHCVETGSQEPMAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 296 LYTSGTTGLPKGVVRPTGGYAvmLNWTMSSIY--GLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVgtpD 373
Cdd:cd05928 180 YFTSGTTGSPKMAEHSHSSLG--LGLKVNGRYwlDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLPRF---D 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 374 AGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETG 453
Cdd:cd05928 255 PLVILKTLSSYPITTFCGAPTVYRMLVQQDL-----SSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 454 spitascIGLGNSKTP--PPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKL-PLPP-GAFSGLWKNQEAFKHLYFEK 529
Cdd:cd05928 330 -------LICANFKGMkiKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVkPIRPfGLFSGYVDNPEKTAATIRGD 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1191882765 530 FpgyYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05928 403 F---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVE 441
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
143-571 |
4.27e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 133.96 E-value: 4.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 143 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAs 222
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 fgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdcvpvlsehPLYILYTSGTT 302
Cdd:cd05934 83 ---------------------------------------------------------------------PASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 303 GLPKGVVRPtggYAVMLNW--TMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEgkpvgTPDAGAYFRV 380
Cdd:cd05934 94 GPPKGVVIT---HANLTFAgyYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP-----RFSASRFWSD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 381 LAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTRFKTLFVAGERCDVETlEWSKKvFRVPVLDHWWQTETGSPITASc 460
Cdd:cd05934 166 VRRYGATVTNYLGAMLSYLLAQPPSP----DDRAHRLRAAYGAPNPPELHE-EFEER-FGVRLLEGYGMTETIVGVIGP- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 461 iglgNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEA----FKHlyfekfpGYYDT 536
Cdd:cd05934 239 ----RDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWGFFKGYYNMPEAtaeaMRN-------GWFHT 307
|
410 420 430
....*....|....*....|....*....|....*
gi 1191882765 537 MDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05934 308 GDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVE 342
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
142-572 |
1.29e-33 |
|
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: 132.89 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA 221
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 222 SfgiepgrkveympileeamRIGQHKPdkvliynrpnmetvplasgrdldwdEEMAKAqsqdcvpvlsehPLYILYTSGT 301
Cdd:cd05903 81 E-------------------RFRQFDP-------------------------AAMPDA------------VALLLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 302 TGLPKGVVRPTggyavmlNWTMSSI------YGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEgkpVGTPDAG 375
Cdd:cd05903 105 TGEPKGVMHSH-------NTLSASIrqyaerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IWDPDKA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 376 AyfRVLAEHGVAALFTAPT----AIRAIRQQDPgaalgkqySLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTE 451
Cdd:cd05903 175 L--ALMREHGVTFMMGATPfltdLLNAVEEAGE--------PLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 452 TGSpitasciGLGNSKTPPPGQA----GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQeafkHLYF 527
Cdd:cd05903 245 CPG-------AVTSITPAPEDRRlytdGRPLPGVEIKVVDDTGATLAPGVEGELLSR---GPSVFLGYLDRP----DLTA 310
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1191882765 528 EKFP-GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05903 311 DAAPeGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVED 356
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
126-571 |
1.07e-32 |
|
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: 130.34 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTASfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdcv 285
Cdd:cd05930 76 LAYILEDSGAKLVLTDP--------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 286 pvlsEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLYE 365
Cdd:cd05930 93 ----DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVLQFTSFSFDVSVWEI-FGALLAGATLVVLP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 366 GKPVGTPDagAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqysLTRFKTLFVAGERCDVETLE-WSKKVFRVPVL 444
Cdd:cd05930 167 EEVRKDPE--ALADLLAEEGITVLHLTPSLLRLLLQELELAA------LPSLRLVLVGGEALPPDLVRrWRELLPGARLV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 445 DHWWQTETGSPITASCIGLGN-SKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW------- 516
Cdd:cd05930 239 NLYGPTEATVDATYYRVPPDDeEDGRVP--IGRPIPNTRVYVLDENLR--------------PVPPGVPGELYiggagla 302
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 517 --------KNQEAFKHLYFekFPG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05930 303 rgylnrpeLTAERFVPNPF--GPGerMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIE 365
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
126-572 |
1.18e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 131.59 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIGQHKPDKVliynrPNMETVPLASGRDLDWDEeMAKAQSQDC- 284
Cdd:PRK08316 100 LAYILDHSGARAFLVDP---------ALAPTAEAALALLPVDTLIL-----SLVLGGREAPGGWLDFAD-WAEAGSVAEp 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 285 -VPVLSEHPLYILYTSGTTGLPKGVVRPTGgyAVMLNWtMSSIYGLKpgevwWAASDlgwVVGHS---YIC------YGP 354
Cdd:PRK08316 165 dVELADDDLAQILYTSGTESLPKGAMLTHR--ALIAEY-VSCIVAGD-----MSADD---IPLHAlplYHCaqldvfLGP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 355 LIH-GNTTVLYEGkpvgtPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPGaalgkQYSLTRFKTLFVAGERCDVETL 432
Cdd:PRK08316 234 YLYvGATNVILDA-----PDPELILRTIEAERITSFFAPPTVwISLLRHPDFD-----TRDLSSLRKGYYGASIMPVEVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 433 EWSKKvfRVPVLDHW---WQTETGSpiTASCIGLGNSKTpPPGQAGKsvPGYNV--MILDDNMQKLKARCLGNIVVKlpl 507
Cdd:PRK08316 304 KELRE--RLPGLRFYncyGQTEIAP--LATVLGPEEHLR-RPGSAGR--PVLNVetRVVDDDGNDVAPGEVGEIVHR--- 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882765 508 PPGAFSGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK08316 374 SPQLMLGYWDDpektAEAFRG-------GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE 435
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
113-572 |
2.36e-32 |
|
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: 130.57 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 113 YNAI---DRHIESGKGDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACAR 189
Cdd:cd05959 3 YNAAtlvDLNLNEGRGDKTAFIDDA------GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 190 IGAIHSLIFGGFASKELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIGQHKpDKVLIYNRPNMETVPLASGRD 269
Cdd:cd05959 77 AGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG---------ELAPVLAAALTKSEHT-LVVLIVSGGAGPEAGALLLAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 270 LdWDEEmakAQSQDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSY 349
Cdd:cd05959 147 L-VAAE---AEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 350 ICYGPLIHGNTTVLYEGKPvgTPDagAYFRVLAEHGVAALFTAPTaIRAIRQQDPGAalgKQYSLTRFKTLFVAGERCDV 429
Cdd:cd05959 223 SLTFPLSVGATTVLMPERP--TPA--AVFKRIRRYRPTVFFGVPT-LYAAMLAAPNL---PSRDLSSLRLCVSAGEALPA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 430 ETLEWSKKVFRVPVLDHWWQTETGSpitascIGLGNskTP---PPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlp 506
Cdd:cd05959 295 EVGERWKARFGLDILDGIGSTEMLH------IFLSN--RPgrvRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVR-- 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 507 lPPGAFSGLWKNQEAFKhlyfEKFPGY-YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05959 365 -GPSSATMYWNNRDKTR----DTFQGEwTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVES 426
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
126-572 |
1.88e-30 |
|
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: 124.73 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:cd05926 2 DAPALV----VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTASFGIEP---GRKVEYMPILEEAMrigqhkpDKVLIYNRPNMETVPLASGrDLDWDEEMAKAQSQ 282
Cdd:cd05926 78 FEFYLADLGSKLVLTPKGELGPasrAASKLGLAILELAL-------DVGVLIRAPSAESLSNLLA-DKKNAKSEGVPLPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 283 DcvPVLsehplyILYTSGTTGLPKGV-VRPTGGYAVMLNwtMSSIYGLKPgevwwaaSDLGWVVghsyicyGPLIHGN-- 359
Cdd:cd05926 150 D--LAL------ILHTSGTTGRPKGVpLTHRNLAASATN--ITNTYKLTP-------DDRTLVV-------MPLFHVHgl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 360 -----TTVLYEGKPVGTP--DAGAYFRVLAEHGvAALFTA-PTaIRAIRQQDPGAALGKQYSLTRFktLFVAGERCDVET 431
Cdd:cd05926 206 vasllSTLAAGGSVVLPPrfSASTFWPDVRDYN-ATWYTAvPT-IHQILLNRPEPNPESPPPKLRF--IRSCSASLPPAV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 432 LEWSKKVFRVPVLDHWWQTETGSPITASCIglgNSKTPPPGQAGKSVpGYNVMILDDNMQKLKARCLGNIVVKlplPPGA 511
Cdd:cd05926 282 LEALEATFGAPVLEAYGMTEAAHQMTSNPL---PPGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLR---GPNV 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191882765 512 FSGLWKNQEAFKHlYFEKFpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05926 355 TRGYLNNPEANAE-AAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDG 413
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
117-571 |
7.83e-30 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 123.62 E-value: 7.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 117 DRHIESgKGDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSL 196
Cdd:PRK13295 31 DACVAS-CPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 197 IFGGFASKELSSRIDHAKPKV-VVTASFgiepgRKVEYmpileEAMRIGQHkPDkvliynRPNMETVPLASGRDLD-WDE 274
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVlVVPKTF-----RGFDH-----AAMARRLR-PE------LPALRHVVVVGGDGADsFEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 275 ---EMAKAQSQDCVPVLSEHPL------YILYTSGTTGLPKGVVRPTggyavmlNWTMSSIY------GLKPGEVWWAAS 339
Cdd:PRK13295 173 lliTPAWEQEPDAPAILARLRPgpddvtQLIYTSGTTGEPKGVMHTA-------NTLMANIVpyaerlGLGADDVILMAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 340 DLGWVVGHSYICYGPLIHGNTTVLYEgkpVGTPDAGAyfRVLAEHGVAalFT---APTAIRAIRQQDPGAalgkqYSLTR 416
Cdd:PRK13295 246 PMAHQTGFMYGLMMPVMLGATAVLQD---IWDPARAA--ELIRTEGVT--FTmasTPFLTDLTRAVKESG-----RPVSS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 417 FKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSpitASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKAR 496
Cdd:PRK13295 314 LRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA---VTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAG 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 497 CLGNIVVKlplPPGAFSGLWKNQeafkHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK13295 391 QIGRLQVR---GCSNFGGYLKRP----QLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIE 458
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
124-572 |
2.04e-29 |
|
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: 121.52 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 124 KGDKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI---HSLIFGG 200
Cdd:cd05936 12 FPDKTALIFM------GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvpLNPLYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 201 fasKELSSRIDHAKPKVVVTA-SF--GIEPGRKVEYMPILeeamrigqHKPDKVLIynrpnmetvplasgrdldwdeema 277
Cdd:cd05936 86 ---RELEHILNDSGAKALIVAvSFtdLLAAGAPLGERVAL--------TPEDVAVL------------------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 278 kaqsqdcvpvlsehplyiLYTSGTTGLPKGVvrptggyavMLnwTMSSIYGLKPGEVWWAASDLgwVVGHSYICYGPLIH 357
Cdd:cd05936 131 ------------------QYTSGTTGVPKGA---------ML--THRNLVANALQIKAWLEDLL--EGDDVVLAALPLFH 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 358 --------------GNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGaalgKQYSLTRFKTLFVA 423
Cdd:cd05936 180 vfgltvalllplalGATIVL-----IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEF----KKRDFSSLRLCISG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 424 GERCDVETLEWSKKVFRVPVLDHWWQTETgSPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVV 503
Cdd:cd05936 251 GAPLPVEVAERFEELTGVPIVEGYGLTET-SPVVAVNPLDGPRK---PGSIGIPLPGTEVKIVDDDGEELPPGEVGELWV 326
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882765 504 KlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05936 327 R---GPQVMKGYWNRPEETAEAFVD---GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEE 389
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
133-571 |
4.63e-29 |
|
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: 119.87 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 133 DSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDH 212
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 213 AKPKVVVTasfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqSQDCVpvlsehp 292
Cdd:cd05919 81 CEARLVVT------------------------------------------------------------SADDI------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 293 LYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDL--GWVVGHSYIcyGPLIHGNTTVLYEGKpvg 370
Cdd:cd05919 94 AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNSLW--FPLAVGASAVLNPGW--- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 371 tPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQT 450
Cdd:cd05919 169 -PTAERVLATLARFRPTVLYGVPTFYANLLDS----CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGAT 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 451 ETGSPITASCIGLGNsktppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLplpPGAFSGLWKNQEAFKHLYFEkf 530
Cdd:cd05919 244 EVGHIFLSNRPGAWR-----LGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG---PSAAVGYWNNPEKSRATFNG-- 313
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1191882765 531 pGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05919 314 -GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVE 353
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
126-571 |
4.72e-29 |
|
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: 123.04 E-value: 4.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMP----MIPqamyTMLACARIGAIHslifggf 201
Cdd:COG1020 491 DAVAVVFGD------QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLErsleMVV----ALLAVLKAGAAY------- 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 202 askeLSsrIDHAKPkvvvtasfgiePGRkVEYMpiLEEAmrigqhKPdKVLIYNRPNMETVPLASGRDLDWDEEMAKAQS 281
Cdd:COG1020 554 ----VP--LDPAYP-----------AER-LAYM--LEDA------GA-RLVLTQSALAARLPELGVPVLALDALALAAEP 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 282 QD--CVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGN 359
Cdd:COG1020 607 ATnpPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAW-MQRRYGLGPGDRVLQFASLSFDASVWEI-FGALLSGA 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 360 TTVLYEgkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERCDVETLE-WSKKV 438
Cdd:COG1020 685 TLVLAP--PEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEA-------LPSLRLVLVGGEALPPELVRrWRARL 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 439 FRVPVLDHWWQTETGspITASCiglgnSKTPPPGQAGKSVP------GYNVMILDDNMQklkarclgnivvklPLPPGAf 512
Cdd:COG1020 756 PGARLVNLYGPTETT--VDSTY-----YEVTPPDADGGSVPigrpiaNTRVYVLDAHLQ--------------PVPVGV- 813
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 513 SG-LW---------------KNQEAFKHLYFEkFPG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:COG1020 814 PGeLYiggaglargylnrpeLTAERFVADPFG-FPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIE 889
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
114-571 |
2.25e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 119.11 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 114 NAIDRHIESgKGDKVAIIYdspvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI 193
Cdd:PRK07786 21 NQLARHALM-QPDAPALRF------LGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 194 HSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKV-EYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLDW 272
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVrDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 273 DEemakaqsqdcvpvlsehPLYILYTSGTTGLPKGVVRPtggYAVMLNWTMSSIYGLK---PGEVWWAASDLGWVVGHSY 349
Cdd:PRK07786 174 DS-----------------PALIMYTSGTTGRPKGAVLT---HANLTGQAMTCLRTNGadiNSDVGFVGVPLFHIAGIGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 350 ICYGPLIhGNTTVLYegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlGKQYSLtRFKTlFVAGERCDV 429
Cdd:PRK07786 234 MLPGLLL-GAPTVIY---PLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAV-CAEQQAR-PRDLAL-RVLS-WGAAPASDT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 430 ETLEWSKKVFRVPVLDHWWQTETgSPITasCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPP 509
Cdd:PRK07786 306 LLRQMAATFPEAQILAAFGQTEM-SPVT--CMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR---AP 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191882765 510 GAFSGLWKNQEAFKhlyfEKFPG-YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK07786 380 TLMSGYWNNPEATA----EAFAGgWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVE 438
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
68-571 |
7.75e-28 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 118.64 E-value: 7.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 68 SVADPERFWGKAAEQ--ISWYKP----WTKTLENRHSSStsWFVEGMLNMCYNAIDRHIESgKGDKVAIIY------DSP 135
Cdd:PLN03052 129 SVENPEVYWSIVLDElsLVFSVPprciLDTSDESNPGGQ--WLPGAVLNVAECCLTPKPSK-TDDSIAIIWrdegsdDLP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 136 VTdtkaTITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 215
Cdd:PLN03052 206 VN----RMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 216 KVVVTASFGIEPGRKVE-YMPILEEAmrigqhKPDKVLIYNRPNMETVPLASGrDLDWDEEMAKA----QSQDCVPVlsE 290
Cdd:PLN03052 282 KAIFTQDVIVRGGKSIPlYSRVVEAK------APKAIVLPADGKSVRVKLREG-DMSWDDFLARAnglrRPDEYKAV--E 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 291 HPL----YILYTSGTTGLPKGVvrPtggyavmlnWTMSSiyGLKPGEVWWAASD------------LGWVVGHsYICYGP 354
Cdd:PLN03052 353 QPVeaftNILFSSGTTGEPKAI--P---------WTQLT--PLRAAADAWAHLDirkgdivcwptnLGWMMGP-WLVYAS 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 355 LIHGNTTVLYEGKPVGTpdagAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTRFKTLFVAGERCDVETLEW 434
Cdd:PLN03052 419 LLNGATLALYNGSPLGR----GFAKFVQDAKVTMLGTVPSIVKTWKNTNCMAGL----DWSSIRCFGSTGEASSVDDYLW 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 435 -SKKVFRVPVLDHWWQTETGSPItascigLGNSKTPPPGQAGKSVP--GYNVMILDDNMQKL--KARCLGNIVVkLPLPP 509
Cdd:PLN03052 491 lMSRAGYKPIIEYCGGTELGGGF------VTGSLLQPQAFAAFSTPamGCKLFILDDSGNPYpdDAPCTGELAL-FPLMF 563
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 510 GAFSGLWkNQEAFKhLYFEKFPGYYDTMDAGYMDE-----EGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PLN03052 564 GASSTLL-NADHYK-VYFKGMPVFNGKILRRHGDIfertsGGYYRAHGRADDTMNLGGIKVSSVEIE 628
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
125-558 |
3.73e-27 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 115.02 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIyDSPvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:cd05904 19 PSRPALI-DAA---TGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRigqhkpdKVLIYNRPnmETVPLASGRDLDWDEEMAKAQsqdc 284
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTA---------ELAEKLASLAL-------PVVLLDSA--EFDSLSFSDLLFEADEAEPPV---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 285 VPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSI-YGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVL 363
Cdd:cd05904 153 VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 364 yegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF-RVP 442
Cdd:cd05904 233 -----MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKS----PIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 443 VLDHWWQTETgSPITASCigLGNSKTP-PPGQAGKSVPGYNVMILDdnmqklkarclgnIVVKLPLPPGaFSG-LW---- 516
Cdd:cd05904 304 LGQGYGMTES-TGVVAMC--FAPEKDRaKYGSVGRLVPNVEAKIVD-------------PETGESLPPN-QTGeLWirgp 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1191882765 517 -------KNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVI 558
Cdd:cd05904 367 simkgylNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELI 413
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
126-572 |
5.09e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 114.29 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK03640 17 DRTAIEFE------EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTASfgiepgrkvEYMPileeamrigQHKPDKVLIYnrpnmetvplasgrdldwdEEMAKAQSQDcV 285
Cdd:PRK03640 91 LLWQLDDAEVKCLITDD---------DFEA---------KLIPGISVKF-------------------AELMNGPKEE-A 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 286 PVLSEHPL----YILYTSGTTGLPKGVVRPTGgyavmlNWTMSSI-----YGLKPGEVWWAASDLGWVVGHSyICYGPLI 356
Cdd:PRK03640 133 EIQEEFDLdevaTIMYTSGTTGKPKGVIQTYG------NHWWSAVgsalnLGLTEDDCWLAAVPIFHISGLS-ILMRSVI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 357 HGNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTrFKTLFVAGERCDVETLEWSK 436
Cdd:PRK03640 206 YGMRVVLVE-----KFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEG----TYPSS-FRCMLLGGGPAPKPLLEQCK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 437 KvFRVPVLDHWWQTETGSPITasciglgnskTPPP-------GQAGKSVPGYNVMILDDNmQKLKARCLGNIVVKLP-LP 508
Cdd:PRK03640 276 E-KGIPVYQSYGMTETASQIV----------TLSPedaltklGSAGKPLFPCELKIEKDG-VVVPPFEEGEIVVKGPnVT 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191882765 509 PGAFSGLWKNQEAFKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK03640 344 KGYLNREDATRETFQD-------GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEE 400
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
125-572 |
3.02e-26 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 113.27 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIYdsPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:COG1022 25 PDRVALRE--KEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVtasfgiepgrkVEYMPILEEAMRIGQHKPD--KVLIYNRPNMETVP--------LASGRDLDWDE 274
Cdd:COG1022 103 EVAYILNDSGAKVLF-----------VEDQEQLDKLLEVRDELPSlrHIVVLDPRGLRDDPrllsldelLALGREVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 275 EMAKAQSQdcvpVLSEHPLYILYTSGTTGLPKGVvrptggyavML---NWT-----MSSIYGLKPGEVW-----WAasdl 341
Cdd:COG1022 172 ELEARRAA----VKPDDLATIIYTSGTTGRPKGV---------MLthrNLLsnaraLLERLPLGPGDRTlsflpLA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 342 gWVVGHSyICYGPLIHGNTTVLYEG-----------KP---VGTPD------AGAYFRVLAEHGVA-ALFTA--PTAIRA 398
Cdd:COG1022 235 -HVFERT-VSYYALAAGATVAFAESpdtlaedlrevKPtfmLAVPRvwekvyAGIQAKAEEAGGLKrKLFRWalAVGRRY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 399 IRQQD----PGAALGKQYSL--------------TRFKTLFVAGERCDVETLEWskkvFR---VPVLDHWWQTETGSPIT 457
Cdd:COG1022 313 ARARLagksPSLLLRLKHALadklvfsklrealgGRLRFAVSGGAALGPELARF----FRalgIPVLEGYGLTETSPVIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 458 ASCigLGNSKtppPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTM 537
Cdd:COG1022 389 VNR--PGDNR---IGTVGPPLPGVEVKIAED----------GEILVR---GPNVMKGYYKNPEATAEAFDAD--GWLHTG 448
|
490 500 510
....*....|....*....|....*....|....*.
gi 1191882765 538 DAGYMDEEGYVYVMSRVDDVINVA-GHRISAGAIEE 572
Cdd:COG1022 449 DIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIEN 484
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
125-572 |
6.83e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 112.36 E-value: 6.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIY--DSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIG---AIHSLIFG 199
Cdd:PRK07529 39 PDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGianPINPLLEP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 200 GfaskELSSRIDHAKPKVVVTAsfGIEPG----RKVEYM--------PILEEAM--RIGQHKPDKVLIYNRPnmetvplA 265
Cdd:PRK07529 119 E----QIAELLRAAGAKVLVTL--GPFPGtdiwQKVAEVlaalpelrTVVEVDLarYLPGPKRLAVPLIRRK-------A 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 266 SGRDLDWDEEMAK--AQSQDCVPVLSEHPLYILY-TSGTTGLPKgVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLG 342
Cdd:PRK07529 186 HARILDFDAELARqpGDRLFSGRPIGPDDVAAYFhTGGTTGMPK-LAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 343 WVVGHSYICYGPLIHGNTTVLyeGKPVGTPDAGAY---FRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKT 419
Cdd:PRK07529 265 HVNALLVTGLAPLARGAHVVL--ATPQGYRGPGVIanfWKIVERYRINFLSGVPTVYAALLQVPVDGH-----DISSLRY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 420 LFVAGERCDVETLEWSKKVFRVPVLDHWWQTEtgspitASCIglgNSKTPP-----PGQAGKSVPGYNV--MILDDN--- 489
Cdd:PRK07529 338 ALCGAAPLPVEVFRRFEAATGVRIVEGYGLTE------ATCV---SSVNPPdgerrIGSVGLRLPYQRVrvVILDDAgry 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 490 MQKLKARCLGNIVVKlplPPGAFSGlWKNQEAFKHLYFEkfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGA 569
Cdd:PRK07529 409 LRDCAVDEVGVLCIA---GPNVFSG-YLEAAHNKGLWLE--DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAA 482
|
...
gi 1191882765 570 IEE 572
Cdd:PRK07529 483 IEE 485
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
174-571 |
5.13e-25 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 108.75 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 174 MPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFGIEPGRKveyMPILEEAMRIGQHKPDKVLI 253
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRA---LPLYSKVVEAAPAKAIVLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 254 YNRPNmeTVPLASGrDLDWDEEMAKAQSQDCV------PVL--SEHPLYILYTSGTTGLPKGVvrptggyavmlNWTMSS 325
Cdd:PLN03051 78 AGEPV--AVPLREQ-DLSWCDFLGVAAAQGSVggneysPVYapVESVTNILFSSGTTGEPKAI-----------PWTHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 326 -IYG---------LKPGEVWWAASDLGWVVGhSYICYGPLIHGNTTVLYEGKPVGtpdaGAYFRVLAEHGVAALFTAPTA 395
Cdd:PLN03051 144 pLRCasdgwahmdIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLG----RGFGKFVQDAGVTVLGLVPSI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 396 IRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW--SKKVFRVPVLDHWWQTETGSPITASCIGLGNSktppPGQ 473
Cdd:PLN03051 219 VKAWRHT--GAFAMEGLDWSKLRVFASTGEASAVDDVLWlsSVRGYYKPVIEYCGGTELASGYISSTLLQPQA----PGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 474 AGKSVPGYNVMILDDNMQKL--KARCLGNIVVKLPLPPGAFSGLWKNQEAfkhLYFEKFPGYY----------DTMDAgy 541
Cdd:PLN03051 293 FSTASLGTRFVLLNDNGVPYpdDQPCVGEVALAPPMLGASDRLLNADHDK---VYYKGMPMYGskgmplrrhgDIMKR-- 367
|
410 420 430
....*....|....*....|....*....|
gi 1191882765 542 mDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PLN03051 368 -TPGGYFCVQGRADDTMNLGGIKTSSVEIE 396
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
142-573 |
6.92e-25 |
|
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: 107.68 E-value: 6.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTa 221
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 222 sfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdlDWDEEMAKaqsqdcvpvlsehplyILYTSGT 301
Cdd:cd05907 84 -------------------------------------------------EDPDDLAT----------------IIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 302 TGLPKGVVRPTGGYAvmlnWTMSSIY---GLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVGTPDagayf 378
Cdd:cd05907 99 TGRPKGVMLSHRNIL----SNALALAerlPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDD----- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 379 rvLAEHGVAALFTAPTAIR----AIRQQDPGAALGKQY---SLTRFKTLFVAGERCDVETLEWSKKvFRVPVLDHWWQTE 451
Cdd:cd05907 170 --LSEVRPTVFLAVPRVWEkvyaAIKVKAVPGLKRKLFdlaVGGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTE 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 452 TGSPITASCIGlgnskTPPPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfP 531
Cdd:cd05907 247 TSAVVTLNPPG-----DNRIGTVGKPLPGVEVRIADD----------GEILVR---GPNVMLGYYKNPEATAEALDA--D 306
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1191882765 532 GYYDTMDAGYMDEEGYVYVMSRVDDVI-NVAGHRISAGAIEEE 573
Cdd:cd05907 307 GWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENA 349
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
144-572 |
2.09e-24 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 107.15 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASF 223
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 224 GIEpgrKVEYMPILEEAMRigqhkpdKVLIYNRPNMETVPLAsgrdLDWDEEMAKAQSQDCVPVLSEHPLYILYTSGTTG 303
Cdd:PRK06155 128 LLA---ALEAADPGDLPLP-------AVWLLDAPASVSVPAG----WSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 304 LPKGVVRPTGGYavmlnwtmssiyglkpgeVWW---AASDLGWVVGHSYICYGPLIHGNT------TVLYEGKPVGTP-- 372
Cdd:PRK06155 194 PSKGVCCPHAQF------------------YWWgrnSAEDLEIGADDVLYTTLPLFHTNAlnaffqALLAGATYVLEPrf 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 373 DAGAYFRVLAEHGvAALFTAPTAIRAIRQQDPGAALGKQYSLTRfkTLFVAGERCDVETLewsKKVFRVPVLDHWWQTET 452
Cdd:PRK06155 256 SASGFWPAVRRHG-ATVTYLLGAMVSILLSQPARESDRAHRVRV--ALGPGVPAALHAAF---RERFGVDLLDGYGSTET 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 453 GSPITASciglgnSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAF-SGLW----KNQEAFKHLYF 527
Cdd:PRK06155 330 NFVIAVT------HGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAD-EPFAFaTGYFgmpeKTVEAWRNLWF 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1191882765 528 EkfpgyydTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK06155 403 H-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQ 440
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
142-572 |
3.07e-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: 105.64 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLV-KHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVT 220
Cdd:cd05958 10 EWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 221 ASfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemaKAQSQDCVPVLSehplyilYTSG 300
Cdd:cd05958 90 AH-------------------------------------------------------ALTASDDICILA-------FTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 301 TTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKpvgTPDAgaYFRV 380
Cdd:cd05958 108 TTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA---TPDL--LLSA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 381 LAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTEtgspitASC 460
Cdd:cd05958 183 IARYKPTVLFTAPTAYRAMLAHPDAA----GPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTE------MFH 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 461 IGLGNSKTPP-PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlppgafSGLWKNQEAFKHLYFEKfpGYYDTMDA 539
Cdd:cd05958 253 IFISARPGDArPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCRYLADKRQRTYVQG--GWNITGDT 324
|
410 420 430
....*....|....*....|....*....|...
gi 1191882765 540 GYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05958 325 YSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVED 357
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
126-571 |
6.77e-24 |
|
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: 105.28 E-value: 6.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:cd05923 16 DACAIA----DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVtasfgiepgrkveympileeamrigqHKPDkvliynRPNMETVPLASGRDLDWDEEMAKAQSQDCV 285
Cdd:cd05923 92 LAELIERGEMTAAV--------------------------IAVD------AQVMDAIFQSGVRVLALSDLVGLGEPESAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 286 PVLS------EHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPG--EVWWAASDLGWVVGHSYICYGPLIH 357
Cdd:cd05923 140 PLIEdpprepEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLF-MSTQAGLRHGrhNVVLGLMPLYHVIGFFAVLVAALAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 358 GNTTVlyegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrqqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKK 437
Cdd:cd05923 219 DGTYV-----VVEEFDPADALKLIEQERVTSLFATPTHLDAL----AAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 438 VFRVPVLDHWWQTETGSPITAsciglgnsKTPPPGQAGKsvPGYN-----VMILDDNMQKLKARCLGNIVVKLPlPPGAF 512
Cdd:cd05923 290 HLPGEKVNIYGTTEAMNSLYM--------RDARTGTEMR--PGFFsevriVRIGGSPDEALANGEEGELIVAAA-ADAAF 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 513 SGLWKNQEA-FKHLYFekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05923 359 TGYLNQPEAtAKKLQD----GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIE 414
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
143-571 |
2.11e-23 |
|
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: 103.03 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 143 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhakpkVVVTAS 222
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGA------------------------VVIPAT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 FGIEPGRkveympiLEEAMRIGQHKPDKVliynrpnmetvplasgrdldwdEEMAKAqsqdcvpvlsEHPLYILYTSGTT 302
Cdd:cd05974 57 TLLTPDD-------LRDRVDRGGAVYAAV----------------------DENTHA----------DDPMLLYFTSGTT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 303 GLPKGVVRPTGGYAVMLNWTMSSIyGLKPGEVWWAASDLGWVvGHSYIC-YGPLIHGNTTVLYEGKPVgtpDAGAYFRVL 381
Cdd:cd05974 98 SKPKLVEHTHRSYPVGHLSTMYWI-GLKPGDVHWNISSPGWA-KHAWSCfFAPWNAGATVFLFNYARF---DAKRVLAAL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 382 AEHGVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKT----LFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPIt 457
Cdd:cd05974 173 VRYGVTTLCAPPTVWRMLIQQD----------LASFDVklreVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALV- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 458 asciglGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKArclGNIVVKL--PLPPGAFSGLWKNQEAFKHLYFEkfpGY 533
Cdd:cd05974 242 ------GNSPGQPvkAGSMGRPLPGYRVALLDPDGAPATE---GEVALDLgdTRPVGLMKGYAGDPDKTAHAMRG---GY 309
|
410 420 430
....*....|....*....|....*....|....*...
gi 1191882765 534 YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05974 310 YRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
133-571 |
2.41e-22 |
|
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: 100.01 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 133 DSPVTDTK-ATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRID 211
Cdd:cd05945 6 DRPAVVEGgRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 212 HAKPKVVVTAsfgiepgrkveympileeamrigqhkPDkvliynrpnmetvPLAsgrdldwdeemakaqsqdcvpvlseh 291
Cdd:cd05945 86 AAKPALLIAD--------------------------GD-------------DNA-------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 292 plYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVlyegkPVG- 370
Cdd:cd05945 101 --YIIFTSGSTGRPKGVQISHDNLVSFTNW-MLSDFPLGPGDVFLNQAPFSFDLSVMDL-YPALASGATLV-----PVPr 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 371 --TPDAGAYFRVLAEHGVAALFTAPTAIRAIRqQDPGAALGKQYSLTRFktLFvAGERCDVETLE-WSKKVFRVPVLDHW 447
Cdd:cd05945 172 daTADPKQLFRFLAEHGITVWVSTPSFAAMCL-LSPTFTPESLPSLRHF--LF-CGEVLPHKTARaLQQRFPDARIYNTY 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 448 WQTETGSPITASCIglgnskTPPPGQAGKSVP-GY-----NVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEa 521
Cdd:cd05945 248 GPTEATVAVTYIEV------TPEVLDGYDRLPiGYakpgaKLVILDEDGRPVPPGEKGELVIS---GPSVSKGYLNNPE- 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1191882765 522 fKHLY-FEKFPGY--YDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05945 318 -KTAAaFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIE 369
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
125-571 |
7.89e-22 |
|
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: 98.52 E-value: 7.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfask 204
Cdd:cd12116 1 PDATAVRDDD------RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAY---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 elssridhakpkVVVTASFgiePGRKVEYMpiLEEAmrigqhKPdKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQDC 284
Cdd:cd12116 65 ------------VPLDPDY---PADRLRYI--LEDA------EP-ALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 285 VPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNwTMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLY 364
Cdd:cd12116 121 TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH-SMRERLGLGPGDRLLAVTTYAFDISLLEL-LLPLLAGARVVIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 365 EGKpvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGkqysltrfKTLFVAGERCDVETLEwsKKVFRVPVL 444
Cdd:cd12116 199 PRE--TQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAG--------LTALCGGEALPPDLAA--RLLSRVGSL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 445 dhwWQ----TETgsPITASCIGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLWKNQE 520
Cdd:cd12116 267 ---WNlygpTET--TIWSTAARVTAAAGPIP--IGRPLANTQVYVLDAALR--------------PVPPGVPGELYIGGD 325
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 521 AFKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd12116 326 GVAQGYLgrpaltaERFvpdpfagPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIE 392
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
145-573 |
8.79e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 99.00 E-value: 8.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 145 YKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASFG 224
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 225 IEPGRKV--EYMPILEEAmrigqhKPDKVLIYNRPNMETVPLASGrDLDWDEEMAKAQSQDCVPVlsEHPLYILYTSGTT 302
Cdd:PRK12406 94 LHGLASAlpAGVTVLSVP------TPPEIAAAYRISPALLTPPAG-AIDWEGWLAQQEPYDGPPV--PQPQSMIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 303 GLPKGVVR--PTGGYAVMLNWTMSSIYGLKPGEVwwaasdlgwvvghsYICYGPLIHG--NTTVLYEGKPVGT----P-- 372
Cdd:PRK12406 165 GHPKGVRRaaPTPEQAAAAEQMRALIYGLKPGIR--------------ALLTGPLYHSapNAYGLRAGRLGGVlvlqPrf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 373 DAGAYFRVLAEHGVAALFTAPTAIraIRQQDPGAALGKQYSLTRFKTLFVAGERCDVET----LEWSKKVfrvpVLDHWW 448
Cdd:PRK12406 231 DPEELLQLIERHRITHMHMVPTMF--IRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEWWGPV----IYEYYG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 449 QTETGSPITASciglGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGaFSglWKNQEAfKHLYFE 528
Cdd:PRK12406 305 STESGAVTFAT----SEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPD-FT--YHNKPE-KRAEID 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1191882765 529 KfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEEE 573
Cdd:PRK12406 377 R-GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAV 420
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
136-571 |
1.14e-21 |
|
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: 98.18 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 136 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 215
Cdd:cd17651 14 LVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 216 KVVVTASfgiepgrkvEYMPILEeamrigqhkpdkvliynrpnmetVPLASGRDLDWDEEMAKAQSQDCVPVLSEHPLYI 295
Cdd:cd17651 94 VLVLTHP---------ALAGELA-----------------------VELVAVTLLDQPGAAAGADAEPDPALDADDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 296 LYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLyeGKPVGTPDAG 375
Cdd:cd17651 142 IYTSGSTGRPKGVVMPHRSLANLVAW-QARASSLGPGARTLQFAGLGFDVSVQEI-FSTLCAGATLVL--PPEEVRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 376 AYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQysLTRFKTLFVAGER--CDVETLEWSKKVFRVPVLDHWWQTETG 453
Cdd:cd17651 218 ALAAWLDEQRISRVFLPTVALRALAEH--GRPLGVR--LAALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTETH 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 454 SpitASCIGLGNSKTPPPGQA--GKSVPGYNVMILDDNMQklkarclgnivvklPLPPG-------AFSGLWKNQEAFKH 524
Cdd:cd17651 294 V---VTALSLPGDPAAWPAPPpiGRPIDNTRVYVLDAALR--------------PVPPGvpgelyiGGAGLARGYLNRPE 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 525 LYFEKF------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17651 357 LTAERFvpdpfvPGarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIE 411
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
114-558 |
2.38e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 97.75 E-value: 2.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 114 NAIDRHiesgkGDKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQA----MYTMLACAR 189
Cdd:PRK06188 20 SALKRY-----PDRPALV------LGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVlmaiGAAQLAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 190 IGAIHSLifggfaskelSSRIDH------AKPKVVVtasfgIEPGrkveymPILEEAMRIGQHKPdkvliyNRPNMETV- 262
Cdd:PRK06188 89 RTALHPL----------GSLDDHayvledAGISTLI-----VDPA------PFVERALALLARVP------SLKHVLTLg 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 263 PLASGRDLDwdEEMAKAQSQDCVPV-LSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMssiyglkpgevwwaaSDL 341
Cdd:PRK06188 142 PVPDGVDLL--AAAAKFGPAPLVAAaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQL---------------AEW 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 342 GWVVGHSYICYGPLIH------------GNTTVLYEGKpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlg 409
Cdd:PRK06188 205 EWPADPRFLMCTPLSHaggafflptllrGGTVIVLAKF-----DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRT-- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 410 kqYSLTRFKTLFVAGERCDVETLEWSKKVFRvPVL-DHWWQTETGSPIT---------------ASCiglgnsktpppgq 473
Cdd:PRK06188 278 --RDLSSLETVYYGASPMSPVRLAEAIERFG-PIFaQYYGQTEAPMVITylrkrdhdpddpkrlTSC------------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 474 aGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGafsGLWK----NQEAFKHlyfekfpGYYDTMDAGYMDEEGYVY 549
Cdd:PRK06188 342 -GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMD---GYWNrpeeTAEAFRD-------GWLHTGDVAREDEDGFYY 410
|
....*....
gi 1191882765 550 VMSRVDDVI 558
Cdd:PRK06188 411 IVDRKKDMI 419
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
126-562 |
2.46e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 97.69 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIyMPMIPQAM-YTMLACARIGAIHSLIFGGFASK 204
Cdd:PRK07788 64 DRAALI------DERGTLTYAELDEQSNALARGLLALGVRAGDGVAV-LARNHRGFvLALYAAGKVGARIILLNTGFSGP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAmrigqhKPD----KVLIYNRPNMETVPlASGRDLDwdeEMAKAQ 280
Cdd:PRK07788 137 QLAEVAAREGVKALVYDD---------EFTDLLSAL------PPDlgrlRAWGGNPDDDEPSG-STDETLD---DLIAGS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 281 SQDCVPVLSEHPLYILYTSGTTGLPKGVVRPT----GGYAVMLNWTmssiyGLKPGEVWWAASDL--GWVVGHSYICYGp 354
Cdd:PRK07788 198 STAPLPKPPKPGGIVILTSGTTGTPKGAPRPEpsplAPLAGLLSRV-----PFRAGETTLLPAPMfhATGWAHLTLAMA- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 355 liHGNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRaiRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEW 434
Cdd:PRK07788 272 --LGSTVVLRR-----RFDPEATLEDIAKHKATALVVVPVMLS--RILDLGPEVLAKYDTSSLKIIFVSGSALSPELATR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 435 SKKVFRvPVLDHWW-QTETGSPITAsciglgnskTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLP 508
Cdd:PRK07788 343 ALEAFG-PVLYNLYgSTEVAFATIA---------TPEdlaeaPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFP 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882765 509 pgaFSGlwknqeafkhlYF-----EKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAG 562
Cdd:PRK07788 413 ---FEG-----------YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGG 457
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
143-572 |
3.94e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 97.03 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 143 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMytmlacarIGAIHSLIFGG--------FASKELSSRIDHAK 214
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAV--------IGYYGTLLAGGivvqtnplYTERELEYQLHDSG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 215 PKVVVTASF------GIEPGRKVEYMPIleeaMRIGQHKP-DKVLIY-----NRPNMETVPLASGRDLDWDEEMAKAQSQ 282
Cdd:PRK06710 122 AKVILCLDLvfprvtNVQSATKIEHVIV----TRIADFLPfPKNLLYpfvqkKQSNLVVKVSESETIHLWNSVEKEVNTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 283 DCVPVLSEHPLYIL-YTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEvwwaasDLGWVVGHSYICYGPLIHGNTT 361
Cdd:PRK06710 198 VEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGE------EVVLGVLPFFHVYGMTAVMNLS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 362 VLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF 439
Cdd:PRK06710 272 IMQGYKMVLIPkfDMKMVFEAIKKHKVTLFPGAPTIYIALLN----SPLLKEYDISSIRACISGSAPLPVEVQEKFETVT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 440 RVPVLDHWWQTETgSPITASCIgLGNSKTPppGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKN 518
Cdd:PRK06710 348 GGKLVEGYGLTES-SPVTHSNF-LWEKRVP--GSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK---GPQIMKGYWNK 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1191882765 519 QEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK06710 421 PEETAAVLQD---GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEE 471
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
61-115 |
5.38e-21 |
|
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: 86.37 E-value: 5.38e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 61 YKRHFAASVADPERFWGKAAEQISWYKPWTKTLENRHSSSTSWFVEGMLNMCYNA 115
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGPFAKWFVGGKLNVCYNC 55
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
136-572 |
8.46e-21 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 96.00 E-value: 8.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 136 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 215
Cdd:TIGR03098 19 LVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 216 KVVVTASfgiepgrkvEYMPILEEAMRiGQHKPDKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQDCVPVLSEHPLYI 295
Cdd:TIGR03098 99 RLLVTSS---------ERLDLLHPALP-GCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGDADPPHPVIDSDMAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 296 LYTSGTTGLPKGVVRP-----TGGYAVmlnwtmSSIYGLKPGEVWWAASDLGWVVGHSYICYGpLIHGNTTVLYE---GK 367
Cdd:TIGR03098 169 LYTSGSTGRPKGVVLShrnlvAGAQSV------ATYLENRPDDRLLAVLPLSFDYGFNQLTTA-FYVGATVVLHDyllPR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 368 PVGT--------------------------PDAGAYFRVLAEHGVAalfTAPTAIRAIRQQDPGAALGKQYSLTR-FKTL 420
Cdd:TIGR03098 242 DVLKalekhgitglaavpplwaqlaqldwpESAAPSLRYLTNSGGA---MPRATLSRLRSFLPNARLFLMYGLTEaFRST 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 421 FVAGERCDVEtlewskkvfrvpvldhwwqtetgspitasciglgnsktppPGQAGKSVPGYNVMILDDnmqkLKARCL-- 498
Cdd:TIGR03098 319 YLPPEEVDRR----------------------------------------PDSIGKAIPNAEVLVLRE----DGSECApg 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 499 --GNIVVKLPLppgAFSGLWKNQEAFKHLyFEKFPGYYDTM----------DAGYMDEEGYVYVMSRVDDVINVAGHRIS 566
Cdd:TIGR03098 355 eeGELVHRGAL---VAMGYWNDPEKTAER-FRPLPPFPGELhlpelavwsgDTVRRDEEGFLYFVGRRDEMIKTSGYRVS 430
|
....*.
gi 1191882765 567 AGAIEE 572
Cdd:TIGR03098 431 PTEVEE 436
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
126-562 |
1.10e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 95.80 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYdspvtdTKATITYKEVLEQVSRLAGVLV-KHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:PRK08314 25 DKTAIVF------YGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEA---MRIG------------QHKPDKVLIYNRPNMETVPLASGRD 269
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGS---------ELAPKVAPAvgnLRLRhvivaqysdylpAEPEIAVPAWLRAEPPLQALAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 270 LDWDEEMAkaqSQDCVPVLSEHP--LYIL-YTSGTTGLPKGVVRPTGgyAVMLNWTMSSI-YGLKPGEVWWAASDLGWVV 345
Cdd:PRK08314 170 VAWKEALA---AGLAPPPHTAGPddLAVLpYTSGTTGVPKGCMHTHR--TVMANAVGSVLwSNSTPESVVLAVLPLFHVT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 346 GHSYICYGPLIHGNTTVLYegkPVGTPDAGAyfRVLAEHGVAALFTAPT------AIRAIRQQD---------PGAALGK 410
Cdd:PRK08314 245 GMVHSMNAPIYAGATVVLM---PRWDREAAA--RLIERYRVTHWTNIPTmvvdflASPGLAERDlsslryiggGGAAMPE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 411 qysltrfktlfVAGERCdvetlewsKKVFRVPVLDHWWQTETGSPITASciglgnsktPP--PGQAGKSVPGYNV--MIL 486
Cdd:PRK08314 320 -----------AVAERL--------KELTGLDYVEGYGLTETMAQTHSN---------PPdrPKLQCLGIPTFGVdaRVI 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882765 487 D-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkFPG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAG 562
Cdd:PRK08314 372 DpETLEELPPGEVGEIVVH---GPQVFKGYWNRPEATAEAFIE-IDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASG 446
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-571 |
4.01e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 95.23 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfASKE 205
Cdd:PRK12467 527 ERPALVFG------EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGG---------AYVP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRidhakpkvvvtasfgiEPGRKVEYMpILEEAMRIGQHKPDKVLIYNRP-NMETVPLASgrDLDWDEEMAKAQSQdc 284
Cdd:PRK12467 592 LDPE----------------YPQDRLAYM-LDDSGVRLLLTQSHLLAQLPVPaGLRSLCLDE--PADLLCGYSGHNPE-- 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 285 VPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLY 364
Cdd:PRK12467 651 VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCV-IAERLQLAADDSMLMVSTFAFDLGVTEL-FGALASGATLHLL 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 365 EgkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAALgkqysLTRFKTLFVAGERCDVETL-EWSKKVFRVPV 443
Cdd:PRK12467 729 P--PDCARDAEAFAALMADQGVTVLKIVPSHLQAL-LQASRVAL-----PRPQRALVCGGEALQVDLLaRVRALGPGARL 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 444 LDHWWQTETGSPITASCIGLGN--SKTPPPGQAgksVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLWKNQEA 521
Cdd:PRK12467 801 INHYGPTETTVGVSTYELSDEErdFGNVPIGQP---LANLGLYILDHYLN--------------PVPVGVVGELYIGGAG 863
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882765 522 FKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK12467 864 LARGYHrrpaltaERFvpdpfgaDGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIE 929
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
125-571 |
5.77e-20 |
|
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: 93.03 E-value: 5.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfask 204
Cdd:cd12117 11 PDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGA------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 elssridhakpkvvvtASFGIEPGRKVEYMP-ILEEAmrigqhkPDKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQD 283
Cdd:cd12117 73 ----------------AYVPLDPELPAERLAfMLADA-------GAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 284 CVPVLSEHPLYILYTSGTTGLPKGV----------VRPTggyavmlNWTmssiyGLKPGEVWWAASDLGWVVGhSYICYG 353
Cdd:cd12117 130 AVPVSPDDLAYVMYTSGSTGRPKGVavthrgvvrlVKNT-------NYV-----TLGPDDRVLQTSPLAFDAS-TFEIWG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 354 PLIHGNTTVLYEGKPVGTPDAGAyfRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERCDVetlE 433
Cdd:cd12117 197 ALLNGARLVLAPKGTLLDPDALG--ALIAEEGVTVLWLTAALFNQLADEDPEC-------FAGLRELLTGGEVVSP---P 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 434 WSKKVFR----VPVLDHWWQTETGSPITASCIglgnskTPPPGQA-----GKSVPGYNVMILDDNMQklkarclgnivvk 504
Cdd:cd12117 265 HVRRVLAacpgLRLVNGYGPTENTTFTTSHVV------TELDEVAgsipiGRPIANTRVYVLDEDGR------------- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 505 lPLPPGAF-------SGLWK---NQEAfkhLYFEKF------PG--YYDTMD-AGYMDEEGYVYVmSRVDDVINVAGHRI 565
Cdd:cd12117 326 -PVPPGVPgelyvggDGLALgylNRPA---LTAERFvadpfgPGerLYRTGDlARWLPDGRLEFL-GRIDDQVKIRGFRI 400
|
....*.
gi 1191882765 566 SAGAIE 571
Cdd:cd12117 401 ELGEIE 406
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
136-571 |
8.36e-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: 92.37 E-value: 8.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 136 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhakp 215
Cdd:cd17643 6 VVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGG----------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 216 kvvvtASFGIEPGRKVEYMP-ILEEAmrigqhkpDKVLIYNRPnmetvplasgrdldwdeemakaqsqdcvpvlsEHPLY 294
Cdd:cd17643 63 -----AYVPIDPAYPVERIAfILADS--------GPSLLLTDP--------------------------------DDLAY 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 295 ILYTSGTTGLPKGVVRPTGGyAVMLNWTMSSIYGLKPGEVWWAAsdlgwvvgHSYI-------CYGPLIHGNTTVLYEGK 367
Cdd:cd17643 98 VIYTSGSTGRPKGVVVSHAN-VLALFAATQRWFGFNEDDVWTLF--------HSYAfdfsvweIWGALLHGGRLVVVPYE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 368 PVGTPDagAYFRVLAEHGVAALFTAPTAIRAIRQ---QDPGAALGKQYsltrfktLFVAGERCDVETLE-WSKKVF--RV 441
Cdd:cd17643 169 VARSPE--DFARLLRDEGVTVLNQTPSAFYQLVEaadRDGRDPLALRY-------VIFGGEALEAAMLRpWAGRFGldRP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 442 PVLDHWWQTETG-----SPITASCIGLGNSKTpppgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW 516
Cdd:cd17643 240 QLVNMYGITETTvhvtfRPLDAADLPAAAASP-----IGRPLPGLRVYVLDADGR--------------PVPPGVVGELY 300
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 517 ----------KNQEAfkhLYFEKF-------PG--YYDTMD-AGYMDEEGYVYvMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17643 301 vsgagvargyLGRPE---LTAERFvanpfggPGsrMYRTGDlARRLPDGELEY-LGRADEQVKIRGFRIELGEIE 371
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
142-572 |
1.49e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 92.03 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhakpkVVVTA 221
Cdd:PRK07470 32 SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA------------------------VWVPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 222 SFGIEPGrKVEYMpileeamriGQHKPDKVLIYNRPNMETVPL--ASGRDLDW-------------DEEMAKAQSQDCVP 286
Cdd:PRK07470 88 NFRQTPD-EVAYL---------AEASGARAMICHADFPEHAAAvrAASPDLTHvvaiggaragldyEALVARHLGARVAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 287 VLSEH--PLYILYTSGTTGLPKGVVRPTGGYAVMLNwtmSSIYGLKPGEvwwAASDLGWVVGhsyicygPLIHGN----- 359
Cdd:PRK07470 158 AAVDHddPCWFFFTSGTTGRPKAAVLTHGQMAFVIT---NHLADLMPGT---TEQDASLVVA-------PLSHGAgihql 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 360 -------TTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTaIRAIRQQDPGAALGKQYSLtrfKTLFVAGE---RCDv 429
Cdd:PRK07470 225 cqvargaATVLLPSERF---DPAEVWALVERHRVTNLFTVPT-ILKMLVEHPAVDRYDHSSL---RYVIYAGApmyRAD- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 430 etlewSKKVFRV--PVLDHWWqtetgspitasciGL----GNSKTPPP-------------GQAGKSVPGYNVMILDDNM 490
Cdd:PRK07470 297 -----QKRALAKlgKVLVQYF-------------GLgevtGNITVLPPalhdaedgpdariGTCGFERTGMEVQIQDDEG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 491 QKLKARCLGNIVVklpLPPGAFSGLWKNQEA----FKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRIS 566
Cdd:PRK07470 359 RELPPGETGEICV---IGPAVFAGYYNNPEAnakaFRD-------GWFRTGDLGHLDARGFLYITGRASDMYISGGSNVY 428
|
....*.
gi 1191882765 567 AGAIEE 572
Cdd:PRK07470 429 PREIEE 434
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
143-571 |
1.22e-18 |
|
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: 88.69 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 143 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAS 222
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 fgiepgrkveympileeamrigqhkpdkvliynrpNMETVPLasgrdldwdeemakaqsqdcvpvlsehplyILYTSGTT 302
Cdd:cd05935 82 -----------------------------------ELDDLAL------------------------------IPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 303 GLPKGVVRpTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLyegkpVGTPDAGAYFRVLA 382
Cdd:cd05935 97 GLPKGCMH-THFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL-----MARWDRETALELIE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 383 EHGVAALFTAPTAIRAIrQQDPGAalgKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGSPITascig 462
Cdd:cd05935 171 KYKVTFWTNIPTMLVDL-LATPEF---KTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTH----- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 463 lgnskTPPPGQAGKS---VPGYNV--MILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWK----NQEAFKHLYFEKFpg 532
Cdd:cd05935 242 -----TNPPLRPKLQclgIP*FGVdaRVIDiETGRELPPNEVGEIVVR---GPQIFKGYWNrpeeTEESFIEIKGRRF-- 311
|
410 420 430
....*....|....*....|....*....|....*....
gi 1191882765 533 yYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05935 312 -FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE 349
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
291-573 |
1.29e-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: 87.08 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 291 HPLYILYTSGTTGLPKGVVRptggyavmlnwtmssiyglkpGEVWWAAS-----DLGWVVGHSYICY-GPLIH-----GN 359
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYR---------------------SERSWIESfvcneDLFNISGEDAILApGPLSHslflyGA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 360 TTVLYEGKPV---GTPDAGAYFRVLAEHGVAALFTAPTAIRA-IRQQDPgaalgkqysLTRFKTLFVAGERCDVETLEWS 435
Cdd:cd17633 60 ISALYLGGTFigqRKFNPKSWIRKINQYNATVIYLVPTMLQAlARTLEP---------ESKIKSIFSSGQKLFESTKKKL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 436 KKVFRVPVLDHWWQTETGSPITASCiglgNSKTPPPGQAGKSVPGYNVMILDDNmqklkARCLGNIVVKLPLppgAFSGL 515
Cdd:cd17633 131 KNIFPKANLIEFYGTSELSFITYNF----NQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEM---VFSGY 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882765 516 WKNQEAFKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEEE 573
Cdd:cd17633 199 VRGGFSNPD-------GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESV 249
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
136-571 |
2.82e-18 |
|
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: 87.72 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 136 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 215
Cdd:cd17646 17 VVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 216 KVVVTASfgiepgrkveympilEEAMRIGQHKPDKVLIYNRPnmetvPLASGRDLDwdeemakaqsqdcVPVLSEHPLYI 295
Cdd:cd17646 97 AVVLTTA---------------DLAARLPAGGDVALLGDEAL-----AAPPATPPL-------------VPPRPDNLAYV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 296 LYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLYEgkPVGTPDAG 375
Cdd:cd17646 144 IYTSGSTGRPKGVMVTHAGIVNRLLW-MQDEYPLGPGDRVLQKTPLSFDVSVWEL-FWPLVAGARLVVAR--PGGHRDPA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 376 AYFRVLAEHGVAALFTAPTAIRA-IRQQDPGAALgkqySLTRfktLFVAGERCDVETLEWSKKVFRVPVLDHWWQTETGS 454
Cdd:cd17646 220 YLAALIREHGVTTCHFVPSMLRVfLAEPAAGSCA----SLRR---VFCSGEALPPELAARFLALPGAELHNLYGPTEAAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 455 PITA-SCIGlgnSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGL----------WKNQEAfk 523
Cdd:cd17646 293 DVTHwPVRG---PAETPSVPIGRPVPNTRLYVLDDALR--------------PVPVGVPGELylggvqlargYLGRPA-- 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882765 524 hLYFEKF------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17646 354 -LTAERFvpdpfgPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIE 408
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
118-562 |
3.25e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 88.17 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 118 RHIESGKGDKVAIIYdspvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLI 197
Cdd:PRK06178 40 RAWARERPQRPAIIF------YGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 198 FGGFASKELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILEEAMRIGQHkpdKVLiynrPNMETVPL------ASGRDLD 271
Cdd:PRK06178 114 SPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLA---DVL----PAEPTLPLpdslraPRLAAAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 272 WDEEMA-----KAQSQDCVPVLSEhPLYILYTSGTTGLPKGVVRpTGGYAVmlnWTMSSIYGLKPG------------EV 334
Cdd:PRK06178 187 AIDLLPalracTAPVPLPPPALDA-LAALNYTGGTTGMPKGCEH-TQRDMV---YTAAAAYAVAVVggedsvflsflpEF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 335 WWAASDLGWVVghsyicygPLIHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALF-TAPTAIRAIrqQDPGAAlgkQYS 413
Cdd:PRK06178 262 WIAGENFGLLF--------PLFSGATLVL-----LARWDAVAFMAAVERYRVTRTVmLVDNAVELM--DHPRFA---EYD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 414 LTRFKTLFVAgercdvetlEWSKKVfrVPVLDHWWQTETGSPITASCIGLGNSKT----------------PPPGQAGKS 477
Cdd:PRK06178 324 LSSLRQVRVV---------SFVKKL--NPDYRQRWRALTGSVLAEAAWGMTETHTcdtftagfqdddfdllSQPVFVGLP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 478 VPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDD 556
Cdd:PRK06178 393 VPGTEFKICDfETGELLPLGAEGEIVVR---TPSLLKGYWNKPEATAEALRD---GWLHTGDIGKIDEQGFLHYLGRRKE 466
|
....*.
gi 1191882765 557 VINVAG 562
Cdd:PRK06178 467 MLKVNG 472
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
144-566 |
4.04e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 87.69 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI-HSLIFGGFAsKELSSRIDHAKPKVVVtas 222
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHTINPRLFP-EQIAYIINHAEDRVVF--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 fgIEPgrkvEYMPILEEAMriGQHKPDKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSQDCVPVLSEH-PLYILYTSGT 301
Cdd:cd12119 103 --VDR----DFLPLLEAIA--PRLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDFDENtAAAICYTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 302 TGLPKGVV---RPTGGYAVMLNwtMSSIYGLKPGEVwwaasdlgwvvghsYICYGPLIHGN------TTVLYEGK---PV 369
Cdd:cd12119 175 TGNPKGVVyshRSLVLHAMAAL--LTDGLGLSESDV--------------VLPVVPMFHVNawglpyAAAMVGAKlvlPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 370 GTPDAGAYFRVLAEHGVAalFTA--PTAIRAIRQQdPGAALGKQYSLTRfktLFVAGERCDVETLEWSKKVFrVPVLDHW 447
Cdd:cd12119 239 PYLDPASLAELIEREGVT--FAAgvPTVWQGLLDH-LEANGRDLSSLRR---VVIGGSAVPRSLIEAFEERG-VRVIHAW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 448 WQTETgSPI-TASCIGLGNSKTPPPGQA------GKSVPGYNVMILDDNMQKLKA--RCLGNIVVKLP-LPPGAFsglwK 517
Cdd:cd12119 312 GMTET-SPLgTVARPPSEHSNLSEDEQLalrakqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPwVTKSYY----K 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1191882765 518 NQEAfKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRIS 566
Cdd:cd12119 387 NDEE-SEALTED--GWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWIS 432
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
125-572 |
4.22e-18 |
|
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: 87.51 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslIFGGFA-- 202
Cdd:COG1021 39 PDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 203 SKELSSRIDHAKPKVVVTASFgiepGRKVEYMPILEEAMRIGQHkPDKVLIYNRPNmETVPLASGRDLDWDEEMAKAQSQ 282
Cdd:COG1021 111 RAEISHFAEQSEAVAYIIPDR----HRGFDYRALARELQAEVPS-LRHVLVVGDAG-EFTSLDALLAAPADLSEPRPDPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 283 DcvpvlsehPLYILYTSGTTGLPKGVVRPTGGYAvmLNWTMSS-IYGLKPGEVWWAASDlgwvVGHSY--IC---YGPLI 356
Cdd:COG1021 185 D--------VAFFQLSGGTTGLPKLIPRTHDDYL--YSVRASAeICGLDADTVYLAALP----AAHNFplSSpgvLGVLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 357 HGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETLEwsk 436
Cdd:COG1021 251 AGGTVVL-----APDPSPDTAFPLIERERVTVTALVPPLALLWLD----AAERSRYDLSSLRVLQVGGAKLSPELAR--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 437 kvfRV-PVLDHWWQ------------TETGSP--ITASCIGLGNSktpppgqagksvPGYNVMILDDNmqklkarclGNi 501
Cdd:COG1021 319 ---RVrPALGCTLQqvfgmaeglvnyTRLDDPeeVILTTQGRPIS------------PDDEVRIVDED---------GN- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 502 vvklPLPPGA-----------FSGLWK----NQEAFKHlyfekfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRIS 566
Cdd:COG1021 374 ----PVPPGEvgelltrgpytIRGYYRapehNARAFTP------DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIA 443
|
....*.
gi 1191882765 567 AGAIEE 572
Cdd:COG1021 444 AEEVEN 449
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
142-572 |
5.69e-18 |
|
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: 86.25 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA 221
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKLDDIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 222 SfgiepgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdcvpvlsehplyILYTSGT 301
Cdd:cd05912 81 T------------------------------------------------------------------------IMYTSGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 302 TGLPKGVVRPTGGY-----AVMLNwtmssiYGLKPGEVWWAASDLGWVVGHSYICYGpLIHGNTTVLYEgkpvgTPDAGA 376
Cdd:cd05912 89 TGKPKGVQQTFGNHwwsaiGSALN------LGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVD-----KFDAEQ 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 377 YFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqYSLTrFKTLFVAGERCDVETLEWSKKvFRVPVLDHWWQTETGSPI 456
Cdd:cd05912 157 VLHLINSGKVTIISVVPTMLQRLLEILGEG-----YPNN-LRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCSQI 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 457 TASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKarcLGNIVVKLP-LPPGAFSGLWKNQEAFKHlyfekfpGYYD 535
Cdd:cd05912 230 VTLSPEDALNK---IGSAGKPLFPVELKIEDDGQPPYE---VGEILLKGPnVTKGYLNRPDATEESFEN-------GWFK 296
|
410 420 430
....*....|....*....|....*....|....*..
gi 1191882765 536 TMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05912 297 TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEE 333
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
144-572 |
5.88e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 87.14 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA-S 222
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAdA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 FgiepgRKVEYMPILEEAMRIGQHKPDKVLIYNR-PNMETVPLASGRD----LDWDEEMAKAQS---QDCVPV---LSEH 291
Cdd:PRK12583 127 F-----KTSDYHAMLQELLPGLAEGQPGALACERlPELRGVVSLAPAPppgfLAWHELQARGETvsrEALAERqasLDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 292 -PLYILYTSGTTGLPKGVVrpTGGYAVMLNWTMSSI-YGLKPGEVWWAASDLgwvvghsYICYGPLI-------HGNTTV 362
Cdd:PRK12583 202 dPINIQYTSGTTGFPKGAT--LSHHNILNNGYFVAEsLGLTEHDRLCVPVPL-------YHCFGMVLanlgcmtVGACLV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 363 LyegkPVGTPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPGAalgkqYSLTRFKTLFVAGERCDVETLEWSKKVFRV 441
Cdd:PRK12583 273 Y----PNEAFDPLATLQAVEEERCTALYGVPTMfIAELDHPQRGN-----FDLSSLRTGIMAGAPCPIEVMRRVMDEMHM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 442 P-VLDHWWQTETgSPITASCiGLGNSKTPPPGQAGKSVPGYNVMILDDnmqklkarcLGNIVvklplPPGA--------- 511
Cdd:PRK12583 344 AeVQIAYGMTET-SPVSLQT-TAADDLERRVETVGRTQPHLEVKVVDP---------DGATV-----PRGEigelctrgy 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191882765 512 --FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK12583 408 svMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEE 468
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-571 |
2.07e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.55 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 205
Cdd:PRK12316 4566 DAVAVVFD------EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAY----------- 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 lssridhakpkvvvtASFGIE-PGRKVEYMpiLEEAmRIGqhkpdkVLIYNRPNMETVPLASGRD---LDWDEEMAKAQS 281
Cdd:PRK12316 4629 ---------------VPLDPEyPRERLAYM--MEDS-GAA------LLLTQSHLLQRLPIPDGLAslaLDRDEDWEGFPA 4684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 282 QDcvPVLSEHP---LYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHG 358
Cdd:PRK12316 4685 HD--PAVRLHPdnlAYVIYTSGSTGRPKGVAVSHGSLVNHLHA-TGERYELTPDDRVLQFMSFSFDGSHEGL-YHPLING 4760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 359 NTTVLyegKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKTLFVAGERCDVETL-EWSKK 437
Cdd:PRK12316 4761 ASVVI---RDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-----EPPSLRVYCFGGEAVAQASYdLAWRA 4832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 438 VFRVPVLDHWWQTETG-SPITASCiglgnSKTPPPGQA----GKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAF 512
Cdd:PRK12316 4833 LKPVYLFNGYGPTETTvTVLLWKA-----RDGDACGAAympiGTPLGNRSGYVLDGQLN--------------PLPVGVA 4893
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 513 SGLWKNQEAFKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK12316 4894 GELYLGGEGVARGYLerpaltaERFvpdpfgaPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIE 4968
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
124-562 |
2.62e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 84.96 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 124 KGDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFAS 203
Cdd:PRK07656 18 FGDKEAYVFGD------QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 204 KELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMrigQHKPDKVLIYNRPNMETVPLASgRDLDWDEEMA-KAQSQ 282
Cdd:PRK07656 92 DEAAYILARGDAKALFVLG---------LFLGVDYSAT---TRLPALEHVVICETEEDDPHTE-KMKTFTDFLAaGDPAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 283 DCVPVLSEHPLYILYTSGTTGLPKGvvrptggyaVMLN----------WtmSSIYGLKPGEVWWAASDLGWVVGHSYICY 352
Cdd:PRK07656 159 RAPEVDPDDVADILFTSGTTGRPKG---------AMLThrqllsnaadW--AEYLGLTEGDRYLAANPFFHVFGYKAGVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 353 GPLIHGNTTVlyegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqyslTRFKTLFVA---GERCDV 429
Cdd:PRK07656 228 APLMRGATIL-----PLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSA-------EDLSSLRLAvtgAASMPV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 430 ETLEWSKKVFRVP-VLDHWWQTETgSPITASCiGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplP 508
Cdd:PRK07656 296 ALLERFESELGVDiVLTGYGLSEA-SGVTTFN-RLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR---G 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1191882765 509 PGAFSGLWKNQEAFKHLYfeKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAG 562
Cdd:PRK07656 371 PNVMKGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGG 422
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
125-571 |
2.69e-17 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 85.12 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIYDSPVTDTKaTITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:PRK08008 21 GHKTALIFESSGGVVR-RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIGQHKPDKVLIyNRPNMETVPLASgrdlDWDEEMAKAQSQDC 284
Cdd:PRK08008 100 ESAWILQNSQASLLVTSA---------QFYPMYRQIQQEDATPLRHICL-TRVALPADDGVS----SFTQLKAQQPATLC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 285 --VPVLSEHPLYILYTSGTTGLPKGVVrptggyAVMLNWTMSSIYGlkpgeVWWAA---SDLgwvvghsYICYGPLIH-- 357
Cdd:PRK08008 166 yaPPLSTDDTAEILFTSGTTSRPKGVV------ITHYNLRFAGYYS-----AWQCAlrdDDV-------YLTVMPAFHid 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 358 ------------GNTTVLYEGKpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAALGKQYSLTRFktLFVAG- 424
Cdd:PRK08008 228 cqctaamaafsaGATFVLLEKY-----SARAFWGQVCKYRATITECIPMMIRTLMVQ-PPSANDRQHCLREV--MFYLNl 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 425 ---ERCDVETLewskkvFRVPVLDHWWQTETgspitascigLGNSKTPPPGQA------GKSVPGYNVMILDDNMQKLKA 495
Cdd:PRK08008 300 sdqEKDAFEER------FGVRLLTSYGMTET----------IVGIIGDRPGDKrrwpsiGRPGFCYEAEIRDDHNRPLPA 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882765 496 RCLGNIVVKlpLPPGA--FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK08008 364 GEIGEICIK--GVPGKtiFKEYYLDPKATAKVLEAD--GWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELE 437
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
139-571 |
3.11e-17 |
|
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: 84.89 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 139 TKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVV 218
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 219 VTASFGIEPGRKVEY-MPILEeamrigqhkpdKVLIynrpnmetvpLASGRDLDWDEEMAKAQSQDCVPVLSEHPL---- 293
Cdd:cd17642 121 FCSKKGLQKVLNVQKkLKIIK-----------TIII----------LDSKEDYKGYQCLYTFITQNLPPGFNEYDFkpps 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 294 --------YILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLGWvvGHSYICY---GPLIHGNTTV 362
Cdd:cd17642 180 fdrdeqvaLIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPF--HHGFGMFttlGYLICGFRVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 363 LyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrqqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVP 442
Cdd:cd17642 258 L-----MYKFEEELFLRSLQDYKVQSALLVPTLFAFF----AKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 443 -VLDHWWQTETGSPITASciglgNSKTPPPGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQE 520
Cdd:cd17642 329 gIRQGYGLTETTSAILIT-----PEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVK---GPMIMKGYVNNPE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1191882765 521 AFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17642 401 ATKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELE 449
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
114-320 |
8.47e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 83.77 E-value: 8.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 114 NAIDRHiesgkGDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI 193
Cdd:PRK08279 45 EAAARH-----PDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 194 HSLIFGGFASKELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMriGQHKPDKVLIYNRPNMETVPLASgRDLDwd 273
Cdd:PRK08279 114 VALLNTQQRGAVLAHSLNLVDAKHLIVGE---------ELVEAFEEAR--ADLARPPRLWVAGGDTLDDPEGY-EDLA-- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882765 274 eEMAKAQSQDCVP----VLSEHPLYILYTSGTTGLPKGVV-------RPTGGYAVMLN 320
Cdd:PRK08279 180 -AAAAGAPTTNPAsrsgVTAKDTAFYIYTSGTTGLPKAAVmshmrwlKAMGGFGGLLR 236
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
66-572 |
1.22e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 83.13 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 66 AASVADPERFWgkaaeqISWYKPWTK-TLENRHSSstswfvegMLNMCYNAIDRHiesgkGDKVAIIYdspvtdTKATIT 144
Cdd:PRK05605 5 QEMSAFADKPW------LQSYAPWTPhDLDYGDTT--------LVDLYDNAVARF-----GDRPALDF------FGATTT 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 145 YKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI---HSLIfggFASKELSSR-IDHAkPKVVV- 219
Cdd:PRK05605 60 YAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvveHNPL---YTAHELEHPfEDHG-ARVAIv 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 220 --TASFGIE------PGRKV------EYMPILeeaMRIGQHKPDKVLIYNR-----PNMETVP----LASGRDLDWDEEM 276
Cdd:PRK05605 136 wdKVAPTVErlrrttPLETIvsvnmiAAMPLL---QRLALRLPIPALRKARaaltgPAPGTVPwetlVDAAIGGDGSDVS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 277 AKAQSQDCVPVlsehplyILYTSGTTGLPKGVVRPTGGyaVMLNWTMSS--IYGLKPG-EVWWAASDLgwvvGHSY---- 349
Cdd:PRK05605 213 HPRPTPDDVAL-------ILYTSGTTGKPKGAQLTHRN--LFANAAQGKawVPGLGDGpERVLAALPM----FHAYgltl 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 350 -ICYGPLIhGNTTVLYegkPvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCD 428
Cdd:PRK05605 280 cLTLAVSI-GGELVLL---P--APDIDLILDAMKKHPPTWLPGVPPLYEKIAE----AAEERGVDLSGVRNAFSGAMALP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 429 VETLE-WSKKVFRVPVlDHWWQTETgSPITascigLGN--SKTPPPGQAGKSVPGYNVMILD-DNMQKLKARC-LGNIVV 503
Cdd:PRK05605 350 VSTVElWEKLTGGLLV-EGYGLTET-SPII-----VGNpmSDDRRPGYVGVPFPDTEVRIVDpEDPDETMPDGeEGELLV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882765 504 KlplPPGAFSGLWKNQEAFKHLYfekFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK05605 423 R---GPQVFKGYWNRPEETAKSF---LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEE 485
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
142-571 |
1.23e-16 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 83.24 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVta 221
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 222 sfgIEPGRKVEymPILEEAMRIgqHKPDKVLI--------YNRPNMETVP--LASGRDLD------WDEEMAKAQSQDcV 285
Cdd:cd17641 89 ---AEDEEQVD--KLLEIADRI--PSVRYVIYcdprgmrkYDDPRLISFEdvVALGRALDrrdpglYEREVAAGKGED-V 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 286 PVLSehplyilYTSGTTGLPKGVVRPTGGYAvmlnwTMSSIY----GLKPGEVWWAASDLGWVVGHSYICYGPLIHGN-- 359
Cdd:cd17641 161 AVLC-------TTSGTTGKPKLAMLSHGNFL-----GHCAAYlaadPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFiv 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 360 ------TTVLYEGKPVG------TP---------------DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGA------ 406
Cdd:cd17641 229 nfpeepETMMEDLREIGptfvllPPrvwegiaadvrarmmDATPFKRFMFELGMKLGLRALDRGKRGRPVSLWLrlaswl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 407 -------ALGKQYSLTRFKTLFVAGERCDVETLewskKVFR---VPVLDHWWQTETGSPITASCIGlgnskTPPPGQAGK 476
Cdd:cd17641 309 adallfrPLRDRLGFSRLRSAATGGAALGPDTF----RFFHaigVPLKQLYGQTELAGAYTVHRDG-----DVDPDTVGV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 477 SVPGYNVMIldDNMqklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDD 556
Cdd:cd17641 380 PFPGTEVRI--DEV--------GEILVR---SPGVFVGYYKNPEATAEDFDED--GWLHTGDAGYFKENGHLVVIDRAKD 444
|
490
....*....|....*.
gi 1191882765 557 VINVA-GHRISAGAIE 571
Cdd:cd17641 445 VGTTSdGTRFSPQFIE 460
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
142-571 |
1.60e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.85 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhakpkvvvtA 221
Cdd:PRK12316 536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGG----------------------------A 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 222 SFGIEPGRKVEYMPILEEAMRIGqhkpdkVLIYNRPNMETVPLASGRD-LDWDEEMAKAQSQ-DCVPVLS---EHPLYIL 296
Cdd:PRK12316 588 YVPLDPEYPAERLAYMLEDSGVQ------LLLSQSHLGRKLPLAAGVQvLDLDRPAAWLEGYsEENPGTElnpENLAYVI 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 297 YTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHsYICYGPLIHGNTTVLyeGKPVGTPDAGA 376
Cdd:PRK12316 662 YTSGSTGKPKGAGNRHRALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVV--AAPGDHRDPAK 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 377 YFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEwskKVF-RVP---VLDHWWQTET 452
Cdd:PRK12316 738 LVELINREGVDTLHFVPSMLQAF-LQDEDVA-----SCTSLRRIVCSGEALPADAQE---QVFaKLPqagLYNLYGPTEA 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 453 GSPIT-ASCIGLGNSKTPppgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVklplppgAFSGLWKNQEAFKHLYFEKF- 530
Cdd:PRK12316 809 AIDVThWTCVEEGGDSVP----IGRPIANLACYILDANLEPVPVGVLGELYL-------AGRGLARGYHGRPGLTAERFv 877
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1191882765 531 PG-------YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK12316 878 PSpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 925
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
289-571 |
2.51e-16 |
|
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: 81.59 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 289 SEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSiyglkpgevwWAASDLGWVVGHSYICY--------GPLIHGNT 360
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAA----------FSAEELAGVLASTSICFdlsvfelfGPLATGGK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 361 TVLYEgkpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQD--PGAAlgkqysltrfKTLFVAGE---RCDVETLEWS 435
Cdd:cd12115 174 VVLAD-------NVLALPDLPAAAEVTLINTVPSAAAELLRHDalPASV----------RVVNLAGEplpRDLVQRLYAR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 436 KKVFRVPVLdhWWQTETGSPITASCIGLGNSKTPPpgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGL 515
Cdd:cd12115 237 LQVERVVNL--YGPSEDTTYSTVAPVPPGASGEVS---IGRPLANTQAYVLDRALQ--------------PVPLGVPGEL 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191882765 516 WKNQEAFKHLYF-------EKF------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd12115 298 YIGGAGVARGYLgrpgltaERFlpdpfgPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIE 368
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
125-571 |
5.12e-16 |
|
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: 80.81 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIYDSPVtdtkatITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFAS 203
Cdd:cd12118 18 PDRTSIVYGDRR------YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTP-AMYELhFGVPMAGAVLNALNTRLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 204 KELSSRIDHAKPKVVVTasfgiepGRKVEYmpilEEAMRIGqhKPDKVLIynRPNMEtvplasgrdldWDeemakaqsqd 283
Cdd:cd12118 91 EEIAFILRHSEAKVLFV-------DREFEY----EDLLAEG--DPDFEWI--PPADE-----------WD---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 284 cvpvlsehPLYILYTSGTTGLPKGVVRPTGGyaVMLNwTMSSIY--GLKPGEVwwaasdlgwvvghsYICYGPLIHGN-- 359
Cdd:cd12118 135 --------PIALNYTSGTTGRPKGVVYHHRG--AYLN-ALANILewEMKQHPV--------------YLWTLPMFHCNgw 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 360 ----TTVLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTRFKTLFVAGERCDVETLE 433
Cdd:cd12118 190 cfpwTVAAVGGTNVCLRkvDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDAR----PLPHRVHVMTAGAPPPAAVLA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 434 WSK----KVFRVPVLdhwwqTETGSPITAsCIGLGNSKT-PPPGQA------GKSVPGYN-VMILDDNMQKLKAR----- 496
Cdd:cd12118 266 KMEelgfDVTHVYGL-----TETYGPATV-CAWKPEWDElPTEERArlkarqGVRYVGLEeVDVLDPETMKPVPRdgkti 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 497 ----CLGNIVVKlplppgafsGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAG 568
Cdd:cd12118 340 geivFRGNIVMK---------GYLKNpeatAEAFRG-------GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSV 403
|
...
gi 1191882765 569 AIE 571
Cdd:cd12118 404 EVE 406
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
132-571 |
7.39e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 80.85 E-value: 7.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 132 YDSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGaihslIFGGFASKELSsRID 211
Cdd:PRK06060 20 YDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARG-----VMAFLANPELH-RDD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 212 HAKPKVVVTASFGIEPGrkveymPILEeamrigQHKPDKVLiynrpnmETVPLASgrdldwdeEMAKAQSQDCVPVLSEH 291
Cdd:PRK06060 94 HALAARNTEPALVVTSD------ALRD------RFQPSRVA-------EAAELMS--------EAARVAPGGYEPMGGDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 292 PLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPgevwwaaSDLGWVVGHSYICYG-------PLIHGNTTVLy 364
Cdd:PRK06060 147 LAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTP-------EDTGLCSARMYFAYGlgnsvwfPLATGGSAVI- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 365 EGKPVGTPDAG---AYFRVLAEHGVAALFT------APTAIRAIRqqdpgaalgkqysltrfkTLFVAGERCDVETLEWS 435
Cdd:PRK06060 219 NSAPVTPEAAAilsARFGPSVLYGVPNFFArvidscSPDSFRSLR------------------CVVSAGEALELGLAERL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 436 KKVF-RVPVLDHWWQTETGSPITASCIglgnsKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSG 514
Cdd:PRK06060 281 MEFFgGIPILDGIGSTEVGQTFVSNRV-----DEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVR---GPAIAKG 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 515 LWKNQEAFkhLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK06060 353 YWNRPDSP--VANE---GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVE 404
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
126-568 |
7.63e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 80.51 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSpvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK13391 12 DKPAVIMAS----TGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTASfgiepgRKVEYMPILEEAmrigqhkpdkvliynrpnmetVPLASGR-DLDWDEEMAKAQS-QD 283
Cdd:PRK13391 88 AAYIVDDSGARALITSA------AKLDVARALLKQ---------------------CPGVRHRlVLDGDGELEGFVGyAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 284 CVPVLSEHPL-------YILYTSGTTGLPKGVVRP--------TGGYAVMLNwtmsSIYGLKPGEVwwaasdlgwvvghs 348
Cdd:PRK13391 141 AVAGLPATPIadeslgtDMLYSSGTTGRPKGIKRPlpeqppdtPLPLTAFLQ----RLWGFRSDMV-------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 349 YICYGPLIH-------------GNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDpgaALGKQYSL 414
Cdd:PRK13391 203 YLSPAPLYHsapqravmlvirlGGTVIVME-----HFDAEQYLALIEEYGVTHTQLVPTMfSRMLKLPE---EVRDKYDL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 415 TRFKTLFVAGERCDVETLEwskkvfrvPVLDhWWqtetgSPIT----ASCIGLGNSKTPP------PGQAGKSVPGyNVM 484
Cdd:PRK13391 275 SSLEVAIHAAAPCPPQVKE--------QMID-WW-----GPIIheyyAATEGLGFTACDSeewlahPGTVGRAMFG-DLH 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 485 ILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAfKHlyfeKFPGYYDTMDAGYMDEEGYVYVMSRVDDVInvaghr 564
Cdd:PRK13391 340 ILDDDGAELPPGEPGTIWFEGGRPFEYLNDPAKTAEA-RH----PDGTWSTVGDIGYVDEDGYLYLTDRAAFMI------ 408
|
....
gi 1191882765 565 ISAG 568
Cdd:PRK13391 409 ISGG 412
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
126-572 |
8.40e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 80.45 E-value: 8.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFASK 204
Cdd:PLN03102 29 NRTSIIYG------KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTP-AMYEMhFAVPMAGAVLNPINTRLDAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRI---GQHKPD-KVLIYNRPNMETVPlaSGRDLDWDEEMAKAQ 280
Cdd:PLN03102 102 SIAAILRHAKPKILFVDR---------SFEPLAREVLHLlssEDSNLNlPVIFIHEIDFPKRP--SSEELDYECLIQRGE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 281 -----SQDCVPVLSEH-PLYILYTSGTTGLPKGVV-RPTGGY----AVMLNWTMssiyGLKPGEVWWAA--SDLGWVvgh 347
Cdd:PLN03102 171 ptpslVARMFRIQDEHdPISLNYTSGTTADPKGVViSHRGAYlstlSAIIGWEM----GTCPVYLWTLPmfHCNGWT--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 348 syICYGPLIHGNTTVLYegKPVGTPDAgayFRVLAEHGVAALFTAPTAIRAIRQQD-------------------PGAAL 408
Cdd:PLN03102 244 --FTWGTAARGGTSVCM--RHVTAPEI---YKNIEMHNVTHMCCVPTVFNILLKGNsldlsprsgpvhvltggspPPAAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 409 GKQYSLTRFKTLFVAGE---RCDVETLEWSKKVFRVPvlDHwWQTETGSPITASCIGLG-----NSKTPppgqagKSVPg 480
Cdd:PLN03102 317 VKKVQRLGFQVMHAYGLteaTGPVLFCEWQDEWNRLP--EN-QQMELKARQGVSILGLAdvdvkNKETQ------ESVP- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 481 ynvmilddnmqkLKARCLGNIVVKlplPPGAFSGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDD 556
Cdd:PLN03102 387 ------------RDGKTMGEIVIK---GSSIMKGYLKNpkatSEAFKH-------GWLNTGDVGVIHPDGHVEIKDRSKD 444
|
490
....*....|....*.
gi 1191882765 557 VINVAGHRISAGAIEE 572
Cdd:PLN03102 445 IIISGGENISSVEVEN 460
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
125-572 |
1.31e-15 |
|
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: 79.68 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:cd05920 29 PDRIAVV------DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVTAsfgiepgrkveympileeamriGQHKPDkvliynrpnmETVPLAsgrdldwdEEMAKAQSQdc 284
Cdd:cd05920 103 ELSAFCAHAEAVAYIVP----------------------DRHAGF----------DHRALA--------RELAESIPE-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 285 vpvlsehPLYILYTSGTTGLPKGVVRPTGGYAVMLNwTMSSIYGLKPGEVWWAASDlgwvVGHSYICYGPLIHGntTVLY 364
Cdd:cd05920 141 -------VALFLLSGGTTGTPKLIPRTHNDYAYNVR-ASAEVCGLDQDTVYLAVLP----AAHNFPLACPGVLG--TLLA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 365 EGKPV--GTPDAGAYFRVLAEHGVaalfTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVP 442
Cdd:cd05920 207 GGRVVlaPDPSPDAAFPLIEREGV----TVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 443 VLDHWWQTEtgspitasciGLGNSKTP--PP----GQAGKSV-PGYNVMILDDNmqklkarclGNivvklPLPPGA---- 511
Cdd:cd05920 283 LQQVFGMAE----------GLLNYTRLddPDeviiHTQGRPMsPDDEIRVVDEE---------GN-----PVPPGEegel 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 512 -------FSGLWK----NQEAFKHlyfekfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05920 339 ltrgpytIRGYYRapehNARAFTP------DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVEN 404
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
126-571 |
2.55e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 78.77 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK06145 17 DRAALVYRD------QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVV-VTASFGIEPGrkveympILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLDwdeemakaqsqdc 284
Cdd:PRK06145 91 VAYILGDAGAKLLlVDEEFDAIVA-------LETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTD------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 285 vpvlsehpLY-ILYTSGTTGLPKGVvrptggyavMLNWtmssiyglkpGEVWWAASD----LGWVVGHSYICYGPLIH-- 357
Cdd:PRK06145 151 --------LVrLMYTSGTTDRPKGV---------MHSY----------GNLHWKSIDhviaLGLTASERLLVVGPLYHvg 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 358 ----GNTTVLYEGKPVGTP---DAGAYFRVLAEHGVAALFTAP---TAIRAIRQQDpgaalgkQYSLTRFKTLFVAGERC 427
Cdd:PRK06145 204 afdlPGIAVLWVGGTLRIHrefDPEAVLAAIERHRLTCAWMAPvmlSRVLTVPDRD-------RFDLDSLAWCIGGGEKT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 428 DVETLEWSKKVF-RVPVLDHWWQTETGSPITASCIGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlp 506
Cdd:PRK06145 277 PESRIRDFTRVFtRARYIDAYGLTETCSGDTLMEAGREIEKI---GSTGRALAHVEIRIADGAGRWLPPNMKGEICMR-- 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 507 lPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK06145 352 -GPKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVE 412
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
142-573 |
3.60e-15 |
|
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: 78.14 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLaGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA 221
Cdd:cd05909 7 SLTYRKLLTGAIAL-ARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 222 S-----FGIEPGRKVEYMP--ILEEAMRIGQHKPDKVLIYnrpnmetvpLASG-RDLDWDEEMAkaqsqdCVPVLSEHPL 293
Cdd:cd05909 86 KqfiekLKLHHLFDVEYDAriVYLEDLRAKISKADKCKAF---------LAGKfPPKWLLRIFG------VAPVQPDDPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 294 YILYTSGTTGLPKGVVRP-----TGGYAVmlnwtmSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLY---- 364
Cdd:cd05909 151 VILFTSGSEGLPKGVVLShknllANVEQI------TAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpnpl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 365 EGKPVGtpdagayfRVLAEHGVAALFTAPTAIRAIrqqdpgAALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVL 444
Cdd:cd05909 225 DYKKIP--------ELIYDKKATILLGTPTFLRGY------ARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRIL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 445 DHWWQTETgSPITASciglgNSKTPP--PGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEA 521
Cdd:cd05909 291 EGYGTTEC-SPVISV-----NTPQSPnkEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVR---GPNVMLGYLNEPEL 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 522 FKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEEE 573
Cdd:cd05909 362 TSFAFGD---GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDI 410
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
142-558 |
4.25e-15 |
|
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: 77.87 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA 221
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 222 sfgiepgrkveympileeamrigqhKPDKVLIynrpnmetvplasgrdldwdeemakaqsqdcvpvlsehplyILYTSGT 301
Cdd:cd05914 87 -------------------------DEDDVAL-----------------------------------------INYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 302 TGLPKGVVRPtgGYAVMLNWTMSSIYG-LKPGEVWWAASDLGwvvgHSYICYG----PLIHGNTTVLYEGKPVGTPDAGA 376
Cdd:cd05914 101 TGNSKGVMLT--YRNIVSNVDGVKEVVlLGKGDKILSILPLH----HIYPLTFtlllPLLNGAHVVFLDKIPSAKIIALA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 377 YFRVLAEHGVAALF-----------------------TAPTAIRAIRQQdPGAALGKQYSlTRFKTLFVAGERCDVETLE 433
Cdd:cd05914 175 FAQVTPTLGVPVPLviekifkmdiipkltlkkfkfklAKKINNRKIRKL-AFKKVHEAFG-GNIKEFVIGGAKINPDVEE 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 434 WSKKVfRVPVLDHWWQTETGsPITASciglgnskTPPP----GQAGKSVPGYNVMILDDNMQKLKarclGNIVVKlplPP 509
Cdd:cd05914 253 FLRTI-GFPYTIGYGMTETA-PIISY--------SPPNrirlGSAGKVIDGVEVRIDSPDPATGE----GEIIVR---GP 315
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1191882765 510 GAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVI 558
Cdd:cd05914 316 NVMKGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMI 362
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
152-572 |
5.01e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 77.48 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 152 VSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIF----GGFASKELSSRIDHAKPKVVvtasfgiep 227
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplnPTLKESVLRYLVADAGGRIV--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 228 grkveympILEEAMRigqHKPDKVLIYNrPNMETVplasgrdLDWDEEMAKAQSQDCVPVLSEHPLYILYTSGTTGLPKG 307
Cdd:cd05922 74 --------LADAGAA---DRLRDALPAS-PDPGTV-------LDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 308 VVRPTggYAVMLNW-TMSSIYGLKPGEVWWAASDLGWvvghsyiCYG------PLIHGNTTVLYEGkpvGTPDAGaYFRV 380
Cdd:cd05922 135 VRLSH--QNLLANArSIAEYLGITADDRALTVLPLSY-------DYGlsvlntHLLRGATLVLTND---GVLDDA-FWED 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 381 LAEHGVAALFTAPT--AI--RAIRQQDPGAAL-------GK--QYSLTRFKTLFVAGercdvetlewskkvfRVPVLdhW 447
Cdd:cd05922 202 LREHGATGLAGVPStyAMltRLGFDPAKLPSLryltqagGRlpQETIARLRELLPGA---------------QVYVM--Y 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 448 WQTETGSPITAsciglgnskTPP------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWkNQEA 521
Cdd:cd05922 265 GQTEATRRMTY---------LPPerilekPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN---VMKGYW-NDPP 331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1191882765 522 FKhLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05922 332 YR-RKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA 381
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
126-571 |
5.05e-15 |
|
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: 77.29 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIhslifggfaske 205
Cdd:cd17652 2 DAPAVVFGD------ETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAA------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 lssridhakpkvvvtasfgiepgrkveYMPIleeamrigqhkpdkvliynrpnmetvplasgrDLDWDEEMAKAQSQDCV 285
Cdd:cd17652 64 ---------------------------YLPL--------------------------------DPAYPAERIAYMLADAR 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 286 PVL----SEHPLYILYTSGTTGLPKGVVRPTGGYAvmlNWTMSSI--YGLKPGEVWWAASDLGWVVGHSYICyGPLIHGN 359
Cdd:cd17652 85 PALllttPDNLAYVIYTSGSTGRPKGVVVTHRGLA---NLAAAQIaaFDVGPGSRVLQFASPSFDASVWELL-MALLAGA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 360 TTVLYEGKPVGTPDAGAyfRVLAEHGVAALFTAPTAIRAIrqqDPGAALGkqysltrFKTLFVAGERCDVETLE-WSKKv 438
Cdd:cd17652 161 TLVLAPAEELLPGEPLA--DLLREHRITHVTLPPAALAAL---PPDDLPD-------LRTLVVAGEACPAELVDrWAPG- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 439 fRVpVLDHWWQTETgsPITASCIGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPG-------A 511
Cdd:cd17652 228 -RR-MINAYGPTET--TVCATMAGPLPGGGVPP--IGRPVPGTRVYVLDARLR--------------PVPPGvpgelyiA 287
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 512 FSGLWK---NQEAfkhLYFEKF-------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17652 288 GAGLARgylNRPG---LTAERFvadpfgaPGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
143-407 |
7.09e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 77.48 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 143 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVtas 222
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLV--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 fgIEPG-RKVEYMPILEEAMRIGQHKPDKVLIYNRPNMET-VPLASGRDLDWDEEMAKAQSQDCVPVLSEHPLYILY-TS 299
Cdd:PRK06164 113 --VWPGfKGIDFAAILAAVPPDALPPLRAIAVVDDAADATpAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFtTS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 300 GTTGLPKGVVRPTGGyAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGplIHGNTTVLYEgkPVGtpDAGAYFR 379
Cdd:PRK06164 191 GTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGA--LAGGAPLVCE--PVF--DAARTAR 263
|
250 260
....*....|....*....|....*...
gi 1191882765 380 VLAEHGVAALFTAPTAIRAIRQQDPGAA 407
Cdd:PRK06164 264 ALRRHRVTHTFGNDEMLRRILDTAGERA 291
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
126-572 |
7.38e-15 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 77.48 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIiydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK06087 38 DKIAV-----VDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTASFgiepGRKVEYMP-ILEEAMRIGQHKPDKVLIYNRPNMETVPLAsgrdldwdEEMAKAQS-QD 283
Cdd:PRK06087 113 LVWVLNKCQAKMFFAPTL----FKQTRPVDlILPLQNQLPQLQQIVGVDKLAPATSSLSLS--------QIIADYEPlTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 284 CVPVLSEHPLYILYTSGTTGLPKGV-------VRPTGGYAVMLNWTMSSIYglkpgevwWAASDLGWVVGHSYICYGPLI 356
Cdd:PRK06087 181 AITTHGDELAAVLFTSGTEGLPKGVmlthnniLASERAYCARLNLTWQDVF--------MMPAPLGHATGFLHGVTAPFL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 357 HGNTTVLYEgkpvgtpdagayfrvlaehgvaaLFTAPTAIRAIRQQDPGAALGkqysltrfKTLFVAGERC-------DV 429
Cdd:PRK06087 253 IGARSVLLD-----------------------IFTPDACLALLEQQRCTCMLG--------ATPFIYDLLNllekqpaDL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 430 ETLEW--------SKKVFR------VPVLDHWWQTETgSPitASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKA 495
Cdd:PRK06087 302 SALRFflcggttiPKKVARecqqrgIKLLSVYGSTES-SP--HAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPP 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 496 RCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK06087 379 GCEGEEASR---GPNVFMGYLDEPELTARALDEE--GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVED 450
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
144-308 |
7.95e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 77.16 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA-S 222
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAdG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 F-----------------GIEPGR-KVEYMPILEEAMRIGQHKPdkvliynrPNMETVP--LASGRDLDwDEEMAKAQSQ 282
Cdd:PRK08315 125 FkdsdyvamlyelapelaTCEPGQlQSARLPELRRVIFLGDEKH--------PGMLNFDelLALGRAVD-DAELAARQAT 195
|
170 180
....*....|....*....|....*..
gi 1191882765 283 dcvpvLSEH-PLYILYTSGTTGLPKGV 308
Cdd:PRK08315 196 -----LDPDdPINIQYTSGTTGFPKGA 217
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
297-572 |
1.15e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 75.59 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 297 YTSGTTGLPKgVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASDLgWVVGHSYICYGPLIHGNTTVLYEGkPVGTPDAGA 376
Cdd:cd05944 9 HTGGTTGTPK-LAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVNGSVVTLLTPLASGAHVVLAG-PAGYRNPGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 377 Y---FRVLAEHGVAALFTAPTAIRAIRQQDPGAALGkqySLtrfKTLFVAGERCDVETLEWSKKVFRVPVLDHWWQTEtg 453
Cdd:cd05944 86 FdnfWKLVERYRITSLSTVPTVYAALLQVPVNADIS---SL---RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTE-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 454 spitASCiglGNSKTPP-----PGQAGKSVPGYNVMIL-DDNMQKLKARC----LGNIVVKlplPPGAFsGLWKNQEAFK 523
Cdd:cd05944 158 ----ATC---LVAVNPPdgpkrPGSVGLRLPYARVRIKvLDGVGRLLRDCapdeVGEICVA---GPGVF-GGYLYTEGNK 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1191882765 524 HLYFEkfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05944 227 NAFVA--DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEE 273
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
115-573 |
1.24e-14 |
|
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: 76.19 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 115 AIDRHIESGKgDKVAiiydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIH 194
Cdd:cd17653 2 AFERIAAAHP-DAVA------VESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 195 SLIFGGFASkelsSRIDHakpkvvvtasfgiepgrkveympILEEAmrigqhkpDKVLIynrpnmetVPLASGRDLdwde 274
Cdd:cd17653 75 VPLDAKLPS----ARIQA-----------------------ILRTS--------GATLL--------LTTDSPDDL---- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 275 emakaqsqdcvpvlsehpLYILYTSGTTGLPKGVVRPTGGYAVMLnWTMSSIYGLKPG----EVWWAASDLG-WVVghsy 349
Cdd:cd17653 108 ------------------AYIIFTSGSTGIPKGVMVPHRGVLNYV-SQPPARLDVGPGsrvaQVLSIAFDACiGEI---- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 350 icYGPLIHGNTTVLyegkpvgtPDAGAYFRVLAEHgVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKTLFVAGERCdv 429
Cdd:cd17653 165 --FSTLCNGGTLVL--------ADPSDPFAHVART-VDALMSTPSILSTLSPQD----------FPNLKTIFLGGEAV-- 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 430 etlewSKkvfrvPVLDHWWQ----------TETgspitaSCIGLGNSKTppPGQA---GKSVPGYNVMILDDNMQKLKAR 496
Cdd:cd17653 222 -----PP-----SLLDRWSPgrrlynaygpTEC------TISSTMTELL--PGQPvtiGKPIPNSTCYILDADLQPVPEG 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 497 CLGNIVVklpLPPGAFSGLWKNQEA----FKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd17653 284 VVGEICI---SGVQVARGYLGNPALtaskFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEE 360
|
.
gi 1191882765 573 E 573
Cdd:cd17653 361 V 361
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
133-571 |
1.52e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 77.01 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 133 DSP-VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRID 211
Cdd:PRK10252 473 DAPaLADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 212 HAKPKVVVTASfgiepgrkveympilEEAMRIgQHKPDKVLiynrpnmetvplasgrdLDWDEEMAKAQSQDCVPVLSEH 291
Cdd:PRK10252 553 DARPSLLITTA---------------DQLPRF-ADVPDLTS-----------------LCYNAPLAPQGAAPLQLSQPHH 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 292 PLYILYTSGTTGLPKGVVrpTGGYAVM--LNWtMSSIYGLKPG----------------EVWWaasdlgwvvghsyicyg 353
Cdd:PRK10252 600 TAYIIFTSGSTGRPKGVM--VGQTAIVnrLLW-MQNHYPLTADdvvlqktpcsfdvsvwEFFW----------------- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 354 PLIHGNTTVLyeGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQ-DPGAALGKQYSLTRfktLFVAGERCDVEtl 432
Cdd:PRK10252 660 PFIAGAKLVM--AEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASlTPEGARQSCASLRQ---VFCSGEALPAD-- 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 433 ewskkvfrvpVLDHWWQTeTGSPI------TASCIGLgnSKTPPPGQA-----GKSVP-GYNV-----MILDDNMQklka 495
Cdd:PRK10252 733 ----------LCREWQQL-TGAPLhnlygpTEAAVDV--SWYPAFGEElaavrGSSVPiGYPVwntglRILDARMR---- 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 496 rclgnivvklPLPPGAfSGlwknqeafkHLYF-----------------EKF------PG--YYDTMDAGYMDEEGYVYV 550
Cdd:PRK10252 796 ----------PVPPGV-AG---------DLYLtgiqlaqgylgrpdltaSRFiadpfaPGerMYRTGDVARWLDDGAVEY 855
|
490 500
....*....|....*....|.
gi 1191882765 551 MSRVDDVINVAGHRISAGAIE 571
Cdd:PRK10252 856 LGRSDDQLKIRGQRIELGEID 876
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
144-571 |
3.08e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 75.23 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTasf 223
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 224 giepgrkveympileeamrigqhkpDKVLIYNRPNMEtvplasgrDLDWDEEMAKAQSQDCVPVL-SEHPLYILYTSGTT 302
Cdd:PRK09088 101 -------------------------DDAVAAGRTDVE--------DLAAFIASADALEPADTPSIpPERVSLILFTSGTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 303 GLPKGV-VRPTGGYAVMLNWtmssiyglkpgevwwaaSDLGWVVGHS-YICYGPLIH--GNTT----VLYEGKPVGTPD- 373
Cdd:PRK09088 148 GQPKGVmLSERNLQQTAHNF-----------------GVLGRVDAHSsFLCDAPMFHiiGLITsvrpVLAVGGSILVSNg 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 374 --AGAYFRVLAEH--GVAALFTAPTAIRAIRQQdPGAALGkqySLTRFKTLFVAGERCDVETLEWSKKVfRVPVLDHWWQ 449
Cdd:PRK09088 211 fePKRTLGRLGDPalGITHYFCVPQMAQAFRAQ-PGFDAA---ALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 450 TETGS----PITASCIglgNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHL 525
Cdd:PRK09088 286 SEAGTvfgmSVDCDVI---RAKA---GAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR---GPNLSPGYWRRPQATARA 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1191882765 526 YFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK09088 357 FTGD--GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIE 400
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
119-390 |
3.17e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 75.31 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 119 HIESGKGDKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIF 198
Cdd:PRK07798 11 AVADAVPDRVALVCGD------RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 199 GGFASKELSSRIDHAKPKVVVtasFGIEPGRKVEymPILEEAMRIgqhkpdKVLIynrpnmeTVPLASGRDLDWD----E 274
Cdd:PRK07798 85 YRYVEDELRYLLDDSDAVALV---YEREFAPRVA--EVLPRLPKL------RTLV-------VVEDGSGNDLLPGavdyE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 275 EMAKAQSQDCVPVL-SEHPLYILYTSGTTGLPKGVV--------------RPTGGYAVMLNWTMSSIYGLKPGEVWWAAS 339
Cdd:PRK07798 147 DALAAGSPERDFGErSPDDLYLLYTGGTTGMPKGVMwrqedifrvllggrDFATGEPIEDEEELAKRAAAGPGMRRFPAP 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191882765 340 dlgwvvghsyicygPLIH-------------GNTTVLYegkPVGTPDAGAYFRVLAEHGVAALF 390
Cdd:PRK07798 227 --------------PLMHgagqwaafaalfsGQTVVLL---PDVRFDADEVWRTIEREKVNVIT 273
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
290-572 |
4.61e-14 |
|
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: 73.45 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 290 EHPLYILYTSGTTGLPKGVV--------RPTGGYAVMLNWTMSSI-YGLKP----GEVWWAASDL----GWVVGHSYICY 352
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLlanktffaVPDILQKEGLNWVVGDVtYLPLPathiGGLWWILTCLihggLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 353 GPLihgnttvlyegkpvgtpdagayFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkQYSlTRFKTLFVAGERC---DV 429
Cdd:cd17635 81 KSL----------------------FKILTTNAVTTTCLVPTLLSKLVSELKSAN---ATV-PSLRLIGYGGSRAiaaDV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 430 ETLEWSKKVfrvPVLDHWWQTETGspiTASCIGLGNSkTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPP 509
Cdd:cd17635 135 RFIEATGLT---NTAQVYGLSETG---TALCLPTDDD-SIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIK---SP 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191882765 510 GAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd17635 205 ANMLGYWNNPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVER 264
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
295-573 |
4.81e-14 |
|
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: 74.25 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 295 ILYTSGTTGLPKGVVRPTGGYAVMLNwTMSsiyglkpgEVW-WAASDlgwVVGHSYicygPLIHGNTTV------LYEGK 367
Cdd:cd05941 94 ILYTSGTTGRPKGVVLTHANLAANVR-ALV--------DAWrWTEDD---VLLHVL----PLHHVHGLVnallcpLFAGA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 368 PV---GTPDAGAYFRVLAEHGVAALFTAPTA----IRAIRQQDPGAALGKQYSLTRFKtLFVAGERC-DVETLEWSKKVF 439
Cdd:cd05941 158 SVeflPKFDPKEVAISRLMPSITVFMGVPTIytrlLQYYEAHFTDPQFARAAAAERLR-LMVSGSAAlPVPTLEEWEAIT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 440 RVPVLDHWWQTETGspITASCiGLGNSKTppPGQAGKSVPGYNVMILDDNMQK-LKARCLGNIVVKlplPPGAFSGLWKN 518
Cdd:cd05941 237 GHTLLERYGMTEIG--MALSN-PLDGERR--PGTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVR---GPSVFKEYWNK 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882765 519 QEAFKhlyfEKFP--GYYDTMDAGYMDEEGYVYVMSRV-DDVINVAGHRISAGAIEEE 573
Cdd:cd05941 309 PEATK----EEFTddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERV 362
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
139-568 |
5.89e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 74.55 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 139 TKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVV 218
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 219 VT-ASFgiepgrkveympiLEEAMRIGQHKPDKVliynrPNMETVPLASGRDLDWDEEMAkAQSQDCVPVLSEHPLyILY 297
Cdd:PRK08276 88 IVsAAL-------------ADTAAELAAELPAGV-----PLLLVVAGPVPGFRSYEEALA-AQPDTPIADETAGAD-MLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 298 TSGTTGLPKGVVRPTGGYAVMLNWTMSsiyglkpgeVWWAASDLGWVVGHSYICYGPLIH-------------GNTTVLY 364
Cdd:PRK08276 148 SSGTTGRPKGIKRPLPGLDPDEAPGMM---------LALLGFGMYGGPDSVYLSPAPLYHtaplrfgmsalalGGTVVVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 365 EG-KPVGTPDAGAYFRVLAEHGVAALFTA----PTAIRAirqqdpgaalgkQYSLTRFKTLFVAGERCDVET----LEWS 435
Cdd:PRK08276 219 EKfDAEEALALIERYRVTHSQLVPTMFVRmlklPEEVRA------------RYDVSSLRVAIHAAAPCPVEVkramIDWW 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 436 KkvfrvPVLDHWWQTETGSPITASciglgNSKT--PPPGQAGKSVPGyNVMILDDNMQKLKARCLGNIVVKLPLPPgaFS 513
Cdd:PRK08276 287 G-----PIIHEYYASSEGGGVTVI-----TSEDwlAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYP--FE 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 514 GLwKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVInvaghrISAG 568
Cdd:PRK08276 354 YH-NDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI------ISGG 399
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
126-553 |
1.66e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 73.12 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIydspVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK13390 12 DRPAVI----VAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVtASFGIEpgrkveympilEEAMRIGQHKPdkvliynrpnmetVPLASGRDLDW--DEEMAKAQSQd 283
Cdd:PRK13390 88 ADYIVGDSGARVLV-ASAALD-----------GLAAKVGADLP-------------LRLSFGGEIDGfgSFEAALAGAG- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 284 cvPVLSEHPL--YILYTSGTTGLPKGV--------VRPTGGYAVMLnwtMSSIYGLKPGEVWWA------ASDLGWvvgh 347
Cdd:PRK13390 142 --PRLTEQPCgaVMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAI---ARAFYDISESDIYYSsapiyhAAPLRW---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 348 syiCygPLIH--GNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIraIRQQDPGAALGKQYSLTRFKTLFVAGE 425
Cdd:PRK13390 213 ---C--SMVHalGGTVVLAK-----RFDAQATLGHVERYRITVTQMVPTMF--VRLLKLDADVRTRYDVSSLRAVIHAAA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 426 RCDVET----LEWSKKVfrvpVLDHWWQTET-GSPITASCIGLGNsktppPGQAGKSVPGyNVMILDDNMQKLKARCLGN 500
Cdd:PRK13390 281 PCPVDVkhamIDWLGPI----VYEYYSSTEAhGMTFIDSPDWLAH-----PGSVGRSVLG-DLHICDDDGNELPAGRIGT 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1191882765 501 IVVKLPLPPGAFSGLWKNQEAFKHlyfEKFPGYYDTMDAGYMDEEGYVYVMSR 553
Cdd:PRK13390 351 VYFERDRLPFRYLNDPEKTAAAQH---PAHPFWTTVGDLGSVDEDGYLYLADR 400
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
295-572 |
6.33e-13 |
|
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: 70.05 E-value: 6.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 295 ILYTSGTTGLPKgvvrptggyAVMLNW---TMS-----SIYGLKPGEVWWAASDLGWVVGhsyicYGPLIHGnttvLYEG 366
Cdd:cd17630 5 VILTSGSTGTPK---------AVVHTAanlLASaaglhSRLGFGGGDSWLLSLPLYHVGG-----LAILVRS----LLAG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 367 KP--VGTPDAGAYFRvLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEWSKKVfRVPVL 444
Cdd:cd17630 67 AElvLLERNQALAED-LAPPGVTHVSLVPTQLQRLLDSGQGPA-----ALKSLRAVLLGGAPIPPELLERAADR-GIPLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 445 DHWWQTETGSPITASCIGLgnsktPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWknqeafkh 524
Cdd:cd17630 140 TTYGMTETASQVATKRPDG-----FGRGGVGVLLPGRELRIVEDGEIWVGGASLAMGYLRGQLVPEFNEDGW-------- 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1191882765 525 lyfekfpgyYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd17630 207 ---------FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEA 245
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
227-571 |
1.79e-12 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 69.71 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 227 PGRKVEYMPILEEAMRIGQHKPDKVLIynrpnMETVPLASGRDLDWDEEMAkAQSQDCVPVLSEhPLYILYTSGTTGLPK 306
Cdd:cd05929 69 PAYKSSRAPRAEACAIIEIKAAALVCG-----LFTGGGALDGLEDYEAAEG-GSPETPIEDEAA-GWKMLYSGGTTGRPK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 307 GVVRPTGGyavmlnwtmssiyGLKPGEVWWAASDL-GWVVGHSYICYGPLIHG------NTTVLYEGKPVGTP--DAGAY 377
Cdd:cd05929 142 GIKRGLPG-------------GPPDNDTLMAAALGfGPGADSVYLSPAPLYHAapfrwsMTALFMGGTLVLMEkfDPEEF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 378 FRVLAEHGVAALFTAPTAIRAIRQQdPGAALGKqYSLTRFKTLFVAGERCDVETLE-----WSKKVfrvpvldhwWQTET 452
Cdd:cd05929 209 LRLIERYRVTFAQFVPTMFVRLLKL-PEAVRNA-YDLSSLKRVIHAAAPCPPWVKEqwidwGGPII---------WEYYG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 453 GSPITASCIGLGNSKTPPPGQAGKSVPGyNVMILDDNMQklkarclgnivvklPLPPGAFSGLW-KNQEAFK-HLYFEKF 530
Cdd:cd05929 278 GTEGQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGN--------------EVPPGEIGEVYfANGPGFEyTNDPEKT 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1191882765 531 P-----GYYDTM-DAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05929 343 AaarneGGWSTLgDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIE 389
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
124-565 |
3.17e-12 |
|
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: 69.19 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 124 KGDKVAIIYDSPVTDTKATITYKEVLEQVSRLAGVLVKHGvSKGDTVVIympMIPQAM---YTMLACARIGAIHSLIF-- 198
Cdd:cd05931 6 RPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLL---LAPPGLdfvAAFLGCLYAGAIAVPLPpp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 199 -GGFASKELSSRIDHAKPKVVVTASfgiepgrkveympileeamriGQHKPDKVLIYNRPNMETVPLasgRDLDWDEEMA 277
Cdd:cd05931 82 tPGRHAERLAAILADAGPRVVLTTA---------------------AALAAVRAFAASRPAAGTPRL---LVVDLLPDTS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 278 KAQSQDCVPVLSEhPLYILYTSGTTGLPKGVVRPTGgyAVMLN-WTMSSIYGLKPGEVWwaAS------DLGWVVGhsyI 350
Cdd:cd05931 138 AADWPPPSPDPDD-IAYLQYTSGSTGTPKGVVVTHR--NLLANvRQIRRAYGLDPGDVV--VSwlplyhDMGLIGG---L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 351 CyGPLIHGNTTVL-----YEGKPVGTPDAGAYFRvlAEHGVAALFTAPTAIRAIRQQDPGAalgkqYSLTRFKTLFVAGE 425
Cdd:cd05931 210 L-TPLYSGGPSVLmspaaFLRRPLRWLRLISRYR--ATISAAPNFAYDLCVRRVRDEDLEG-----LDLSSWRVALNGAE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 426 RCDVETLE----------WSKKVFR-------------VPVLDHWWQTETGSPITASCIGLGNSKTPPPGQA----GKSV 478
Cdd:cd05931 282 PVRPATLRrfaeafapfgFRPEAFRpsyglaeatlfvsGGPPGTGPVVLRVDRDALAGRAVAVAADDPAARElvscGRPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 479 PGYNVMILDDN-MQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKFP----GYYDTMDAGYMDeEGYVYVMSR 553
Cdd:cd05931 362 PDQEVRIVDPEtGRELPDGEVGEIWVR---GPSVASGYWGRPEATAETFGALAAtdegGWLRTGDLGFLH-DGELYITGR 437
|
490
....*....|..
gi 1191882765 554 VDDVINVAGHRI 565
Cdd:cd05931 438 LKDLIIVRGRNH 449
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
137-565 |
3.51e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 68.88 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 137 TDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPK 216
Cdd:PRK05857 36 CDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 217 VVVTAsfgiePGRKV--EYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLDWDEemakaqsqdcvpvlsehPLY 294
Cdd:PRK05857 116 AALVA-----PGSKMasSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSED-----------------PLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 295 ILYTSGTTGLPKGVVRPTGGYAVM--------LNW--------TMSSIYGLKPGEVWWAASdlgwvvghsyiCygpLIHG 358
Cdd:PRK05857 174 MIFTSGTTGEPKAVLLANRTFFAVpdilqkegLNWvtwvvgetTYSPLPATHIGGLWWILT-----------C---LMHG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 359 NTTVlyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTRFKTLFVAGER---CDVETLEWS 435
Cdd:PRK05857 240 GLCV------TGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANA----TVPSLRLVGYGGSRaiaADVRFIEAT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 436 KkvfrVPVLDHWWQTETGSpiTASCIGLGNSKTP--PPGQAGKSVPGYNVMILDDN------MQKLKARCLGNIVVKlpl 507
Cdd:PRK05857 310 G----VRTAQVYGLSETGC--TALCLPTDDGSIVkiEAGAVGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIK--- 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882765 508 PPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRI 565
Cdd:PRK05857 381 SPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNI 435
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
108-568 |
3.75e-12 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 68.75 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 108 MLNMCYNAIDRHIESGkgDKVAIIydspvTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLAC 187
Cdd:PRK07514 1 MNNNLFDALRAAFADR--DAPFIE-----TPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 188 ARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAsfgiePGRKVEYMPILEEAmrigqhkpdkvliyNRPNMETVPLASG 267
Cdd:PRK07514 74 LRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD-----PANFAWLSKIAAAA--------------GAPHVETLDADGT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 268 RDLdwdEEMAKAQSQD--CVPVLSEHPLYILYTSGTTGLPKGvvrptggyAVMLNWTMSS-------IYGLKPGEVwwaa 338
Cdd:PRK07514 135 GSL---LEAAAAAPDDfeTVPRGADDLAAILYTSGTTGRSKG--------AMLSHGNLLSnaltlvdYWRFTPDDV---- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 339 sdlgwvvghsyicygpLIH-------------GNTTVLYEGKPVGTP--DAGAYFRVLAE----HGVAALFTaptaiRAI 399
Cdd:PRK07514 200 ----------------LIHalpifhthglfvaTNVALLAGASMIFLPkfDPDAVLALMPRatvmMGVPTFYT-----RLL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 400 rqQDPGaaLGKQysLTRFKTLFVAGER-CDVETL-EWSKKVFRvPVLDHWWQTETGSpitasciglgNSKTP-----PPG 472
Cdd:PRK07514 259 --QEPR--LTRE--AAAHMRLFISGSApLLAETHrEFQERTGH-AILERYGMTETNM----------NTSNPydgerRAG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 473 QAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLW----KNQEAFKHlyfekfPGYYDTMDAGYMDEEGY 547
Cdd:PRK07514 322 TVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK---GPNVFKGYWrmpeKTAEEFRA------DGFFITGDLGKIDERGY 392
|
490 500
....*....|....*....|.
gi 1191882765 548 VYVMSRVDDVInvaghrISAG 568
Cdd:PRK07514 393 VHIVGRGKDLI------ISGG 407
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
136-571 |
2.13e-11 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 66.45 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 136 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 215
Cdd:PRK05852 37 VTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 216 KVVVTASFGiePG-RKVEYMPILEEAMRIGQhkpdkvliyNRPNMETVPLAsgrDLDWDEEMAKAQSQDcvPVLSEHPLY 294
Cdd:PRK05852 117 RVVLIDADG--PHdRAEPTTRWWPLTVNVGG---------DSGPSGGTLSV---HLDAATEPTPATSTP--EGLRPDDAM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 295 ILYTSGTTGLPKgvvrptggyavMLNWTMSSIYGLKPGEVwwAASDLGwvVGHSYICYGPLIHGNTTV------LYEGKP 368
Cdd:PRK05852 181 IMFTGGTTGLPK-----------MVPWTHANIASSVRAII--TGYRLS--PRDATVAVMPLYHGHGLIaallatLASGGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 369 VGTPDAGAY----FRVLAEHGVAALFTAPTAIRAIRQQDPGAalgKQYSLTRFKTLFVagERC----DVETLEWSKKVFR 440
Cdd:PRK05852 246 VLLPARGRFsahtFWDDIKAVGATWYTAVPTIHQILLERAAT---EPSGRKPAALRFI--RSCsaplTAETAQALQTEFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 441 VPVLDHWWQTETGSPITASCI-GLGNSKTP--PPGQAGKSVpGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWK 517
Cdd:PRK05852 321 APVVCAFGMTEATHQVTTTQIeGIGQTENPvvSTGLVGRST-GAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 518 NQEA-FKHlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK05852 400 ITAAnFTD-------GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVE 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-571 |
2.29e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.29 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 205
Cdd:PRK12316 2018 EAIAVVFG------DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY----------- 2080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 lssridhakpkVVVTASFgiePGRKVEYMpiLEEAmRIGqhkpdkVLIYNRPNMETVPLASG---RDLDWDEEMAKAQSQ 282
Cdd:PRK12316 2081 -----------VPLDPNY---PAERLAYM--LEDS-GAA------LLLTQRHLLERLPLPAGvarLPLDRDAEWADYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 283 DCVPVLSEHPL-YILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYiCYGPLIHGNTT 361
Cdd:PRK12316 2138 APAVQLAGENLaYVIYTSGSTGLPKGVAVSHGALVAHCQA-AGERYELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARV 2215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 362 VLyegKPVGTPDAGAYFRVLAEHGVAALFTAPT-----AIRAIRQQDPGAAlgkqysltrfKTLFVAGERCDVETLE-WS 435
Cdd:PRK12316 2216 LI---RDDELWDPEQLYDEMERHGVTILDFPPVylqqlAEHAERDGRPPAV----------RVYCFGGEAVPAASLRlAW 2282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 436 KKVFRVPVLDHWWQTETG-SPITASC--IGLGNSKTPPPGQAGKSVPGYnvmILDDNMQklkarclgnivvklPLPPGAF 512
Cdd:PRK12316 2283 EALRPVYLFNGYGPTEAVvTPLLWKCrpQDPCGAAYVPIGRALGNRRAY---ILDADLN--------------LLAPGMA 2345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882765 513 SGLWKNQEAFKHLYFEKfPG-----------------YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK12316 2346 GELYLGGEGLARGYLNR-PGltaerfvpdpfsasgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIE 2420
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
125-572 |
3.21e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 65.74 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIYDspvtdtKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFAS 203
Cdd:PRK08162 32 PDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIP-AMVEAhFGVPMAGAVLNTLNTRLDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 204 KELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLASGRDLD-----WDEEMAK 278
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIVDT---------EFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEaflasGDPDFAW 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 279 AQSQDCVPVLSehplyILYTSGTTGLPKGVV---RptGGYavmLNwTMSSI--YGLKPGEVWWaasdlgWVVghsyicyg 353
Cdd:PRK08162 176 TLPADEWDAIA-----LNYTSGTTGNPKGVVyhhR--GAY---LN-ALSNIlaWGMPKHPVYL------WTL-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 354 PLIHGN------TTVLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGE 425
Cdd:PRK08162 231 PMFHCNgwcfpwTVAARAGTNVCLRkvDPKLIFDLIREHGVTHYCGAPIVLSALIN----APAEWRAGIDHPVHAMVAGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 426 RCDVETLEWSKKV-FRVpvlDHWWQ-TETGSPITASCIGLGNSKTPPPGQAG-KSVPGYN------VMILD-DNMQKLKA 495
Cdd:PRK08162 307 APPAAVIAKMEEIgFDL---THVYGlTETYGPATVCAWQPEWDALPLDERAQlKARQGVRyplqegVTVLDpDTMQPVPA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 496 ----------RclGNIVVKlplppgafsGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHR 564
Cdd:PRK08162 384 dgetigeimfR--GNIVMK---------GYLKNPKATE----EAFAgGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGEN 448
|
....*...
gi 1191882765 565 ISAGAIEE 572
Cdd:PRK08162 449 ISSIEVED 456
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
126-571 |
3.27e-11 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGaihslifGGFASke 205
Cdd:cd17655 12 DHTAVVFED------QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAG-------GAYLP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 lssrIDHAKPKvvvtasfgiepgRKVEYMpiLEE---AMRIGQHKpdkvLIYNRPNMETVPLasgrdLDWDEEMAKAQSQ 282
Cdd:cd17655 77 ----IDPDYPE------------ERIQYI--LEDsgaDILLTQSH----LQPPIAFIGLIDL-----LDEDTIYHEESEN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 283 DCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYglkPGEvwwaASDLGWVVGHSY------IcYGPLI 356
Cdd:cd17655 130 LEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIY---QGE----HLRVALFASISFdasvteI-FASLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 357 HGNTTVLYEGKPVGtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqysltRFKTLFVAGERCDVETLEWSK 436
Cdd:cd17655 202 SGNTLYIVRKETVL--DGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGL-------SLKHLIVGGEALSTELAKKII 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 437 KVFR--VPVLDHWWQTETgsPITAS---CIGLGNSKTPPPgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGA 511
Cdd:cd17655 273 ELFGtnPTITNAYGPTET--TVDASiyqYEPETDQQVSVP--IGKPLGNTRIYILDQYGRPQPVGVAGELYIG---GEGV 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882765 512 FSGLWKNQEafkhLYFEKF------PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17655 346 ARGYLNRPE----LTAEKFvddpfvPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIE 409
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
143-571 |
3.79e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.52 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 143 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTas 222
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS-- 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 fgiepgrkveympilEEAMRIGQHKPDKVLiynrpnmetvplasgrDLDWDEEMAKAQSQDcVPVLSEHPLYILYTSGTT 302
Cdd:PRK12316 3161 ---------------QSHLRLPLAQGVQVL----------------DLDRGDENYAEANPA-IRTMPENLAYVIYTSGST 3208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 303 GLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLyeGKPVGTPDAGAYFRVLA 382
Cdd:PRK12316 3209 GKPKGVGIRHSALSNHLCW-MQQAYGLGVGDRVLQFTTFSFDVFVEEL-FWPLMSGARVVL--AGPEDWRDPALLVELIN 3284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 383 EHGVAALFTAPTAIRAIrQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEwsKKVFRVPVLDHWWQTETGSPITASCIG 462
Cdd:PRK12316 3285 SEGVDVLHAYPSMLQAF-LEEEDAH-----RCTSLKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCV 3356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 463 LGNSKTPPpgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVK-LPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGY 541
Cdd:PRK12316 3357 EEGKDAVP---IGRPIANRACYILDGSLEPVPVGALGELYLGgEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLAR 3433
|
410 420 430
....*....|....*....|....*....|
gi 1191882765 542 MDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK12316 3434 YRADGVIEYIGRVDHQVKIRGFRIELGEIE 3463
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
125-309 |
6.85e-11 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 65.00 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 125 GDKVAIIyDSPvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:PLN02246 37 SDRPCLI-DGA---TGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVTASFGIEPGRKVEYMPILeEAMRIGQHkPDKVLIYNrpnmetvplasgrdldwdeEMAKAQSQDC 284
Cdd:PLN02246 113 EIAKQAKASGAKLIITQSCYVDKLKGLAEDDGV-TVVTIDDP-PEGCLHFS-------------------ELTQADENEL 171
|
170 180
....*....|....*....|....*...
gi 1191882765 285 vPVLSEHP---LYILYTSGTTGLPKGVV 309
Cdd:PLN02246 172 -PEVEISPddvVALPYSSGTTGLPKGVM 198
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
144-571 |
7.20e-11 |
|
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: 64.80 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAsf 223
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 224 giepgrKVEYMPileeAMRIGQhkPDKVLIYNRPnmetvPLASGRDLD-WDEEMAKAQ-SQDCVPVLSEHPLYILYTSGT 301
Cdd:cd05932 86 ------KLDDWK----AMAPGV--PEGLISISLP-----PPSAANCQYqWDDLIAQHPpLEERPTRFPEQLATLIYTSGT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 302 TGLPKGVVRPTGGYAvmlnWTMSSI---YGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYE-----------GK 367
Cdd:cd05932 149 TGQPKGVMLTFGSFA----WAAQAGiehIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAEsldtfvedvqrAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 368 P---VGTPDAGAYF--RVLAEHGVAA---LFTAPTAIRAIRQQdpgaaLGKQYSLTRFKTLFVAGERCDVETLEWSKKVf 439
Cdd:cd05932 225 PtlfFSVPRLWTKFqqGVQDKIPQQKlnlLLKIPVVNSLVKRK-----VLKGLGLDQCRLAGCGSAPVPPALLEWYRSL- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 440 RVPVLDHWWQTETG--SPITASciglGNSKTpppGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWK 517
Cdd:cd05932 299 GLNILEAYGMTENFaySHLNYP----GRDKI---GTVGNAGPGVEVRISED----------GEILVR---SPALMMGYYK 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 518 NQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVA-GHRISAGAIE 571
Cdd:cd05932 359 DPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIE 411
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
287-571 |
8.09e-11 |
|
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: 64.31 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 287 VLSEHP---LYILYTSGTTGLPKGVVRPTGGYAVMLNWTMsSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVL 363
Cdd:cd17649 88 LLTHHPrqlAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA-ERYGLTPGDRELQFASFNFDGAHEQL-LPPLICGACVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 364 YEGKPVGTPDagAYFRVLAEHGVAALFTAPT-------AIRAIRQQDPGAalgkqysltrFKTLFVAGERCDVETLeWSK 436
Cdd:cd17649 166 RPDELWASAD--ELAEMVRELGVTVLDLPPAylqqlaeEADRTGDGRPPS----------LRLYIFGGEALSPELL-RRW 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 437 KVFRVPVLDHWWQTETGSPITASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW 516
Cdd:cd17649 233 LKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADLN--------------PVPVGVTGELY 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 517 KNQEAFKHLYF-------EKF-------PG--YYDTMD-AGYMDeEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17649 299 IGGEGLARGYLgrpeltaERFvpdpfgaPGsrLYRTGDlARWRD-DGVIEYLGRVDHQVKIRGFRIELGEIE 369
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
141-553 |
8.83e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 64.40 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 141 ATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVvt 220
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 221 asfgiepgrkveympileeamrIGqhkpdkvliynrpnmetVPLAsgrdldwDEEMAkaqsqdcvpvlsehplyILYTSG 300
Cdd:cd05910 79 ----------------------IG-----------------IPKA-------DEPAA-----------------ILFTSG 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 301 TTGLPKGVVRPTGGYAVMLNwTMSSIYGLKPGEVWWAASDLgwvvghsYICYGPLIhGNTTVLYEGKPV--GTPDAGAYF 378
Cdd:cd05910 96 STGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGPAL-GLTSVIPDMDPTrpARADPQKLV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 379 RVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQysLTRFKTLFVAGERCDVETLEWSKKVF--RVPVLDHWWQTETgSPI 456
Cdd:cd05910 167 GAIRQYGVSIVFGSPALLERVARY--CAQHGIT--LPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEA-LPV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 457 TAscIG---LGNSKTPPPGQA-----GKSVPGYNVMILD---------DNMQKLKARCLGNIVVKLPL---------PPG 510
Cdd:cd05910 242 SS--IGsreLLATTTAATSGGagtcvGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTvtptyvnrpVAT 319
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1191882765 511 AFSGLWKNQEAFKHlyfekfpgyyDTMDAGYMDEEGYVYVMSR 553
Cdd:cd05910 320 ALAKIDDNSEGFWH----------RMGDLGYLDDEGRLWFCGR 352
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
143-571 |
9.14e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 65.18 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 143 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaskelssridhakpkvvvtAS 222
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAY--------------------------VP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 FGIE-PGRKVEYMPileEAMRIGqhkpdkVLIYNRPNMETVPLASG-RDLDWDEEMAKAQSQDCV-PVLSEHP---LYIL 296
Cdd:PRK12467 1654 LDPEyPRERLAYMI---EDSGIE------LLLTQSHLQARLPLPDGlRSLVLDQEDDWLEGYSDSnPAVNLAPqnlAYVI 1724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 297 YTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLyeGKPVGTPDAGA 376
Cdd:PRK12467 1725 YTSGSTGRPKGAGNRHGALVNRLCA-TQEAYQLSAADVVLQFTSFAFDVSVWEL-FWPLINGARLVI--APPGAHRDPEQ 1800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 377 YFRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRfktLFVAGERCDVETLE-WSKKVFRVPVLDHWWQTETGSP 455
Cdd:PRK12467 1801 LIQLIERQQVTTLHFVPSMLQQLLQMDE--QVEHPLSLRR---VVCGGEALEVEALRpWLERLPDTGLFNLYGPTETAVD 1875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 456 ITASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplppGAfsGLWKNQEAFKHLYFEKF----- 530
Cdd:PRK12467 1876 VTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLG-----GV--GLARGYLNRPALTAERFvadpf 1948
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1191882765 531 --PG--YYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK12467 1949 gtVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
126-424 |
1.84e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 63.38 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIY----DSPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGD-TVVIYMPMIPqaMYT-MLACARIGAIHSLIFG 199
Cdd:PRK09274 21 DQLAVAVpggrGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMrAVLMVTPSLE--FFAlTFALFKAGAVPVLVDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 200 GFASKELSSRIDHAKPKVVVtasfGIepgrkveymPILEEAMRI-GQHKPD-KVLIynrpNMETVPLASGRDLDWDEEMA 277
Cdd:PRK09274 99 GMGIKNLKQCLAEAQPDAFI----GI---------PKAHLARRLfGWGKPSvRRLV----TVGGRLLWGGTTLATLLRDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 278 KAQSQDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNwTMSSIYGLKPGEVwwaasDLgwvvgHSYicygPLIH 357
Cdd:PRK09274 162 AAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIE-ALREDYGIEPGEI-----DL-----PTF----PLFA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882765 358 ------GNTTVLYE---GKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAG 424
Cdd:PRK09274 227 lfgpalGMTSVIPDmdpTRP-ATVDPAKLFAAIERYGVTNLFGSPALLERLGR----YGEANGIKLPSLRRVISAG 297
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
133-573 |
3.16e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 62.88 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 133 DSPVT----DTKATITYKEVLEQVSRLAGVLVKH-GVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELS 207
Cdd:PRK05620 25 DTTVTtwggAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 208 SRIDHAKPKVVVT-ASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLAS---GR--DLDWdeemakaqs 281
Cdd:PRK05620 105 HIINHAEDEVIVAdPRLAEQLGEILKECPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEAlldGRstVYDW--------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 282 qdcvPVLSEH-PLYILYTSGTTGLPKGVVrptggYAVMLNWTMSsiYGLKpgevwwAASDLGWVVGHSYICYGPLIHgnt 360
Cdd:PRK05620 176 ----PELDETtAAAICYSTGTTGAPKGVV-----YSHRSLYLQS--LSLR------TTDSLAVTHGESFLCCVPIYH--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 361 tVLYEGKPVGTPDAGAYFrVLAEHGVaalfTAPTAIRAIRQQDPGAALG-----------------KQYSLTrfkTLFVA 423
Cdd:PRK05620 236 -VLSWGVPLAAFMSGTPL-VFPGPDL----SAPTLAKIIATAMPRVAHGvptlwiqlmvhylknppERMSLQ---EIYVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 424 GERCDVETLE-WSKKvFRVPVLDHWWQTETgSPItasciglGNSKTPPPGQAGKSVPGYNV------------MILDDNM 490
Cdd:PRK05620 307 GSAVPPILIKaWEER-YGVDVVHVWGMTET-SPV-------GTVARPPSGVSGEARWAYRVsqgrfpasleyrIVNDGQV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 491 QKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYF---------EKFP--GYYDTMDAGYMDEEGYVYVMSRVDDVIN 559
Cdd:PRK05620 378 MESTDRNEGEIQVRGNWVTASYYHSPTEEGGGAASTFrgedvedanDRFTadGWLRTGDVGSVTRDGFLTIHDRARDVIR 457
|
490
....*....|....
gi 1191882765 560 VAGHRISAGAIEEE 573
Cdd:PRK05620 458 SGGEWIYSAQLENY 471
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
142-571 |
5.13e-10 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 61.91 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAK------- 214
Cdd:cd05906 39 FQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLRhiwqllg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 215 -PKVVVTasfgiePGRKVEYMPILEEAmrigQHKPDKVLIynrpnMETVpLASGRDLDWdeemakaqsqdcVPVLSEHPL 293
Cdd:cd05906 119 sPVVLTD------AELVAEFAGLETLS----GLPGIRVLS-----IEEL-LDTAADHDL------------PQSRPDDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 294 YILYTSGTTGLPKGVVRPTGGYAVMLNWTMsSIYGLKPGEVWwaasdLGWVvghsyicygPLIHGNTTVLYEGKPVgtpD 373
Cdd:cd05906 171 LLMLTSGSTGFPKAVPLTHRNILARSAGKI-QHNGLTPQDVF-----LNWV---------PLDHVGGLVELHLRAV---Y 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 374 AGA----------------YFRVLAEHGVAALFtAPT-AIRAIRQQDPGAAlGKQYSLTRFKTLFVAGERCDVET----L 432
Cdd:cd05906 233 LGCqqvhvpteeiladplrWLDLIDRYRVTITW-APNfAFALLNDLLEEIE-DGTWDLSSLRYLVNAGEAVVAKTirrlL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 433 EWSKK------VFRvPVldhWWQTETGSPIT--ASCIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVK 504
Cdd:cd05906 311 RLLEPyglppdAIR-PA---FGMTETCSGVIysRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVR 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 505 LPLppgAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDeEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05906 387 GPV---VTKGYYNNPEANAEAFTED--GWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIE 447
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
126-571 |
5.69e-10 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 61.92 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSpvtdTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PLN02330 43 DKVAFVEAV----TGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTASFGIEPGRKVEyMPILEeamrIGQHKpdkvlIYNRPNMETVPLASGRDLDWDEEMAKAQSQDCV 285
Cdd:PLN02330 119 IKKQAEAAGAKLIVTNDTNYGKVKGLG-LPVIV----LGEEK-----IEGAVNWKELLEAADRAGDTSDNEEILQTDLCA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 286 pvlsehplyILYTSGTTGLPKGVVRPTGGYAVMLnwtMSSIYGLKPgEVWWAASDLGWV-VGHSY----ICYGPLIHGNT 360
Cdd:PLN02330 189 ---------LPFSSGTTGISKGVMLTHRNLVANL---CSSLFSVGP-EMIGQVVTLGLIpFFHIYgitgICCATLRNKGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 361 TVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPgaaLGKQYSLTRFK--TLFVAGERCDVETL-EWSKK 437
Cdd:PLN02330 256 VVV-----MSRFELRTFLNALITQEVSFAPIVPPIILNL-VKNP---IVEEFDLSKLKlqAIMTAAAPLAPELLtAFEAK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 438 VFRVPVLDHWWQTEtgspitASCIGLGNSKtPPPGQA-------GKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPP 509
Cdd:PLN02330 327 FPGVQVQEAYGLTE------HSCITLTHGD-PEKGHGiakknsvGFILPNLEVKFIDpDTGRSLPKNTPGELCVR---SQ 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 510 GAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PLN02330 397 CVMQGYYNNKEETDRTIDED--GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELE 456
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
126-393 |
7.53e-10 |
|
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: 61.52 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSPvtdtkaTITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 205
Cdd:cd12114 2 DATAVICGDG------TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAY----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 lssridhakpkvvVTASFGIEPGRKVEympILEEAMR---IGQHKPDKVLIynRPNMETVPLASGRDLDWDEEMAKAQSQ 282
Cdd:cd12114 65 -------------VPVDIDQPAARREA---ILADAGArlvLTDGPDAQLDV--AVFDVLILDLDALAAPAPPPPVDVAPD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 283 DcvpvlsehPLYILYTSGTTGLPKGVVRPTGGyavMLNwTMSSI---YGLKPGEVWWAASDLGW---VvghsYICYGPLI 356
Cdd:cd12114 127 D--------LAYVIFTSGSTGTPKGVMISHRA---ALN-TILDInrrFAVGPDDRVLALSSLSFdlsV----YDIFGALS 190
|
250 260 270
....*....|....*....|....*....|....*..
gi 1191882765 357 HGNTTVLYEGKPVGTPDAGAyfRVLAEHGVAALFTAP 393
Cdd:cd12114 191 AGATLVLPDEARRRDPAHWA--ELIERHGVTLWNSVP 225
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
269-571 |
7.65e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 61.58 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 269 DLDWDEEMAKAQsqDCVP---VLSEHPLYILYTSGTTGLPKGVvRPTGGYAVMLNWTMSSIYGLKPGEVwwaasdlgwvv 345
Cdd:PRK13388 128 TPAYAELVAAAG--ALTPhreVDAMDPFMLIFTSGTTGAPKAV-RCSHGRLAFAGRALTERFGLTRDDV----------- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 346 ghSYICYgPLIHGNTTV------LYEGKPVGTPDAGAYFRVLA---EHGvAALFT----APTAIRAIRQQDPGAalgkQY 412
Cdd:PRK13388 194 --CYVSM-PLFHSNAVMagwapaVASGAAVALPAKFSASGFLDdvrRYG-ATYFNyvgkPLAYILATPERPDDA----DN 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 413 SLTR-FKTlfVAGERcDVEtlEWSKKvFRVPVLDHWWQTETGSPITASciglgnsKTPPPGQAGKSVPGynVMILDDNMQ 491
Cdd:PRK13388 266 PLRVaFGN--EASPR-DIA--EFSRR-FGCQVEDGYGSSEGAVIVVRE-------PGTPPGSIGRGAPG--VAIYNPETL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 492 KLKARC--------------LGNIVVKLPlpPGAFSGLWKNQEA----FKHlyfekfpGYYDTMDAGYMDEEGYVYVMSR 553
Cdd:PRK13388 331 TECAVArfdahgallnadeaIGELVNTAG--AGFFEGYYNNPEAtaerMRH-------GMYWSGDLAYRDADGWIYFAGR 401
|
330
....*....|....*...
gi 1191882765 554 VDDVINVAGHRISAGAIE 571
Cdd:PRK13388 402 TADWMRVDGENLSAAPIE 419
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
126-562 |
5.06e-09 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 59.00 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK13382 58 DRPGLI------DELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRigqHKPDKVLIYNRPNMETVPLAsgrdldwdEEMAKAQSQDCV 285
Cdd:PRK13382 132 LAEVVTREGVDTVIYDE---------EFSATVDRALA---DCPQATRIVAWTDEDHDLTV--------EVLIAAHAGQRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 286 PVLSEHPLYILYTSGTTGLPKGVVRP-TGGYAvmlnwTMSSIYGLKPgevwWAASDLGWVVghsyicyGPLIH--GNTTV 362
Cdd:PRK13382 192 EPTGRKGRVILLTSGTTGTPKGARRSgPGGIG-----TLKAILDRTP----WRAEEPTVIV-------APMFHawGFSQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 363 LYEGKPVGTP------DAGAYFRVLAEHGVAALFTAPTAIRaiRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSK 436
Cdd:PRK13382 256 VLAASLACTIvtrrrfDPEATLDLIDRHRATGLAVVPVMFD--RIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 437 KVFRVPVLDHWWQTETGSPITAsciglgnskTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVK-LPLPPG 510
Cdd:PRK13382 334 DQFGDVIYNNYNATEAGMIATA---------TPAdlraaPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRnDTQFDG 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 511 AFSGLWKNQEAfkhlyfekfpGYYDTMDAGYMDEEGYVYVMSRVDDVInVAG 562
Cdd:PRK13382 405 YTSGSTKDFHD----------GFMASGDVGYLDENGRLFVVGRDDEMI-VSG 445
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
205-571 |
6.79e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 58.54 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 ELSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAmrigqhkpdkvliynRPNMETVPLASgrdLDWDEEMAKAQSQDC 284
Cdd:PRK07867 92 ALARDIAHADCQLVLTES---------AHAELLDGL---------------DPGVRVINVDS---PAWADELAAHRDAEP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 285 VP--VLSEHPLYILYTSGTTGLPKGVvRPTGGYAVMLNWTMSSIYGLKPGEVwwaasdlgwvvghSYICYgPLIHGNTTV 362
Cdd:PRK07867 145 PFrvADPDDLFMLIFTSGTSGDPKAV-RCTHRKVASAGVMLAQRFGLGPDDV-------------CYVSM-PLFHSNAVM 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 363 lyegkpvgtpdaGAYFRVLAEHGVAAL---FTAPTAIRAIRQQdpGAA----LGK--QYSLT-------RFKTLFVA--- 423
Cdd:PRK07867 210 ------------AGWAVALAAGASIALrrkFSASGFLPDVRRY--GATyanyVGKplSYVLAtperpddADNPLRIVygn 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 424 -GERCDVETLEwskKVFRVPVLDHWWQTETGSPITasciglgnsKTP--PPGQAGKSVPGYNVM-----------ILDDN 489
Cdd:PRK07867 276 eGAPGDIARFA---RRFGCVVVDGFGSTEGGVAIT---------RTPdtPPGALGPLPPGVAIVdpdtgtecppaEDADG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 490 MQKLKARCLGNIVVklPLPPGAFSGLWKNQEAFKhlyfEKF-PGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAG 568
Cdd:PRK07867 344 RLLNADEAIGELVN--TAGPGGFEGYYNDPEADA----ERMrGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTA 417
|
...
gi 1191882765 569 AIE 571
Cdd:PRK07867 418 PIE 420
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
294-571 |
1.02e-08 |
|
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: 57.80 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 294 YILYTSGTTGLPKGVVRPTGGyAVMLNWTMSSIYGLKPGEVWWAASDLGWVVGHSY--ICYGpLIHGNTTVLYEGKPVGT 371
Cdd:cd17648 98 YAIYTSGTTGKPKGVLVEHGS-VVNLRTSLSERYFGRDNGDEAVLFFSNYVFDFFVeqMTLA-LLNGQKLVVPPDEMRFD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 372 PDagAYFRVLAEHGVAALFTAPTAIRAIRqqdpgaaLGKQYSLTRfktLFVAGERCDVETLEWSKKVFRVPVLDHWWQTE 451
Cdd:cd17648 176 PD--RFYAYINREKVTYLSGTPSVLQQYD-------LARLPHLKR---VDAAGEEFTAPVFEKLRSRFAGLIINAYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 452 TGspITasciglgNSKTPPPGQA------GKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGL---------- 515
Cdd:cd17648 244 TT--VT-------NHKRFFPGDQrfdkslGRPVRNTKCYVLNDAMK--------------RVPVGAVGELylggdgvarg 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 516 WKNQEAfkhLYFEKF----------------PGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17648 301 YLNRPE---LTAERFlpnpfqteqerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVE 369
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
142-540 |
2.31e-08 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 56.67 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVI-------YMPMIPQAMYTMLACARIGAIHSLIFGGFAskELSSRIDHAK 214
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLIlsgnsieHALMALAAMYAGVPAAPVSPAYSLMSQDLA--KLKHLFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 215 PKVVVTASFGIEPGRKVEYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLAsgrdlDWDEEMAKAQSqDCVPVLsehply 294
Cdd:cd05921 103 PGLVFAQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTA-----AVDAAFAAVGP-DTVAKF------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 295 iLYTSGTTGLPKGVV---RPTGGYAVMLNWTMSSIYGLKPGEVWWAAsdlgWvvGHSY---ICYGPLIH-GNTTVLYEGK 367
Cdd:cd05921 171 -LFTSGSTGLPKAVIntqRMLCANQAMLEQTYPFFGEEPPVLVDWLP----W--NHTFggnHNFNLVLYnGGTLYIDDGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 368 PvgTPDA-GAYFRVLAEHGVAALFTAPTA----IRAIRQQDpgaALGKQYsLTRFKTLFVAGERCD------VETLEWSK 436
Cdd:cd05921 244 P--MPGGfEETLRNLREISPTVYFNVPAGwemlVAALEKDE---ALRRRF-FKRLKLMFYAGAGLSqdvwdrLQALAVAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 437 KVFRVPVLDHWWQTETGsPITASCIGL----GNSKTPPPGQAGKSVPgynvmilddNMQKLKARCLGnivvklplpPGAF 512
Cdd:cd05921 318 VGERIPMMAGLGATETA-PTATFTHWPtersGLIGLPAPGTELKLVP---------SGGKYEVRVKG---------PNVT 378
|
410 420
....*....|....*....|....*...
gi 1191882765 513 SGLWKNQEAFKHLYFEKfpGYYDTMDAG 540
Cdd:cd05921 379 PGYWRQPELTAQAFDEE--GFYCLGDAA 404
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
126-571 |
3.18e-08 |
|
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: 56.29 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSPvTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:cd05915 9 GRKEVVSRLH-TGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTASfgiepgrkvEYMPILEEAMRIgqhkpdkvliynRPNMETVPLASGRDLDWDEEMAKAQS--QD 283
Cdd:cd05915 88 IAYILNHAEDKVLLFDP---------NLLPLVEAIRGE------------LKTVQHFVVMDEKAPEGYLAYEEALGeeAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 284 CVPVLSEHPLYILYTSGTTGLPKGVVRPTGGyaVMLNWTMSSI---YGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNT 360
Cdd:cd05915 147 PVRVPERAACGMAYTTGTTGLPKGVVYSHRA--LVLHSLAASLvdgTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 361 TVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIrqQDPGAALGKQYSLTrfkTLFVAGERCDVETLEWSKKVFR 440
Cdd:cd05915 225 VLPGP-----RLDPASLVELFDGEGVTFTAGVPTVWLAL--ADYLESTGHRLKTL---RRLVVGGSAAPRSLIARFERMG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 441 VPVLDHWWQTETGSPITAsCIGLGNSKTPPPGQA--GKSVPGYN-----VMILDDNMQKLKARclGNIVVKLPLPPGA-F 512
Cdd:cd05915 295 VEVRQGYGLTETSPVVVQ-NFVKSHLESLSEEEKltLKAKTGLPiplvrLRVADEEGRPVPKD--GKALGEVQLKGPWiT 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882765 513 SGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05915 372 GGYYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLE 428
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
141-363 |
4.20e-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: 55.82 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 141 ATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVt 220
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 221 asfgiepgrkveympileeamrigqhkpdkvliynrpnmetVPLAsgrdldwdeemakaqsqdcvpvlsehpLYIlYTSG 300
Cdd:cd05940 81 -----------------------------------------VDAA---------------------------LYI-YTSG 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191882765 301 TTGLPKGVVRPTGGYAVMLNWTMSSiYGLKPGEVWW--------AASDLGWVVGhsyicygpLIHGNTTVL 363
Cdd:cd05940 92 TTGLPKAAIISHRRAWRGGAFFAGS-GGALPSDVLYtclplyhsTALIVGWSAC--------LASGATLVI 153
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
126-571 |
4.64e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 55.56 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSPVtdtkatITYKEVLEQVSRLAGVLvKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK07638 16 NKIAIKENDRV------LTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTASFGIEpgrkveymPILEEAMRIgqhkpdkvliynrpnmetvplasgrdLDWDE--EMAKAQSQD 283
Cdd:PRK07638 89 LKERLAISNADMIVTERYKLN--------DLPDEEGRV--------------------------IEIDEwkRMIEKYLPT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 284 CVPV--LSEHPLYILYTSGTTGLPKGVVRptggyaVMLNWTMS-----SIYGLKPGEVWWAASDLgwvvGHSYICYGPL- 355
Cdd:PRK07638 135 YAPIenVQNAPFYMGFTSGSTGKPKAFLR------AQQSWLHSfdcnvHDFHMKREDSVLIAGTL----VHSLFLYGAIs 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 356 -IHGNTTVLYEGK--PVGTPDAgayfrvLAEHGVAALFTAPTAIRAIrqqdpgaalgkqYSLTRFK----TLFVAGERCD 428
Cdd:PRK07638 205 tLYVGQTVHLMRKfiPNQVLDK------LETENISVMYTVPTMLESL------------YKENRVIenkmKIISSGAKWE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 429 VETLEWSKKVFRVPVLDHWWQTETGSPITAScigLGNSKTPPPGQAGKsvPGYNVMILDDNM--QKLKARCLGNIVVKLP 506
Cdd:PRK07638 267 AEAKEKIKNIFPYAKLYEFYGASELSFVTAL---VDEESERRPNSVGR--PFHNVQVRICNEagEEVQKGEIGTVYVKSP 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191882765 507 LppgAFSGlWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK07638 342 Q---FFMG-YIIGGVLARELNAD--GWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIE 400
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
295-573 |
4.97e-08 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 56.09 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 295 ILYTSGTTGLPKGVVrpTGGYAVMLNW-TMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVlYEGKPVgtpD 373
Cdd:PRK08633 787 IIFSSGSEGEPKGVM--LSHHNILSNIeQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVV-YHPDPT---D 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 374 AGAYFRVLAEHGVAALFTAPTAIRA-IRQQ--DPgaalgkqyslTRFKTL--FVAG-ERCDVETLEWSKKVFRVPVLDHW 447
Cdd:PRK08633 861 ALGIAKLVAKHRATILLGTPTFLRLyLRNKklHP----------LMFASLrlVVAGaEKLKPEVADAFEEKFGIRILEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 448 WQTETGSPITASC-----------IGlgnSKtppPGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGL 515
Cdd:PRK08633 931 GATETSPVASVNLpdvlaadfkrqTG---SK---EGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG---GPQVMKGY 1001
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 516 WKNQ----EAFKHLyfeKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEEE 573
Cdd:PRK08633 1002 LGDPektaEVIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEE 1060
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
290-571 |
6.51e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 55.38 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 290 EHPLYILYTSGTTGLPKGVVRPTGGYAVMLNwtmssiyGLkpGEVW-WAASDL-----------GWVVGhsyiCYGPLIH 357
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSRRAIAADLD-------AL--AEAWqWTADDVlvhglplfhvhGLVLG----VLGPLRI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 358 GNtTVLYEGKPvgTPDagAYFRVLAEHGvAALFTAPTAIRAIrQQDPGAAlgKQYSLTRfktLFVAGE----RCDVETLE 433
Cdd:PRK07787 195 GN-RFVHTGRP--TPE--AYAQALSEGG-TLYFGVPTVWSRI-AADPEAA--RALRGAR---LLVSGSaalpVPVFDRLA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 434 wskKVFRVPVLDHWWQTETgsPITASCIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKA--RCLGNIVVKlplPPGA 511
Cdd:PRK07787 263 ---ALTGHRPVERYGMTET--LITLSTRADGERR---PGWVGLPLAGVETRLVDEDGGPVPHdgETVGELQVR---GPTL 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191882765 512 FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVD-DVINVAGHRISAGAIE 571
Cdd:PRK07787 332 FDGYLNRPDATAAAFTAD--GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIE 390
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
134-571 |
6.55e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 55.39 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 134 SPVTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHA 213
Cdd:PRK13383 52 TAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 214 KPKVVVTASfgiepgrkveympilEEAMRIGQhKPDKVLIYnrpnmetvplasgrdldwDEEMAKAQSQDCVPVLSEHPL 293
Cdd:PRK13383 132 HISTVVADN---------------EFAERIAG-ADDAVAVI------------------DPATAGAEESGGRPAVAAPGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 294 YILYTSGTTGLPKGVVR-PTGGYAVMLNWTMSSIYGLKPGEVWWAASdlgwvvghsyicygPLIHGN-----TTVLYEGK 367
Cdd:PRK13383 178 IVLLTSGTTGKPKGVPRaPQLRSAVGVWVTILDRTRLRTGSRISVAM--------------PMFHGLglgmlMLTIALGG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 368 PVGTP---DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLFVAGERCDVETLEWSKKVFRVPVL 444
Cdd:PRK13383 244 TVLTHrhfDAEAALAQASLHRADAFTAVPVVLARILELPP--RVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 445 DHWWQTEtgspitascIGLGNSKTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGlwKNQ 519
Cdd:PRK13383 322 NGYGSTE---------VGIGALATPAdlrdaPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD--GGG 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 520 EAFkhlyfekFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK13383 391 KAV-------VDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVE 435
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
136-571 |
6.70e-08 |
|
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: 55.17 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 136 VTDTKATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKP 215
Cdd:cd17650 6 VSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 216 KVVVTasfgiEPgrkveympileeamrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqdcvpvlsEHPLYI 295
Cdd:cd17650 86 KLLLT-----QP--------------------------------------------------------------EDLAYV 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 296 LYTSGTTGLPKGVVRPTGGYAVM-LNWtmSSIYGL--KPGEVWWAASdLGWVVGHSYICYGpLIHGNTTVLYegkPVGTP 372
Cdd:cd17650 99 IYTSGTTGKPKGVMVEHRNVAHAaHAW--RREYELdsFPVRLLQMAS-FSFDVFAGDFARS-LLNGGTLVIC---PDEVK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 373 -DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF--RVPVLDHWWQ 449
Cdd:cd17650 172 lDPAALYDLILKSRITLMESTPALIRPVMAY----VYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFgqGMRIINSYGV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 450 TET---GSPITASCIGLGNSKTPPpgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW---------- 516
Cdd:cd17650 248 TEAtidSTYYEEGRDPLGDSANVP---IGRPLPNTAMYVLDERLQ--------------PQPVGVAGELYiggagvargy 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 517 -----KNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17650 311 lnrpeLTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIE 370
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
436-572 |
1.14e-07 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 54.50 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 436 KKVFRVPVLDHWWQTETgSPitASCIglgNSKTPPP--GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFS 513
Cdd:PRK08751 350 KQVTGLTLVEAYGLTET-SP--AACI---NPLTLKEynGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK---GPQVMK 420
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1191882765 514 GLWKNQEAFKHLYfeKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK08751 421 GYWKRPEETAKVM--DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIED 477
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
144-571 |
1.19e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 54.47 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPqAMY-TMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAS 222
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIP-AMYeAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 223 fgiepgrkvEYMPILEEAMRI------GQHKPDKVLIYNRPNMETVPL--ASGRDL--------DWDEEMAKAQSQDcvp 286
Cdd:PLN02479 126 ---------EFFTLAEEALKIlaekkkSSFKPPLLIVIGDPTCDPKSLqyALGKGAieyekfleTGDPEFAWKPPAD--- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 287 vlSEHPLYILYTSGTTGLPKGVV-RPTGGYAVMLNWTMssIYGLKPGEVWWaasdlgWVVghsyicygPLIHGN------ 359
Cdd:PLN02479 194 --EWQSIALGYTSGTTASPKGVVlHHRGAYLMALSNAL--IWGMNEGAVYL------WTL--------PMFHCNgwcftw 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 360 TTVLYEGKPV--GTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqYSLTRFKTLFVAGERCDVETL-EWSK 436
Cdd:PLN02479 256 TLAALCGTNIclRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETI---LPLPRVVHVMTAGAAPPPSVLfAMSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 437 KVFRVPvldHWWQ-TETGSPITASCIGLGNSKTPPPGQA------GKSVPGYNVMILDD--NMQKLKA--RCLGNIVVKl 505
Cdd:PLN02479 333 KGFRVT---HTYGlSETYGPSTVCAWKPEWDSLPPEEQArlnarqGVRYIGLEGLDVVDtkTMKPVPAdgKTMGEIVMR- 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 506 plPPGAFSGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PLN02479 409 --GNMVMKGYLKNPKANE----EAFAnGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVE 469
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
143-357 |
2.69e-07 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 53.37 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 143 ITYKEVLEQVSRLAGVLVKHGV--SKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVt 220
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 221 asfgIEPGRKVEympILEEAMRIGqhkpdkvliynRPNMETVPLASGRDLdwdeemakaqsqdCVpvlsehplyILYTSG 300
Cdd:cd05927 85 ----CDAGVKVY---SLEEFEKLG-----------KKNKVPPPPPKPEDL-------------AT---------ICYTSG 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 301 TTGLPKGVVRPTGGYA---VMLNWTMSSIYGLKPGEVwwaasdlgwvvghsYICYGPLIH 357
Cdd:cd05927 125 TTGNPKGVMLTHGNIVsnvAGVFKILEILNKINPTDV--------------YISYLPLAH 170
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
142-357 |
2.81e-07 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 53.37 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhakpkVVVTA 221
Cdd:cd17639 5 YMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNI------------------------PIVTV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 222 sfgiepgrkveYMPILEEAMRIGQHKPDKVLIYNRPNMETVPLasgrdldwdeemakaqsqdcvpvlsehplyILYTSGT 301
Cdd:cd17639 61 -----------YATLGEDALIHSLNETECSAIFTDGKPDDLAC------------------------------IMYTSGS 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 302 TGLPKGVvrptggyaVMLNWTM-SSIYGLKPGEVWWAASDlgwvvgHSYICYGPLIH 357
Cdd:cd17639 100 TGNPKGV--------MLTHGNLvAGIAGLGDRVPELLGPD------DRYLAYLPLAH 142
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
141-309 |
3.28e-07 |
|
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: 53.23 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 141 ATITYKEVLEQVSRLAGVL-VKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVv 219
Cdd:cd17632 66 ETITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 220 TASfgiepgrkVEYMPILEEAMRIGQHKPDKVLIYNRPNMET--VPLASGR-------------DLDWDEEMAKAQSQDC 284
Cdd:cd17632 145 AVS--------AEHLDLAVEAVLEGGTPPRLVVFDHRPEVDAhrAALESARerlaavgipvttlTLIAVRGRDLPPAPLF 216
|
170 180
....*....|....*....|....*.
gi 1191882765 285 VPVLSEHPLYIL-YTSGTTGLPKGVV 309
Cdd:cd17632 217 RPEPDDDPLALLiYTSGSTGTPKGAM 242
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
133-308 |
3.41e-07 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 52.98 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 133 DSPVTDTK-ATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIG------AIHSlifggfASKE 205
Cdd:PRK04813 17 DFPAYDYLgEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayipvDVSS------PAER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTasfgiepgrkVEYMPILEEAMRIgqHKPDKVliynrpnmetvplasgrdldwdEEMAKAQsqdcV 285
Cdd:PRK04813 91 IEMIIEVAKPSLIIA----------TEELPLEILGIPV--ITLDEL----------------------KDIFATG----N 132
|
170 180
....*....|....*....|....*....
gi 1191882765 286 PVLSEHPL------YILYTSGTTGLPKGV 308
Cdd:PRK04813 133 PYDFDHAVkgddnyYIIFTSGTTGKPKGV 161
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
142-572 |
3.49e-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: 52.82 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVK-HGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKEL--SSRIDHAKpKVV 218
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLihCLKLSGSR-FVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 219 VTasfgiepgrkveympileeamrigqhkPDKVLIynrpnmetvplasgrdldwdeemakaqsqdcvpvlsehplyILYT 298
Cdd:cd05937 84 VD---------------------------PDDPAI-----------------------------------------LIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 299 SGTTGLPKGVVRPTGGYAVMlNWTMSSIYGLKPGEVWWAASDLGWVVGHSYICYGPLIHGNTTVLYEGKPVGT-----PD 373
Cdd:cd05937 96 SGTTGLPKAAAISWRRTLVT-SNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQfwkdvRD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 374 AGAYFRVLAEHGVAALFTAPTAIRAiRQQDPGAALGKqysltrfktlfvaGERCDVetleWSK--KVFRVPVLDHWWQTE 451
Cdd:cd05937 175 SGATIIQYVGELCRYLLSTPPSPYD-RDHKVRVAWGN-------------GLRPDI----WERfrERFNVPEIGEFYAAT 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 452 TG---------SPITASCIG---------LGNSKTP----PPGQagksvpgynvMILDDNMQKLKARCL----GNIVVKL 505
Cdd:cd05937 237 EGvfaltnhnvGDFGAGAIGhhglirrwkFENQVVLvkmdPETD----------DPIRDPKTGFCVRAPvgepGEMLGRV 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191882765 506 PLPP-GAFSGLWKNQEAFKHLY----FEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:cd05937 307 PFKNrEAFQGYLHNEDATESKLvrdvFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVAD 378
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
447-553 |
3.98e-07 |
|
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: 52.27 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 447 WW----QTETGSPITascIGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWKNQEAF 522
Cdd:cd17637 139 FWslygQTETSGLVT---LSPYRER---PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPL---VFQGYWNLPELT 209
|
90 100 110
....*....|....*....|....*....|.
gi 1191882765 523 KHLYFEkfpGYYDTMDAGYMDEEGYVYVMSR 553
Cdd:cd17637 210 AYTFRN---GWHHTGDLGRFDEDGYLWYAGR 237
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
475-572 |
4.50e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 52.70 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 475 GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLyfeKFPGYYDTMDAGYMdEEGYVYVMSRV 554
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR---GPSLMSGYFRDEESQDVL---AADGWLDTGDLGYL-LDGYLYITGRA 460
|
90
....*....|....*...
gi 1191882765 555 DDVINVAGHRISAGAIEE 572
Cdd:PRK09192 461 KDLIIINGRNIWPQDIEW 478
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
250-571 |
4.79e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 53.24 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 250 KVLIYNRPNMETVPLASGR---DLDWDEEMAKAQSQDCVPVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSI 326
Cdd:PRK12467 3194 KLLLTQAHLLEQLPAPAGDtalTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCW-IAEA 3272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 327 YGLKPGEVWWAASDLGWVVGHSYIcYGPLIHGNTTVLYEGKpVGTPDagAYFRVLAEHGVAALFTAPTAIRAIrqqdpgA 406
Cdd:PRK12467 3273 YELDANDRVLLFMSFSFDGAQERF-LWTLICGGCLVVRDND-LWDPE--ELWQAIHAHRISIACFPPAYLQQF------A 3342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 407 ALGKQYSLTRFKTLFVAGERCDVETLEWSKKVF-RVPVLDHWWQTETGSPITASCIGLGNSKTPPPGQAGKSVPGYNVMI 485
Cdd:PRK12467 3343 EDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLkPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYV 3422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 486 LDDNMQklkarclgnivvklPLPPGAFSGLWKNQEAFKHLYFEK------------FPG----YYDTMDAGYMDEEGYVY 549
Cdd:PRK12467 3423 LDGQLN--------------PVPVGVAGELYIGGVGLARGYHQRpsltaerfvadpFSGsggrLYRTGDLARYRADGVIE 3488
|
330 340
....*....|....*....|..
gi 1191882765 550 VMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIE 3510
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
448-572 |
1.24e-06 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 51.17 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 448 WQTETGSPITAsciGLGNSKTPP------------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGL 515
Cdd:PRK07059 347 WLEMTGCPITE---GYGLSETSPvatcnpvdatefSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR---GPQVMAGY 420
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 516 WKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK07059 421 WNRPDETAKVMTAD--GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEE 475
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
86-571 |
3.73e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 49.60 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 86 YKPWTKTLENRHSSSTSWFVEGMLNMcynaIDRHIESgkgDKVAIIydspvtDTKATITYKEVLEQVSRLAGVLVKHGVS 165
Cdd:PRK10946 5 FTRWPEEFARRYREKGYWQDLPLTDI----LTRHAAS---DAIAVI------CGERQFSYRELNQASDNLACSLRRQGIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 166 KGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTASfgiepgrkveympileeamrigQ 245
Cdd:PRK10946 72 PGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNAYASQIEPALLIADR----------------------Q 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 246 HK--PDKV----LIYNRPNMETVPLasgRDLDWDEEMAKAQSQDCV-----PVLSEHPLYILYTSGTTGLPKGVVRPTGG 314
Cdd:PRK10946 130 HAlfSDDDflntLVAEHSSLRVVLL---LNDDGEHSLDDAINHPAEdftatPSPADEVAFFQLSGGSTGTPKLIPRTHND 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 315 YavmlnwtmssIYGLKpgevwwAASDLGWVVGHS-YICYGPLIH-------GNTTVLYEGKPV---GTPDAGAYFRVLAE 383
Cdd:PRK10946 207 Y----------YYSVR------RSVEICGFTPQTrYLCALPAAHnypmsspGALGVFLAGGTVvlaPDPSATLCFPLIEK 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 384 HGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDvETLewskkVFRVPVL------------------- 444
Cdd:PRK10946 271 HQVNVTALVPPAVSLWLQA--IAEGGSRAQLASLKLLQVGGARLS-ETL-----ARRIPAElgcqlqqvfgmaeglvnyt 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 445 ------DHWWQTEtGSPITasciglgnsktpppgqagksvPGYNVMILDDNmqklkarclGNivvklPLPPG-------- 510
Cdd:PRK10946 343 rlddsdERIFTTQ-GRPMS---------------------PDDEVWVADAD---------GN-----PLPQGevgrlmtr 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191882765 511 ---AFSGLWK----NQEAFKHlyfekfPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK10946 387 gpyTFRGYYKspqhNASAFDA------NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIE 448
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
448-572 |
5.01e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 49.38 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 448 WQTETGSPItasCIGLGNSKTPP-----------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLW 516
Cdd:PRK05677 346 WKEVTGCAI---CEGYGMTETSPvvsvnpsqaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK---GPQVMKGYW 419
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882765 517 KNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK05677 420 QRPEATDEILDSD--GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELED 473
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
126-571 |
5.02e-06 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 49.39 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSpvtdtkATITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:cd17656 3 DAVAVVFEN------QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 206 LSSRIDHAKPKVVVTASfgiepgrkveympileeamrigqHKPDKVliynRPNMETVPLasgrdlDWDEEMAKAQSQDCV 285
Cdd:cd17656 77 RIYIMLDSGVRVVLTQR-----------------------HLKSKL----SFNKSTILL------EDPSISQEDTSNIDY 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 286 PVLSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVWWAASdlgwvvgHSY-ICY----GPLIHGNT 360
Cdd:cd17656 124 INNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFAT-------CSFdVCYqeifSTLLSGGT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 361 tvLYEGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaalgKQYS---LTRFKTLFVAGERCDVETLewSKK 437
Cdd:cd17656 197 --LYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSE-------REFInrfPTCVKHIITAGEQLVITNE--FKE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 438 VFR---VPVLDHWWQTETgSPITASCIGLGNS--KTPPpgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVK-LPLPPGA 511
Cdd:cd17656 266 MLHehnVHLHNHYGPSET-HVVTTYTINPEAEipELPP---IGKPISNTWIYILDQEQQLQPQGIVGELYISgASVARGY 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 512 FSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17656 342 LNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIE 401
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
143-370 |
6.06e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 49.34 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 143 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACAR-------IGA-------IHSLifggfASKELSS 208
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRqnitvvtIYAslgeealCHSL-----NETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 209 RI-DHAKPKVVVTASFGIEPGRKVEYMPilEEAMRIGQhkpdkvliyNRPNMETVPLASGRDLdwdEEMAKAQSQDCVPV 287
Cdd:PLN02387 182 VIcDSKQLKKLIDISSQLETVKRVIYMD--DEGVDSDS---------SLSGSSNWTVSSFSEV---EKLGKENPVDPDLP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 288 LSEHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWTMSSIYGLKPGEVwwaasdlgwvvghsYICYGPLIH-----GNTTV 362
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPLAHilelaAESVM 313
|
....*...
gi 1191882765 363 LYEGKPVG 370
Cdd:PLN02387 314 AAVGAAIG 321
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
290-425 |
8.98e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.01 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 290 EHPLYILYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGEVWWAASDLGWVVGhSYICYGPLIHGNTTVLyeGKPV 369
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQW-MQATYALDDSDVLMQKAPISFDVS-VWECFWPLITGCRLVL--AGPG 1348
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1191882765 370 GTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkqySLTRFKTLFVAGE 425
Cdd:PRK05691 1349 EHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDE-PLAA-----ACTSLRRLFSGGE 1398
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
142-357 |
1.49e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 48.05 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTA 221
Cdd:PTZ00216 121 YITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 222 sfgiepGRKVeymPILEEAMRIGQhKPDKVLIYNRPNMETVPLASGRDLDWDEEMAKAQSqdcvpVLSEHPL-------- 293
Cdd:PTZ00216 201 ------GKNV---PNLLRLMKSGG-MPNTTIIYLDSLPASVDTEGCRLVAWTDVVAKGHS-----AGSHHPLnipenndd 265
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 294 --YILYTSGTTGLPKGVVRPTG----GYAVMLNWTMSSIYGLKPGEVwwaasdlgwvvghsYICYGPLIH 357
Cdd:PTZ00216 266 laLIMYTSGTTGDPKGVMHTHGsltaGILALEDRLNDLIGPPEEDET--------------YCSYLPLAH 321
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
144-309 |
1.82e-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: 47.42 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVTAsf 223
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 224 giepgrkveympileeamrigQHKPDKVLIYNRPNmetvplasgrdldwdeemakaqSQDCVPVLSEhpLYILYTSGTTG 303
Cdd:cd05939 83 ---------------------LLDPLLTQSSTEPP----------------------SQDDVNFRDK--LFYIYTSGTTG 117
|
....*.
gi 1191882765 304 LPKGVV 309
Cdd:cd05939 118 LPKAAV 123
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
475-572 |
3.15e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 46.91 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 475 GKSVPGYNVMILDDNMQKLKARCLGNIVVKLP-LPPG--AFSGLWKNQEAfkhlyfekfPGYYDTMDAGYMDEEGYVYVM 551
Cdd:PRK07768 363 GPPLPGLEVRVVDEDGQVLPPRGVGVIELRGEsVTPGylTMDGFIPAQDA---------DGWLDTGDLGYLTEEGEVVVC 433
|
90 100
....*....|....*....|.
gi 1191882765 552 SRVDDVINVAGHRISAGAIEE 572
Cdd:PRK07768 434 GRVKDVIIMAGRNIYPTDIER 454
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
143-545 |
3.36e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 46.58 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 143 ITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAI-------HSLIFGGFAskELSSRIDHAKP 215
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPaapvspaYSLMSHDHA--KLKHLFDLVKP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 216 KVVVtasfgiepgrkVEYMPILEEAMRI-GQHKPDKVLIYNRPNME-TVPLAsgrdlDW-----DEEMAKAQSQ---DCV 285
Cdd:PRK12582 159 RVVF-----------AQSGAPFARALAAlDLLDVTVVHVTGPGEGIaSIAFA-----DLaatppTAAVAAAIAAitpDTV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 286 PvlsehplYILYTSGTTGLPKGVVRPTGGYAVMLNWTMssiyGLKPGEVWWAASD-LGW-----VVGHSYICYGPLIHGN 359
Cdd:PRK12582 223 A-------KYLFTSGSTGMPKAVINTQRMMCANIAMQE----QLRPREPDPPPPVsLDWmpwnhTMGGNANFNGLLWGGG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 360 TTVLYEGKPVgtpdAGAY---FRVLAEHGVAALFTAPTAIRAI---RQQDPgaALGKQYsLTRFKTLFVAGERCDVETLE 433
Cdd:PRK12582 292 TLYIDDGKPL----PGMFeetIRNLREISPTVYGNVPAGYAMLaeaMEKDD--ALRRSF-FKNLRLMAYGGATLSDDLYE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 434 WSKKV------FRVPVLDHWWQTETgSPITASC---------IGLgnsktPPPGQAGKSVPgynvmilddNMQKLKARCL 498
Cdd:PRK12582 365 RMQALavrttgHRIPFYTGYGATET-APTTTGThwdtervglIGL-----PLPGVELKLAP---------VGDKYEVRVK 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1191882765 499 GNIVVKlplppgafsGLWKNQEAFKHLYFEKfpGYYDTMDAG-YMDEE 545
Cdd:PRK12582 430 GPNVTP---------GYHKDPELTAAAFDEE--GFYRLGDAArFVDPD 466
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
142-309 |
4.02e-05 |
|
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: 46.38 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEvLEQVS-RLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGaihslifGGFASkelssrIDHAKPkvvvt 220
Cdd:cd05918 24 SLTYAE-LDRLSsRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAG-------GAFVP------LDPSHP----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 221 asfgiePGRKVEympILEEAmrigqhkpdkvliynrpnmetvplasgrdldwdeemakaqsqDCVPVLSEHP---LYILY 297
Cdd:cd05918 85 ------LQRLQE---ILQDT------------------------------------------GAKVVLTSSPsdaAYVIF 113
|
170
....*....|..
gi 1191882765 298 TSGTTGLPKGVV 309
Cdd:cd05918 114 TSGSTGKPKGVV 125
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
142-572 |
4.28e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 46.35 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 142 TITYKEVLEQVSRLAGVLVKH-GVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVVVT 220
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 221 AS-FG-----IEPGRKVEYmpiLEEAmRIGQHKP-----------DK----VLIYNRPnmETVP----LASGRDLdwdEE 275
Cdd:PRK12492 129 LNmFGklvqeVLPDTGIEY---LIEA-KMGDLLPaakgwlvntvvDKvkkmVPAYHLP--QAVPfkqaLRQGRGL---SL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 276 MAKAQSQDCVPVLSehplyilYTSGTTGLPKGVVRPTGG--------YAVMLNWTMSSIYGLKPG-EVWWAASDLGWVVG 346
Cdd:PRK12492 200 KPVPVGLDDIAVLQ-------YTGGTTGLAKGAMLTHGNlvanmlqvRACLSQLGPDGQPLMKEGqEVMIAPLPLYHIYA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 347 HSYICYGPLIHGNTTVLyegkpVGTP-DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAalgKQYSLTRFKTLFVAGE 425
Cdd:PRK12492 273 FTANCMCMMVSGNHNVL-----ITNPrDIPGFIKELGKWRFSALLGLNTLFVALMDH-PGF---KDLDFSALKLTNSGGT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 426 RCDVETLEWSKKVFRVPVLDHWWQTETgSPItASCIGLGNSKTPppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKl 505
Cdd:PRK12492 344 ALVKATAERWEQLTGCTIVEGYGLTET-SPV-ASTNPYGELARL--GTVGIPVPGTALKVIDDDGNELPLGERGELCIK- 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191882765 506 plPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK12492 419 --GPQVMKGYWQQPEATAEALDAE--GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIED 481
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
295-571 |
8.83e-05 |
|
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: 44.80 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 295 ILYTSGTTGLPKGVV---RPTggyavmlnwtmssiygLKPGEVWwaaSDLGWVV-GHSYICYGPLIH------GNTTVLY 364
Cdd:cd17638 5 IMFTSGTTGRSKGVMcahRQT----------------LRAAAAW---ADCADLTeDDRYLIINPFFHtfgykaGIVACLL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 365 EGK---PVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAalgKQYSLTRFKTLFVAGERCDVETLEWSKKVFRV 441
Cdd:cd17638 66 TGAtvvPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDH-PGR---KKFDLSSLRAAVTGAATVPVELVRRMRSELGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 442 -PVLDHWWQTETGspiTASCIGLGNSKTPPPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQE 520
Cdd:cd17638 142 eTVLTAYGLTEAG---VATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVR---GYNVMQGYLDDPE 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1191882765 521 AFKHLYFEKfpGYYDTMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd17638 206 ATAEAIDAD--GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVE 254
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
289-572 |
1.25e-04 |
|
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: 44.68 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 289 SEHPLYILYTSGTTGLPKGVVRPTGGYAVML---------NWTMSSIYGLK----PGEVWWAASdlgwvvghsyicygPL 355
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEDIFRMLmggadfgtgEFTPSEDAHKAaaaaAGTVMFPAP--------------PL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 356 IHGNTTVLYEGKPVGTP---------DAGAYFRVLAEHGVAALFTAPTA-----IRAIRqqDPGAalgkqYSLTRFKTLF 421
Cdd:cd05924 68 MHGTGSWTAFGGLLGGQtvvlpddrfDPEEVWRTIEKHKVTSMTIVGDAmarplIDALR--DAGP-----YDLSSLFAIS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 422 VAGercdvetLEWSKKVfRVPVLDHWWQ---------TETGSpitascIGLGNSKTPPPGQAGKSVPGYNVMILDDNMQK 492
Cdd:cd05924 141 SGG-------ALLSPEV-KQGLLELVPNitlvdafgsSETGF------TGSGHSAGSGPETGPFTRANPDTVVLDDDGRV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 493 LK--ARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEK--FPGYYDTMDAGymdeeGYVYVMSRVDDVINVAGHRISAG 568
Cdd:cd05924 207 VPpgSGGVGWIARRGHIPLGYYGDEAKTAETFPEVDGVRyaVPGDRATVEAD-----GTVTLLGRGSVCINTGGEKVFPE 281
|
....
gi 1191882765 569 AIEE 572
Cdd:cd05924 282 EVEE 285
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
536-572 |
1.65e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 44.26 E-value: 1.65e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1191882765 536 TMDAGYMDEEGYVYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVED 331
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
126-333 |
2.43e-04 |
|
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: 44.05 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 126 DKVAIIYDSPVTDTKA-TITYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLifggfask 204
Cdd:cd17647 3 ERTCVVETPSLNSSKTrSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSV-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 205 elssrIDHAKPkvvvtasfgiePGRKVEYMPILEEAMRIGQHKPDKVLiynrpnmetvplasgrdldwdeemakaqSQDC 284
Cdd:cd17647 75 -----IDPAYP-----------PARQNIYLGVAKPRGLIVIRAAGVVV----------------------------GPDS 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1191882765 285 VPVLSehplyilYTSGTTGLPKGVVRPTGGYAVMLNWtMSSIYGLKPGE 333
Cdd:cd17647 111 NPTLS-------FTSGSEGIPKGVLGRHFSLAYYFPW-MAKRFNLSEND 151
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
472-572 |
3.15e-04 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 43.50 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 472 GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYVYVM 551
Cdd:PRK08974 378 GSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK---GPQVMLGYWQRPEATDEVIKD---GWLATGDIAVMDEEGFLRIV 451
|
90 100
....*....|....*....|.
gi 1191882765 552 SRVDDVINVAGHRISAGAIEE 572
Cdd:PRK08974 452 DRKKDMILVSGFNVYPNEIED 472
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
144-309 |
3.83e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 43.47 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 144 TYKEVLEQVSRLAGVLVKHGVSKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHAKPKVV----- 218
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVfveek 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 219 -VTASFGIEPGrKVEYMpilEEAMRIGQHKPDKvliynRPNMETVPLASgrdLDWDE--EMAKAQSQDcVPVLSEHPL-Y 294
Cdd:PLN02614 161 kISELFKTCPN-STEYM---KTVVSFGGVSREQ-----KEEAETFGLVI---YAWDEflKLGEGKQYD-LPIKKKSDIcT 227
|
170
....*....|....*
gi 1191882765 295 ILYTSGTTGLPKGVV 309
Cdd:PLN02614 228 IMYTSGTTGDPKGVM 242
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
270-571 |
5.34e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.15 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 270 LDWDEEMAKAQSQDCVPVLS--EHPLYILYTSGTTGLPKGVVRPTGGYAvMLNWTMSSIYGLKPGEV--------WWAAS 339
Cdd:PRK05691 2311 LEDDAAALAAYSDAPLPFLSlpQHQAYLIYTSGSTGKPKGVVVSHGEIA-MHCQAVIERFGMRADDCelhfysinFDAAS 2389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 340 DLGWVvghsyicygPLIHGNTTVLyegKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaaLGKQYSLTRFKT 419
Cdd:PRK05691 2390 ERLLV---------PLLCGARVVL---RAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQW-----LAGQGEQLPVRM 2452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 420 LFVAGERCDVETLEWSKKVFRVPVL-DHWWQTETGSPITASCIGlgnsKTPPPGQA----GKSVPGYNVMILDDNMqklk 494
Cdd:PRK05691 2453 CITGGEALTGEHLQRIRQAFAPQLFfNAYGPTETVVMPLACLAP----EQLEEGAAsvpiGRVVGARVAYILDADL---- 2524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191882765 495 arclgnivvkLPLPPGAFSGLWKNQEAFKHLYFEKfPG-----------------YYDTMDAGYMDEEGYVYVMSRVDDV 557
Cdd:PRK05691 2525 ----------ALVPQGATGELYVGGAGLAQGYHDR-PGltaerfvadpfaadggrLYRTGDLVRLRADGLVEYVGRIDHQ 2593
|
330
....*....|....
gi 1191882765 558 INVAGHRISAGAIE 571
Cdd:PRK05691 2594 VKIRGFRIELGEIE 2607
|
|
| |
