|
Name |
Accession |
Description |
Interval |
E-value |
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
62-679 |
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: 1175.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 62 YKTHFAASVTDPERFWGKAAEQISWYKPWTKTLENKHSPSTRWFVEGMLNICYNAVDRHIENGKGDKIAIIYDSPVTNTK 141
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPPFTRWFVGGRLNTCYNALDRHVEAGRGDQIALIYDSPVTGTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 142 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 221
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 ASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYILYTSG 301
Cdd:cd05967 161 ASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQVPADLTKPGRDLDWSELLAKAEPVDCVPVAATDPLYILYTSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 302 TTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVGTPDAGAYFRV 381
Cdd:cd05967 241 TTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVGTPDPGAFWRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 382 LAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASC 461
Cdd:cd05967 321 IEKYQVNALFTAPTAIRAIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 462 VGLGNsKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAG 541
Cdd:cd05967 401 VGLEP-LPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 542 YMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVK 621
Cdd:cd05967 480 YKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVA 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 13375727 622 HVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSIFGHV 679
Cdd:cd05967 560 LVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDEI 617
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
103-681 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 715.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 103 RWFVEGMLNICYNAVDRHIEnGKGDKIAIIYDSpVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAM 182
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAE-GRGDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 183 YTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFGIEPGRRVEYVPLVEEALKiGQHKPDKILIYNRPNMEA 262
Cdd:COG0365 79 IAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALE-ELPSLEHVIVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 263 vplAPGRDLDWDEEMAKA-QSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASD 341
Cdd:COG0365 158 ---PMEGDLDWDELLAAAsAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 342 LGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTL 421
Cdd:COG0365 235 IGWATGHSYIVYGPLLNGATVVLYEGRPD-FPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGD--EPLKKYDLSSLRLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 422 FVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGlgnskTPP-PGQAGKSVPGYNVMILDDNMQKLKARCLG 500
Cdd:COG0365 312 GSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPG-----LPVkPGSMGKPVPGYDVAVVDEDGNPVPPGEEG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 501 NIVVKLPLpPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGT 580
Cdd:COG0365 387 ELVIKGPW-PGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 581 VADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVN 660
Cdd:COG0365 466 VAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELA-KELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
570 580
....*....|....*....|.
gi 13375727 661 GKPYKITSTIEDPSIFGHVEE 681
Cdd:COG0365 545 GRPLGDTSTLEDPEALDEIKE 565
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
62-685 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 675.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 62 YKTHFAASVTDPERFWGKAAEQISWYKPWTKTLENKHSPSTRWFVEGMLNICYNAVDRHIEnGKGDKIAIIYDSPVTNTK 141
Cdd:PRK10524 4 YSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSNPPFARWFVGGRTNLCHNAVDRHLA-KRPEQLALIAVSTETDEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 142 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 221
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 ASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRpNMEAVPLAPGRDLDWDEEMAKAQSHDcVPVL---SEHPLYILY 298
Cdd:PRK10524 163 ADAGSRGGKVVPYKPLLDEAIALAQHKPRHVLLVDR-GLAPMARVAGRDVDYATLRAQHLGAR-VPVEwleSNEPSYILY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 299 TSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAY 378
Cdd:PRK10524 241 TSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPT-RPDAGIW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 379 FRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPIT 458
Cdd:PRK10524 320 WRIVEKYKVNRMFSAPTAIRVLKKQDP--ALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGWPIL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 459 ASCVGLGnSKTPPPGQAGKSVPGYNVMILDDNM-QKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKF-PGYYD 536
Cdd:PRK10524 398 AIARGVE-DRPTRLGSPGVPMYGYNVKLLNEVTgEPCGPNEKGVLVIEGPLPPGCMQTVWGDDDRFVKTYWSLFgRQVYS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 537 TMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRK-DINATEEQV 615
Cdd:PRK10524 477 TFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDsDSLADREAR 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13375727 616 LE---EIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSIFGHVEEMLKQ 685
Cdd:PRK10524 557 LAlekEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDPGDLTTIEDPAALQQIRQALEE 629
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
61-672 |
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: 639.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 61 EYKTHFAASVTDPERFWGKAAEQISWYKPWTKTLE-NKHSPSTRWFVEGMLNICYNAVDRHIENgKGDKIAIIYDSPVTN 139
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDwSKGPPFIKWFEGGKLNISYNCLDRHLKE-RGDKVAIIWEGDEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 140 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 219
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 220 VTASFGIEPGRRVEYVPLVEEALKIGqHKPDKILIYNRPNMEaVPLAPGRDLDWDEEMAKA-QSHDCVPVLSEHPLYILY 298
Cdd:cd05966 161 ITADGGYRGGKVIPLKEIVDEALEKC-PSVEKVLVVKRTGGE-VPMTEGRDLWWHDLMAKQsPECEPEWMDSEDPLFILY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 299 TSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAY 378
Cdd:cd05966 239 TSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPT-YPDPGRY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 379 FRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNV---FRVPVLDHWWQTETGS 455
Cdd:cd05966 318 WDIVEKHKVTIFYTAPTAIRALMKF--GDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVigkERCPIVDTWWQTETGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 456 PITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLpPGAFSGLWKNQEAFKHLYFEKFPGYY 535
Cdd:cd05966 396 IMITPLPGATPLK---PGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPW-PGMARTIYGDHERYEDTYFSKFPGYY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 536 DTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqV 615
Cdd:cd05966 472 FTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDE-L 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 13375727 616 LEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNG-KPYKITSTIED 672
Cdd:cd05966 551 RKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGeEELGDTSTLAD 608
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
61-681 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 620.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 61 EYKTHFAASVTDPERFWGK-AAEQISWYKPWTKTLENKHSPSTRWFVEGMLNICYNAVDRHIENgKGDKIAIIYDSPVTN 139
Cdd:TIGR02188 6 QYKELYEESIEDPDKFWAKlARELLDWFKPFTKVLDWSFPPFYKWFVGGELNVSYNCVDRHLEA-RPDKVAIIWEGDEPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 140 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 219
Cdd:TIGR02188 85 EVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 220 VTASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKaQSHDCVP--VLSEHPLYIL 297
Cdd:TIGR02188 165 ITADEGLRGGKVIPLKAIVDEALEKCPVSVEHVLVVRRTGNPVVPWVEGRDVWWHDLMAK-ASAYCEPepMDSEDPLFIL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 298 YTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGA 377
Cdd:TIGR02188 244 YTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPT-YPDPGR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 378 YFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTETG 454
Cdd:TIGR02188 323 FWEIIEKHKVTIFYTAPTAIRALMRL--GDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVgkeRCPIVDTWWQTETG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 455 SPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNI-VVKLPLpPGAFSGLWKNQEAFKHLYFEKFPG 533
Cdd:TIGR02188 401 GIMITPLPGATPTK---PGSATLPFFGIEPAVVDEEGNPVEGPGEGGYlVIKQPW-PGMLRTIYGDHERFVDTYFSPFPG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 534 YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEE 613
Cdd:TIGR02188 477 YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 614 qVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKP--YKITSTIEDPSIFGHVEE 681
Cdd:TIGR02188 557 -LRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAeiLGDTSTLEDPSVVEELIE 625
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
61-676 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 619.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 61 EYKTHFAASVTDPERFWGKAAEQISWYKPWTKTLeNKHSPSTRWFVEGMLNICYNAVDRHIENGkGDKIAIIY--DSPVT 138
Cdd:PRK00174 18 QYKALYQESVEDPEGFWAEQAKRLDWFKPFDTVL-DWNAPFIKWFEDGELNVSYNCLDRHLKTR-GDKVAIIWegDDPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 139 NTKatFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKV 218
Cdd:PRK00174 96 SRK--ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 219 VVTASFGIEPGRRVEYVPLVEEALKIGqHKPDKILIYNRPNmEAVPLAPGRDLDWDEEMAKAQS-HDCVPVLSEHPLYIL 297
Cdd:PRK00174 174 VITADEGVRGGKPIPLKANVDEALANC-PSVEKVIVVRRTG-GDVDWVEGRDLWWHELVAGASDeCEPEPMDAEDPLFIL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 298 YTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGA 377
Cdd:PRK00174 252 YTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPN-YPDPGR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 378 YFRVLAEHGVAALFTAPTAIRA-IRQqdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTET 453
Cdd:PRK00174 331 FWEVIDKHKVTIFYTAPTAIRAlMKE---GDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVggeRCPIVDTWWQTET 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 454 GSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLpPGAFSGLWKNQEAFKHLYFEKFPG 533
Cdd:PRK00174 408 GGIMITPLPGATPLK---PGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPW-PGMMRTIYGDHERFVKTYFSTFKG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 534 YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEE 613
Cdd:PRK00174 484 MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDE 563
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13375727 614 qVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPykI---TSTIEDPSIF 676
Cdd:PRK00174 564 -LRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE--IlgdTSTLADPSVV 626
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
62-650 |
0e+00 |
|
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: 603.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 62 YKTHFAASVTDPERFWGKAAEQISWYKPWTK---TLENKHSPSTRWFVEGMLNICYNAVDRHIENGkGDKIAIIYDSPVT 138
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKvknTSFAPGAPSIKWFEDATLNLAANALDRHLREN-GDRTAIIYEGDDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 139 NTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKV 218
Cdd:cd17634 80 SQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 219 VVTASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMeAVPLAPGRDLDWDEEMAKAQ-SHDCVPVLSEHPLYIL 297
Cdd:cd17634 160 LITADGGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGS-DIDWQEGRDLWWRDLIAKASpEHQPEAMNAEDPLFIL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 298 YTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVGtPDAGA 377
Cdd:cd17634 239 YTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNW-PTPAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 378 YFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGkqYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTETG 454
Cdd:cd17634 318 MWQVVDKHGVNILYTAPTAIRALMAAGDDAIEG--TDRSSLRILGSVGEPINPEAYEWYWKKIgkeKCPVVDTWWQTETG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 455 SPITASCVGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEaFKHLYFEKFPGY 534
Cdd:cd17634 396 GFMITPLPGAIELKA---GSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHER-FEQTYFSTFKGM 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 535 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEq 614
Cdd:cd17634 472 YFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPE- 550
|
570 580 590
....*....|....*....|....*....|....*.
gi 13375727 615 VLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 650
Cdd:cd17634 551 LYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| propion_prpE |
TIGR02316 |
propionate--CoA ligase; This family contains one of three readily separable clades of proteins ... |
62-685 |
0e+00 |
|
propionate--CoA ligase; This family contains one of three readily separable clades of proteins in the group of acetate and propionate--CoA ligases. Characterized members of this family act on propionate. From propionyl-CoA, there is a cyclic degradation pathway: it is ligated by PrpC to the TCA cycle intermediate oxaloacetate, acted upon further by PrpD and an aconitase, then cleaved by PrpB to pyruvate and the TCA cycle intermediate succinate.
Pssm-ID: 131369 [Multi-domain] Cd Length: 628 Bit Score: 569.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 62 YKTHFAASVTDPERFWGKAAEQISWYKPWTKTLENKHSPSTRWFVEGMLNICYNAVDRHIENgKGDKIAIIYDSPVTNTK 141
Cdd:TIGR02316 3 YEEFYQRSIEQPEAFWAEQARRIDWQTPPQRILDYSNPPFARWFAGGRTNLCHNALDRHLDE-RGEQLALVTVSSETGQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 142 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 221
Cdd:TIGR02316 82 RTLTYRQLHREVNVFASALRALGVGRGDRVLIYMPMIAEAVFAMLACARIGAIHSVVFGGFASHSLALRIDDATPKLIVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 ASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRpNMEAVPLAPGRDLDWdEEMAKAQSHDCVPVL---SEHPLYILY 298
Cdd:TIGR02316 162 ADAGMRGGKVIPYKPLLDAAIAEAQHPPPHVLLVDR-GLAPMRLIPGRDVDY-AALRTQHEDAQVPVEwleSNEPSYILY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 299 TSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAY 378
Cdd:TIGR02316 240 TSGTTGKPKGVQRDVGGYAVALALSMWAIFGIRAGQVMFSASDVGWVVGHSYIVYAPLLAGAATVLYEGLPT-NPDPGVW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 379 FRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPIT 458
Cdd:TIGR02316 319 WSIVERYGVRTMFSAPTAIRVLKKQDA--AWLRKHDLSSLHWLFLAGEPLDEPTAHWITDGLGKPVIDNYWQTETGWPVL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 459 ASCVGLgNSKTPPPGQAGKSVPGYNVMILDDNM-QKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKFPG-YYD 536
Cdd:TIGR02316 397 AIMPGL-DLKPVKLGSPGLPMYGYHLRVLDEATgRPCGPNEKGVLTVVPPLPPGCLSTVWGDDARFLKTYWSHFKRpLYS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 537 TMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQ-- 614
Cdd:TIGR02316 476 SFDWGIRDEDGYTFILGRTDDVINVAGHRLGTREIEESVSSHPSVAEVAVVGVHDELKGQVAVVFAILKESDSAGDAHdp 555
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13375727 615 --VLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSIFGHVEEMLKQ 685
Cdd:TIGR02316 556 haVETGMMDCVVRQLGAVARPARVYFVAALPKTRSGKLLRRSIQALAEGRDPGDLTTIDDPGALEQVRRAMER 628
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
52-686 |
8.62e-137 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 416.61 E-value: 8.62e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 52 RALSSgSGSEYKTHFAASVTDPERFWGKAAEQISWYKPW------TKTLENKHSP-STRWFVEGMLNICYNAVDRHIENG 124
Cdd:PLN02654 23 QALVS-SPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWegdevcSENLDVRKGPiSIEWFKGGKTNICYNCLDRNVEAG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 125 KGDKIAIIYDSPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFAS 204
Cdd:PLN02654 102 NGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 205 KELSSRIDHVKPKVVVTASfGIEPGRRVEYVP-LVEEALKIGQHKP---DKILIY-NRPNM--EAVPLAPGRDLDWDEEM 277
Cdd:PLN02654 182 ESLAQRIVDCKPKVVITCN-AVKRGPKTINLKdIVDAALDESAKNGvsvGICLTYeNQLAMkrEDTKWQEGRDVWWQDVV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 278 AK-AQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPL 356
Cdd:PLN02654 261 PNyPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPM 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 357 LHGNTTVLYEGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWS 436
Cdd:PLN02654 341 LNGATVLVFEGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRD--GDEYVTRHSRKSLRVLGSVGEPINPSAWRWF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 437 KNVF---RVPVLDHWWQTETGSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLpPGAF 513
Cdd:PLN02654 418 FNVVgdsRCPISDTWWQTETGGFMITPLPGAWPQK---PGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSW-PGAF 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 514 SGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPL 593
Cdd:PLN02654 494 RTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEV 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 594 KGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKI--TSTIE 671
Cdd:PLN02654 574 KGQGIYAFVTLVEGVPYSEE-LRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELgdTSTLA 652
|
650
....*....|....*
gi 13375727 672 DPSIfghVEEMLKQA 686
Cdd:PLN02654 653 DPGV---VDQLIALA 664
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
62-685 |
3.68e-127 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 391.03 E-value: 3.68e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 62 YKTHFAASVTDPERFWGKAAEQiswYKPWTKTLENKHS-----PStrWFVEGMLNICYNAVDRHIENG-KGDKIAIIYDS 135
Cdd:PTZ00237 10 YENDSNYANSNPESFWDEVAKK---YVHWDKMYDKVYSgdeiyPD--WFKGGELNTCYNVLDIHVKNPlKRDQDALIYEC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 136 PVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVK 215
Cdd:PTZ00237 85 PYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 216 PKVVVTASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPN---------MEAVPLAPGrDLDWDEEMAK----AQS 282
Cdd:PTZ00237 165 PKLIITTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRNDitsesdlkkIETIPTIPN-TLSWYDEIKKikenNQS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 283 --HDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGN 360
Cdd:PTZ00237 244 pfYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSLGN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 361 TTVLYEGKPVGTPDAGAYF-RVLAEHGVAALFTAPTAIRAIRQQDPGAA-LGKQYSLTRFKTLFVAGERCDVETLEWSKN 438
Cdd:PTZ00237 323 TFVMFEGGIIKNKHIEDDLwNTIEKHKVTHTLTLPKTIRYLIKTDPEATiIRSKYDLSNLKEIWCGGEVIEESIPEYIEN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 439 VFRVPVLDHWWQTETGspiTASCVGLGNSKTpPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWK 518
Cdd:PTZ00237 403 KLKIKSSRGYGQTEIG---ITYLYCYGHINI-PYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPPSFATTFYK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 519 NQEAFKHLyFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVP 598
Cdd:PTZ00237 479 NDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVP 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 599 LALCVLRKDINATE---EQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSI 675
Cdd:PTZ00237 558 IGLLVLKQDQSNQSidlNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSNYQLPDNVNDSEI 637
|
650
....*....|
gi 13375727 676 FGHVEEMLKQ 685
Cdd:PTZ00237 638 FYKIKELYMK 647
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
104-672 |
1.80e-120 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 371.15 E-value: 1.80e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 104 WFVEGMLNICYNAVDRHIENGKGDKIAIIYDSPvtNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMY 183
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADGGRKDKVALRYLDA--SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 184 TMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAsfgiepgrrveyvplveEALKigQHKPDKILiynrPNMEAV 263
Cdd:PRK04319 114 ALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITT-----------------PALL--ERKPADDL----PSLKHV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 264 PL------APGRDLDWDEEMAKAQSH-DCVPVLSEHPLYILYTSGTTGLPKGVIRPTGgyAVMLHWsMSSIYGL--QPGE 334
Cdd:PRK04319 171 LLvgedveEGPGTLDFNALMEQASDEfDIEWTDREDGAILHYTSGSTGKPKGVLHVHN--AMLQHY-QTGKYVLdlHEDD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 335 VWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYS 414
Cdd:PRK04319 248 VYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGRF----SPERWYRILEDYKVTVWYTAPTAIRMLMGA--GDDLVKKYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 415 LTRFKtlFVA--GERCDVETLEWSKNVFRVPVLDHWWQTETGSPITAscvglgNSKTPP--PGQAGKSVPGYNVMILDDN 490
Cdd:PRK04319 322 LSSLR--HILsvGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIA------NYPAMDikPGSMGKPLPGIEAAIVDDQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 491 MQKLKARCLGNIVVKLPLPpGAFSGLWKNQEAFKHlYFEkfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGA 570
Cdd:PRK04319 394 GNELPPNRMGNLAIKKGWP-SMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 571 IEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 650
Cdd:PRK04319 470 VESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEE-LKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
|
570 580
....*....|....*....|..
gi 13375727 651 PRSALSAIVNGKPYKITSTIED 672
Cdd:PRK04319 549 MRRVLKAWELGLPEGDLSTMED 570
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
61-673 |
4.05e-111 |
|
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: 348.33 E-value: 4.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 61 EYKTHFAASVTDPERFWGKAAEQ--ISWYKPWTKTLE-NKHSPSTRWFVEGMLNICYNAVDRHIENGKgDKIAIIYDSPV 137
Cdd:cd05968 8 DLEAFLERSAEDNAWFWGEFVKDvgIEWYEPPYQTLDlSGGKPWAAWFVGGRMNIVEQLLDKWLADTR-TRPALRWEGED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 138 TNTKaTFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPK 217
Cdd:cd05968 87 GTSR-TLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 218 VVVTASFGIEPGRRVEyvpLVEEALKIGQHKP--DKILIYNRPNMeAVPLAPGRDLDWDEEMAKAQSHdCVPVLSEHPLY 295
Cdd:cd05968 166 ALITADGFTRRGREVN---LKEEADKACAQCPtvEKVVVVRHLGN-DFTPAKGRDLSYDEEKETAGDG-AERTESEDPLM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 296 ILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGhSYICYGPLLHGNTTVLYEGKPvGTPDA 375
Cdd:cd05968 241 IIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAP-DHPKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 376 GAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTE 452
Cdd:cd05968 319 DRLWRMVEDHEITHLGLSPTLIRALKPR--GDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVgkgRNPIINYSGGTE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 453 TGSPItascvgLGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKARcLGNIVVKLPLPpGAFSGLWKNQEAFKHLYFEK 530
Cdd:cd05968 397 ISGGI------LGNVLIKPikPSSFNGPVPGMKADVLDESGKPARPE-VGELVLLAPWP-GMTRGFWRDEDRYLETYWSR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 531 FPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINA 610
Cdd:cd05968 469 FDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTP 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13375727 611 TEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDP 673
Cdd:cd05968 549 TEA-LAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
144-657 |
1.21e-106 |
|
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: 330.45 E-value: 1.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAS 223
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 224 fgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdcvpvlsEHPLYILYTSGTT 303
Cdd:cd05972 81 -------------------------------------------------------------------EDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 304 GLPKGVIRPTGgyAVMLHWS-MSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgtpDAGAYFRVL 382
Cdd:cd05972 94 GLPKGVLHTHS--YPLGHIPtAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF---DAERILELL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 383 AEHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGspitascV 462
Cdd:cd05972 169 ERYGVTSFCGPPTAYRMLIKQDL-----SSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETG-------L 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 463 GLGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDA 540
Cdd:cd05972 237 TVGNFPDMPvkPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLP-PPGLFLGYVGDPEKTEASIRG---DYYLTGDR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 541 GYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIV 620
Cdd:cd05972 313 AYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELA-EELQ 391
|
490 500 510
....*....|....*....|....*....|....*..
gi 13375727 621 KHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:cd05972 392 GHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
144-658 |
3.04e-105 |
|
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: 327.54 E-value: 3.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAs 223
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 224 fgiepgrrveyvplvEEalkigqhkpdkilIYNRPNMEavplapgrdldwdeemakaqshdcvpvlseHPLYILYTSGTT 303
Cdd:cd05969 80 ---------------EE-------------LYERTDPE------------------------------DPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 304 GLPKGVIRPTGgyAVMLHW-SMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPvgtpDAGAYFRVL 382
Cdd:cd05969 102 GTPKGVLHVHD--AMIFYYfTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF----DAESWYGII 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 383 AEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCV 462
Cdd:cd05969 176 ERVKVTVWYTAPTAIRMLMKE--GDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 463 GLgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlPLPPGAFSGLWKNQEAFKhLYFEKfpGYYDTMDAGY 542
Cdd:cd05969 254 CM----PIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALK-PGWPSMFRGIWNDEERYK-NSFID--GWYLTGDLAY 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 543 MDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKH 622
Cdd:cd05969 326 RDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDE-LKEEIINF 404
|
490 500 510
....*....|....*....|....*....|....*.
gi 13375727 623 VRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 658
Cdd:cd05969 405 VRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
126-655 |
9.70e-90 |
|
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: 287.09 E-value: 9.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 205
Cdd:COG0318 13 PDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 ELSSRIDHVKPKVVVTAsfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdc 285
Cdd:COG0318 87 ELAYILEDSGARALVTA--------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 286 vpvlsehplYILYTSGTTGLPKGVIRPTGGYAVMLhWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLY 365
Cdd:COG0318 104 ---------LILYTSGTTGRPKGVMLTHRNLLANA-AAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 366 EGkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVL 445
Cdd:COG0318 174 PR-----FDPERVLELIERERVTVLFGVPTMLARLLRH-PEFA---RYDLSSLRLVVSGGAPLPPELLERFEERFGVRIV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 446 DHWWQTETGSPITascVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKh 525
Cdd:COG0318 245 EGYGLTETSPVVT---VNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR---GPNVMKGYWNDPEATA- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 526 lyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVL 604
Cdd:COG0318 318 ---EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVL 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 13375727 605 RKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:COG0318 395 RPGAELDAEELRA----FLRERLARYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
123-562 |
6.71e-88 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 281.12 E-value: 6.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 123 NGKGDKIAIIYDSPVTntkatFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGF 202
Cdd:pfam00501 6 ARTPDKTALEVGEGRR-----LTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 203 ASKELSSRIDHVKPKVVVTASFGIepgrrveyVPLVEEALKIGQHKPDKILIYnrpnmeAVPLAPGRDLDWDEEMAKAQS 282
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALK--------LEELLEALGKLEVVKLVLVLD------RDPVLKEEPLPEEAKPADVPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 283 HDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGG--YAVMLHWSMS-SIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHG 359
Cdd:pfam00501 147 PPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNlvANVLSIKRVRpRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 360 NTTVLYEGKPvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalGKQYSLTRFKTLFVAGERCDVETLEWSKNV 439
Cdd:pfam00501 227 ATVVLPPGFP--ALDPAALLELIERYKVTVLYGVPTLLNMLLEAGA----PKRALLSSLRLVLSGGAPLPPELARRFREL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 440 FRVPVLDHWWQTETGSPITasCVGLGNSKTPPPGQAGKSVPGYNVMILDDN-MQKLKARCLGNIVVKlplPPGAFSGLWK 518
Cdd:pfam00501 301 FGGALVNGYGLTETTGVVT--TPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR---GPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 13375727 519 NQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVA 562
Cdd:pfam00501 376 DPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
292-650 |
1.14e-82 |
|
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: 264.92 E-value: 1.14e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 292 HPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVvGHSYICYGPLLHGNTTVLYEGkpvg 371
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAA-LAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 372 tPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQT 451
Cdd:cd04433 75 -FDPEAALELIEREKVTILLGVPTLLARLLKAPESAG----YDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 452 ETGSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPpgaFSGLWKNQEAFkhlYFEKF 531
Cdd:cd04433 150 ETGGTVATGPPDDDARK---PGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV---MKGYWNNPEAT---AAVDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 532 PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAT 611
Cdd:cd04433 221 DGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLD 300
|
330 340 350
....*....|....*....|....*....|....*....
gi 13375727 612 EeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 650
Cdd:cd04433 301 A----EELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
144-655 |
2.78e-74 |
|
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: 246.28 E-value: 2.78e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTas 223
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 224 fgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrDLDwdeemakaQSHDcvpvLSEHPLYILYTSGTT 303
Cdd:cd05973 79 ----------------------------------------------DAA--------NRHK----LDSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 304 GLPKGVIRPTGgYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKpvGTPDAgaYFRVLA 383
Cdd:cd05973 101 GLPKGVPVPLR-ALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG--FSVES--TWRVIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 384 EHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTlfvAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPItasCVG 463
Cdd:cd05973 176 RLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSS---AGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVL---ANH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 464 LGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPP-GAFSGLWK-NQEAFKHlyfekfpGYYDTMDAG 541
Cdd:cd05973 250 HALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPlMWFRGYQLpDTPAIDG-------GYYLTGDTV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 542 YMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVK 621
Cdd:cd05973 323 EFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPA-LADELQL 401
|
490 500 510
....*....|....*....|....*....|....
gi 13375727 622 HVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05973 402 HVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
139-657 |
1.74e-71 |
|
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: 238.87 E-value: 1.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 139 NTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKV 218
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 219 VVTasfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwDEemakaqshdcvpvlSEHPLYILY 298
Cdd:cd05971 82 LVT----------------------------------------------------DG--------------SDDPALIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 299 TSGTTGLPKGVIRptgGYAVML-H---WSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgtpD 374
Cdd:cd05971 96 TSGTTGPPKGALH---AHRVLLgHlpgVQFPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF---D 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 375 AGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaalGKQYSLT--RFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTE 452
Cdd:cd05971 170 PKAALDLMSRYGVTTAFLPPTALKMMRQQ------GEQLKHAqvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 453 tGSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEAFKhlyfEKFP 532
Cdd:cd05971 244 -CNLVIGNCSALFPIK---PGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELP-DPVAFLGYWNNPSATE----KKMA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 533 G-YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDInAT 611
Cdd:cd05971 315 GdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGE-TP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 13375727 612 EEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:cd05971 394 SDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
140-650 |
7.16e-67 |
|
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: 227.87 E-value: 7.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 140 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 219
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 220 VTASFGIEPgrrveyvplVEEALKIGQHKPDKILIYNRP----NMEAVPLAPGRDLDWDEEMAKAQSHDcvpvlseHPLY 295
Cdd:cd05911 87 FTDPDGLEK---------VKEAAKELGPKDKIIVLDDKPdgvlSIEDLLSPTLGEEDEDLPPPLKDGKD-------DTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 296 ILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYG-LQPGEVWWAASDLGWVVG-HSYICYgpLLHGNTTVLYEGkpvgtP 373
Cdd:cd05911 151 ILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGlFTTLAS--LLNGATVIIMPK-----F 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 374 DAGAYFRVLAEHGVAALFTAPtAIRAIRQQDPgaaLGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWW-QTE 452
Cdd:cd05911 224 DSELFLDLIEKYKITFLYLVP-PIAAALAKSP---LLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYgMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 453 TGSPITascvglgnsKTPP----PGQAGKSVPGYNVMILDDN-MQKLKARCLGNIVVKLPLppgAFSGLWKNQEAFKHLY 527
Cdd:cd05911 300 TGGILT---------VNPDgddkPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQ---VMKGYYNNPEATKETF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 528 FEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKD 607
Cdd:cd05911 368 DED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 13375727 608 INATEeqvlEEIVKHVRQNIGPVAAFRNAV-FVKQLPKTRSGKI 650
Cdd:cd05911 446 EKLTE----KEVKDYVAKKVASYKQLRGGVvFVDEIPKSASGKI 485
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
111-655 |
6.06e-65 |
|
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: 223.91 E-value: 6.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 111 NICYNAVDRHIENgKGDKIAIIYDSPVTNTKaTFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACAR 190
Cdd:cd05970 17 NFAYDVVDAMAKE-YPDKLALVWCDDAGEER-IFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 191 IGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFGIEPGR---RVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAP 267
Cdd:cd05970 95 LGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEiekAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDFE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 268 GRdldwdeemakaqsHDCVPVLSEHPLYILYTSGTTGLPKGV----IRPTGGYAVMLHWsmssiYGLQPGEVWWAASDLG 343
Cdd:cd05970 175 RP-------------TANSYPCGEDILLVYFSSGTTGMPKMVehdfTYPLGHIVTAKYW-----QNVREGGLHLTVADTG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 344 WVVGHSYICYGPLLHGNTTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTLFV 423
Cdd:cd05970 237 WGKAVWGKIYGQWIAGAAVFVYDYDKF---DPKALLEKLSKYGVTTFCAPPTIYRFLIREDL-----SRYDLSSLRYCTT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 424 AGERCDVETLEWSKNVFRVPVLDHWWQTETGSPI-TASCVglgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNI 502
Cdd:cd05970 309 AGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIaTFPWM------EPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 503 VVKLP--LPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGT 580
Cdd:cd05970 383 VIRTSkgKPVGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPA 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13375727 581 VADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05970 460 VLECAVTGVPDPIRGQVVKATIVLAKGYEPSEE-LKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
126-652 |
5.02e-62 |
|
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: 213.24 E-value: 5.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 205
Cdd:cd17631 9 PDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 ELSSRIDHVKPKVVVtasfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqsHDc 285
Cdd:cd17631 83 EVAYILADSGAKVLF--------------------------------------------------------------DD- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 286 vpvlsehPLYILYTSGTTGLPKGVIRPtggYAVMLHWSMSSIY--GLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTV 363
Cdd:cd17631 100 -------LALLMYTSGTTGRPKGAMLT---HRNLLWNAVNALAalDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 364 LYEGkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkQYSLTRFKTLFVAGERCDVETLE-WSknVFRV 442
Cdd:cd17631 170 ILRK-----FDPETVLDLIERHRVTSFFLVPTMIQALLQH-PRFA---TTDLSSLRAVIYGGAPMPERLLRaLQ--ARGV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 443 PVLDHWWQTETGSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEA 522
Cdd:cd17631 239 KFVQGYGMTETSPGVTFLSPEDHRRK---LGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR---GPHVMAGYWNRPEA 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 523 ----FKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVP 598
Cdd:cd17631 313 taaaFRD-------GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAV 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 13375727 599 LALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 652
Cdd:cd17631 386 VAVVVPRPGAELDE----DELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
69-673 |
7.81e-62 |
|
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: 217.52 E-value: 7.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 69 SVTDPERFWGKAAE--QISWYKPWTKTLENKH-SPSTRWFVEGMLNICYNAVdRHIENGkgDKIAIIYDSpvTNTKATFT 145
Cdd:cd05943 26 SVDDPGAFWAAVWDfsGVRGSKPYDVVVVSGRiMPGARWFPGARLNYAENLL-RHADAD--DPAAIYAAE--DGERTEVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 146 YKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFG 225
Cdd:cd05943 101 WAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 226 IEPGRRveyVPLVEEALKIGQHKPDKI------LIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYILYT 299
Cdd:cd05943 181 TYNGKR---HDVREKVAELVKGLPSLLavvvvpYTVAAGQPDLSKIAKALTLEDFLATGAAGELEFEPLPFDHPLYILYS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 300 SGTTGLPKGVIRPTGGY------AVMLHWSMssiyglQPGEVWWAASDLGWVVGHSYIcyGPLLHGNTTVLYEGKPvGTP 373
Cdd:cd05943 258 SGTTGLPKCIVHGAGGTllqhlkEHILHCDL------RPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGSP-FYP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 374 DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW-SKNVFRvpvlDHWWQTE 452
Cdd:cd05943 329 DTNALWDLADEEGITVFGTSAKYLDALEKA--GLKPAETHDLSSLRTILSTGSPLKPESFDYvYDHIKP----DVLLASI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 453 TGSPITASCVGLGNSKTPP-PGQAGKSVPGYNVMILDDNMQKLKARcLGNIVVKLPLP--PGAFsglWKNQEA--FKHLY 527
Cdd:cd05943 403 SGGTDIISCFVGGNPLLPVyRGEIQCRGLGMAVEAFDEEGKPVWGE-KGELVCTKPFPsmPVGF---WNDPDGsrYRAAY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 528 FEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDP-LKGHVPLALcVLRK 606
Cdd:cd05943 479 FAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKdGDERVILFV-KLRE 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13375727 607 DINATEEqVLEEIVKHVRQNIGPvaafR---NAVF-VKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDP 673
Cdd:cd05943 558 GVELDDE-LRKRIRSTIRSALSP----RhvpAKIIaVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANP 623
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
69-663 |
8.58e-62 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 218.13 E-value: 8.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 69 SVTDPERFWGKAAE--QISWYKPWTKTLENKHSPSTRWFVEGMLNICYNAVdRHienGKGDKIAIIYDSPvTNTKATFTY 146
Cdd:PRK03584 43 SVEDLEAFWQSVWDffGVIGSTPYTVVLAGRRMPGARWFPGARLNYAENLL-RH---RRDDRPAIIFRGE-DGPRRELSW 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 147 KEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA---S 223
Cdd:PRK03584 118 AELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVdgyR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 224 FGiepGRRVEYVPLVEE---ALKIGQHkpdkILIYNRPNMEAVPLAPGRDLDWDE--EMAKAQSHDCVPVLSEHPLYILY 298
Cdd:PRK03584 198 YG---GKAFDRRAKVAElraALPSLEH----VVVVPYLGPAAAAAALPGALLWEDflAPAEAAELEFEPVPFDHPLWILY 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 299 TSGTTGLPKGVIRPTGG------YAVMLHWsmssiyGLQPGE-VWWAASdLGW------VVGhsyicygpLLHGNTTVLY 365
Cdd:PRK03584 271 SSGTTGLPKCIVHGHGGillehlKELGLHC------DLGPGDrFFWYTT-CGWmmwnwlVSG--------LLVGATLVLY 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 366 EGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW-SKNVFRvpv 444
Cdd:PRK03584 336 DGSP-FYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKA--GLVPGETHDLSALRTIGSTGSPLPPEGFDWvYEHVKA--- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 445 lDHWWQTETGSPITASCVGLGNSKTPP-PGQAGKSVPGYNVMILDDNMQKLKARcLGNIVVKLPLP--PgafSGLW--KN 519
Cdd:PRK03584 410 -DVWLASISGGTDICSCFVGGNPLLPVyRGEIQCRGLGMAVEAWDEDGRPVVGE-VGELVCTKPFPsmP---LGFWndPD 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 520 QEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAG-------AIEEsilshgtVADCAVVGKEDP 592
Cdd:PRK03584 485 GSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAeiyrqveALPE-------VLDSLVIGQEWP 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13375727 593 LKG-HVPLaLCVLRKDINATEEqVLEEIVKHVRQNIGP--VAAfrNAVFVKQLPKTRSGKIPRSALSAIVNGKP 663
Cdd:PRK03584 558 DGDvRMPL-FVVLAEGVTLDDA-LRARIRTTIRTNLSPrhVPD--KIIAVPDIPRTLSGKKVELPVKKLLHGRP 627
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
126-655 |
9.22e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 215.05 E-value: 9.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAiiydspVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI-HSL-IFggFA 203
Cdd:PRK06187 20 PDKEA------VYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVlHPInIR--LK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 204 SKELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPgrdlDWDEEMAKAQSH 283
Cdd:PRK06187 92 PEEIAYILNDAEDRVVLVDS---------EFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVG----EYEELLAAASDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 284 DCVPVLSEHPLY-ILYTSGTTGLPKGVIrptggYA---VMLHwSMSSIYGLQpgevwWAASDLGWVV---GHSY---ICY 353
Cdd:PRK06187 159 FDFPDIDENDAAaMLYTSGTTGHPKGVV-----LShrnLFLH-SLAVCAWLK-----LSRDDVYLVIvpmFHVHawgLPY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 354 GPLLHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETL 433
Cdd:PRK06187 228 LALMAGAKQVI-----PRRFDPENLLDLIETERVTFFFAVPTIWQMLLK----APRAYFVDFSSLRLVIYGGAALPPALL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 434 EWSKNVFRVPVLDHWWQTETGSPITAScvglgnsktPPPGQ----------AGKSVPGYNVMILDDNMQKLKARC--LGN 501
Cdd:PRK06187 299 REFKEKFGIDLVQGYGMTETSPVVSVL---------PPEDQlpgqwtkrrsAGRPLPGVEARIVDDDGDELPPDGgeVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 502 IVVKlplPPGAFSGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGT 580
Cdd:PRK06187 370 IIVR---GPWLMQGYWNRPEATA----ETIDgGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPA 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13375727 581 VADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK06187 443 VAEVAVIGVPDEKWGERPVAVVVLKPGATLDA----KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
123-655 |
4.60e-59 |
|
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: 207.70 E-value: 4.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 123 NGKGDKIaiiydspvtntkaTFTYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIhsLIFGG 201
Cdd:cd05928 34 NGKGDEV-------------KWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLV--FIPGT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 202 --FASKELSSRIDHVKPKVVVTASfgiEPGRRVEYVPLVEEALKIgqhkpdKILIYNRPnmeavplapgRD--LDWDEEM 277
Cdd:cd05928 99 iqLTAKDILYRLQASKAKCIVTSD---ELAPEVDSVASECPSLKT------KLLVSEKS----------RDgwLNFKELL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 278 AKA-QSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPL 356
Cdd:cd05928 160 NEAsTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 357 LHGNTTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWS 436
Cdd:cd05928 240 IQGACVFVHHLPRF---DPLVILKTLSSYPITTFCGAPTVYRMLVQQDL-----SSYKFPSLQHCVTGGEPLNPEVLEKW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 437 KNVFRVPVLDHWWQTETGspitascVGLGNSKTP--PPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKL-PLPP-GA 512
Cdd:cd05928 312 KAQTGLDIYEGYGQTETG-------LICANFKGMkiKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVkPIRPfGL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 513 FSGLWKNQEAFKHLYFEKFpgyYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDP 592
Cdd:cd05928 385 FSGYVDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13375727 593 LKGHVPLALCVLRKDINATE-EQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05928 462 IRGEVVKAFVVLAPQFLSHDpEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
125-655 |
3.22e-50 |
|
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: 181.99 E-value: 3.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 125 KGDKIAIIydspvtNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI---HSLIFGG 201
Cdd:cd05936 12 FPDKTALI------FMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvpLNPLYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 202 fasKELSSRIDHVKPKVVVTA-SFgiepgrrveyvplvEEALKIGqhkpdkiliynrpnmEAVPLAPGRDLDwdeemaka 280
Cdd:cd05936 86 ---RELEHILNDSGAKALIVAvSF--------------TDLLAAG---------------APLGERVALTPE-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 281 qshD-CVpvlsehplyILYTSGTTGLPKGVirptggyavML-HWSMSSIygLQPGEVWWAASDLGwvvGHSYICYGPLLH 358
Cdd:cd05936 126 ---DvAV---------LQYTSGTTGVPKGA---------MLtHRNLVAN--ALQIKAWLEDLLEG---DDVVLAALPLFH 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 359 --------------GNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGaalgKQYSLTRFKTLFVA 424
Cdd:cd05936 180 vfgltvalllplalGATIVL-----IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEF----KKRDFSSLRLCISG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 425 GERCDVETLEWSKNVFRVPVLDHWWQTETgSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVV 504
Cdd:cd05936 251 GAPLPVEVAERFEELTGVPIVEGYGLTET-SPVVAVNPLDGPRK---PGSIGIPLPGTEVKIVDDDGEELPPGEVGELWV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 505 KlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADC 584
Cdd:cd05936 327 R---GPQVMKGYWNRPEETAEAFVD---GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEA 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13375727 585 AVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05936 401 AVVGVPDPYSGEAVKAFVVLKEGASLTE----EEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
144-655 |
8.95e-50 |
|
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: 179.41 E-value: 8.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAs 223
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 224 fgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdcvpvlsehPLYILYTSGTT 303
Cdd:cd05934 83 ---------------------------------------------------------------------PASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 304 GLPKGVIRPtggYAVMLHW--SMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEgkpvgTPDAGAYFRV 381
Cdd:cd05934 94 GPPKGVVIT---HANLTFAgyYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP-----RFSASRFWSD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 382 LAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTRFKTLFVAGERCDVETlEWSKNvFRVPVLDHWWQTETGSPITASC 461
Cdd:cd05934 166 VRRYGATVTNYLGAMLSYLLAQPPSP----DDRAHRLRAAYGAPNPPELHE-EFEER-FGVRLLEGYGMTETIVGVIGPR 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 462 VGlgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEA----FKHlyfekfpGYYDT 537
Cdd:cd05934 240 DE-----PRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWGFFKGYYNMPEAtaeaMRN-------GWFHT 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 538 MDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlE 617
Cdd:cd05934 308 GDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDP----E 383
|
490 500 510
....*....|....*....|....*....|....*...
gi 13375727 618 EIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05934 384 ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
114-655 |
1.10e-48 |
|
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: 178.72 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 114 YNA---VDRHIENGKGDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACAR 190
Cdd:cd05959 3 YNAatlVDLNLNEGRGDKTAFIDDA------GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 191 IGAIHSLIFGGFASKELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIGQHKpDKILIYNRPNMEAVPLAPGRD 270
Cdd:cd05959 77 AGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG---------ELAPVLAAALTKSEHT-LVVLIVSGGAGPEAGALLLAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 271 L--DWDEEMAKAQSHdcvpvlSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGH 348
Cdd:cd05959 147 LvaAEAEQLKPAATH------ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 349 SYICYGPLLHGNTTVLYEGKPvgTPDAgaYFRVLAEHGVAALFTAPTaIRAIRQQDPGAalgKQYSLTRFKTLFVAGERC 428
Cdd:cd05959 221 GNSLTFPLSVGATTVLMPERP--TPAA--VFKRIRRYRPTVFFGVPT-LYAAMLAAPNL---PSRDLSSLRLCVSAGEAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 429 DVETLEWSKNVFRVPVLDHWWQTETGSpitascVGLGNskTP---PPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVK 505
Cdd:cd05959 293 PAEVGERWKARFGLDILDGIGSTEMLH------IFLSN--RPgrvRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 506 lplPPGAFSGLWKNQEAFKhlyfEKFPGY-YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADC 584
Cdd:cd05959 365 ---GPSSATMYWNNRDKTR----DTFQGEwTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEA 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13375727 585 AVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05959 438 AVVGVEDEDGLTKPKAFVVLRPGYEDSEA-LEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
137-656 |
4.43e-47 |
|
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: 173.65 E-value: 4.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 137 VTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKP 216
Cdd:cd05926 8 VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 217 KVVVTASFGIEP---GRRVEYVPLVEEALkigqhkpDKILIYNRPNMEAVPLAPGrDLDWDEEMAKAQSHDcvPVLsehp 293
Cdd:cd05926 88 KLVLTPKGELGPasrAASKLGLAILELAL-------DVGVLIRAPSAESLSNLLA-DKKNAKSEGVPLPDD--LAL---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 294 lyILYTSGTTGLPKGV-IRPTggyavMLHWSMSSI---YGLQPgevwwaaSDLGWVVGhsyicygPLLHGN-------TT 362
Cdd:cd05926 154 --ILHTSGTTGRPKGVpLTHR-----NLAASATNItntYKLTP-------DDRTLVVM-------PLFHVHglvasllST 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 363 VLYEGKPVGTP--DAGAYFRVLAEHGvAALFTA-PTaIRAIRQQDPGAALGKQYSLTRFktLFVAGERCDVETLEWSKNV 439
Cdd:cd05926 213 LAAGGSVVLPPrfSASTFWPDVRDYN-ATWYTAvPT-IHQILLNRPEPNPESPPPKLRF--IRSCSASLPPAVLEALEAT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 440 FRVPVLDHWWQTETGSPITASCVglgNSKTPPPGQAGKSVpGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKN 519
Cdd:cd05926 289 FGAPVLEAYGMTEAAHQMTSNPL---PPGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLR---GPNVTRGYLNN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 520 QEAFKHlYFEKFpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPL 599
Cdd:cd05926 362 PEANAE-AAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVA 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 600 ALCVLRKDINATEeqvlEEIVKHVRQNIgpvAAF---RNAVFVKQLPKTRSGKIPRSALS 656
Cdd:cd05926 440 AAVVLREGASVTE----EELRAFCRKHL---AAFkvpKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
127-650 |
4.78e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 174.35 E-value: 4.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 206
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 LSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKigQHKPDKILiynRPNMEAVPLAPGRDLDWDEeMAKAQS--HD 284
Cdd:PRK08316 100 LAYILDHSGARAFLVDP---------ALAPTAEAALA--LLPVDTLI---LSLVLGGREAPGGWLDFAD-WAEAGSvaEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 285 CVPVLSEHPLYILYTSGTTGLPKGvirptggyAVMLHWS-----MSSIYGLQpgevwWAASDlgwVVGHS---YIC---- 352
Cdd:PRK08316 165 DVELADDDLAQILYTSGTESLPKG--------AMLTHRAliaeyVSCIVAGD-----MSADD---IPLHAlplYHCaqld 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 353 --YGPLLH-GNTTVLYEGkpvgtPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPGaalgkQYSLTRFKTLFVAGERC 428
Cdd:PRK08316 229 vfLGPYLYvGATNVILDA-----PDPELILRTIEAERITSFFAPPTVwISLLRHPDFD-----TRDLSSLRKGYYGASIM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 429 DVETLEWSKNvfRVPVLDHW---WQTETGSPITAscvgLGnsktpP------PGQAGKsvPGYNV--MILDDNMQKLKAR 497
Cdd:PRK08316 299 PVEVLKELRE--RLPGLRFYncyGQTEIAPLATV----LG-----PeehlrrPGSAGR--PVLNVetRVVDDDGNDVAPG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 498 CLGNIVVKlplPPGAFSGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEE 573
Cdd:PRK08316 366 EVGEIVHR---SPQLMLGYWDDpektAEAFRG-------GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13375727 574 SILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 650
Cdd:PRK08316 436 ALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE----DELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
127-655 |
8.34e-47 |
|
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: 171.94 E-value: 8.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIhslifggfaske 206
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 lssridhvkpkvvvtasfgiepgrrveYVPLveealkigqhkpdkiliynrpnmeavplapgrDLDWDEEMAKAQSHDCV 286
Cdd:cd05930 64 ---------------------------YVPL--------------------------------DPSYPAERLAYILEDSG 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 287 PVL----SEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTT 362
Cdd:cd05930 85 AKLvltdPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVLQFTSFSFDVSVWEI-FGALLAGATL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 363 VLYEGKPVGTPDAgaYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqyslTRFKTLFVAGERCDVETLE-WSKNVFR 441
Cdd:cd05930 163 VVLPEEVRKDPEA--LADLLAEEGITVLHLTPSLLRLLLQELELAAL------PSLRLVLVGGEALPPDLVRrWRELLPG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 442 VPVLDHWWQTETGSPITASCVGLGN-SKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW--- 517
Cdd:cd05930 235 ARLVNLYGPTEATVDATYYRVPPDDeEDGRVP--IGRPIPNTRVYVLDENLR--------------PVPPGVPGELYigg 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 518 ------------KNQEAFKHLYFekFPG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVAD 583
Cdd:cd05930 299 aglargylnrpeLTAERFVPNPF--GPGerMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVRE 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13375727 584 CAVVGKEDPLKGHVPLALCVLRKDinatEEQVLEEIVKHVRQNIGPV---AAFrnaVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05930 377 AAVVAREDGDGEKRLVAYVVPDEG----GELDEEELRAHLAERLPDYmvpSAF---VVLDALPLTPNGKVDRKAL 444
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
143-655 |
1.57e-45 |
|
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: 168.04 E-value: 1.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLV-KHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 221
Cdd:cd05958 10 EWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 AsfgiepgrrveyvplveEALKigqhKPDKILIYNrpnmeavplapgrdldwdeemakaqshdcvpvlsehplyilYTSG 301
Cdd:cd05958 90 A-----------------HALT----ASDDICILA-----------------------------------------FTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 302 TTGLPKGVIRPTGGY-AVMLHWSMSsIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKpvgTPDAgaYFR 380
Cdd:cd05958 108 TTGAPKATMHFHRDPlASADRYAVN-VLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA---TPDL--LLS 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 381 VLAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETgspitas 460
Cdd:cd05958 182 AIARYKPTVLFTAPTAYRAMLAHPDAA----GPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEM------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 461 cVGLGNSKTPP---PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlppgafSGLWKNQEAFKHLYFEKfpGYYDT 537
Cdd:cd05958 251 -FHIFISARPGdarPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCRYLADKRQRTYVQG--GWNIT 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 538 MDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDInATEEQVLE 617
Cdd:cd05958 322 GDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGV-IPGPVLAR 400
|
490 500 510
....*....|....*....|....*....|....*...
gi 13375727 618 EIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05958 401 ELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
127-662 |
1.94e-43 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 163.21 E-value: 1.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDspvtNTKATFtyKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 206
Cdd:PRK03640 17 DRTAIEFE----EKKVTF--MELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 LSSRIDHVKPKVVVTASfGIEPGRRVEYVPLVEEAlkigqhkpdkiliynrPNMEAVPLAPGRDLDWDEEMAkaqshdcv 286
Cdd:PRK03640 91 LLWQLDDAEVKCLITDD-DFEAKLIPGISVKFAEL----------------MNGPKEEAEIQEEFDLDEVAT-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 287 pvlsehplyILYTSGTTGLPKGVIRPTGGyavmlHW--SMSSI--YGLQPGEVWWAASDLGWVVGHSyICYGPLLHGNTT 362
Cdd:PRK03640 146 ---------IMYTSGTTGKPKGVIQTYGN-----HWwsAVGSAlnLGLTEDDCWLAAVPIFHISGLS-ILMRSVIYGMRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 363 VLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTrFKTLFVAGERCDVETLEWSKNvFRV 442
Cdd:PRK03640 211 VLVE-----KFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEG----TYPSS-FRCMLLGGGPAPKPLLEQCKE-KGI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 443 PVLDHWWQTETGSPITascvglgnskTPPP-------GQAGKSVPGYNVMILDDNmQKLKARCLGNIVVKLP-LPPGAFS 514
Cdd:PRK03640 280 PVYQSYGMTETASQIV----------TLSPedaltklGSAGKPLFPCELKIEKDG-VVVPPFEEGEIVVKGPnVTKGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 515 GLWKNQEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLK 594
Cdd:PRK03640 349 REDATRETFQD-------GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKW 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13375727 595 GHVPLALCVLRKDINateeqvLEEIVKHVRQNIG----PVAAFrnavFVKQLPKTRSGKIPRSALSAIVNGK 662
Cdd:PRK03640 422 GQVPVAFVVKSGEVT------EEELRHFCEEKLAkykvPKRFY----FVEELPRNASGKLLRHELKQLVEEM 483
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
126-655 |
4.77e-43 |
|
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: 162.79 E-value: 4.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIyDSPvtnTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 205
Cdd:cd05904 19 PSRPALI-DAA---TGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 ELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKigqhkpdKILIYNRPnmEAVPLAPGRDLDWDEEMAKAQshdc 285
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTA---------ELAEKLASLAL-------PVVLLDSA--EFDSLSFSDLLFEADEAEPPV---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 286 VPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVM---LHWSMSSiyGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTT 362
Cdd:cd05904 153 VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMvaqFVAGEGS--NSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 363 VLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF-R 441
Cdd:cd05904 231 VV-----MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKS----PIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 442 VPVLDHWWQTETgSPITASCVGLGNSKTPPpGQAGKSVPGYNVMILDdnmqklkarclgnIVVKLPLPPGaFSG-LW--- 517
Cdd:cd05904 302 VDLGQGYGMTES-TGVVAMCFAPEKDRAKY-GSVGRLVPNVEAKIVD-------------PETGESLPPN-QTGeLWirg 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 518 --------KNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGK 589
Cdd:cd05904 366 psimkgylNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPY 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13375727 590 EDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVrqniGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05904 444 PDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQV----APYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
143-655 |
4.70e-42 |
|
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: 158.39 E-value: 4.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 222
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 sfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwDEEMAkaqshdcvpvlsehplYILYTSGT 302
Cdd:cd05919 90 ---------------------------------------------------ADDIA----------------YLLYSSGT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 303 TGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDL--GWVVGHSYIcyGPLLHGNTTVLYEGKPvgtpDAGAYFR 380
Cdd:cd05919 103 TGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNSLW--FPLAVGASAVLNPGWP----TAERVLA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 381 VLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITAS 460
Cdd:cd05919 177 TLARFRPTVLYGVPTFYANLLDS----CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSN 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 461 CVGLGNsktppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlppGAFSGLWKNQEAFKHLYFEkfpGYYDTMDA 540
Cdd:cd05919 253 RPGAWR-----LGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGP---SAAVGYWNNPEKSRATFNG---GWYRTGDK 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 541 GYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDpLKGHVPLALCVLRKDINATEEQVLEEIV 620
Cdd:cd05919 322 FCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPE-STGLSRLTAFVVLKSPAAPQESLARDIH 400
|
490 500 510
....*....|....*....|....*....|....*
gi 13375727 621 KHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05919 401 RHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
145-586 |
4.72e-41 |
|
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: 154.73 E-value: 4.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVK-HGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASkelsSRIDHV----KPKVV 219
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA----ERLAFIledaGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 220 VTASfgiepgrrvEYVPLVEEalkigqhkpdkiliynrpnMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYILYT 299
Cdd:TIGR01733 77 LTDS---------ALASRLAG-------------------LVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 300 SGTTGLPKGVIRPTGGyAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLYEGKPVGtPDAGAYF 379
Cdd:TIGR01733 129 SGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEI-FGALLAGATLVVPPEDEER-DDAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 380 RVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERCDVETLE-WSKNVFRVPVLDHWWQTET--GSP 456
Cdd:TIGR01733 206 ALIAEHPVTVLNLTPSLLALLAAALPPA-------LASLRLVILGGEALTPALVDrWRARGPGARLINLYGPTETtvWST 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 457 ITASCVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVklpLPPGAFSGLW----KNQEAFK-HLYF-EK 530
Cdd:TIGR01733 279 ATLVDPDDAPRESPVP--IGRPLANTRLYVLDDDLRPVPVGVVGELYI---GGPGVARGYLnrpeLTAERFVpDPFAgGD 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 13375727 531 FPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAV 586
Cdd:TIGR01733 354 GARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
143-650 |
7.65e-41 |
|
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: 154.85 E-value: 7.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTa 222
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 sfgiePGRrveyvplveealkIGQHKPdkiliynrpnmEAVPLAPGrdldwdeemakaqshdcvpvlsehplYILYTSGT 302
Cdd:cd05903 80 -----PER-------------FRQFDP-----------AAMPDAVA--------------------------LLLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 303 TGLPKGVIRPtggyAVMLHWSMSSI---YGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEgkpVGTPDAGAyf 379
Cdd:cd05903 105 TGEPKGVMHS----HNTLSASIRQYaerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IWDPDKAL-- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 380 RVLAEHGVAALFTAPT----AIRAIRQQDPgaalgkqySLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGS 455
Cdd:cd05903 176 ALMREHGVTFMMGATPfltdLLNAVEEAGE--------PLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 456 pitascvGLGNSKTPPPGQA----GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQeafkHLYFEKF 531
Cdd:cd05903 248 -------AVTSITPAPEDRRlytdGRPLPGVEIKVVDDTGATLAPGVEGELLSR---GPSVFLGYLDRP----DLTADAA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 532 P-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINA 610
Cdd:cd05903 314 PeGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALL 393
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 13375727 611 TeeqvLEEIVKHV-RQNIGPVAAFRNAVFVKQLPKTRSGKI 650
Cdd:cd05903 394 T----FDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
142-655 |
4.59e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 151.85 E-value: 4.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 142 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 221
Cdd:PRK07786 41 NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 ASF--GIEPGRRvEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEemakaqshdcvpvlsehPLYILYT 299
Cdd:PRK07786 121 EAAlaPVATAVR-DIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDS-----------------PALIMYT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 300 SGTTGLPKGvirptggyAVMLHWSMSS-----IYGLQ---PGEVWWAASDLGWVVGHSYICYGPLLhGNTTVLYegkPVG 371
Cdd:PRK07786 183 SGTTGRPKG--------AVLTHANLTGqamtcLRTNGadiNSDVGFVGVPLFHIAGIGSMLPGLLL-GAPTVIY---PLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 372 TPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlGKQYSLtRFKTlFVAGERCDVETLEWSKNVFRVPVLDHWWQT 451
Cdd:PRK07786 251 AFDPGQLLDVLEAEKVTGIFLVPAQWQAV-CAEQQAR-PRDLAL-RVLS-WGAAPASDTLLRQMAATFPEAQILAAFGQT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 452 ETgSPITasCVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKhlyfEKF 531
Cdd:PRK07786 327 EM-SPVT--CMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR---APTLMSGYWNNPEATA----EAF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 532 PG-YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdiNA 610
Cdd:PRK07786 397 AGgWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVR---ND 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 13375727 611 TEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK07786 474 DAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
144-657 |
6.43e-39 |
|
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: 149.26 E-value: 6.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHvkpkvvvtas 223
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 224 fgiepGRRVeyVPLVEEAlkigQHKPDKILIYnrpnmeavplapgrdldwdeemakaqshdcvpvlsehplyilYTSGTT 303
Cdd:cd05974 71 -----GGAV--YAAVDEN----THADDPMLLY------------------------------------------FTSGTT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 304 GLPKGVIRPTGGYAVMlHWSMSSIYGLQPGEVWWAASDLGWVvGHSYIC-YGPLLHGNTTVLYEGKPVgtpDAGAYFRVL 382
Cdd:cd05974 98 SKPKLVEHTHRSYPVG-HLSTMYWIGLKPGDVHWNISSPGWA-KHAWSCfFAPWNAGATVFLFNYARF---DAKRVLAAL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 383 AEHGVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKT----LFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPIt 458
Cdd:cd05974 173 VRYGVTTLCAPPTVWRMLIQQD----------LASFDVklreVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALV- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 459 ascvglGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKArclGNIVVKL--PLPPGAFSGLWKNQEAFKHLYFEkfpGY 534
Cdd:cd05974 242 ------GNSPGQPvkAGSMGRPLPGYRVALLDPDGAPATE---GEVALDLgdTRPVGLMKGYAGDPDKTAHAMRG---GY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 535 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQ 614
Cdd:cd05974 310 YRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPET 389
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 13375727 615 VLeEIVKHVRQNIGPVAAFRNAVFVkQLPKTRSGKIPRSALSA 657
Cdd:cd05974 390 AL-EIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRR 430
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
115-657 |
4.48e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 148.60 E-value: 4.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 115 NAVDRHiengkGDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQA----MYTMLACAR 190
Cdd:PRK06188 20 SALKRY-----PDRPALVLGD------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVlmaiGAAQLAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 191 IGAIHSLifggfaskelSSRIDHVkpkvVVTASFGIEpGRRVEYVPLVEEALKIGQHKPdkiliyNRPNMEAV-PLAPGR 269
Cdd:PRK06188 89 RTALHPL----------GSLDDHA----YVLEDAGIS-TLIVDPAPFVERALALLARVP------SLKHVLTLgPVPDGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 270 DLdwdeeMAKAQSHDCVPVLSEH----PLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSsiyglqpgevwwaasDLGWV 345
Cdd:PRK06188 148 DL-----LAAAAKFGPAPLVAAAlppdIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLA---------------EWEWP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 346 VGHSYICYGPLLH------------GNTTVLYEGKpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqY 413
Cdd:PRK06188 208 ADPRFLMCTPLSHaggafflptllrGGTVIVLAKF-----DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRT----R 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 414 SLTRFKTLFVAGERCD----VETLEWSKNVFrvpvLDHWWQTETGSPIT---------------ASCvglgnsktpppgq 474
Cdd:PRK06188 279 DLSSLETVYYGASPMSpvrlAEAIERFGPIF----AQYYGQTEAPMVITylrkrdhdpddpkrlTSC------------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 475 aGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGafsGLWK----NQEAFKHlyfekfpGYYDTMDAGYMDEEGYLY 550
Cdd:PRK06188 342 -GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMD---GYWNrpeeTAEAFRD-------GWLHTGDVAREDEDGFYY 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 551 VMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPV 630
Cdd:PRK06188 411 IVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA----AELQAHVKERKGSV 486
|
570 580
....*....|....*....|....*..
gi 13375727 631 AAFRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:PRK06188 487 HAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
126-655 |
1.05e-37 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 148.95 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIY--DSPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIG---AIHSLIFG 200
Cdd:PRK07529 39 PDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGianPINPLLEP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 201 GfaskELSSRIDHVKPKVVVTAsfGIEPGRRV-EYVPLVEEALKIGQHkpdkILIYN------RPNMEAVPL----APGR 269
Cdd:PRK07529 119 E----QIAELLRAAGAKVLVTL--GPFPGTDIwQKVAEVLAALPELRT----VVEVDlarylpGPKRLAVPLirrkAHAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 270 DLDWDEEMAK--AQSHDCVPVLSEHPLYILY-TSGTTGLPKGVIRPTGGYAVMlHWSMSSIYGLQPGEVWWAASDLGWVV 346
Cdd:PRK07529 189 ILDFDAELARqpGDRLFSGRPIGPDDVAAYFhTGGTTGMPKLAQHTHGNEVAN-AWLGALLLGLGPGDTVFCGLPLFHVN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 347 GHSYICYGPLLHGNTTVLyeGKPVGTPDAGAY---FRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKTLFV 423
Cdd:PRK07529 268 ALLVTGLAPLARGAHVVL--ATPQGYRGPGVIanfWKIVERYRINFLSGVPTVYAALLQVPVDGH-----DISSLRYALC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 424 AGERCDVETLEWSKNVFRVPVLDHWWQTEtgspitASCVglgNSKTPP-----PGQAGKSVPGYNV--MILDDN---MQK 493
Cdd:PRK07529 341 GAAPLPVEVFRRFEAATGVRIVEGYGLTE------ATCV---SSVNPPdgerrIGSVGLRLPYQRVrvVILDDAgryLRD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 494 LKARCLGNIVVKlplPPGAFSGlWKNQEAFKHLYFEkfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEE 573
Cdd:PRK07529 412 CAVDEVGVLCIA---GPNVFSG-YLEAAHNKGLWLE--DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 574 SILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAV-FVKQLPKTRSGKIPR 652
Cdd:PRK07529 486 ALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLA----FARDHIAERAAVPKHVrILDALPKTAVGKIFK 561
|
...
gi 13375727 653 SAL 655
Cdd:PRK07529 562 PAL 564
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
144-658 |
2.42e-37 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 146.83 E-value: 2.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAS 223
Cdd:PRK06155 47 WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 224 FGIEpgrRVEYVPLVEEALKigqhkpdKILIYNRPNMEAVPLAPgrdlDWDEEMAKAQSHDCVPVLSEHPLYILYTSGTT 303
Cdd:PRK06155 127 ALLA---ALEAADPGDLPLP-------AVWLLDAPASVSVPAGW----STAPLPPLDAPAPAAAVQPGDTAAILYTSGTT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 304 GLPKGVIRPTGGYavmlhwsmssiyglqpgeVWW---AASDLGWVVGHSYICYGPLLHGNT------TVLYEGKPVGTP- 373
Cdd:PRK06155 193 GPSKGVCCPHAQF------------------YWWgrnSAEDLEIGADDVLYTTLPLFHTNAlnaffqALLAGATYVLEPr 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 374 -DAGAYFRVLAEHGvAALFTAPTAIRAIRQQDPGAALGKQYSLT---------RFKTLFvaGERcdvetlewsknvFRVP 443
Cdd:PRK06155 255 fSASGFWPAVRRHG-ATVTYLLGAMVSILLSQPARESDRAHRVRvalgpgvpaALHAAF--RER------------FGVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 444 VLDHWWQTETGSPITAScvglgnSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAF-SGLW----K 518
Cdd:PRK06155 320 LLDGYGSTETNFVIAVT------HGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAD-EPFAFaTGYFgmpeK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 519 NQEAFKHLYFEkfpgyydTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVP 598
Cdd:PRK06155 393 TVEAWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13375727 599 LALCVLRkdinatEEQVLE--EIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 658
Cdd:PRK06155 466 MAAVVLR------DGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
144-655 |
2.00e-35 |
|
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: 140.84 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI-HSLIFGGFAsKELSSRIDHVKPKVVVta 222
Cdd:cd12119 26 YTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHTINPRLFP-EQIAYIINHAEDRVVF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 sfgIEPgrrvEYVPLVEEALkiGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEH-PLYILYTSG 301
Cdd:cd12119 103 ---VDR----DFLPLLEAIA--PRLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPDFDENtAAAICYTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 302 TTGLPKGVIrptggY---AVMLHwSMSSiygLQPGEVWWAASDlgwvvghSYICYGPLLHGN------TTVLYEGK---P 369
Cdd:cd12119 174 TTGNPKGVV-----YshrSLVLH-AMAA---LLTDGLGLSESD-------VVLPVVPMFHVNawglpyAAAMVGAKlvlP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 370 VGTPDAGAYFRVLAEHGVAalFTA--PTAIRAIRQQdPGAALGKQYSLTRfktLFVAGERCDVETLEWsknvFR---VPV 444
Cdd:cd12119 238 GPYLDPASLAELIEREGVT--FAAgvPTVWQGLLDH-LEANGRDLSSLRR---VVIGGSAVPRSLIEA----FEergVRV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 445 LDHWWQTETgSPI-TASCVGLGNSKTPPPGQA------GKSVPGYNVMILDDNMQKLKA--RCLGNIVVKLP-LPPGAFs 514
Cdd:cd12119 308 IHAWGMTET-SPLgTVARPPSEHSNLSEDEQLalrakqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPwVTKSYY- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 515 glwKNQEAfKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLK 594
Cdd:cd12119 386 ---KNDEE-SEALTED--GWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKW 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13375727 595 GHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd12119 460 GERPLAVVVLKEGATVTA----EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
145-655 |
4.00e-35 |
|
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: 138.38 E-value: 4.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASf 224
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 225 giepgrrveyvplveealkigqhkpdkiliynrpNMEAVPLAPgrdldwdeemakaqshdcvpvlsehplyilYTSGTTG 304
Cdd:cd05935 82 ----------------------------------ELDDLALIP------------------------------YTSGTTG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 305 LPKGVIRpTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLyegkpVGTPDAGAYFRVLAE 384
Cdd:cd05935 98 LPKGCMH-THFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL-----MARWDRETALELIEK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 385 HGVAALFTAPTAIRAIrQQDPGAalgKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITascvgl 464
Cdd:cd05935 172 YKVTFWTNIPTMLVDL-LATPEF---KTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTH------ 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 465 gnskTPPPGQAGKS---VPGYNV--MILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWK----NQEAFKHLYFEKFpgy 534
Cdd:cd05935 242 ----TNPPLRPKLQclgIP*FGVdaRVIDiETGRELPPNEVGEIVVR---GPQIFKGYWNrpeeTEESFIEIKGRRF--- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 535 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQ 614
Cdd:cd05935 312 FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTE 391
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 13375727 615 vlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05935 392 --EDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
127-657 |
4.91e-35 |
|
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: 143.07 E-value: 4.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMP----MIPqamyTMLACARIGAihslifggf 202
Cdd:COG1020 491 DAVAVVFGD------QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLErsleMVV----ALLAVLKAGA--------- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 203 askelssridhvkpkvvvtAsfgiepgrrveYVPL------------VEEAlkigqhKPdKILIYNRPNMEAVPLAPGRD 270
Cdd:COG1020 552 -------------------A-----------YVPLdpaypaerlaymLEDA------GA-RLVLTQSALAARLPELGVPV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 271 LDWDEEMAKAQSHD--CVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGH 348
Cdd:COG1020 595 LALDALALAAEPATnpPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAW-MQRRYGLGPGDRVLQFASLSFDASV 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 349 SYIcYGPLLHGNTTVLYEgkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERC 428
Cdd:COG1020 674 WEI-FGALLSGATLVLAP--PEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEA-------LPSLRLVLVGGEAL 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 429 DVETLE-WSKNVFRVPVLDHWWQTETGspITASCvglgnSKTPPPGQAGKSVP------GYNVMILDDNMQklkarclgn 501
Cdd:COG1020 744 PPELVRrWRARLPGARLVNLYGPTETT--VDSTY-----YEVTPPDADGGSVPigrpiaNTRVYVLDAHLQ--------- 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 502 ivvklPLPPGAfSG-LW---------------KNQEAFKHLYFEkFPG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAG 563
Cdd:COG1020 808 -----PVPVGV-PGeLYiggaglargylnrpeLTAERFVADPFG-FPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 564 HRISAGAIEESILSHGTVADCAVVGKEDPLkGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFrnaVFVKQLP 643
Cdd:COG1020 881 FRIELGEIEAALLQHPGVREAVVVAREDAP-GDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAV---VLLLPLP 956
|
570
....*....|....
gi 13375727 644 KTRSGKIPRSALSA 657
Cdd:COG1020 957 LTGNGKLDRLALPA 970
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
126-652 |
1.02e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 139.02 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfask 205
Cdd:PRK07470 21 PDRIALVWGD------RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 elssridhvkpkVVVTASFGIEPGrrveyvplveEALKIGQHKPDKILIYNRPNMEAVPL---------------APGRD 270
Cdd:PRK07470 83 ------------VWVPTNFRQTPD----------EVAYLAEASGARAMICHADFPEHAAAvraaspdlthvvaigGARAG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 271 LDWDEEMAKAQSHDCVPVLSEH--PLYILYTSGTTGLPKGvirptggyAVMLHWSMSSIYG-----LQPGEvwwAASDLG 343
Cdd:PRK07470 141 LDYEALVARHLGARVANAAVDHddPCWFFFTSGTTGRPKA--------AVLTHGQMAFVITnhladLMPGT---TEQDAS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 344 WVVGhsyicygPLLHGN------------TTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTaIRAIRQQDPGAALGK 411
Cdd:PRK07470 210 LVVA-------PLSHGAgihqlcqvargaATVLLPSERF---DPAEVWALVERHRVTNLFTVPT-ILKMLVEHPAVDRYD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 412 QYSLtrfKTLFVAGE---RCDvetlewSKNVFRV--PVLDHWWqtetgspitascvGL----GNSKTPPP---------- 472
Cdd:PRK07470 279 HSSL---RYVIYAGApmyRAD------QKRALAKlgKVLVQYF-------------GLgevtGNITVLPPalhdaedgpd 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 473 ---GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVklpLPPGAFSGLWKNQEA----FKHlyfekfpGYYDTMDAGYMDE 545
Cdd:PRK07470 337 ariGTCGFERTGMEVQIQDDEGRELPPGETGEICV---IGPAVFAGYYNNPEAnakaFRD-------GWFRTGDLGHLDA 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 546 EGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQ 625
Cdd:PRK07470 407 RGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLA----WLDG 482
|
570 580
....*....|....*....|....*..
gi 13375727 626 NIGPVAAFRNAVFVKQLPKTRSGKIPR 652
Cdd:PRK07470 483 KVARYKLPKRFFFWDALPKSGYGKITK 509
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
143-655 |
2.75e-34 |
|
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: 135.55 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 222
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKLDDIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 SfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdcvpvlsehplyILYTSGT 302
Cdd:cd05912 81 T------------------------------------------------------------------------IMYTSGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 303 TGLPKGVIRPTGGyavmlHW-----SMSSIyGLQPGEVWWAASDLGWVVGHSYICYGpLLHGNTTVLYEgkpvgTPDAGA 377
Cdd:cd05912 89 TGKPKGVQQTFGN-----HWwsaigSALNL-GLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVD-----KFDAEQ 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 378 YFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqYSLTrFKTLFVAGERCDVETLEWSKNvFRVPVLDHWWQTETGSPI 457
Cdd:cd05912 157 VLHLINSGKVTIISVVPTMLQRLLEILGEG-----YPNN-LRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCSQI 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 458 TASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKarcLGNIVVKLP-LPPGAFSGLWKNQEAFKHlyfekfpGYYD 536
Cdd:cd05912 230 VTLSPEDALNK---IGSAGKPLFPVELKIEDDGQPPYE---VGEILLKGPnVTKGYLNRPDATEESFEN-------GWFK 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 537 TMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAteeqvl 616
Cdd:cd05912 297 TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISE------ 370
|
490 500 510
....*....|....*....|....*....|....*....
gi 13375727 617 EEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05912 371 EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
59-655 |
9.57e-34 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 137.90 E-value: 9.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 59 GSEYK---THFAA----SVTDPERFWGKAAEQ--ISWYKPWTKTLE--NKHSPSTRWFVEGMLNI---CYNAVDrhieNG 124
Cdd:PLN03052 112 GSKYKdpiSSFSEfqrfSVENPEVYWSIVLDElsLVFSVPPRCILDtsDESNPGGQWLPGAVLNVaecCLTPKP----SK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 125 KGDKIAIIY------DSPVTntkaTFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLI 198
Cdd:PLN03052 188 TDDSIAIIWrdegsdDLPVN----RMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 199 FGGFASKELSSRIDHVKPKVVVTASFGIEPGRRVEYVPLVEEAlkigqHKPDKILIYNRPNMEAVPLAPGrDLDWDEEMA 278
Cdd:PLN03052 264 ADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA-----KAPKAIVLPADGKSVRVKLREG-DMSWDDFLA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 279 KAQSHDC----VPVlsEHPL----YILYTSGTTGLPKGV--IRPTGGYAVMLHWSMSSIyglQPGEVWWAASDLGWVVGH 348
Cdd:PLN03052 338 RANGLRRpdeyKAV--EQPVeaftNILFSSGTTGEPKAIpwTQLTPLRAAADAWAHLDI---RKGDIVCWPTNLGWMMGP 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 349 sYICYGPLLHGNTTVLYEGKPVGTpdagAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTRFKTLFVAGERC 428
Cdd:PLN03052 413 -WLVYASLLNGATLALYNGSPLGR----GFAKFVQDAKVTMLGTVPSIVKTWKNTNCMAGL----DWSSIRCFGSTGEAS 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 429 DVETLEW--SKNVFRvPVLDHWWQTETGSP-ITASCVglgnsktPPPGQAGKSVP--GYNVMILDDNMQKL--KARCLGN 501
Cdd:PLN03052 484 SVDDYLWlmSRAGYK-PIIEYCGGTELGGGfVTGSLL-------QPQAFAAFSTPamGCKLFILDDSGNPYpdDAPCTGE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 502 IVVkLPLPPGAFSGLWkNQEAFKhLYFEKFPGYYDTMDAGYMDE-----EGYLYVMSRVDDVINVAGHRISAGAIEESI- 575
Cdd:PLN03052 556 LAL-FPLMFGASSTLL-NADHYK-VYFKGMPVFNGKILRRHGDIfertsGGYYRAHGRADDTMNLGGIKVSSVEIERVCn 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 576 LSHGTVADCAVVGKEDPLKGhvPLALC---VLRKDINATEEqvLEEIVK----HVRQNIGPVAAFRNAVFVKQLPKTRSG 648
Cdd:PLN03052 633 AADESVLETAAIGVPPPGGG--PEQLViaaVLKDPPGSNPD--LNELKKifnsAIQKKLNPLFKVSAVVIVPSFPRTASN 708
|
....*..
gi 13375727 649 KIPRSAL 655
Cdd:PLN03052 709 KVMRRVL 715
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
127-655 |
2.04e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 135.44 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIyMPMIPQAM-YTMLACARIGAIHSLIFGGFASK 205
Cdd:PRK07788 64 DRAALIDE------RGTLTYAELDEQSNALARGLLALGVRAGDGVAV-LARNHRGFvLALYAAGKVGARIILLNTGFSGP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 ELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEAlkigqhKPD--KILIYNRPNMEAVPLAPG-RDLDwdeEMAKAQS 282
Cdd:PRK07788 137 QLAEVAAREGVKALVYDD---------EFTDLLSAL------PPDlgRLRAWGGNPDDDEPSGSTdETLD---DLIAGSS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 283 HDCVPVLSEHPLYILYTSGTTGLPKGVIRPTggyavmlhwsmssIYGLQPgevwwAASDLGWV---VGHSYICYGPLLH- 358
Cdd:PRK07788 199 TAPLPKPPKPGGIVILTSGTTGTPKGAPRPE-------------PSPLAP-----LAGLLSRVpfrAGETTLLPAPMFHa 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 359 ------------GNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRaiRQQDPGAALGKQYSLTRFKTLFVAGE 426
Cdd:PRK07788 261 tgwahltlamalGSTVVLRR-----RFDPEATLEDIAKHKATALVVVPVMLS--RILDLGPEVLAKYDTSSLKIIFVSGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 427 RCDVETLEWSKNVFRvPVLDHWW-QTETGSPITAscvglgnskTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCLG 500
Cdd:PRK07788 334 ALSPELATRALEAFG-PVLYNLYgSTEVAFATIA---------TPEdlaeaPGTVGRPPKGVTVKILDENGNEVPRGVVG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 501 NIVVKLPLPpgaFSGlwknqeafkhlYF-----EKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESI 575
Cdd:PRK07788 404 RIFVGNGFP---FEG-----------YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 576 LSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK07788 470 AGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKD----YVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
145-655 |
1.59e-32 |
|
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: 131.86 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASf 224
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 225 gIEPGRRVEYVPLVEEaLKIGQHKPDKILIYNRPNMEAVPLAPgrdldwdeemakaqshdcvpvlsEHPLYILYTSGTTG 304
Cdd:cd05923 109 -DAQVMDAIFQSGVRV-LALSDLVGLGEPESAGPLIEDPPREP-----------------------EQPAFVFYTSGTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 305 LPKGVIRP----------TGGYAVMLHWSMSSIYGLQPgevwwaasdLGWVVGHSYICYGPLLHGNTTVlyegkPVGTPD 374
Cdd:cd05923 164 LPKGAVIPqraaesrvlfMSTQAGLRHGRHNVVLGLMP---------LYHVIGFFAVLVAALALDGTYV-----VVEEFD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 375 AGAYFRVLAEHGVAALFTAPTAIRAIrqqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETG 454
Cdd:cd05923 230 PADALKLIEQERVTSLFATPTHLDAL----AAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 455 SPITAscvglgnsKTPPPGQAGKsvPGYN-----VMILDDNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEA-FKHLYF 528
Cdd:cd05923 306 NSLYM--------RDARTGTEMR--PGFFsevriVRIGGSPDEALANGEEGELIVAAA-ADAAFTGYLNQPEAtAKKLQD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 529 ekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLAlCVLRKDI 608
Cdd:cd05923 375 ----GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTA-CVVPREG 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 13375727 609 NATEEQvLEEIVKHvrqniGPVAAF---RNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05923 450 TLSADE-LDQFCRA-----SELADFkrpRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
118-663 |
1.64e-32 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 132.48 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 118 DRHIENgKGDKIAIIYDSPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSL 197
Cdd:PRK13295 31 DACVAS-CPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 198 IFGGFASKELSSRIDHVKPKV-VVTASF----------GIEPGrrveyVPLVEEALKIGQHKPDkiliynrpNMEAVPLA 266
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVlVVPKTFrgfdhaamarRLRPE-----LPALRHVVVVGGDGAD--------SFEALLIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 267 PgrdlDWDEEmakaqsHDCVPVLSEHPL------YILYTSGTTGLPKGVirptggyavmLHWS---MSSIY------GLQ 331
Cdd:PRK13295 177 P----AWEQE------PDAPAILARLRPgpddvtQLIYTSGTTGEPKGV----------MHTAntlMANIVpyaerlGLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 332 PGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEgkpVGTPDAGAyfRVLAEHGVAalFT---APTAIRAIRQQDPGAa 408
Cdd:PRK13295 237 ADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD---IWDPARAA--ELIRTEGVT--FTmasTPFLTDLTRAVKESG- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 409 lgkqYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSpitASCVGLGNSKTPPPGQAGKSVPGYNVMILD 488
Cdd:PRK13295 309 ----RPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA---VTLTKLDDPDERASTTDGCPLPGVEVRVVD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 489 DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQeafkHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISA 568
Cdd:PRK13295 382 ADGAPLPAGQIGRLQVR---GCSNFGGYLKRP----QLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 569 GAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinATEEQVLEEIV-----KHVRQNIGPvaafRNAVFVKQLP 643
Cdd:PRK13295 455 VEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR----PGQSLDFEEMVeflkaQKVAKQYIP----ERLVVRDALP 526
|
570 580
....*....|....*....|
gi 13375727 644 KTRSGKIPRSALSAIVNGKP 663
Cdd:PRK13295 527 RTPSGKIQKFRLREMLRGED 546
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
137-657 |
3.86e-32 |
|
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: 131.06 E-value: 3.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 137 VTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKP 216
Cdd:TIGR03098 19 LVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 217 KVVVTASfgiepgrrvEYVPLVEEALKiGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYI 296
Cdd:TIGR03098 99 RLLVTSS---------ERLDLLHPALP-GCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGDADPPHPVIDSDMAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 297 LYTSGTTGLPKGVIRP-----TGGYAVmlhwsmSSIYGLQPGEVWWAASDLGWVVGHSYICYGpLLHGNTTVLYE---GK 368
Cdd:TIGR03098 169 LYTSGSTGRPKGVVLShrnlvAGAQSV------ATYLENRPDDRLLAVLPLSFDYGFNQLTTA-FYVGATVVLHDyllPR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 369 PVGT--------------------------PDAGAYFRVLAEHGVAalfTAPTAIRAIRQQDPGAALGKQYSLTR-FKTL 421
Cdd:TIGR03098 242 DVLKalekhgitglaavpplwaqlaqldwpESAAPSLRYLTNSGGA---MPRATLSRLRSFLPNARLFLMYGLTEaFRST 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 422 FVAGERCDVEtlewsknvfrvpvldhwwqtetgspitascvglgnsktppPGQAGKSVPGYNVMILDDnmqkLKARCL-- 499
Cdd:TIGR03098 319 YLPPEEVDRR----------------------------------------PDSIGKAIPNAEVLVLRE----DGSECApg 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 500 --GNIVVKLPLppgAFSGLWKNQEAFKHLyFEKFPGYYDTM----------DAGYMDEEGYLYVMSRVDDVINVAGHRIS 567
Cdd:TIGR03098 355 eeGELVHRGAL---VAMGYWNDPEKTAER-FRPLPPFPGELhlpelavwsgDTVRRDEEGFLYFVGRRDEMIKTSGYRVS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 568 AGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPvaafRNAVFVKQLPKTRS 647
Cdd:TIGR03098 431 PTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVP----ALIHVRQALPRNAN 506
|
570
....*....|
gi 13375727 648 GKIPRSALSA 657
Cdd:TIGR03098 507 GKIDRKALAK 516
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
140-658 |
5.24e-32 |
|
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: 130.72 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 140 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 219
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 220 VTASFGIEPgrrveyVPLVEEALKIGQhkpdKILIynrpnmeavpLAPGRDLDWDEEMAKAQSHDCVPVLSEHPL----- 294
Cdd:cd17642 121 FCSKKGLQK------VLNVQKKLKIIK----TIII----------LDSKEDYKGYQCLYTFITQNLPPGFNEYDFkppsf 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 295 -------YILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVvgHSYICY---GPLLHGNTTVL 364
Cdd:cd17642 181 drdeqvaLIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFH--HGFGMFttlGYLICGFRVVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 365 yegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrqqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVP- 443
Cdd:cd17642 259 -----MYKFEEELFLRSLQDYKVQSALLVPTLFAFF----AKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPg 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 444 VLDHWWQTETGSPITAScvglgNSKTPPPGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEA 522
Cdd:cd17642 330 IRQGYGLTETTSAILIT-----PEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVK---GPMIMKGYVNNPEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 523 FKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALC 602
Cdd:cd17642 402 TKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 13375727 603 VLRKDINATEEqvleEIVKHVRQNIGPVAAFRNAV-FVKQLPKTRSGKIPRSALSAI 658
Cdd:cd17642 480 VLEAGKTMTEK----EVMDYVASQVSTAKRLRGGVkFVDEVPKGLTGKIDRRKIREI 532
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
126-655 |
1.74e-31 |
|
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: 128.56 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfask 205
Cdd:cd12116 1 PDATAVRDDD------RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAY---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 elssridhvkpkVVVTASFgiePGRRVEYVplVEEAlkigqhKPDKILIynRPNMEAVPLAPGRDLDWDEEMAKAQSHDC 285
Cdd:cd12116 65 ------------VPLDPDY---PADRLRYI--LEDA------EPALVLT--DDALPDRLPAGLPVLLLALAAAAAAPAAP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 286 -VPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHwSMSSIYGLQPGEVWWAASDlgwvvghsyIC--------YGPL 356
Cdd:cd12116 120 rTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH-SMRERLGLGPGDRLLAVTT---------YAfdisllelLLPL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 357 LHGNTTVLYEGKpvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKqysltrfkTLFVAGERCDVETLEws 436
Cdd:cd12116 190 LAGARVVIAPRE--TQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGL--------TALCGGEALPPDLAA-- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 437 KNVFRVPVLdhwWQ----TETgsPITASCVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGA 512
Cdd:cd12116 258 RLLSRVGSL---WNlygpTET--TIWSTAARVTAAAGPIP--IGRPLANTQVYVLDAALR--------------PVPPGV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 513 FSGLWKNQEAFKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 576
Cdd:cd12116 317 PGELYIGGDGVAQGYLgrpaltaERFvpdpfagPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALA 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13375727 577 SHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRnavfVKQLPKTRSGKIPRSAL 655
Cdd:cd12116 397 AHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVR----LDALPLTANGKLDRKAL 470
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
126-655 |
1.95e-31 |
|
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: 129.11 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslIFGGFA-- 203
Cdd:COG1021 39 PDRIAVVDG------ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 204 SKELSSRIDHVKPKVVVTAsfgiepgRRVE---YVPLVEEALKigQHkpdkiliynrPNMEAVPLA--PGRDLDWDEEMA 278
Cdd:COG1021 111 RAEISHFAEQSEAVAYIIP-------DRHRgfdYRALARELQA--EV----------PSLRHVLVVgdAGEFTSLDALLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 279 KAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLhWSMSSIYGLQPGEVWWAASDlgwvVGHSY--IC---Y 353
Cdd:COG1021 172 APADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSV-RASAEICGLDADTVYLAALP----AAHNFplSSpgvL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 354 GPLLHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETL 433
Cdd:COG1021 247 GVLYAGGTVVL-----APDPSPDTAFPLIERERVTVTALVPPLALLWLD----AAERSRYDLSSLRVLQVGGAKLSPELA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 434 EwsknvfRV-PVLDHWWQ------------TETGSP--ITASCVGLGNSktpppgqagksvPGYNVMILDDNmqklkarc 498
Cdd:COG1021 318 R------RVrPALGCTLQqvfgmaeglvnyTRLDDPeeVILTTQGRPIS------------PDDEVRIVDED-------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 499 lGNivvklPLPPGA-----------FSGLWK----NQEAFKHlyfekfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAG 563
Cdd:COG1021 372 -GN-----PVPPGEvgelltrgpytIRGYYRapehNARAFTP------DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 564 HRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinaTEEQVLEEIVKHVRQnIGpVAAFR---NAVFVK 640
Cdd:COG1021 440 EKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-----GEPLTLAELRRFLRE-RG-LAAFKlpdRLEFVD 512
|
570
....*....|....*
gi 13375727 641 QLPKTRSGKIPRSAL 655
Cdd:COG1021 513 ALPLTAVGKIDKKAL 527
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
143-637 |
4.80e-31 |
|
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: 126.94 E-value: 4.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTa 222
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 sfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdlDWDEEMAKaqshdcvpvlsehplyILYTSGT 302
Cdd:cd05907 84 -------------------------------------------------EDPDDLAT----------------IIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 303 TGLPKGvirptggyaVMLHWS--MSSIYGLqpGEVWWAASD--------LGWVVGHSYICYGPLLHGNTTVLYEGKPVGT 372
Cdd:cd05907 99 TGRPKG---------VMLSHRniLSNALAL--AERLPATEGdrhlsflpLAHVFERRAGLYVPLLAGARIYFASSAETLL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 373 PDagayfrvLAEHGVAALFTAPTAIR----AIRQQDPGAALGKQY---SLTRFKTLFVAGERCDVETLEWsknvFR---V 442
Cdd:cd05907 168 DD-------LSEVRPTVFLAVPRVWEkvyaAIKVKAVPGLKRKLFdlaVGGRLRFAASGGAPLPAELLHF----FRalgI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 443 PVLDHWWQTETGSPITASCVGlgnskTPPPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQEA 522
Cdd:cd05907 237 PVYEGYGLTETSAVVTLNPPG-----DNRIGTVGKPLPGVEVRIADD----------GEILVR---GPNVMLGYYKNPEA 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 523 FKHLYFEkfPGYYDTMDAGYMDEEGYLYVMSRVDDVI-NVAGHRISAGAIEESILSHGTVADCAVVGKEDPlkghVPLAL 601
Cdd:cd05907 299 TAEALDA--DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVAL 372
|
490 500 510
....*....|....*....|....*....|....*....
gi 13375727 602 CVLRKDIN---ATEEQVLEEIVKHVRQNIGPVAAFRNAV 637
Cdd:cd05907 373 IVPDPEALeawAEEHGIAYTDVAELAANPAVRAEIEAAV 411
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
125-655 |
1.09e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 126.56 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 125 KGDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFAS 204
Cdd:PRK07656 18 FGDKEAYVFGD------QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 205 KELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEAlkigQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHD 284
Cdd:PRK07656 92 DEAAYILARGDAKALFVLG---------LFLGVDYSA----TTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 285 CVPVLS-EHPLYILYTSGTTGLPKGVirptggyaVMLHWSMSSIY-------GLQPGEVWWAASDLGWVVGHSYICYGPL 356
Cdd:PRK07656 159 RAPEVDpDDVADILFTSGTTGRPKGA--------MLTHRQLLSNAadwaeylGLTEGDRYLAANPFFHVFGYKAGVNAPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 357 LHGNTTVlyegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqyslTRFKTLFVA---GERCDVETL 433
Cdd:PRK07656 231 MRGATIL-----PLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSA-------EDLSSLRLAvtgAASMPVALL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 434 EWSKNVFRVP-VLDHWWQTETgSPITASCvGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGA 512
Cdd:PRK07656 299 ERFESELGVDiVLTGYGLSEA-SGVTTFN-RLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR---GPNV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 513 FSGLWKNQEAFKHLYfeKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDP 592
Cdd:PRK07656 374 MKGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDE 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13375727 593 LKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIgpvAAF---RNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK07656 452 RLGEVGKAYVVLKPGAELTEEELIA----YCREHL---AKYkvpRSIEFLDELPKNATGKVLKRAL 510
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
143-655 |
4.35e-30 |
|
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: 123.90 E-value: 4.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 222
Cdd:cd05945 16 TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 sfgiepgrrveyvplveealkigqhkPDkiliynrpnmeavPLApgrdldwdeemakaqshdcvpvlsehplYILYTSGT 302
Cdd:cd05945 96 --------------------------GD-------------DNA----------------------------YIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 303 TGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVlyegkPVG---TPDAGAYF 379
Cdd:cd05945 109 TGRPKGVQISHDNLVSFTNW-MLSDFPLGPGDVFLNQAPFSFDLSVMDL-YPALASGATLV-----PVPrdaTADPKQLF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 380 RVLAEHGVAALFTAPTAIRAIRQqDPGAALGKQYSLTRFktLFvAGERCDVETLEWSKNVF-RVPVLDHWWQTETgspiT 458
Cdd:cd05945 182 RFLAEHGITVWVSTPSFAAMCLL-SPTFTPESLPSLRHF--LF-CGEVLPHKTARALQQRFpDARIYNTYGPTEA----T 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 459 ASCVG-------LGNSKTPPPGQAgksVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEafKHLY-FEK 530
Cdd:cd05945 254 VAVTYievtpevLDGYDRLPIGYA---KPGAKLVILDEDGRPVPPGEKGELVIS---GPSVSKGYLNNPE--KTAAaFFP 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 531 FPGY--YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdi 608
Cdd:cd05945 326 DEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPK--- 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 13375727 609 NATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05945 403 PGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
127-661 |
5.69e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 124.23 E-value: 5.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 206
Cdd:PRK06145 17 DRAALVYRD------QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 LSSRIDHVKPKVV-VTASFGIEPGrrveyvpLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLDwdeemakaqshdc 285
Cdd:PRK06145 91 VAYILGDAGAKLLlVDEEFDAIVA-------LETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTD------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 286 vpvlsehpLY-ILYTSGTTGLPKGVirptggyavMLHWsmssiyglqpGEVWWAASD----LGWVVGHSYICYGPLLH-- 358
Cdd:PRK06145 151 --------LVrLMYTSGTTDRPKGV---------MHSY----------GNLHWKSIDhviaLGLTASERLLVVGPLYHvg 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 359 ----GNTTVLYEGKPVGTP---DAGAYFRVLAEHGVAALFTAP---TAIRAIRQQDpgaalgkQYSLTRFKTLFVAGERC 428
Cdd:PRK06145 204 afdlPGIAVLWVGGTLRIHrefDPEAVLAAIERHRLTCAWMAPvmlSRVLTVPDRD-------RFDLDSLAWCIGGGEKT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 429 -DVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlp 507
Cdd:PRK06145 277 pESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKI---GSTGRALAHVEIRIADGAGRWLPPNMKGEICMR-- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 508 lPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVV 587
Cdd:PRK06145 352 -GPKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13375727 588 GKEDPLKGHVPLALCVLRKDINATeeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNG 661
Cdd:PRK06145 428 GVHDDRWGERITAVVVLNPGATLT----LEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
126-650 |
6.41e-30 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 123.95 E-value: 6.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIYDSPVtntkatFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFAS 204
Cdd:cd12118 18 PDRTSIVYGDRR------YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTP-AMYELhFGVPMAGAVLNALNTRLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 205 KELSSRIDHVKPKVV-VTASFgiepgrrvEYvplvEEALKIGqhKPDKILIynRPNMEavplapgrdldWDeemakaqsh 283
Cdd:cd12118 91 EEIAFILRHSEAKVLfVDREF--------EY----EDLLAEG--DPDFEWI--PPADE-----------WD--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 284 dcvpvlsehPLYILYTSGTTGLPKGVIRPTGGYAVMlhwSMSSIY--GLQPGEVwwaasdlgwvvghsYICYGPLLHGN- 360
Cdd:cd12118 135 ---------PIALNYTSGTTGRPKGVVYHHRGAYLN---ALANILewEMKQHPV--------------YLWTLPMFHCNg 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 361 -----TTVLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTRFKTLFVAGERCDVETL 433
Cdd:cd12118 189 wcfpwTVAAVGGTNVCLRkvDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDAR----PLPHRVHVMTAGAPPPAAVL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 434 EWSKNV-FRVpvlDH-WWQTETGSPITAsCVGLGNSKT-PPPGQA------GKSVPGYN-VMILDDNMQKLKAR------ 497
Cdd:cd12118 265 AKMEELgFDV---THvYGLTETYGPATV-CAWKPEWDElPTEERArlkarqGVRYVGLEeVDVLDPETMKPVPRdgktig 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 498 ---CLGNIVVKlplppgafsGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGA 570
Cdd:cd12118 341 eivFRGNIVMK---------GYLKNpeatAEAFRG-------GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 571 IEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIgpvAAF---RNAVFVkQLPKTRS 647
Cdd:cd12118 405 VEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE----EEIIAFCREHL---AGFmvpKTVVFG-ELPKTST 476
|
...
gi 13375727 648 GKI 650
Cdd:cd12118 477 GKI 479
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
127-650 |
7.25e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 124.69 E-value: 7.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAII-YDSPVTntkatftYKEVLEQVSKLAGVLV-KHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFAS 204
Cdd:PRK08314 25 DKTAIVfYGRAIS-------YRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 205 KELSSRIDHVKPKVVVTAS---FGIEP---GRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMA 278
Cdd:PRK08314 98 EELAHYVTDSGARVAIVGSelaPKVAPavgNLRLRHVIVAQYSDYLPAEPEIAVPAWLRAEPPLQALAPGGVVAWKEALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 279 kaqSHDCVPVLSEHP--LYIL-YTSGTTGLPKGVIRPTGgyAVM------LHWSMSSiyglqPGEVWWAASDLGWVVGHS 349
Cdd:PRK08314 178 ---AGLAPPPHTAGPddLAVLpYTSGTTGVPKGCMHTHR--TVManavgsVLWSNST-----PESVVLAVLPLFHVTGMV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 350 YICYGPLLHGNTTVLYegkPVGTPDAGAyfRVLAEHGVAALFTAPT------AIRAIRQQD---------PGAALGK--- 411
Cdd:PRK08314 248 HSMNAPIYAGATVVLM---PRWDREAAA--RLIERYRVTHWTNIPTmvvdflASPGLAERDlsslryiggGGAAMPEava 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 412 QYSLTRFKTLFVAGercdvetlewsknvfrvpvldhWWQTETGSPITAScvglgnsktPP--PGQAGKSVPGYNV--MIL 487
Cdd:PRK08314 323 ERLKELTGLDYVEG----------------------YGLTETMAQTHSN---------PPdrPKLQCLGIPTFGVdaRVI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 488 D-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkFPG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGH 564
Cdd:PRK08314 372 DpETLEELPPGEVGEIVVH---GPQVFKGYWNRPEATAEAFIE-IDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 565 RISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQvlEEIVKHVRQNIGPVAAFRNAVFVKQLPK 644
Cdd:PRK08314 448 KVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTE--EEIIAWAREHMAAYKYPRIVEFVDSLPK 525
|
....*.
gi 13375727 645 TRSGKI 650
Cdd:PRK08314 526 SGSGKI 531
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
127-661 |
9.20e-30 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 124.75 E-value: 9.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFASK 205
Cdd:PLN03102 29 NRTSIIYG------KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTP-AMYEMhFAVPMAGAVLNPINTRLDAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 ELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKI-----GQHKPDKILIYNrpnMEAVPLAPGRDLDWDEEMAKA 280
Cdd:PLN03102 102 SIAAILRHAKPKILFVDR---------SFEPLAREVLHLlssedSNLNLPVIFIHE---IDFPKRPSSEELDYECLIQRG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 281 QShdcVPVLS--------EH-PLYILYTSGTTGLPKGV-IRPTGGYAVMLhwsmSSIYGLQPG--EVW-WAASDL---GW 344
Cdd:PLN03102 170 EP---TPSLVarmfriqdEHdPISLNYTSGTTADPKGVvISHRGAYLSTL----SAIIGWEMGtcPVYlWTLPMFhcnGW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 345 VvghsyICYGPLLHGNTTVLYegKPVGTPDAgayFRVLAEHGVAALFTAPTAIRAIRQQD-------------------P 405
Cdd:PLN03102 243 T-----FTWGTAARGGTSVCM--RHVTAPEI---YKNIEMHNVTHMCCVPTVFNILLKGNsldlsprsgpvhvltggspP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 406 GAALGKQYSLTRFKTLFVAGER---CDVETLEWSKNVFRVPvlDHWW----QTETGSPITASCVGLGNSKTPppgqagKS 478
Cdd:PLN03102 313 PAALVKKVQRLGFQVMHAYGLTeatGPVLFCEWQDEWNRLP--ENQQmelkARQGVSILGLADVDVKNKETQ------ES 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 479 VPgynvmilddnmqkLKARCLGNIVVKlplPPGAFSGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSR 554
Cdd:PLN03102 385 VP-------------RDGKTMGEIVIK---GSSIMKGYLKNpkatSEAFKH-------GWLNTGDVGVIHPDGHVEIKDR 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 555 VDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLE------EIVKHVRQNIG 628
Cdd:PLN03102 442 SKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKlvtrerDLIEYCRENLP 521
|
570 580 590
....*....|....*....|....*....|...
gi 13375727 629 PVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNG 661
Cdd:PLN03102 522 HFMCPRKVVFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
145-655 |
1.03e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 124.38 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMytmlacarIGAIHSLIFGG--------FASKELSSRIDHVKP 216
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAV--------IGYYGTLLAGGivvqtnplYTERELEYQLHDSGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 217 KVVVTASFGIEPGRRVEYVPLVEEAL--KIGQHKP-DKILIY-----NRPNMeAVPLAPGRDLD-WDEEMAKAQSHDCVP 287
Cdd:PRK06710 123 KVILCLDLVFPRVTNVQSATKIEHVIvtRIADFLPfPKNLLYpfvqkKQSNL-VVKVSESETIHlWNSVEKEVNTGVEVP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 288 VLSEHPLYIL-YTSGTTGLPKGVIRP----TGGYAVMLHWsmssIYGLQPGEvwwaasDLGWVVGHSYICYGPLLHGNTT 362
Cdd:PRK06710 202 CDPENDLALLqYTGGTTGFPKGVMLThknlVSNTLMGVQW----LYNCKEGE------EVVLGVLPFFHVYGMTAVMNLS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 363 VLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF 440
Cdd:PRK06710 272 IMQGYKMVLIPkfDMKMVFEAIKKHKVTLFPGAPTIYIALLN----SPLLKEYDISSIRACISGSAPLPVEVQEKFETVT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 441 RVPVLDHWWQTETgSPITASCVgLGNSKTPppGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKN 519
Cdd:PRK06710 348 GGKLVEGYGLTES-SPVTHSNF-LWEKRVP--GSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK---GPQIMKGYWNK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 520 QEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPL 599
Cdd:PRK06710 421 PEETAAVLQD---GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVK 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 13375727 600 ALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK06710 498 AFVVLKEGTECSE----EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
126-588 |
1.09e-29 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 124.44 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIYdsPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 205
Cdd:COG1022 25 PDRVALRE--KEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 ELSSRIDHVKPKVVVtasfgiepgrrVEYVPLVEEALKIGQHKPD--KILIYNRPNMEAVP--------LAPGRDLDWDE 275
Cdd:COG1022 103 EVAYILNDSGAKVLF-----------VEDQEQLDKLLEVRDELPSlrHIVVLDPRGLRDDPrllsldelLALGREVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 276 EMAKAQSHdcvpVLSEHPLYILYTSGTTGLPKGvirptggyaVML-HWSMSS-------IYGLQPGEVW-----WAasdl 342
Cdd:COG1022 172 ELEARRAA----VKPDDLATIIYTSGTTGRPKG---------VMLtHRNLLSnaralleRLPLGPGDRTlsflpLA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 343 gWVVGHSYICYgpLLHGNTTVLY------------EGKP---VGTPD------AGAYFRVLAEHGVA-ALFTA--PTAIR 398
Cdd:COG1022 235 -HVFERTVSYY--ALAAGATVAFaespdtlaedlrEVKPtfmLAVPRvwekvyAGIQAKAEEAGGLKrKLFRWalAVGRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 399 AIRQQD----PGAALGKQYSL--------------TRFKTLFVAGERCDVETLEWsknvFR---VPVLDHWWQTETGSPI 457
Cdd:COG1022 312 YARARLagksPSLLLRLKHALadklvfsklrealgGRLRFAVSGGAALGPELARF----FRalgIPVLEGYGLTETSPVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 458 TASCvgLGNSKtppPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDT 537
Cdd:COG1022 388 TVNR--PGDNR---IGTVGPPLPGVEVKIAED----------GEILVR---GPNVMKGYYKNPEATAEAFDAD--GWLHT 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 13375727 538 MDAGYMDEEGYLYVMSRVDDVINVA-GHRISAGAIEESILSHGTVADCAVVG 588
Cdd:COG1022 448 GDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
126-655 |
1.25e-29 |
|
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: 123.08 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfask 205
Cdd:cd12117 11 PDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAY---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 eLSSRIDHvkpkvvvtasfgiePGRRVEYvpLVEEAlkigqhkPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDC 285
Cdd:cd12117 75 -VPLDPEL--------------PAERLAF--MLADA-------GAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 286 VPVLSEHPLYILYTSGTTGLPKGVIRPtggyavmlHWSMSSIY------GLQPGEVWWAASDLGWVVGhSYICYGPLLHG 359
Cdd:cd12117 131 VPVSPDDLAYVMYTSGSTGRPKGVAVT--------HRGVVRLVkntnyvTLGPDDRVLQTSPLAFDAS-TFEIWGALLNG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 360 NTTVLYEGKPVGTPDAGAyfRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERCDVetlewsKNV 439
Cdd:cd12117 202 ARLVLAPKGTLLDPDALG--ALIAEEGVTVLWLTAALFNQLADEDPEC-------FAGLRELLTGGEVVSP------PHV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 440 FRvpVLDHW-----WQ----TETGSPITASCVglgnskTPPPGQA-----GKSVPGYNVMILDDNMQklkarclgnivvk 505
Cdd:cd12117 267 RR--VLAACpglrlVNgygpTENTTFTTSHVV------TELDEVAgsipiGRPIANTRVYVLDEDGR------------- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 506 lPLPPGAF-------SGLWK---NQEAfkhLYFEKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRIS 567
Cdd:cd12117 326 -PVPPGVPgelyvggDGLALgylNRPA---LTAERFvadpfgPGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIE 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 568 AGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAteeqvlEEIVKHVRQNIGPV---AAFrnaVFVKQLPK 644
Cdd:cd12117 402 LGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDA------AELRAFLRERLPAYmvpAAF---VVLDELPL 472
|
570
....*....|.
gi 13375727 645 TRSGKIPRSAL 655
Cdd:cd12117 473 TANGKVDRRAL 483
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
127-655 |
1.72e-29 |
|
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: 122.03 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaske 206
Cdd:cd17643 2 EAVAVVDED------RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGG------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 lssridhvkpkvvvtasfgiepgrrvEYVPLveealkigqhkpdkiliynrpnmeavplapgrDLDWDEEMAKAQSHDCV 286
Cdd:cd17643 63 --------------------------AYVPI--------------------------------DPAYPVERIAFILADSG 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 287 PVL----SEHPLYILYTSGTTGLPKGVIRPTGGyAVMLHWSMSSIYGLQPGEVWWAAsdlgwvvgHSYI-------CYGP 355
Cdd:cd17643 85 PSLlltdPDDLAYVIYTSGSTGRPKGVVVSHAN-VLALFAATQRWFGFNEDDVWTLF--------HSYAfdfsvweIWGA 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 356 LLHGNTTVLYEGKPVGTPDAgaYFRVLAEHGVAALFTAPTAIRAIRQ---QDPGAALGKQYsltrfktLFVAGERCDVET 432
Cdd:cd17643 156 LLHGGRLVVVPYEVARSPED--FARLLRDEGVTVLNQTPSAFYQLVEaadRDGRDPLALRY-------VIFGGEALEAAM 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 433 LE-WSKNVF--RVPVLDHWWQTETG-----SPITASCVGLGNSKTpppgqAGKSVPGYNVMILDDNMQklkarclgnivv 504
Cdd:cd17643 227 LRpWAGRFGldRPQLVNMYGITETTvhvtfRPLDAADLPAAAASP-----IGRPLPGLRVYVLDADGR------------ 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 505 klPLPPGAFSGLW----------KNQEAfkhLYFEKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHR 565
Cdd:cd17643 290 --PVPPGVVGELYvsgagvargyLGRPE---LTAERFvanpfggPGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 566 ISAGAIEESILSHGTVADCAVVGKEDPLKGHVpLALCVlrkDINATEEQVLEEIVKHVRQNIGPV---AAFrnaVFVKQL 642
Cdd:cd17643 365 IELGEIEAALATHPSVRDAAVIVREDEPGDTR-LVAYV---VADDGAAADIAELRALLKELLPDYmvpARY---VPLDAL 437
|
570
....*....|...
gi 13375727 643 PKTRSGKIPRSAL 655
Cdd:cd17643 438 PLTVNGKLDRAAL 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
142-655 |
1.90e-29 |
|
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: 122.45 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 142 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 221
Cdd:cd17651 19 RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 AsfgiepgrrveyvPLVEEALkigqhkpdkiliynrpnmeAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYILYTSG 301
Cdd:cd17651 99 H-------------PALAGEL-------------------AVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 302 TTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLyeGKPVGTPDAGAYFRV 381
Cdd:cd17651 147 STGRPKGVVMPHRSLANLVAW-QARASSLGPGARTLQFAGLGFDVSVQEI-FSTLCAGATLVL--PPEEVRTDPPALAAW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 382 LAEHGVAALFTAPTAIRAIRQQdpGAALGKQysLTRFKTLFVAGER--CDVETLEWSKNVFRVPVLDHWWQTETgSPITA 459
Cdd:cd17651 223 LDEQRISRVFLPTVALRALAEH--GRPLGVR--LAALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTET-HVVTA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 460 SCVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPG-------AFSGLWKNQEAFKHLYFEKF- 531
Cdd:cd17651 298 LSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALR--------------PVPPGvpgelyiGGAGLARGYLNRPELTAERFv 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 532 -----PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVL 604
Cdd:cd17651 364 pdpfvPGarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVG 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 13375727 605 RkdinATEEQVLEEIVKHVRQNIGP---VAAFrnaVFVKQLPKTRSGKIPRSAL 655
Cdd:cd17651 444 D----PEAPVDAAELRAALATHLPEymvPSAF---VLLDALPLTPNGKLDRRAL 490
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
175-655 |
3.00e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 122.23 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 175 MPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFGIEPGRRveyVPLVEEALKIGQHKPDKILI 254
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRA---LPLYSKVVEAAPAKAIVLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 255 YNRPNmeAVPLAPGrDLDWDEEMAKAQSHDCV------PVL--SEHPLYILYTSGTTGLPKGV-------IR-PTGGYAV 318
Cdd:PLN03051 78 AGEPV--AVPLREQ-DLSWCDFLGVAAAQGSVggneysPVYapVESVTNILFSSGTTGEPKAIpwthlspLRcASDGWAH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 319 MlhwsmssiyGLQPGEVWWAASDLGWVVGhSYICYGPLLHGNTTVLYEGKPVGtpdaGAYFRVLAEHGVAALFTAPTAIR 398
Cdd:PLN03051 155 M---------DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLG----RGFGKFVQDAGVTVLGLVPSIVK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 399 AIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW--SKNVFRVPVLDHWWQTETGSPITASCVGLGNSktppPGQAG 476
Cdd:PLN03051 221 AWRHT--GAFAMEGLDWSKLRVFASTGEASAVDDVLWlsSVRGYYKPVIEYCGGTELASGYISSTLLQPQA----PGAFS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 477 KSVPGYNVMILDDNMQKL--KARCLGNIVVKLPLPPGAFSGLWKNQEAfkhLYFEKFPGYY----------DTMDAgymD 544
Cdd:PLN03051 295 TASLGTRFVLLNDNGVPYpdDQPCVGEVALAPPMLGASDRLLNADHDK---VYYKGMPMYGskgmplrrhgDIMKR---T 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 545 EEGYLYVMSRVDDVINVAGHRISAGAIEESIL-SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKH- 622
Cdd:PLN03051 369 PGGYFCVQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKKGFDQARPEALQKk 448
|
490 500 510
....*....|....*....|....*....|....*..
gi 13375727 623 ----VRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PLN03051 449 fqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVL 485
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
127-657 |
3.31e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 122.84 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSPVTntkatfTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 206
Cdd:PRK06178 48 QRPAIIFYGHVI------TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 LSSRIDHVKPKVVVTASFGIEPGRRVEYVPLVEEALKIGQHK--PDKILIYNRPNMEAVPLAPGrdlDWDEEMAkAQSHD 284
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADvlPAEPTLPLPDSLRAPRLAAA---GAIDLLP-ALRAC 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 285 CVPVLSEHP----LYIL-YTSGTTGLPKGVIRPTG--------GYAVMLHWSMSSIY-GLQPgEVWWAASDLGWVVghsy 350
Cdd:PRK06178 198 TAPVPLPPPaldaLAALnYTGGTTGMPKGCEHTQRdmvytaaaAYAVAVVGGEDSVFlSFLP-EFWIAGENFGLLF---- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 351 icygPLLHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALF-TAPTAIRAIrqQDPGAAlgkQYSLTRFKTLFVAGErcd 429
Cdd:PRK06178 273 ----PLFSGATLVL-----LARWDAVAFMAAVERYRVTRTVmLVDNAVELM--DHPRFA---EYDLSSLRQVRVVSF--- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 430 VETLEwsknvfrvPVLDHWWQTETGSPITASCVGLGNSKT----------------PPPGQAGKSVPGYNVMILD-DNMQ 492
Cdd:PRK06178 336 VKKLN--------PDYRQRWRALTGSVLAEAAWGMTETHTcdtftagfqdddfdllSQPVFVGLPVPGTEFKICDfETGE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 493 KLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIE 572
Cdd:PRK06178 408 LLPLGAEGEIVVR---TPSLLKGYWNKPEATAEALRD---GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 573 ESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGP--VAAFRnavFVKQLPKTRSGKI 650
Cdd:PRK06178 482 ALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA----AALQAWCRENMAVykVPEIR---IVDALPMTATGKV 554
|
....*..
gi 13375727 651 PRSALSA 657
Cdd:PRK06178 555 RKQDLQA 561
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
126-656 |
7.65e-29 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 120.94 E-value: 7.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIYDSPVTNTKaTFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 205
Cdd:PRK08008 21 GHKTALIFESSGGVVR-RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 ELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIGQHKPDKILIYNrpnmEAVPLAPGRdLDWDEEMAK--AQSH 283
Cdd:PRK08008 100 ESAWILQNSQASLLVTSA---------QFYPMYRQIQQEDATPLRHICLTR----VALPADDGV-SSFTQLKAQqpATLC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 284 DCVPVLSEHPLYILYTSGTTGLPKGVirptggyaVMLHWSM--SSIYGlqpgeVWWAA---SDLgwvvghsYICYGPLLH 358
Cdd:PRK08008 166 YAPPLSTDDTAEILFTSGTTSRPKGV--------VITHYNLrfAGYYS-----AWQCAlrdDDV-------YLTVMPAFH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 359 --------------GNTTVLYEGKpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAALGKQYSLTRFktLFVA 424
Cdd:PRK08008 226 idcqctaamaafsaGATFVLLEKY-----SARAFWGQVCKYRATITECIPMMIRTLMVQ-PPSANDRQHCLREV--MFYL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 425 G----ERCDVETLewsknvFRVPVLDHWWQTETgspitasCVGLgnsKTPPPGQA------GKSVPGYNVMILDDNMQKL 494
Cdd:PRK08008 298 NlsdqEKDAFEER------FGVRLLTSYGMTET-------IVGI---IGDRPGDKrrwpsiGRPGFCYEAEIRDDHNRPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 495 KARCLGNIVVKLPlpPGA--FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIE 572
Cdd:PRK08008 362 PAGEIGEICIKGV--PGKtiFKEYYLDPKATAKVLEAD--GWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 573 ESILSHGTVADCAVVGKEDPLKGHVPLALCVLrkdiNATEEQVLEEIVKHVRQNIgpvAAFRNAVFV---KQLPKTRSGK 649
Cdd:PRK08008 438 NIIATHPKIQDIVVVGIKDSIRDEAIKAFVVL----NEGETLSEEEFFAFCEQNM---AKFKVPSYLeirKDLPRNCSGK 510
|
....*..
gi 13375727 650 IPRSALS 656
Cdd:PRK08008 511 IIKKNLK 517
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
292-652 |
1.23e-28 |
|
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: 116.74 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 292 HPLYILYTSGTTGLPKGVIRPtggyavmlHWSmssiyglqpgevwWAAS-----DLGWVVGHSYICY-GPLLH-----GN 360
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRS--------ERS-------------WIESfvcneDLFNISGEDAILApGPLSHslflyGA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 361 TTVLYEGKPV---GTPDAGAYFRVLAEHGVAALFTAPTAIRA-IRQQDPgaalgkqysLTRFKTLFVAGERCDVETLEWS 436
Cdd:cd17633 60 ISALYLGGTFigqRKFNPKSWIRKINQYNATVIYLVPTMLQAlARTLEP---------ESKIKSIFSSGQKLFESTKKKL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 437 KNVFRVPVLDHWWQTETGSPITASCvglgNSKTPPPGQAGKSVPGYNVMILDDNmqklkARCLGNIVVKLPLppgAFSGL 516
Cdd:cd17633 131 KNIFPKANLIEFYGTSELSFITYNF----NQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEM---VFSGY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 517 WKNQEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGH 596
Cdd:cd17633 199 VRGGFSNPD-------GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 13375727 597 VPLALCVLRKdinATEEQVLEEIVKHVRQNIGPvaafRNAVFVKQLPKTRSGKIPR 652
Cdd:cd17633 272 IAVALYSGDK---LTYKQLKRFLKQKLSRYEIP----KKIIFVDSLPYTSSGKIAR 320
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
298-655 |
4.02e-28 |
|
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: 116.43 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 298 YTSGTTGLPKgVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLgWVVGHSYICYGPLLHGNTTVLYEGkPVGTPDAGA 377
Cdd:cd05944 9 HTGGTTGTPK-LAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVNGSVVTLLTPLASGAHVVLAG-PAGYRNPGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 378 Y---FRVLAEHGVAALFTAPTAIRAIRQQDPGAALGkqySLtrfKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTEtg 454
Cdd:cd05944 86 FdnfWKLVERYRITSLSTVPTVYAALLQVPVNADIS---SL---RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTE-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 455 spitASCVglgNSKTPP-----PGQAGKSVPGYNVMIL-DDNMQKLKARC----LGNIVVKlplPPGAFsGLWKNQEAFK 524
Cdd:cd05944 158 ----ATCL---VAVNPPdgpkrPGSVGLRLPYARVRIKvLDGVGRLLRDCapdeVGEICVA---GPGVF-GGYLYTEGNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 525 HLYFEkfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVL 604
Cdd:cd05944 227 NAFVA--DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQL 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 13375727 605 RKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFV-KQLPKTRSGKIPRSAL 655
Cdd:cd05944 305 KPGAVVEEEELLA----WARDHVPERAAVPKHIEVlEELPVTAVGKVFKPAL 352
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
263-655 |
4.28e-28 |
|
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: 117.80 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 263 VPLAPGRDLDWDEEMAkaQSHDCVPVL--SEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSiyglqpgevwWAAS 340
Cdd:cd12115 77 VPLDPAYPPERLRFIL--EDAQARLVLtdPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAA----------FSAE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 341 DLGWVVGHSYICY--------GPLLHGNTTVLYEgkpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQD--PGAAlg 410
Cdd:cd12115 145 ELAGVLASTSICFdlsvfelfGPLATGGKVVLAD-------NVLALPDLPAAAEVTLINTVPSAAAELLRHDalPASV-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 411 kqysltrfKTLFVAGE---RCDVETLEWSKNVFRVPVLdhWWQTETGSPITASCVGLGNSKTPPpgqAGKSVPGYNVMIL 487
Cdd:cd12115 216 --------RVVNLAGEplpRDLVQRLYARLQVERVVNL--YGPSEDTTYSTVAPVPPGASGEVS---IGRPLANTQAYVL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 488 DDNMQklkarclgnivvklPLPPGAFSGLWKNQEAFKHLYF-------EKF------PG--YYDTMDAGYMDEEGYLYVM 552
Cdd:cd12115 283 DRALQ--------------PVPLGVPGELYIGGAGVARGYLgrpgltaERFlpdpfgPGarLYRTGDLVRWRPDGLLEFL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 553 SRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinATEEQVLEEIVKHVRQNIGPVAA 632
Cdd:cd12115 349 GRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAE----PGAAGLVEDLRRHLGTRLPAYMV 424
|
410 420
....*....|....*....|...
gi 13375727 633 FRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd12115 425 PSRFVRLDALPLTPNGKIDRSAL 447
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
296-659 |
1.04e-27 |
|
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: 114.35 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 296 ILYTSGTTGLPKGVIRptgGYAVMLHWSMS--SIYGLQPGEVWWAASDLGWVVGhsyicYGPLLHGnttvLYEGKP--VG 371
Cdd:cd17630 5 VILTSGSTGTPKAVVH---TAANLLASAAGlhSRLGFGGGDSWLLSLPLYHVGG-----LAILVRS----LLAGAElvLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 372 TPDAGAYFRvLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEWSKNVfRVPVLDHWWQT 451
Cdd:cd17630 73 ERNQALAED-LAPPGVTHVSLVPTQLQRLLDSGQGPA-----ALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 452 ETGSPITASCVGLgnsktPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWknqeafkhlyfekf 531
Cdd:cd17630 146 ETASQVATKRPDG-----FGRGGVGVLLPGRELRIVEDGEIWVGGASLAMGYLRGQLVPEFNEDGW-------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 532 pgyYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinat 611
Cdd:cd17630 207 ---FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGR------ 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 13375727 612 EEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIV 659
Cdd:cd17630 278 GPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
146-650 |
1.27e-27 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 117.49 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 146 YKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFG 225
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 226 IEPGRRV--EYVPLVEEAlkigqhKPDKILIYNRPNMEAVPLAPGrDLDWDEEMAKAQSHDCVPVlsEHPLYILYTSGTT 303
Cdd:PRK12406 94 LHGLASAlpAGVTVLSVP------TPPEIAAAYRISPALLTPPAG-AIDWEGWLAQQEPYDGPPV--PQPQSMIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 304 GLPKGVIR--PTGGYAVMLHWSMSSIYGLQPGEVwwaasdlgwvvghsYICYGPLLHG--NTTVLYEGKPVGT----P-- 373
Cdd:PRK12406 165 GHPKGVRRaaPTPEQAAAAEQMRALIYGLKPGIR--------------ALLTGPLYHSapNAYGLRAGRLGGVlvlqPrf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 374 DAGAYFRVLAEHGVAALFTAPTAIraIRQQDPGAALGKQYSLTRFKTLFVAGERCDVET----LEWSKNVfrvpVLDHWW 449
Cdd:PRK12406 231 DPEELLQLIERHRITHMHMVPTMF--IRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEWWGPV----IYEYYG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 450 QTETGSPITAScvglGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGaFSglWKNQEAfKHLYFE 529
Cdd:PRK12406 305 STESGAVTFAT----SEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPD-FT--YHNKPE-KRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 530 KfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHvplALC-VLRKDI 608
Cdd:PRK12406 377 R-GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGE---ALMaVVEPQP 452
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 13375727 609 NATEEqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 650
Cdd:PRK12406 453 GATLD--EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKI 492
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
153-655 |
1.37e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 116.39 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 153 VSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIF----GGFASKELSSRIDHVKPKVVVTASfgiep 228
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplnPTLKESVLRYLVADAGGRIVLADA----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 229 grrveyvPLVEEALKIGQHKPDKILIYnrpnmeavplapgrdlDWDEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKG 308
Cdd:cd05922 78 -------GAADRLRDALPASPDPGTVL----------------DADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 309 VIRPTggYAVMLHW-SMSSIYGLQPGEVWWAASDLGWvvghsyiCYG------PLLHGNTTVLYEGkpvGTPDAGaYFRV 381
Cdd:cd05922 135 VRLSH--QNLLANArSIAEYLGITADDRALTVLPLSY-------DYGlsvlntHLLRGATLVLTND---GVLDDA-FWED 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 382 LAEHGVAALFTAPT--AI--RAIRQQDPGAAL-------GK--QYSLTRFKTLFVAGercdvetlewsknvfRVPVLdhW 448
Cdd:cd05922 202 LREHGATGLAGVPStyAMltRLGFDPAKLPSLryltqagGRlpQETIARLRELLPGA---------------QVYVM--Y 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 449 WQTETGSPITAscvglgnskTPP------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWkNQEA 522
Cdd:cd05922 265 GQTEATRRMTY---------LPPerilekPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN---VMKGYW-NDPP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 523 FKhLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVplALC 602
Cdd:cd05922 332 YR-RKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKL--ALF 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 13375727 603 VLRKDinateEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05922 409 VTAPD-----KIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
140-650 |
1.50e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 116.93 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 140 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 219
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 220 VTaSFGiepgrrveyvpLVEEALKIGQHKPDKIliynrPNMEAVPLAPGRDLDWDEEMAkAQSHDcvPVLSEHPLY-ILY 298
Cdd:PRK08276 88 IV-SAA-----------LADTAAELAAELPAGV-----PLLLVVAGPVPGFRSYEEALA-AQPDT--PIADETAGAdMLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 299 TSGTTGLPKGVIRPtggyavmlhwsmssIYGLQPGEV-----WWAASDLGWVVGHSYICYGPLLH-------------GN 360
Cdd:PRK08276 148 SSGTTGRPKGIKRP--------------LPGLDPDEApgmmlALLGFGMYGGPDSVYLSPAPLYHtaplrfgmsalalGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 361 TTVLYEG-KPVGTPDAGAYFRVLAEHGVAALFTA----PTAIRAirqqdpgaalgkQYSLTRFKTLFVAGERCDVET--- 432
Cdd:PRK08276 214 TVVVMEKfDAEEALALIERYRVTHSQLVPTMFVRmlklPEEVRA------------RYDVSSLRVAIHAAAPCPVEVkra 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 433 -LEWSKnvfrvPVLDHWWQTETGSPITAScvglgNSKT--PPPGQAGKSVPGyNVMILDDNMQKLKARCLGNIVVKLPLP 509
Cdd:PRK08276 282 mIDWWG-----PIIHEYYASSEGGGVTVI-----TSEDwlAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGY 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 510 PgaFSGLwKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVInvaghrISAGA------IEESILSHGTVAD 583
Cdd:PRK08276 351 P--FEYH-NDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI------ISGGVniypqeIENLLVTHPKVAD 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13375727 584 CAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 650
Cdd:PRK08276 420 VAVFGVPDEEMGERVKAVVQPADGADAGDALA-AELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
126-655 |
1.51e-27 |
|
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: 116.66 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 205
Cdd:cd05920 29 PDRIAVVDG------DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 ELSSRIDHVKPKVVVTAsfgiEPGRRVEYVPLVEEalkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdc 285
Cdd:cd05920 103 ELSAFCAHAEAVAYIVP----DRHAGFDHRALARE--------------------------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 286 vpVLSEHP--LYILYTSGTTGLPKGVIRPTGGYAVMLHWSmSSIYGLQPGEVWWAASDlgwvVGHSYICYGP-----LLH 358
Cdd:cd05920 134 --LAESIPevALFLLSGGTTGTPKLIPRTHNDYAYNVRAS-AEVCGLDQDTVYLAVLP----AAHNFPLACPgvlgtLLA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 359 GNTTVLyegkpVGTPDAGAYFRVLAEHGVaalfTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEwskn 438
Cdd:cd05920 207 GGRVVL-----APDPSPDAAFPLIEREGV----TVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALAR---- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 439 vfRV-PVLDHWWQTETGspiTAScvGLGNSKTP--PP----GQAGKSV-PGYNVMILDDNmqklkarclGNivvklPLPP 510
Cdd:cd05920 274 --RVpPVLGCTLQQVFG---MAE--GLLNYTRLddPDeviiHTQGRPMsPDDEIRVVDEE---------GN-----PVPP 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 511 GA-----------FSGLWK----NQEAFKHlyfekfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESI 575
Cdd:cd05920 333 GEegelltrgpytIRGYYRapehNARAFTP------DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLL 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 576 LSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinatEEQVLEEIVKHVRQNIGpVAAFR---NAVFVKQLPKTRSGKIPR 652
Cdd:cd05920 407 LRHPAVHDAAVVAMPDELLGERSCAFVVLR------DPPPSAAQLRRFLRERG-LAAYKlpdRIEFVDSLPLTAVGKIDK 479
|
...
gi 13375727 653 SAL 655
Cdd:cd05920 480 KAL 482
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
296-655 |
2.61e-27 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 115.46 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 296 ILYTSGTTGLPKGVirptggyaVMLHWSMSS-IYGLQpgEVW-WAASD-----LGWVVGHSYI--CYGPLLHGNTTVLye 366
Cdd:cd05941 94 ILYTSGTTGRPKGV--------VLTHANLAAnVRALV--DAWrWTEDDvllhvLPLHHVHGLVnaLLCPLFAGASVEF-- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 367 gkpVGTPDAGAYFRVLAEHGVAALFTAPTA----IRAIRQQDPGAALGKQYSLTRFKtLFVAGERC-DVETLEWSKNVFR 441
Cdd:cd05941 162 ---LPKFDPKEVAISRLMPSITVFMGVPTIytrlLQYYEAHFTDPQFARAAAAERLR-LMVSGSAAlPVPTLEEWEAITG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 442 VPVLDHWWQTETGspITASCvGLGNSKTPppGQAGKSVPGYNVMILDDNMQK-LKARCLGNIVVKlplPPGAFSGLWKNQ 520
Cdd:cd05941 238 HTLLERYGMTEIG--MALSN-PLDGERRP--GTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVR---GPSVFKEYWNKP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 521 EAFKhlyfEKFP--GYYDTMDAGYMDEEGYLYVMSRV-DDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHV 597
Cdd:cd05941 310 EATK----EEFTddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGER 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 13375727 598 PLALCVLRKDINATEeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05941 386 VVAVVVLRAGAAALS---LEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
127-655 |
2.85e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 116.26 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIydspVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 206
Cdd:PRK13390 12 DRPAVI----VAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 LSSRIDHVKPKVVVTASfgiepgrrveyvPLVEEALKIGQHKPDKILIYNRPNMEAvplapgrdlDWDEEMAKAQshdcv 286
Cdd:PRK13390 88 ADYIVGDSGARVLVASA------------ALDGLAAKVGADLPLRLSFGGEIDGFG---------SFEAALAGAG----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 287 PVLSEHPL--YILYTSGTTGLPKGvIRPT---------GGYAVMLhwsMSSIYGLQPGEVWWA------ASDLGWvvghs 349
Cdd:PRK13390 142 PRLTEQPCgaVMLYSSGTTGFPKG-IQPDlpgrdvdapGDPIVAI---ARAFYDISESDIYYSsapiyhAAPLRW----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 350 yiCygPLLH--GNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIraIRQQDPGAALGKQYSLTRFKTLFVAGER 427
Cdd:PRK13390 213 --C--SMVHalGGTVVLAK-----RFDAQATLGHVERYRITVTQMVPTMF--VRLLKLDADVRTRYDVSSLRAVIHAAAP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 428 CDVET----LEWSKNVfrvpVLDHWWQTET-GSPITASCVGLGNsktppPGQAGKSVPGyNVMILDDNMQKLKARCLGNI 502
Cdd:PRK13390 282 CPVDVkhamIDWLGPI----VYEYYSSTEAhGMTFIDSPDWLAH-----PGSVGRSVLG-DLHICDDDGNELPAGRIGTV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 503 VVKLPLPPGAFSGLWKNQEAFKHlyfEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVA 582
Cdd:PRK13390 352 YFERDRLPFRYLNDPEKTAAAQH---PAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVH 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13375727 583 DCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK13390 429 DVAVIGVPDPEMGEQVKAVIQLVEGIRGSDE-LARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
144-650 |
5.79e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 115.64 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA- 222
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 SFgiepgRRVEYVPLVEEALKIGQHKPDKILIYNR-PNMEAV----PLAPGRDLDWDEEMAKA------------QSHDC 285
Cdd:PRK12583 126 AF-----KTSDYHAMLQELLPGLAEGQPGALACERlPELRGVvslaPAPPPGFLAWHELQARGetvsrealaerqASLDR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 286 vpvlsEHPLYILYTSGTTGLPKGvirptggyAVMLHWSMssiyglqpgevwwaaSDLGWVVGHS---------------Y 350
Cdd:PRK12583 201 -----DDPINIQYTSGTTGFPKG--------ATLSHHNI---------------LNNGYFVAESlgltehdrlcvpvplY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 351 ICYGPLL-------HGNTTVLyegkPVGTPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPGAalgkqYSLTRFKTLF 422
Cdd:PRK12583 253 HCFGMVLanlgcmtVGACLVY----PNEAFDPLATLQAVEEERCTALYGVPTMfIAELDHPQRGN-----FDLSSLRTGI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 423 VAGERCDVETLEWSKNVFRVP-VLDHWWQTETgSPIT------------ASCVG-------------LGNskTPPPGQAG 476
Cdd:PRK12583 324 MAGAPCPIEVMRRVMDEMHMAeVQIAYGMTET-SPVSlqttaaddlerrVETVGrtqphlevkvvdpDGA--TVPRGEIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 477 K-SVPGYNVMIlddnmqklkarclgnivvklplppgafsGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRV 555
Cdd:PRK12583 401 ElCTRGYSVMK----------------------------GYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 556 DDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRN 635
Cdd:PRK12583 451 KDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASE----EELREFCKARIAHFKVPRY 526
|
570
....*....|....*
gi 13375727 636 AVFVKQLPKTRSGKI 650
Cdd:PRK12583 527 FRFVDEFPMTVTGKV 541
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
127-658 |
6.27e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.96 E-value: 6.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIydspvtNTKATFTYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 205
Cdd:PRK06839 17 DRIAII------TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 ELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIgqhkpdkilIYNRPNMEAVPLApgrdldwdeEMAKAQSHDC 285
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEK---------TFQNMALSMQKV---------SYVQRVISITSLK---------EIEDRKIDNF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 286 VPVLSEHPLYILYTSGTTGLPKGvirptggyAVMLHWSM--SSIYGLqpgevwwAASDLgwVVGHSYICYGPLLH-GNTT 362
Cdd:PRK06839 144 VEKNESASFIICYTSGTTGKPKG--------AVLTQENMfwNALNNT-------FAIDL--TMHDRSIVLLPLFHiGGIG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 363 V-----LYEGKPVGTP---DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVetle 434
Cdd:PRK06839 207 LfafptLFAGGVIIVPrkfEPTKALSMIEKHKVTVVMGVPTIHQALIN----CSKFETTNLQSVRWFYNGGAPCPE---- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 435 wsknvfrvPVLDHWwqTETGSPITAscvGLGNSKTPP-------------PGQAGKSVPGYNVMILDDNMQKLKARCLGN 501
Cdd:PRK06839 279 --------ELMREF--IDRGFLFGQ---GFGMTETSPtvfmlseedarrkVGSIGKPVLFCDYELIDENKNKVEVGEVGE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 502 IVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTV 581
Cdd:PRK06839 346 LLIR---GPNVMKEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDV 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13375727 582 ADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 658
Cdd:PRK06839 420 YEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIE----HCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
127-655 |
1.71e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 110.94 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSpvtnTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIfggfaske 206
Cdd:PRK13391 12 DKPAVIMAS----TGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 lSSRIdhvkpkvvvtasfgiepgrrveyvpLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGR--------DLDWDEEMA 278
Cdd:PRK13391 80 -NSHL-------------------------TPAEAAYIVDDSGARALITSAAKLDVARALLKQcpgvrhrlVLDGDGELE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 279 KAQSH-DCVPVLSEHPL-------YILYTSGTTGLPKGVIRP--------TGGYAVMLHwsmsSIYGLQPGEVwwaasdl 342
Cdd:PRK13391 134 GFVGYaEAVAGLPATPIadeslgtDMLYSSGTTGRPKGIKRPlpeqppdtPLPLTAFLQ----RLWGFRSDMV------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 343 gwvvghsYICYGPLLH-------------GNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDpgaA 408
Cdd:PRK13391 203 -------YLSPAPLYHsapqravmlvirlGGTVIVME-----HFDAEQYLALIEEYGVTHTQLVPTMfSRMLKLPE---E 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 409 LGKQYSLTRFKTLFVAGERCDVETLEwsknvfrvPVLDhWWqtetgSPIT----ASCVGLGNSKTPP------PGQAGKS 478
Cdd:PRK13391 268 VRDKYDLSSLEVAIHAAAPCPPQVKE--------QMID-WW-----GPIIheyyAATEGLGFTACDSeewlahPGTVGRA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 479 VPGyNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAfKHlyfeKFPGYYDTMDAGYMDEEGYLYVMSRVDDV 558
Cdd:PRK13391 334 MFG-DLHILDDDGAELPPGEPGTIWFEGGRPFEYLNDPAKTAEA-RH----PDGTWSTVGDIGYVDEDGYLYLTDRAAFM 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 559 INVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVF 638
Cdd:PRK13391 408 IISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPA-LAAELIAFCRQRLSRQKCPRSIDF 486
|
570
....*....|....*..
gi 13375727 639 VKQLPKTRSGKIPRSAL 655
Cdd:PRK13391 487 EDELPRLPTGKLYKRLL 503
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
126-650 |
2.11e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 110.81 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 126 GDKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFAS 204
Cdd:PRK08162 32 PDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIP-AMVEAhFGVPMAGAVLNTLNTRLDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 205 KELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIGQHkpDKILIYNRPNMEAVPLAPGRDLDW-------DEEM 277
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIVDT---------EFAEVAREALALLPG--PKPLVIDVDDPEYPGGRFIGALDYeaflasgDPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 278 AKAQSHDCVPVLSehplyILYTSGTTGLPKGVIRPTGGYAVM-----LHWSMS--SIYglqpgevwwaasdLgWVVghsy 350
Cdd:PRK08162 174 AWTLPADEWDAIA-----LNYTSGTTGNPKGVVYHHRGAYLNalsniLAWGMPkhPVY-------------L-WTL---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 351 icygPLLHGN------TTVLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLF 422
Cdd:PRK08162 231 ----PMFHCNgwcfpwTVAARAGTNVCLRkvDPKLIFDLIREHGVTHYCGAPIVLSALIN----APAEWRAGIDHPVHAM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 423 VAGERCDVETLEWSKNV-FRVpvlDHWWQ-TETGSPITASCVGLGNSKTPPPGQAG-KSVPGYN------VMILD-DNMQ 492
Cdd:PRK08162 303 VAGAAPPAAVIAKMEEIgFDL---THVYGlTETYGPATVCAWQPEWDALPLDERAQlKARQGVRyplqegVTVLDpDTMQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 493 KLKA----------RclGNIVVKlplppgafsGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINV 561
Cdd:PRK08162 380 PVPAdgetigeimfR--GNIVMK---------GYLKNPKATE----EAFAgGWFHTGDLAVLHPDGYIKIKDRSKDIIIS 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 562 AGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIgpvAAFR--NAVFV 639
Cdd:PRK08162 445 GGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATE----EEIIAHCREHL---AGFKvpKAVVF 517
|
570
....*....|.
gi 13375727 640 KQLPKTRSGKI 650
Cdd:PRK08162 518 GELPKTSTGKI 528
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
143-657 |
4.79e-25 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 109.85 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 222
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 SfgiepgrrvEYVPLVEEALKigqHKPDKILIynrpnmEAVPLAPGRDLDwdEEMAKAQSHDCVPVLSEHPLYILYTSGT 302
Cdd:PRK13382 148 E---------EFSATVDRALA---DCPQATRI------VAWTDEDHDLTV--EVLIAAHAGQRPEPTGRKGRVILLTSGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 303 TGLPKGVIRP-TGGYAVMlhwsmSSIYGLQPgevwWAASDLGWVVGhsyicygPLLH--GNTTVLYEGKPVGTP------ 373
Cdd:PRK13382 208 TGTPKGARRSgPGGIGTL-----KAILDRTP----WRAEEPTVIVA-------PMFHawGFSQLVLAASLACTIvtrrrf 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 374 DAGAYFRVLAEHGVAALFTAPTAIRaiRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTET 453
Cdd:PRK13382 272 DPEATLDLIDRHRATGLAVVPVMFD--RIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 454 GSPITASCVGLGNSktppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVK-LPLPPGAFSGLWKNQEAfkhlyfekfp 532
Cdd:PRK13382 350 GMIATATPADLRAA----PDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRnDTQFDGYTSGSTKDFHD---------- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 533 GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATE 612
Cdd:PRK13382 416 GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATP 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 13375727 613 eqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:PRK13382 496 ----ETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
137-655 |
4.83e-25 |
|
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: 109.29 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 137 VTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKP 216
Cdd:cd17646 17 VVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 217 KVVVTASFGIEPGRRVEYVPLVEEalkigqhkpdkiliynrpnmEAVPLAPGRDLDwdeemakaqshdcVPVLSEHPLYI 296
Cdd:cd17646 97 AVVLTTADLAARLPAGGDVALLGD--------------------EALAAPPATPPL-------------VPPRPDNLAYV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 297 LYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLYEgkPVGTPDAG 376
Cdd:cd17646 144 IYTSGSTGRPKGVMVTHAGIVNRLLW-MQDEYPLGPGDRVLQKTPLSFDVSVWEL-FWPLVAGARLVVAR--PGGHRDPA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 377 AYFRVLAEHGVAALFTAPTAIRA-IRQQDPGAALgkqySLTRfktLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGS 455
Cdd:cd17646 220 YLAALIREHGVTTCHFVPSMLRVfLAEPAAGSCA----SLRR---VFCSGEALPPELAARFLALPGAELHNLYGPTEAAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 456 PITA-SCVGlgnSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGL----------WKNQEAfk 524
Cdd:cd17646 293 DVTHwPVRG---PAETPSVPIGRPVPNTRLYVLDDALR--------------PVPVGVPGELylggvqlargYLGRPA-- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 525 hLYFEKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGH 596
Cdd:cd17646 354 -LTAERFvpdpfgPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAA 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13375727 597 VPLALCVLRKDINATEEQVLEEivkHVRQNIGPV---AAFrnaVFVKQLPKTRSGKIPRSAL 655
Cdd:cd17646 433 RLVGYVVPAAGAAGPDTAALRA---HLAERLPEYmvpAAF---VVLDALPLTANGKLDRAAL 488
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
228-655 |
5.26e-25 |
|
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: 109.00 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 228 PGRRVEYVPLVEEALKIGQHKPDKILiynrPNMEAVPLAPGRDLDWDEEMAkAQSHDCVPVLSEhPLYILYTSGTTGLPK 307
Cdd:cd05929 68 CPAYKSSRAPRAEACAIIEIKAAALV----CGLFTGGGALDGLEDYEAAEG-GSPETPIEDEAA-GWKMLYSGGTTGRPK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 308 GVIRPTGGyavmlhwsmssiyGLQPGEVWWAASDL-GWVVGHSYICYGPLLHG------NTTVLYEGKPVGTP--DAGAY 378
Cdd:cd05929 142 GIKRGLPG-------------GPPDNDTLMAAALGfGPGADSVYLSPAPLYHAapfrwsMTALFMGGTLVLMEkfDPEEF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 379 FRVLAEHGVAALFTAPTAIRAIRQQdPGAALGKqYSLTRFKTLFVAGERCDVET----LEWSKnvfrvPVLdhwWQTETG 454
Cdd:cd05929 209 LRLIERYRVTFAQFVPTMFVRLLKL-PEAVRNA-YDLSSLKRVIHAAAPCPPWVkeqwIDWGG-----PII---WEYYGG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 455 SPITASCVGLGNSKTPPPGQAGKSVPGyNVMILDDNMQklkarclgnivvklPLPPGAFSGLW-KNQEAFK-HLYFEKFP 532
Cdd:cd05929 279 TEGQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGN--------------EVPPGEIGEVYfANGPGFEyTNDPEKTA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 533 -----GYYDTM-DAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALcVLRK 606
Cdd:cd05929 344 aarneGGWSTLgDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAV-VQPA 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 13375727 607 DINATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05929 423 PGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
571-649 |
7.84e-25 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 98.39 E-value: 7.84e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13375727 571 IEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGK 649
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLE----EELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
144-655 |
8.70e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 108.36 E-value: 8.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTas 223
Cdd:PRK09088 23 WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 224 fgiepgrrveyvplveealkigqhkpDKILIYNRPNMEAVplapgrdldwDEEMAKAQSHDCVPVLS---EHPLYILYTS 300
Cdd:PRK09088 101 --------------------------DDAVAAGRTDVEDL----------AAFIASADALEPADTPSippERVSLILFTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 301 GTTGLPKGVirptggyavmlhwsMSSIYGLQPGEVWWaaSDLGWVVGHS-YICYGPLLH--GNTT----VLYEGKPVGTP 373
Cdd:PRK09088 145 GTSGQPKGV--------------MLSERNLQQTAHNF--GVLGRVDAHSsFLCDAPMFHiiGLITsvrpVLAVGGSILVS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 374 D---AGAYFRVLAEH--GVAALFTAPTAIRAIRQQdPGAALGkqySLTRFKTLFVAGERCDVETLEWSKNVfRVPVLDHW 448
Cdd:PRK09088 209 NgfePKRTLGRLGDPalGITHYFCVPQMAQAFRAQ-PGFDAA---ALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 449 WQTETGS--PITASCvGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHL 526
Cdd:PRK09088 284 GMSEAGTvfGMSVDC-DVIRAKA---GAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR---GPNLSPGYWRRPQATARA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 527 YFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLaLCVLRK 606
Cdd:PRK09088 357 FTGD--GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGY-LAIVPA 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 13375727 607 DINATEeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK09088 434 DGAPLD---LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
127-655 |
9.50e-25 |
|
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: 107.72 E-value: 9.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIhslifggfaske 206
Cdd:cd17652 2 DAPAVVFGD------ETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAA------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 lssridhvkpkvvvtasfgiepgrrveYVPLveealkigqhkpdkiliynrpnmeavplapgrDLDWDEEMAKAQSHDCV 286
Cdd:cd17652 64 ---------------------------YLPL--------------------------------DPAYPAERIAYMLADAR 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 287 PVL----SEHPLYILYTSGTTGLPKGVirptggyaVMLHWSMSSI-------YGLQPGEVWWAASDLGWVVGHSYICyGP 355
Cdd:cd17652 85 PALllttPDNLAYVIYTSGSTGRPKGV--------VVTHRGLANLaaaqiaaFDVGPGSRVLQFASPSFDASVWELL-MA 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 356 LLHGNTTVLyegKPVGTPDAGAYF-RVLAEHGVAALFTAPTAIRAIrqqDPGAALGkqysltrFKTLFVAGERCDVETLE 434
Cdd:cd17652 156 LLAGATLVL---APAEELLPGEPLaDLLREHRITHVTLPPAALAAL---PPDDLPD-------LRTLVVAGEACPAELVD 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 435 -WSKNvfRVpVLDHWWQTETgsPITASCVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPG-- 511
Cdd:cd17652 223 rWAPG--RR-MINAYGPTET--TVCATMAGPLPGGGVPP--IGRPVPGTRVYVLDARLR--------------PVPPGvp 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 512 -----AFSGLWK---NQEAfkhLYFEKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEES 574
Cdd:cd17652 282 gelyiAGAGLARgylNRPG---LTAERFvadpfgaPGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAA 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 575 ILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPvAAFrnaVFVKQLPKTRSGKIPRSA 654
Cdd:cd17652 359 LTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVP-AAF---VVLDALPLTPNGKLDRRA 434
|
.
gi 13375727 655 L 655
Cdd:cd17652 435 L 435
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
139-657 |
1.32e-24 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 108.53 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 139 NTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKV 218
Cdd:PLN02246 46 ATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 219 VVTASFGIEPGRRVEYVPLVEeALKIGQHkPDKILIYNrpnmeavplapgrdldwdeEMAKAQSHDCvPVLSEHP---LY 295
Cdd:PLN02246 126 IITQSCYVDKLKGLAEDDGVT-VVTIDDP-PEGCLHFS-------------------ELTQADENEL-PEVEISPddvVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 296 ILYTSGTTGLPKGVirptggyavML-HWSM-SSIYGLQPGEVwwaaSDLGWVVGHSYICYGPLLH--GNTTVLYEGKPVG 371
Cdd:PLN02246 184 LPYSSGTTGLPKGV---------MLtHKGLvTSVAQQVDGEN----PNLYFHSDDVILCVLPMFHiySLNSVLLCGLRVG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 372 TP-------DAGAYFRVLAEHGV-AALFTAP----------------TAIR---------------AIRQQDPGAALGKQ 412
Cdd:PLN02246 251 AAilimpkfEIGALLELIQRHKVtIAPFVPPivlaiakspvvekydlSSIRmvlsgaaplgkeledAFRAKLPNAVLGQG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 413 YSLTRfktlfvAGercdvetlewsknvfrvPVLdhwwqtetgspitASCvgLGNSKTP---PPGQAGKSVPGYNVMILDD 489
Cdd:PLN02246 331 YGMTE------AG-----------------PVL-------------AMC--LAFAKEPfpvKSGSCGTVVRNAELKIVDP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 490 NMQKLKARCL-GNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISA 568
Cdd:PLN02246 373 ETGASLPRNQpGEICIR---GPQIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAP 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 569 GAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHV--RQNIGPVaafrnaVFVKQLPKTR 646
Cdd:PLN02246 448 AELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVvfYKRIHKV------FFVDSIPKAP 521
|
570
....*....|.
gi 13375727 647 SGKIPRSALSA 657
Cdd:PLN02246 522 SGKILRKDLRA 532
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
127-655 |
1.34e-24 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 108.30 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIiydspVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 206
Cdd:PRK06087 38 DKIAV-----VDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 LSSRIDHVKPKVVVTASFGiepgRRVEYVPL---VEEALKIGQHKP--DKiliyNRPNMEAVPLApgRDLDWDEEMAKAq 281
Cdd:PRK06087 113 LVWVLNKCQAKMFFAPTLF----KQTRPVDLilpLQNQLPQLQQIVgvDK----LAPATSSLSLS--QIIADYEPLTTA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 282 shdcVPVLSEHPLYILYTSGTTGLPKGVIRpTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNT 361
Cdd:PRK06087 182 ----ITTHGDELAAVLFTSGTEGLPKGVML-THNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 362 TVLYEgkpvgtpdagayfrvlaehgvaaLFTAPTAIRAIRQQDPGAALGKqysltrfkTLFVAGERCDVETLEWSKNVFR 441
Cdd:PRK06087 257 SVLLD-----------------------IFTPDACLALLEQQRCTCMLGA--------TPFIYDLLNLLEKQPADLSALR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 442 --------VP--VLDHWWQTET------GSpiTASC----VGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGN 501
Cdd:PRK06087 306 fflcggttIPkkVARECQQRGIkllsvyGS--TESSphavVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 502 IVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTV 581
Cdd:PRK06087 384 EASR---GPNVFMGYLDEPELTARALDEE--GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKI 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13375727 582 ADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvLEEIV-----KHVRQNIGPvaafRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK06087 459 HDACVVAMPDERLGERSCAYVVLKAPHHSLT---LEEVVaffsrKRVAKYKYP----EHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
127-655 |
2.45e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 109.48 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfASKE 206
Cdd:PRK12467 527 ERPALVFG------EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGG---------AYVP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 LSSRidhvkpkvvvtasfgiEPGRRVEYVpLVEEALKIGQHKPDKILIYNRP-NMEAVPLapgrDLDWDEEMAKAQSHDC 285
Cdd:PRK12467 592 LDPE----------------YPQDRLAYM-LDDSGVRLLLTQSHLLAQLPVPaGLRSLCL----DEPADLLCGYSGHNPE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 286 VPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLY 365
Cdd:PRK12467 651 VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCV-IAERLQLAADDSMLMVSTFAFDLGVTEL-FGALASGATLHLL 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 366 EgkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAALgkqysLTRFKTLFVAGERCDVETL-EWSKNVFRVPV 444
Cdd:PRK12467 729 P--PDCARDAEAFAALMADQGVTVLKIVPSHLQAL-LQASRVAL-----PRPQRALVCGGEALQVDLLaRVRALGPGARL 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 445 LDHWWQTETGSPITA-SCVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLWKNQEAF 523
Cdd:PRK12467 801 INHYGPTETTVGVSTyELSDEERDFGNVP--IGQPLANLGLYILDHYLN--------------PVPVGVVGELYIGGAGL 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 524 KHLYF-------EKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADcAVV 587
Cdd:PRK12467 865 ARGYHrrpaltaERFvpdpfgaDGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVRE-AVV 943
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13375727 588 GKEDPLKGHVPLALCVLRKDINATEEQVL-EEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK12467 944 LAQPGDAGLQLVAYLVPAAVADGAEHQATrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
62-116 |
3.11e-23 |
|
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: 92.92 E-value: 3.11e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 13375727 62 YKTHFAASVTDPERFWGKAAEQISWYKPWTKTLENKHSPSTRWFVEGMLNICYNA 116
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGPFAKWFVGGKLNVCYNC 55
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
140-655 |
6.86e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 103.14 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 140 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 219
Cdd:PLN02330 52 TGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 220 VT--ASFGIEPGRRVEYVPLVEEAlkigqhkpdkilIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDCVpvlsehplyIL 297
Cdd:PLN02330 132 VTndTNYGKVKGLGLPVIVLGEEK------------IEGAVNWKELLEAADRAGDTSDNEEILQTDLCA---------LP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 298 YTSGTTGLPKGVIRPTGGYAVMLhwsMSSIYGLQPgEVWWAASDLGWV-VGHSY----ICYGPLLHGNTTVLyegkpVGT 372
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVANL---CSSLFSVGP-EMIGQVVTLGLIpFFHIYgitgICCATLRNKGKVVV-----MSR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 373 PDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPgaaLGKQYSLTRFK--TLFVAGERCDVETLEWSKNVF-RVPVLDHWW 449
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNL-VKNP---IVEEFDLSKLKlqAIMTAAAPLAPELLTAFEAKFpGVQVQEAYG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 450 QTEtgspitASCVGLGNSKtPPPGQA-------GKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQE 521
Cdd:PLN02330 338 LTE------HSCITLTHGD-PEKGHGiakknsvGFILPNLEVKFIDpDTGRSLPKNTPGELCVR---SQCVMQGYYNNKE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 522 AFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLAL 601
Cdd:PLN02330 408 ETDRTIDED--GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAAC 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 13375727 602 CVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PLN02330 486 VVINPKAKESEEDILN----FVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
133-669 |
1.07e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 103.19 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 133 YDSPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGaihslIFGGFASKELSsRID 212
Cdd:PRK06060 20 YDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARG-----VMAFLANPELH-RDD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 213 HVKPKVVVTASFGIEPGrrveyvPLVEealkigQHKPDKILiynrpnmEAVPLApgrdldwdEEMAKAQSHDCVPVLSEH 292
Cdd:PRK06060 94 HALAARNTEPALVVTSD------ALRD------RFQPSRVA-------EAAELM--------SEAARVAPGGYEPMGGDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 293 PLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPgevwwaaSDLGWVVGHSYICYG-------PLLHGNTTVLy 365
Cdd:PRK06060 147 LAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTP-------EDTGLCSARMYFAYGlgnsvwfPLATGGSAVI- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 366 EGKPVGTPDAG---AYFRVLAEHGVAALFT------APTAIRAIRqqdpgaalgkqysltrfkTLFVAGERCDVETLEWS 436
Cdd:PRK06060 219 NSAPVTPEAAAilsARFGPSVLYGVPNFFArvidscSPDSFRSLR------------------CVVSAGEALELGLAERL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 437 KNVFR-VPVLDHWWQTETGSPITASCVGLGNsktppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSG 515
Cdd:PRK06060 281 MEFFGgIPILDGIGSTEVGQTFVSNRVDEWR-----LGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVR---GPAIAKG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 516 LWKNQEAFkhLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKG 595
Cdd:PRK06060 353 YWNRPDSP--VANE---GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGA 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 596 HVPLALCVlrkdiNATEEQVLEEIVKHV-RQNIGPVAAF----RNAVfVKQLPKTRSGKIPRSALSAIVNGKP-YKITST 669
Cdd:PRK06060 428 STLQAFLV-----ATSGATIDGSVMRDLhRGLLNRLSAFkvphRFAV-VDRLPRTPNGKLVRGALRKQSPTKPiWELSLT 501
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
145-681 |
8.08e-22 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 99.86 E-value: 8.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT-A 222
Cdd:PRK05620 40 TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAdP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 SFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAV---PLAPGR--DLDWdeemakaqshdcvPVLSEH-PLYI 296
Cdd:PRK05620 120 RLAEQLGEILKECPCVRAVVFIGPSDADSAAAHMPEGIKVYsyeALLDGRstVYDW-------------PELDETtAAAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 297 LYTSGTTGLPKGVIrptggyavmlhWSMSSIYgLQPGEVWWAASdLGWVVGHSYICYGPLLHgnttVLYEGKPVGTPDAG 376
Cdd:PRK05620 187 CYSTGTTGAPKGVV-----------YSHRSLY-LQSLSLRTTDS-LAVTHGESFLCCVPIYH----VLSWGVPLAAFMSG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 377 AYFrVLAEHGVaalfTAPTAIRAIRQQDPGAALG-----------------KQYSLTrfkTLFVAGERCDVETLEWSKNV 439
Cdd:PRK05620 250 TPL-VFPGPDL----SAPTLAKIIATAMPRVAHGvptlwiqlmvhylknppERMSLQ---EIYVGGSAVPPILIKAWEER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 440 FRVPVLDHWWQTETgSPItascvglGNSKTPPPGQAGKSVPGYNV------------MILDDNMQKLKARCLGNIVVKLP 507
Cdd:PRK05620 322 YGVDVVHVWGMTET-SPV-------GTVARPPSGVSGEARWAYRVsqgrfpasleyrIVNDGQVMESTDRNEGEIQVRGN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 508 LPPGAFSGLWKNQEAFKHLYF---------EKFP--GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 576
Cdd:PRK05620 394 WVTASYYHSPTEEGGGAASTFrgedvedanDRFTadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 577 SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALS 656
Cdd:PRK05620 474 AAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETA-ERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
570 580
....*....|....*....|....*
gi 13375727 657 AIVNGKPYKITsTIEDPSIFGHVEE 681
Cdd:PRK05620 553 QHLADGDFEII-KLKGPGESGESDS 576
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
291-652 |
1.54e-21 |
|
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: 96.56 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 291 EHPLYILYTSGTTGLPKGV-IRPTGGYAVMLH-------WSMSSI-YGLQP----GEVWWAASDL----GWVVGHSYICY 353
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVlLANKTFFAVPDIlqkeglnWVVGDVtYLPLPathiGGLWWILTCLihggLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 354 GPLlhgnttvlyegkpvgtpdagayFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkQYSlTRFKTLFVAGERC---DV 430
Cdd:cd17635 81 KSL----------------------FKILTTNAVTTTCLVPTLLSKLVSELKSAN---ATV-PSLRLIGYGGSRAiaaDV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 431 ETLEWSKNVfrvPVLDHWWQTETGspiTASCVGLGNSkTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPP 510
Cdd:cd17635 135 RFIEATGLT---NTAQVYGLSETG---TALCLPTDDD-SIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIK---SP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 511 GAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKE 590
Cdd:cd17635 205 ANMLGYWNNPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEIS 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13375727 591 DPLKGHVpLALCVLRKDINatEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 652
Cdd:cd17635 282 DEEFGEL-VGLAVVASAEL--DENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
88-652 |
1.57e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 98.92 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 88 KPWTKTLENKHSPSTRWFVEGMLNICYNAVDRHiengkGDKIAIIYdspvtnTKATFTYKEVLEQVSKLAGVLVKHGIKK 167
Cdd:PRK05605 13 KPWLQSYAPWTPHDLDYGDTTLVDLYDNAVARF-----GDRPALDF------FGATTTYAELGKQVRRAAAGLRALGVRP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 168 GDTVVIYMPMIPQAMYTMLACARIGAI---HSLIfggFASKELSSR-IDHvKPKVVV----TASF--GIEPGRRVEYV-- 235
Cdd:PRK05605 82 GDRVAIVLPNCPQHIVAFYAVLRLGAVvveHNPL---YTAHELEHPfEDH-GARVAIvwdkVAPTveRLRRTTPLETIvs 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 236 -------PLVEE-ALKIgqhkPDKILIYNRPNMEAVplAPGRdLDWDEEMAKA-----QSHDCVPVLSEHPLYILYTSGT 302
Cdd:PRK05605 158 vnmiaamPLLQRlALRL----PIPALRKARAALTGP--APGT-VPWETLVDAAiggdgSDVSHPRPTPDDVALILYTSGT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 303 TGLPKGVIRPTGGY---AVM-LHWsmssIYGLQPG-EVWWAASDLgwvvghsYICYGPLLHGNTTVLYEGKPV--GTPDA 375
Cdd:PRK05605 231 TGKPKGAQLTHRNLfanAAQgKAW----VPGLGDGpERVLAALPM-------FHAYGLTLCLTLAVSIGGELVllPAPDI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 376 GAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETLEwsknvfrvpvldhWWQTETG- 454
Cdd:PRK05605 300 DLILDAMKKHPPTWLPGVPPLYEKIAE----AAEERGVDLSGVRNAFSGAMALPVSTVE-------------LWEKLTGg 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 455 -----------SPITascvgLGN--SKTPPPGQAGKSVPGYNVMILD-DNMQKLKARC-LGNIVVKlplPPGAFSGLWKN 519
Cdd:PRK05605 363 llvegygltetSPII-----VGNpmSDDRRPGYVGVPFPDTEVRIVDpEDPDETMPDGeEGELLVR---GPQVFKGYWNR 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 520 QEAFKHLYfekFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVG--KEDplkGHV 597
Cdd:PRK05605 435 PEETAKSF---LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGlpRED---GSE 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 13375727 598 PLALCVLRKDINATEEQVLEEivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 652
Cdd:PRK05605 509 EVVAAVVLEPGAALDPEGLRA---YCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
288-655 |
2.91e-21 |
|
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: 97.05 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 288 VLSEHP---LYILYTSGTTGLPKGVIRPTGGYAvMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVL 364
Cdd:cd17649 88 LLTHHPrqlAYVIYTSGSTGTPKGVAVSHGPLA-AHCQATAERYGLTPGDRELQFASFNFDGAHEQL-LPPLICGACVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 365 YEGKPVGTPDagAYFRVLAEHGVAALFTAPT-------AIRAIRQQDPGAalgkqysltrFKTLFVAGERCDVETLeWSK 437
Cdd:cd17649 166 RPDELWASAD--ELAEMVRELGVTVLDLPPAylqqlaeEADRTGDGRPPS----------LRLYIFGGEALSPELL-RRW 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 438 NVFRVPVLDHWWQTETGSPITASCVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW 517
Cdd:cd17649 233 LKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADLN--------------PVPVGVTGELY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 518 KNQEAFKHLYF-------EKF-------PG--YYDTMD-AGYMDeEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGT 580
Cdd:cd17649 299 IGGEGLARGYLgrpeltaERFvpdpfgaPGsrLYRTGDlARWRD-DGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPG 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13375727 581 VADCAVVGKEDPLkGHVPLALCVLRKDinATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd17649 378 VREAAVVALDGAG-GKQLVAYVVLRAA--AAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
127-657 |
6.34e-21 |
|
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: 96.63 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 206
Cdd:cd17655 12 DHTAVVFED------QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 LSSRIDHVKPKVVVTASFGIEPGRRVEYVPLVEEalkigqhkpDKILIYNRPNMEavplapgrdldwdeemakaqshdcV 286
Cdd:cd17655 86 IQYILEDSGADILLTQSHLQPPIAFIGLIDLLDE---------DTIYHEESENLE------------------------P 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 287 PVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQpgevwwaASDLGWVVGHSY------IcYGPLLHGN 360
Cdd:cd17655 133 VSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGE-------HLRVALFASISFdasvteI-FASLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 361 TTVLYEGKPVGtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqysltRFKTLFVAGERCDVETLEWSKNVF 440
Cdd:cd17655 205 TLYIVRKETVL--DGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGL-------SLKHLIVGGEALSTELAKKIIELF 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 441 R--VPVLDHWWQTETgsPITAS---CVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSG 515
Cdd:cd17655 276 GtnPTITNAYGPTET--TVDASiyqYEPETDQQVSVP--IGKPLGNTRIYILDQYGRPQPVGVAGELYIG---GEGVARG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 516 LWKNQEafkhLYFEKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVV 587
Cdd:cd17655 349 YLNRPE----LTAEKFvddpfvPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVI 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13375727 588 GKEDPLKGHVPLALCVLRKDInaTEEQVLEEIVKHVRQNIGPvaafrnAVFVK--QLPKTRSGKIPRSALSA 657
Cdd:cd17655 425 ARKDEQGQNYLCAYIVSEKEL--PVAQLREFLARELPDYMIP------SYFIKldEIPLTPNGKVDRKALPE 488
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
127-655 |
8.22e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.49 E-value: 8.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 206
Cdd:PRK12316 4566 DAVAVVFD------EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAY----------- 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 lssridhvkpkvvvtASFGIE-PGRRVEYvpLVEEAlkiGQHkpdkILIYNRPNMEAVPLAPGRD---LDWDEEMAKAQS 282
Cdd:PRK12316 4629 ---------------VPLDPEyPRERLAY--MMEDS---GAA----LLLTQSHLLQRLPIPDGLAslaLDRDEDWEGFPA 4684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 283 HDcvPVLSEHP---LYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHG 359
Cdd:PRK12316 4685 HD--PAVRLHPdnlAYVIYTSGSTGRPKGVAVSHGSLVNHLHA-TGERYELTPDDRVLQFMSFSFDGSHEGL-YHPLING 4760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 360 NTTVLyegKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKTLFVAGERCDVETL-EWSKN 438
Cdd:PRK12316 4761 ASVVI---RDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-----EPPSLRVYCFGGEAVAQASYdLAWRA 4832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 439 VFRVPVLDHWWQTETG-SPITASCvglgnSKTPPPGQA----GKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAF 513
Cdd:PRK12316 4833 LKPVYLFNGYGPTETTvTVLLWKA-----RDGDACGAAympiGTPLGNRSGYVLDGQLN--------------PLPVGVA 4893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 514 SGLWKNQEAFKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILS 577
Cdd:PRK12316 4894 GELYLGGEGVARGYLerpaltaERFvpdpfgaPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLRE 4973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 578 HGTVADCAVVGKEDPLKGH-----VPLALCVLrkDINATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 652
Cdd:PRK12316 4974 HPAVREAVVIAQEGAVGKQlvgyvVPQDPALA--DADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDR 5051
|
...
gi 13375727 653 SAL 655
Cdd:PRK12316 5052 KAL 5054
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
145-649 |
1.45e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 95.72 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIH----------------------SLIFG-G 201
Cdd:PRK07798 30 TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPvnvnyryvedelryllddsdavALVYErE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 202 FASK--ELSSRIDHVKPKVVVTASFGIEPGRR-VEYvplvEEALKIGqhkpdkiliynrpnmeavplAPGRDldwdeema 278
Cdd:PRK07798 110 FAPRvaEVLPRLPKLRTLVVVEDGSGNDLLPGaVDY----EDALAAG--------------------SPERD-------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 279 kaqshdcVPVLSEHPLYILYTSGTTGLPKGV--------------IRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDL-- 342
Cdd:PRK07798 158 -------FGERSPDDLYLLYTGGTTGMPKGVmwrqedifrvllggRDFATGEPIEDEEELAKRAAAGPGMRRFPAPPLmh 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 343 G---WVVghsyicYGPLLHGNTTVLYegkPVGTPDAGAYFRVLAEHGVAALFTAPTA-----IRAIRQqdpgaalGKQYS 414
Cdd:PRK07798 231 GagqWAA------FAALFSGQTVVLL---PDVRFDADEVWRTIEREKVNVITIVGDAmarplLDALEA-------RGPYD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 415 LTRFKTLFVAG----ERCDVETLEWSKNVFrvpVLDHWWQTETGSpitascVGLGNSKTPPPGQAGKSV-PGYNVMILDD 489
Cdd:PRK07798 295 LSSLFAIASGGalfsPSVKEALLELLPNVV---LTDSIGSSETGF------GGSGTVAKGAVHTGGPRFtIGPRTVVLDE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 490 NMQKLK---------ARClGNIvvklPLppgafsGLWKNQEAFKHLYFEK------FPGYYDTMDAgymdeEGYLYVMSR 554
Cdd:PRK07798 366 DGNPVEpgsgeigwiARR-GHI----PL------GYYKDPEKTAETFPTIdgvryaIPGDRARVEA-----DGTITLLGR 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 555 VDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFR 634
Cdd:PRK07798 430 GSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL----AELRAHCRSSLAGYKVPR 505
|
570
....*....|....*
gi 13375727 635 NAVFVKQLPKTRSGK 649
Cdd:PRK07798 506 AIWFVDEVQRSPAGK 520
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
143-657 |
1.75e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.34 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaskelssridhvkpkVVVTA 222
Cdd:PRK12316 536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAY----------------------VPLDP 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 SFgiePGRRVEYvpLVEEAlKIGqhkpdkILIYNRPNMEAVPLAPGRD-LDWDEEMAKAQSH-DCVPVLS---EHPLYIL 297
Cdd:PRK12316 594 EY---PAERLAY--MLEDS-GVQ------LLLSQSHLGRKLPLAAGVQvLDLDRPAAWLEGYsEENPGTElnpENLAYVI 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 298 YTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHsYICYGPLLHGNTTVLyeGKPVGTPDAGA 377
Cdd:PRK12316 662 YTSGSTGKPKGAGNRHRALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVV--AAPGDHRDPAK 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 378 YFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEwskNVF-RVP---VLDHWWQTET 453
Cdd:PRK12316 738 LVELINREGVDTLHFVPSMLQAF-LQDEDVA-----SCTSLRRIVCSGEALPADAQE---QVFaKLPqagLYNLYGPTEA 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 454 GSPIT-ASCVGLGNSKTPppgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVklplppgAFSGLWKNQEAFKHLYFEKF- 531
Cdd:PRK12316 809 AIDVThWTCVEEGGDSVP----IGRPIANLACYILDANLEPVPVGVLGELYL-------AGRGLARGYHGRPGLTAERFv 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 532 PG-------YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEdplkGHVPLALCVL 604
Cdd:PRK12316 878 PSpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVL 953
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 13375727 605 RKDINATEEQVLEEIVKHVRQNIGPVaafrNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:PRK12316 954 ESEGGDWREALKAHLAASLPEYMVPA----QWLALERLPLTPNGKLDRKALPA 1002
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
144-650 |
2.96e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 94.88 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA- 222
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAd 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 SFgiepgRRVEYVPLVEE-ALKIGQHKPDKILIYNRPNMEAV-----PLAPGRdLDWDEEMAKAQSHDCVPV------LS 290
Cdd:PRK08315 124 GF-----KDSDYVAMLYElAPELATCEPGQLQSARLPELRRViflgdEKHPGM-LNFDELLALGRAVDDAELaarqatLD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 291 EH-PLYILYTSGTTGLPKGvirptggyaVMLhwSMSSIyglqpgevwwaasdL--GWVVGHS---------------YIC 352
Cdd:PRK08315 198 PDdPINIQYTSGTTGFPKG---------ATL--THRNI--------------LnnGYFIGEAmklteedrlcipvplYHC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 353 YGPLL-------HGNTTVLyegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlgkQYSLTRFKTLFVAG 425
Cdd:PRK08315 253 FGMVLgnlacvtHGATMVY----PGEGFDPLATLAAVEEERCTALYGVPTMFIAE-LDHPDFA---RFDLSSLRTGIMAG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 426 ERCDVETLEwsknvfRVPVLDH-------WWQTETgSPI---TA---------SCVG------------LGNSKTPPPGQ 474
Cdd:PRK08315 325 SPCPIEVMK------RVIDKMHmsevtiaYGMTET-SPVstqTRtddplekrvTTVGralphlevkivdPETGETVPRGE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 475 AGKSVP-GYNVMilddnmqklkarclgnivvklplppgafSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMS 553
Cdd:PRK08315 398 QGELCTrGYSVM----------------------------KGYWNDPEKTAEAIDAD--GWMHTGDLAVMDEEGYVNIVG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 554 RVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLE---------EIVKHVR 624
Cdd:PRK08315 448 RIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDfcrgkiahyKIPRYIR 527
|
570 580
....*....|....*....|....*.
gi 13375727 625 qnigpvaafrnavFVKQLPKTRSGKI 650
Cdd:PRK08315 528 -------------FVDEFPMTVTGKI 540
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
145-655 |
3.37e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 94.70 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI--------------HSL---------IFGG 201
Cdd:PRK07059 50 TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVvvnvnplytpreleHQLkdsgaeaivVLEN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 202 FASKeLSSRIDHVKPKVVVTASFGIEPG----------RRV-EYVPlveeALKIGQHKPdkiliYNRPnmeavpLAPGRd 270
Cdd:PRK07059 130 FATT-VQQVLAKTAVKHVVVASMGDLLGfkghivnfvvRRVkKMVP----AWSLPGHVR-----FNDA------LAEGA- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 271 ldwdeemakAQSHDCVPVLSEHPLYILYTSGTTGLPKGvirptggyAVMLHWSMSSIYgLQpGEVWW-AASDLGWVVGH- 348
Cdd:PRK07059 193 ---------RQTFKPVKLGPDDVAFLQYTGGTTGVSKG--------ATLLHRNIVANV-LQ-MEAWLqPAFEKKPRPDQl 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 349 SYICYGPLLH-GNTTVlyegkpvgtpdagAYFRVLAEHGVAALFTAPTAIrairqqdPG--AALGKqYSLTRF---KTLF 422
Cdd:PRK07059 254 NFVCALPLYHiFALTV-------------CGLLGMRTGGRNILIPNPRDI-------PGfiKELKK-YQVHIFpavNTLY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 423 VA-GERCDVETLEWSKNVFRV--------PVLDHWWQTeTGSPITAscvGLGNSKTPP------------PGQAGKSVPG 481
Cdd:PRK07059 313 NAlLNNPDFDKLDFSKLIVANgggmavqrPVAERWLEM-TGCPITE---GYGLSETSPvatcnpvdatefSGTIGLPLPS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 482 YNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINV 561
Cdd:PRK07059 389 TEVSIRDDDGNDLPLGEPGEICIR---GPQVMAGYWNRPDETAKVMTAD--GFFRTGDVGVMDERGYTKIVDRKKDMILV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 562 AGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQ 641
Cdd:PRK07059 464 SGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEA-VKLFVVKKDPALTE----EDVKAFCKERLTNYKRPKFVEFRTE 538
|
570
....*....|....
gi 13375727 642 LPKTRSGKIPRSAL 655
Cdd:PRK07059 539 LPKTNVGKILRREL 552
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
448-652 |
6.42e-20 |
|
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: 91.56 E-value: 6.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 448 WW----QTETGSPITASCVglgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWKNQEAF 523
Cdd:cd17637 139 FWslygQTETSGLVTLSPY------RERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPL---VFQGYWNLPELT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 524 KHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRV--DDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLAL 601
Cdd:cd17637 210 AYTFRN---GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAV 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13375727 602 CVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 652
Cdd:cd17637 287 CVLKPGATLTA----DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
143-652 |
1.26e-19 |
|
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: 92.51 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 222
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 sfgiepgrrveyvplveealkigqhKPDKILIynrpnmeavplapgrdldwdeemakaqshdcvpvlsehplyILYTSGT 302
Cdd:cd05914 87 -------------------------DEDDVAL-----------------------------------------INYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 303 TGLPKGVIRP--------TGGYAVMLhwsmssiygLQPGEVWWAASDLGwvvgHSYICYG----PLLHGNTTVLYEGKPV 370
Cdd:cd05914 101 TGNSKGVMLTyrnivsnvDGVKEVVL---------LGKGDKILSILPLH----HIYPLTFtlllPLLNGAHVVFLDKIPS 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 371 GTPDAGAYFRVLAEHGVAALF-----------------------TAPTAIRAIRQQdPGAALGKQYSlTRFKTLFVAGER 427
Cdd:cd05914 168 AKIIALAFAQVTPTLGVPVPLviekifkmdiipkltlkkfkfklAKKINNRKIRKL-AFKKVHEAFG-GNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 428 CDVETLEWSKNVfRVPVLDHWWQTETGsPITAScvglgnskTPPP----GQAGKSVPGYNVMILDDNMQKLKarclGNIV 503
Cdd:cd05914 246 INPDVEEFLRTI-GFPYTIGYGMTETA-PIISY--------SPPNrirlGSAGKVIDGVEVRIDSPDPATGE----GEII 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 504 VKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVI-NVAGHRISAGAIEESILSHGTVA 582
Cdd:cd05914 312 VR---GPNVMKGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVL 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13375727 583 DCAVVGKEDPLKGHV---PLALCVLRKDINATEEQVLEEIVKHVRQNigpVAAFRNAVFVK----QLPKTRSGKIPR 652
Cdd:cd05914 387 ESLVVVQEKKLVALAyidPDFLDVKALKQRNIIDAIKWEVRDKVNQK---VPNYKKISKVKivkeEFEKTPKGKIKR 460
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
86-655 |
1.30e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 92.98 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 86 WYKPWTKTLENKHsPSTRWFVEGMLNICYNAVDRHIENGkgdkiaiiyDSPVTNTKATF--TYKEVLEQVSKLA-GVLVK 162
Cdd:PLN02574 17 WYSPETGIYSSKH-PPVPLPSDPNLDAVSFIFSHHNHNG---------DTALIDSSTGFsiSYSELQPLVKSMAaGLYHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 163 HGIKKGDTVV------IYMPMIpqamytMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFGIE--PGRRVEy 234
Cdd:PLN02574 87 MGVRQGDVVLlllpnsVYFPVI------FLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEklSPLGVP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 235 VPLVEEALKIgqhkpDKILIYNRPNMEAVPLAPgrdldwdeemakaqshDCV--PVLSEHPLY-ILYTSGTTGLPKGVIR 311
Cdd:PLN02574 160 VIGVPENYDF-----DSKRIEFPKFYELIKEDF----------------DFVpkPVIKQDDVAaIMYSSGTTGASKGVVL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 312 PTGGYAVMLHWSM---SSIYGLQPGE-VWWAASDLGWVVGHSYICYGPLLHGNTTVLYEgkpvgTPDAGAYFRVLAEHGV 387
Cdd:PLN02574 219 THRNLIAMVELFVrfeASQYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMR-----RFDASDMVKVIDRFKV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 388 AALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVEtlEWSKNVFRVPVLDHWWQTETGSPITAscvGLGNS 467
Cdd:PLN02574 294 THFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQ--DFVQTLPHVDFIQGYGMTESTAVGTR---GFNTE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 468 KTPPPGQAGKSVPGYNVMILDdnmqkLKARCLgnivvklpLPPGAFSGLW-----------KNQEAFKHLYFEKfpGYYD 536
Cdd:PLN02574 369 KLSKYSSVGLLAPNMQAKVVD-----WSTGCL--------LPPGNCGELWiqgpgvmkgylNNPKATQSTIDKD--GWLR 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 537 TMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVL 616
Cdd:PLN02574 434 TGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVI 513
|
570 580 590
....*....|....*....|....*....|....*....
gi 13375727 617 EEIVKHVrqniGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PLN02574 514 NYVAKQV----APYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
137-656 |
1.37e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 92.64 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 137 VTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKP 216
Cdd:PRK05852 37 VTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 217 KVVVTASFGiePGRRVEyvplveealkiGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQShdcVPV-LSEHPLY 295
Cdd:PRK05852 117 RVVLIDADG--PHDRAE-----------PTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATS---TPEgLRPDDAM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 296 ILYTSGTTGLPKGVIRPTGGYAVMLHwSMSSIYGLQPGEVWWAASdlgwvvghsyicygPLLHGNTTV------LYEGKP 369
Cdd:PRK05852 181 IMFTGGTTGLPKMVPWTHANIASSVR-AIITGYRLSPRDATVAVM--------------PLYHGHGLIaallatLASGGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 370 VGTPDAGAY----FRVLAEHGVAALFTAPTAIRAIRQQDPGAalgKQYSLTRFKTLFVagERC----DVETLEWSKNVFR 441
Cdd:PRK05852 246 VLLPARGRFsahtFWDDIKAVGATWYTAVPTIHQILLERAAT---EPSGRKPAALRFI--RSCsaplTAETAQALQTEFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 442 VPVLDHWWQTETGSPITASCV-GLGNSKTP--PPGQAGKSVpGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWK 518
Cdd:PRK05852 321 APVVCAFGMTEATHQVTTTQIeGIGQTENPvvSTGLVGRST-GAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 519 NQEA-FKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHV 597
Cdd:PRK05852 400 ITAAnFTD-------GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEA 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13375727 598 PLALCVLRKDINATEeqvlEEIVKHVRQNIGPV---AAFRNAvfvKQLPKTRSGKIPRSALS 656
Cdd:PRK05852 473 VAAVIVPRESAPPTA----EELVQFCRERLAAFeipASFQEA---SGLPHTAKGSLDRRAVA 527
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
145-659 |
5.41e-19 |
|
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: 90.47 E-value: 5.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLaGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASF 224
Cdd:cd05909 9 TYRKLLTGAIAL-ARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 225 GIEPGRRVEYVPLVEEA-------LKIGQHKPDKILIYnrPNMEAVPLAPGRDLDwdeemakaqshdCVPVLSEHPLYIL 297
Cdd:cd05909 88 FIEKLKLHHLFDVEYDArivyledLRAKISKADKCKAF--LAGKFPPKWLLRIFG------------VAPVQPDDPAVIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 298 YTSGTTGLPKGVirptggyaVMLHWSMSS-------IYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLY----E 366
Cdd:cd05909 154 FTSGSEGLPKGV--------VLSHKNLLAnveqitaIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpnplD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 367 GKPVGtpdagayfRVLAEHGVAALFTAPTAIRAIrqqdpgAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLD 446
Cdd:cd05909 226 YKKIP--------ELIYDKKATILLGTPTFLRGY------ARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 447 HWWQTETgSPITAScvglgNSKTPP--PGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAF 523
Cdd:cd05909 292 GYGTTEC-SPVISV-----NTPQSPnkEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVR---GPNVMLGYLNEPELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 524 KHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSH-GTVADCAVVGKEDPLKGHVpLALC 602
Cdd:cd05909 363 SFAFGD---GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEK-IVLL 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 13375727 603 VLRKDINATEeqvLEEIVKHVrqNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIV 659
Cdd:cd05909 439 TTTTDTDPSS---LNDILKNA--GISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
142-654 |
7.85e-19 |
|
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: 90.38 E-value: 7.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 142 ATFTYKEVLEQVSKLAGVLVKHGiKKGDTVVIympMIPQAM---YTMLACARIGAIHSLIF---GGFASKELSSRIDHVK 215
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG-KPGDRVLL---LAPPGLdfvAAFLGCLYAGAIAVPLPpptPGRHAERLAAILADAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 216 PKVVVTASfgiepgrrvEYVPLVEEALKigqhkpdkiliynrpNMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEhPLY 295
Cdd:cd05931 99 PRVVLTTA---------AALAAVRAFAA---------------SRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDD-IAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 296 ILYTSGTTGLPKGV-IRptggYAVMLH--WSMSSIYGLQPGEVWwaAS------DLGWVVGhsyICyGPLLHGNTTVL-- 364
Cdd:cd05931 154 LQYTSGSTGTPKGVvVT----HRNLLAnvRQIRRAYGLDPGDVV--VSwlplyhDMGLIGG---LL-TPLYSGGPSVLms 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 365 ---YEGKPVGtpdagaYFRVLAEHGvaALFT-APT-----AIRAIRQQDPGAalgkqYSLTRFKTLFVAGERCDVETLE- 434
Cdd:cd05931 224 paaFLRRPLR------WLRLISRYR--ATISaAPNfaydlCVRRVRDEDLEG-----LDLSSWRVALNGAEPVRPATLRr 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 435 ---------WSKNVFR-------------VPVLDHWWQTETGSPITASCVGLGNSKTPPPGQA----GKSVPGYNVMILD 488
Cdd:cd05931 291 faeafapfgFRPEAFRpsyglaeatlfvsGGPPGTGPVVLRVDRDALAGRAVAVAADDPAARElvscGRPLPDQEVRIVD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 489 DN-MQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKFP----GYYDTMDAGYMDEeGYLYVMSRVDDVINVAG 563
Cdd:cd05931 371 PEtGRELPDGEVGEIWVR---GPSVASGYWGRPEATAETFGALAAtdegGWLRTGDLGFLHD-GELYITGRLKDLIIVRG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 564 HRISAGAIEESILSH------GTVADCAVVGKEDplkGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGpVAAfRNAV 637
Cdd:cd05931 447 RNHYPQDIEATAEEAhpalrpGCVAAFSVPDDGE---ERLVVVAEVERGADPADLAAIAAAIRAAVAREHG-VAP-ADVV 521
|
570
....*....|....*....
gi 13375727 638 FVKQ--LPKTRSGKIPRSA 654
Cdd:cd05931 522 LVRPgsIPRTSSGKIQRRA 540
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
293-652 |
2.01e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 87.33 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 293 PLYILYTSGTTGLPKGVirptggyavML-HWSMSSiYGLQPGEVwwaasdLGWVVGHSYICYGPLLH------GNTTVLY 365
Cdd:cd05917 4 VINIQFTSGTTGSPKGA---------TLtHHNIVN-NGYFIGER------LGLTEQDRLCIPVPLFHcfgsvlGVLACLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 366 EGKPVGTP----DAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWSKNVF 440
Cdd:cd05917 68 HGATMVFPspsfDPLAVLEAIEKEKCTALHGVPTMfIAELEHPDF-----DKFDLSSLRTGIMAGAPCPPELMKRVIEVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 441 RVP-VLDHWWQTETgSPIT------------------------ASCVGLGNSKTPPPGQAGK-SVPGYNVMIlddnmqkl 494
Cdd:cd05917 143 NMKdVTIAYGMTET-SPVStqtrtddsiekrvntvgrimphteAKIVDPEGGIVPPVGVPGElCIRGYSVMK-------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 495 karclgnivvklplppgafsGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEES 574
Cdd:cd05917 214 --------------------GYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEF 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13375727 575 ILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 652
Cdd:cd05917 272 LHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTE----EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
122-661 |
2.57e-18 |
|
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: 88.88 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 122 ENGKGDKIAIIYDspvTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGG 201
Cdd:cd05906 21 ERGPTKGITYIDA---DGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 202 FASKELSSRIDHVK--------PKVVVTAsfgiepgrrvEYVPLVEEALKIGQHKPDKILIYnrpnmeavplapgrdldw 273
Cdd:cd05906 98 PTYDEPNARLRKLRhiwqllgsPVVLTDA----------ELVAEFAGLETLSGLPGIRVLSI------------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 274 DEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVirptggyaVMLHWSM-------SSIYGLQPGEVWwaasdLGWVv 346
Cdd:cd05906 150 EELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAV--------PLTHRNIlarsagkIQHNGLTPQDVF-----LNWV- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 347 ghsyicygPLLHGNTTVLYEGKPVgtpDAGA----------------YFRVLAEHGVAALFtAPT-AIRAIRQQDPGAAl 409
Cdd:cd05906 216 --------PLDHVGGLVELHLRAV---YLGCqqvhvpteeiladplrWLDLIDRYRVTITW-APNfAFALLNDLLEEIE- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 410 GKQYSLTRFKTLFVAGERCDVET-------LEWSK---NVFRvPVldhWWQTETGSPITASCVglgnSKTPPPGQA---- 475
Cdd:cd05906 283 DGTWDLSSLRYLVNAGEAVVAKTirrllrlLEPYGlppDAIR-PA---FGMTETCSGVIYSRS----FPTYDHSQAlefv 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 476 --GKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEeGYLYVMS 553
Cdd:cd05906 355 slGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPV---VTKGYYNNPEANAEAFTED--GWFRTGDLGFLDN-GNLTITG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 554 RVDDVINVAG-----HRISAgAIEE-SILSHGTVADCAVvgkEDPLKGHVPLALC-VLRKDINATEEQVLEEIVKHVRQN 626
Cdd:cd05906 429 RTKDTIIVNGvnyysHEIEA-AVEEvPGVEPSFTAAFAV---RDPGAETEELAIFfVPEYDLQDALSETLRAIRSVVSRE 504
|
570 580 590
....*....|....*....|....*....|....*.
gi 13375727 627 IGPVAAFRNAVFVKQLPKTRSGKIPRSAL-SAIVNG 661
Cdd:cd05906 505 VGVSPAYLIPLPKEEIPKTSLGKIQRSKLkAAFEAG 540
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
142-666 |
4.04e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 88.14 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 142 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 221
Cdd:PRK05857 40 SALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 AsfgiePGRRVEyvplvEEALKIGQHKPDKIliynRPNMEAVPLAPGRDLDWDEEMAKAQSHdcvpvlSEHPLYILYTSG 301
Cdd:PRK05857 120 A-----PGSKMA-----SSAVPEALHSIPVI----AVDIAAVTRESEHSLDAASLAGNADQG------SEDPLAMIFTSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 302 TTGLPKGVIRPTGGYAVM--------LHW--------SMSSIYGLQPGEVWWAASdlgwvvghsyiCygpLLHGNTTVly 365
Cdd:PRK05857 180 TTGEPKAVLLANRTFFAVpdilqkegLNWvtwvvgetTYSPLPATHIGGLWWILT-----------C---LMHGGLCV-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 366 egkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTRFKTLFVAGER---CDVETLEWSKnvfrV 442
Cdd:PRK05857 244 ----TGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANA----TVPSLRLVGYGGSRaiaADVRFIEATG----V 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 443 PVLDHWWQTETGSpiTASCVGLGNSKTP--PPGQAGKSVPGYNVMILDDN------MQKLKARCLGNIVVKlplPPGAFS 514
Cdd:PRK05857 312 RTAQVYGLSETGC--TALCLPTDDGSIVkiEAGAVGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIK---SPANML 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 515 GLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLK 594
Cdd:PRK05857 387 GYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEF 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13375727 595 GH-VPLALcVLRKDINATEEQVLEE-IVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKI 666
Cdd:PRK05857 464 GAlVGLAV-VASAELDESAARALKHtIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARV 536
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
291-657 |
4.71e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 87.35 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 291 EHPLYILYTSGTTGLPKGVIRPTGGYAvmlhwsmSSIYGLqpGEVW-WAASDL-----------GWVVGhsyiCYGPLLH 358
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSRRAIA-------ADLDAL--AEAWqWTADDVlvhglplfhvhGLVLG----VLGPLRI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 359 GNTtVLYEGKPvgTPDAgaYFRVLAEHGvAALFTAPTAIRAIrQQDPGAAlgKQYSLTRfktLFVAGE----RCDVETLE 434
Cdd:PRK07787 195 GNR-FVHTGRP--TPEA--YAQALSEGG-TLYFGVPTVWSRI-AADPEAA--RALRGAR---LLVSGSaalpVPVFDRLA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 435 WSKNVfrvPVLDHWWQTETgsPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKA--RCLGNIVVKlplPPGA 512
Cdd:PRK07787 263 ALTGH---RPVERYGMTET--LITLSTRADGERR---PGWVGLPLAGVETRLVDEDGGPVPHdgETVGELQVR---GPTL 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 513 FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVD-DVINVAGHRISAGAIEESILSHGTVADCAVVGKED 591
Cdd:PRK07787 332 FDGYLNRPDATAAAFTAD--GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPD 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13375727 592 PLKGHVPLALCVLRKDINAteeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:PRK07787 410 DDLGQRIVAYVVGADDVAA------DELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
143-592 |
5.10e-18 |
|
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: 87.86 E-value: 5.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 222
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 SFG-----IEPGRR---VEYVPLVEEAlkiGQHKpdkiliYNRPNMEAVP--LAPGRDLDWD-----EEMAKAQSHDCVP 287
Cdd:cd17641 91 DEEqvdklLEIADRipsVRYVIYCDPR---GMRK------YDDPRLISFEdvVALGRALDRRdpglyEREVAAGKGEDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 288 VLSehplyilYTSGTTGLPKGVIRPTGGYAvmlhwSMSSIY----GLQPGEVWWAASDLGWVVGHSYICYGPLLHGN--- 360
Cdd:cd17641 162 VLC-------TTSGTTGKPKLAMLSHGNFL-----GHCAAYlaadPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFivn 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 361 -----TTVLYEGKPVG------TP---------------DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGA------- 407
Cdd:cd17641 230 fpeepETMMEDLREIGptfvllPPrvwegiaadvrarmmDATPFKRFMFELGMKLGLRALDRGKRGRPVSLWLrlaswla 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 408 ------ALGKQYSLTRFKTLFVAGERCDVETLEWsknvFR---VPVLDHWWQTETGSPITASCVGlgnskTPPPGQAGKS 478
Cdd:cd17641 310 dallfrPLRDRLGFSRLRSAATGGAALGPDTFRF----FHaigVPLKQLYGQTELAGAYTVHRDG-----DVDPDTVGVP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 479 VPGYNVMIldDNMqklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDV 558
Cdd:cd17641 381 FPGTEVRI--DEV--------GEILVR---SPGVFVGYYKNPEATAEDFDED--GWLHTGDAGYFKENGHLVVIDRAKDV 445
|
490 500 510
....*....|....*....|....*....|....*
gi 13375727 559 INVA-GHRISAGAIEESILSHGTVADCAVVGKEDP 592
Cdd:cd17641 446 GTTSdGTRFSPQFIENKLKFSPYIAEAVVLGAGRP 480
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
115-360 |
5.46e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 88.01 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 115 NAVDRHiengkGDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI 194
Cdd:PRK08279 45 EAAARH-----PDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 195 HSLIFGGFASKELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEAlkiGQHKPDKILIYnrPNMEAVPLAPGRDLDWD 274
Cdd:PRK08279 114 VALLNTQQRGAVLAHSLNLVDAKHLIVGE---------ELVEAFEEA---RADLARPPRLW--VAGGDTLDDPEGYEDLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 275 EEMAKAQSHD---CVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWwaasdlgwvvghsYI 351
Cdd:PRK08279 180 AAAAGAPTTNpasRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGG-FGGLLRLTPDDVL-------------YC 245
|
....*....
gi 13375727 352 CYgPLLHGN 360
Cdd:PRK08279 246 CL-PLYHNT 253
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
142-655 |
5.66e-18 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 88.95 E-value: 5.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 142 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 221
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLIT 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 ASfgiepgrrveyvplvEEALKIgQHKPD-KILIYNrpnmeaVPLAPgrdldwdeemakAQSHDCVPVLSEHPLYILYTS 300
Cdd:PRK10252 562 TA---------------DQLPRF-ADVPDlTSLCYN------APLAP------------QGAAPLQLSQPHHTAYIIFTS 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 301 GTTGLPKGVIrpTGGYAVM--LHWsMSSIYGLQPG----------------EVWWaasdlgwvvghsyicygPLLHGNTT 362
Cdd:PRK10252 608 GSTGRPKGVM--VGQTAIVnrLLW-MQNHYPLTADdvvlqktpcsfdvsvwEFFW-----------------PFIAGAKL 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 363 VLyeGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQ-DPGAALGKQYSLTRfktLFVAGERCDVEtlewsknvfr 441
Cdd:PRK10252 668 VM--AEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASlTPEGARQSCASLRQ---VFCSGEALPAD---------- 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 442 vpVLDHWWQTeTGSPI------TASCVGLgnSKTPPPGQA-----GKSVP-GYNV-----MILDDNMQklkarclgnivv 504
Cdd:PRK10252 733 --LCREWQQL-TGAPLhnlygpTEAAVDV--SWYPAFGEElaavrGSSVPiGYPVwntglRILDARMR------------ 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 505 klPLPPGAfSGlwknqeafkHLYF-----------------EKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVI 559
Cdd:PRK10252 796 --PVPPGV-AG---------DLYLtgiqlaqgylgrpdltaSRFiadpfaPGerMYRTGDVARWLDDGAVEYLGRSDDQL 863
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 560 NVAGHRISAGAIEESILSHGTVADCAVV-----------GKEDPLKGHVPlALCVLRKDINATEEQVLEEIVKHVRqnig 628
Cdd:PRK10252 864 KIRGQRIELGEIDRAMQALPDVEQAVTHacvinqaaatgGDARQLVGYLV-SQSGLPLDTSALQAQLRERLPPHMV---- 938
|
570 580
....*....|....*....|....*..
gi 13375727 629 PVAafrnAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK10252 939 PVV----LLQLDQLPLSANGKLDRKAL 961
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
134-655 |
5.74e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 87.62 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 134 DSPV-TNTKATFTYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSR- 210
Cdd:PRK08751 40 DRPAyHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 211 IDHVKPKVVVTASFG-----IEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVP-LAPGRDLDWDEEMAKAQSHD 284
Cdd:PRK08751 120 IDSGASVLVVIDNFGttvqqVIADTPVKQVITTGLGDMLGFPKAALVNFVVKYVKKLVPeYRINGAIRFREALALGRKHS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 285 CVPVLSEHP--LYILYTSGTTGLPKGvirptggyAVMLHWSMssIYGLQPGEVWWAASDLGWVVGHSYICYGPLLH---- 358
Cdd:PRK08751 200 MPTLQIEPDdiAFLQYTGGTTGVAKG--------AMLTHRNL--VANMQQAHQWLAGTGKLEEGCEVVITALPLYHifal 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 359 -GNTTVLYE----GKPVGTP-DAGAYFRVLAEhgvaALFTAPTAIRAIRQ---QDPGAAlgkQYSLTRFKTLFVAGERCD 429
Cdd:PRK08751 270 tANGLVFMKiggcNHLISNPrDMPGFVKELKK----TRFTAFTGVNTLFNgllNTPGFD---QIDFSSLKMTLGGGMAVQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 430 VETLEWSKNVFRVPVLDHWWQTETgSPitASCVglgNSKTPPP--GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlp 507
Cdd:PRK08751 343 RSVAERWKQVTGLTLVEAYGLTET-SP--AACI---NPLTLKEynGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK-- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 508 lPPGAFSGLWKNQEAFKHLYfeKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVV 587
Cdd:PRK08751 415 -GPQVMKGYWKRPEETAKVM--DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAV 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13375727 588 GKEDPLKGHVpLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK08751 492 GVPDEKSGEI-VKVVIVKKDPALTAEDVKA----HARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
127-655 |
6.84e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 87.14 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSPVtntkatFTYKEVLEQVSKLAGVLVKHGiKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 206
Cdd:PRK07638 16 NKIAIKENDRV------LTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 LSSRIDHVKPKVVVTASFGIEPGRRVEyvplveealkigqhkpdkiliynrpnmeavplapGRDLDWDE--EMAKAQSHD 284
Cdd:PRK07638 89 LKERLAISNADMIVTERYKLNDLPDEE----------------------------------GRVIEIDEwkRMIEKYLPT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 285 CVPV--LSEHPLYILYTSGTTGLPKGVIRPtggyavmlHWS-MSSI------YGLQPGEVWWAASDLGwvvgHSYICYGP 355
Cdd:PRK07638 135 YAPIenVQNAPFYMGFTSGSTGKPKAFLRA--------QQSwLHSFdcnvhdFHMKREDSVLIAGTLV----HSLFLYGA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 356 L--LHGNTTVLYEGK--PVGTPDAgayfrvLAEHGVAALFTAPTAIRAIrqqdpgaalgkqYSLTRFK----TLFVAGER 427
Cdd:PRK07638 203 IstLYVGQTVHLMRKfiPNQVLDK------LETENISVMYTVPTMLESL------------YKENRVIenkmKIISSGAK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 428 CDVETLEWSKNVFRVPVLDHWWQTETGSPITAScvgLGNSKTPPPGQAGKsvPGYNVMILDDNM--QKLKARCLGNIVVK 505
Cdd:PRK07638 265 WEAEAKEKIKNIFPYAKLYEFYGASELSFVTAL---VDEESERRPNSVGR--PFHNVQVRICNEagEEVQKGEIGTVYVK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 506 LPLppgAFSGlWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCA 585
Cdd:PRK07638 340 SPQ---FFMG-YIIGGVLARELNAD--GWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIV 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 586 VVGKEDPLKGHVPLALCvlrkDINATEEQvleeIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK07638 414 VIGVPDSYWGEKPVAII----KGSATKQQ----LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
134-655 |
7.71e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 87.51 E-value: 7.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 134 DSPV-TNTKATFTYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRI 211
Cdd:PRK05677 39 DKPAfSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 212 DHVKPK-VVVTASF-----GIEPGRRVEYVPLVEEAlkiGQHKPDKILI--------------YNRPNmeAVP----LAP 267
Cdd:PRK05677 119 NDSGAKaLVCLANMahlaeKVLPKTGVKHVIVTEVA---DMLPPLKRLLinavvkhvkkmvpaYHLPQ--AVKfndaLAK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 268 GRDLDWDEemAKAQSHDcVPVLSehplyilYTSGTTGLPKG-VIRPTGGYAVMLHWSMSSIYGLQPG-EVWWAASDLGWV 345
Cdd:PRK05677 194 GAGQPVTE--ANPQADD-VAVLQ-------YTGGTTGVAKGaMLTHRNLVANMLQCRALMGSNLNEGcEILIAPLPLYHI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 346 VGHSYICYGPLLHGNTTVLyegkpVGTP-DAGAYFRVLAEH------GVAALFTAPTAIRAIRQQDpgaalgkqysLTRF 418
Cdd:PRK05677 264 YAFTFHCMAMMLIGNHNIL-----ISNPrDLPAMVKELGKWkfsgfvGLNTLFVALCNNEAFRKLD----------FSAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 419 KTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETgSPItascVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARC 498
Cdd:PRK05677 329 KLTLSGGMALQLATAERWKEVTGCAICEGYGMTET-SPV----VSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 499 LGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSH 578
Cdd:PRK05677 404 VGELCVK---GPQVMKGYWQRPEATDEILDSD--GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13375727 579 GTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK05677 479 PGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVME----HMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
109-627 |
9.04e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 87.26 E-value: 9.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 109 MLNICynavdRHIE---NGKGDKIAIIY----DSPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGD-TVVIYMPMIPq 180
Cdd:PRK09274 5 MANIA-----RHLPraaQERPDQLAVAVpggrGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMrAVLMVTPSLE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 181 aMYT-MLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVtasfGIEP---GRR--------VEYVPLVEEALKIGQHK 248
Cdd:PRK09274 79 -FFAlTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI----GIPKahlARRlfgwgkpsVRRLVTVGGRLLWGGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 249 PDKILIynRPNMEAVPLApgrDLDWDEEMAkaqshdcvpvlsehplyILYTSGTTGLPKGVIRPTGGYAVMLHwSMSSIY 328
Cdd:PRK09274 154 LATLLR--DGAAAPFPMA---DLAPDDMAA-----------------ILFTSGSTGTPKGVVYTHGMFEAQIE-ALREDY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 329 GLQPGEVwwaasDLgwvvgHSYicygPL--LH----GNTTVLYE---GKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRA 399
Cdd:PRK09274 211 GIEPGEI-----DL-----PTF----PLfaLFgpalGMTSVIPDmdpTRP-ATVDPAKLFAAIERYGVTNLFGSPALLER 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 400 IRQqdpgAALGKQYSLTRFKTLFVAG--------ERC------DVETLewskNVF----RVPV---------LDHWWQTE 452
Cdd:PRK09274 276 LGR----YGEANGIKLPSLRRVISAGapvpiaviERFramlppDAEIL----TPYgateALPIssiesreilFATRAATD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 453 TGSPItasCVglgnsktpppgqaGKSVPGYNVMILD---------DNMQKLKARCLGNIVVKLPL-------PPGA--FS 514
Cdd:PRK09274 348 NGAGI---CV-------------GRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMvtrsyynRPEAtrLA 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 515 GLWKNQEAFKHlyfekfpgyyDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKedPLK 594
Cdd:PRK09274 412 KIPDGQGDVWH----------RMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGV--GVP 479
|
570 580 590
....*....|....*....|....*....|....
gi 13375727 595 GHVPLALCV-LRKDINATEEQVLEEIVKHVRQNI 627
Cdd:PRK09274 480 GAQRPVLCVeLEPGVACSKSALYQELRALAAAHP 513
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
144-657 |
1.27e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 86.82 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPqAMY-TMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 222
Cdd:PLN02479 46 YTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIP-AMYeAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 SfgiepgrrvEYVPLVEEALKI------GQHKPDKILIYNRPNMEAVPL--APGRDL--------DWDEEMAKAQSHDcv 286
Cdd:PLN02479 125 Q---------EFFTLAEEALKIlaekkkSSFKPPLLIVIGDPTCDPKSLqyALGKGAieyekfleTGDPEFAWKPPAD-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 287 pvlSEHPLYILYTSGTTGLPKGVI-RPTGGYAVMLhwSMSSIYGLQPGEVW-WAASDL---GWvvghsyiCYG---PLLH 358
Cdd:PLN02479 194 ---EWQSIALGYTSGTTASPKGVVlHHRGAYLMAL--SNALIWGMNEGAVYlWTLPMFhcnGW-------CFTwtlAALC 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 359 GNTTVLYEgkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqYSLTRFKTLFVAGERCDVETL-EWSK 437
Cdd:PLN02479 262 GTNICLRQ------VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETI---LPLPRVVHVMTAGAAPPPSVLfAMSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 438 NVFRVPvldHWWQ-TETGSPITASCVGLGNSKTPPPGQA------GKSVPGYNVMILDD--NMQKLKA--RCLGNIVVKl 506
Cdd:PLN02479 333 KGFRVT---HTYGlSETYGPSTVCAWKPEWDSLPPEEQArlnarqGVRYIGLEGLDVVDtkTMKPVPAdgKTMGEIVMR- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 507 plPPGAFSGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCA 585
Cdd:PLN02479 409 --GNMVMKGYLKNPKANE----EAFAnGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEAS 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13375727 586 VVGKEDPLKGHVPLALCVLRKDINATEEQVL-EEIVKHVRQNIGPVAAFRNAVFvKQLPKTRSGKIPRSALSA 657
Cdd:PLN02479 483 VVARPDERWGESPCAFVTLKPGVDKSDEAALaEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRA 554
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
296-650 |
1.48e-17 |
|
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: 84.47 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 296 ILYTSGTTGLPKGVIrptggyavMLHwsmssiygLQPGEVWWAASDLGWVV-GHSYICYGPLLH------GNTTVLYEGK 368
Cdd:cd17638 5 IMFTSGTTGRSKGVM--------CAH--------RQTLRAAAAWADCADLTeDDRYLIINPFFHtfgykaGIVACLLTGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 369 ---PVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAalgKQYSLTRFKTLFVAGERCDVETLEWSKNVFRV-PV 444
Cdd:cd17638 69 tvvPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDH-PGR---KKFDLSSLRAAVTGAATVPVELVRRMRSELGFeTV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 445 LDHWWQTETGspiTASCVGLGNSKTPPPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQEAFK 524
Cdd:cd17638 145 LTAYGLTEAG---VATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVR---GYNVMQGYLDDPEATA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 525 HLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVL 604
Cdd:cd17638 209 EAIDAD--GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 13375727 605 RKDINATEEQVleeiVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 650
Cdd:cd17638 287 RPGVTLTEEDV----IAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
145-655 |
2.22e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 85.95 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVtasf 224
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLV---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 225 gIEPG-RRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLD-WDEEMAKAQSHDCVPVLSEHPLYILY-TSG 301
Cdd:PRK06164 113 -VWPGfKGIDFAAILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQlFALPDPAPPAAAGERAADPDAGALLFtTSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 302 TTGLPKGVIRPTGgyAVMLH-WSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGplLHGNTTVLYEgkPVGtpDAGAYFR 380
Cdd:PRK06164 192 TTSGPKLVLHRQA--TLLRHaRAIARAYGYDPGAVLLAALPFCGVFGFSTLLGA--LAGGAPLVCE--PVF--DAARTAR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 381 VLAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTlFVAGERcdvETLEWsknvfrvpVLDHwwqtetGSPITas 460
Cdd:PRK06164 264 ALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFAS-FAPALG---ELAAL--------ARAR------GVPLT-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 461 cvGL-GNSK----------TPP------PGQAGKSvPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEA 522
Cdd:PRK06164 324 --GLyGSSEvqalvalqpaTDPvsvrieGGGRPAS-PEARVRARDpQDGALLPDGESGEIEIR---APSLMRGYLDNPDA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 523 FKHLYFEKfpGYYDTMDAGYMDEEG-YLYVmSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEdpLKGH-VPLA 600
Cdd:PRK06164 398 TARALTDD--GYFRTGDLGYTRGDGqFVYQ-TRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT--RDGKtVPVA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 13375727 601 LCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSG---KIPRSAL 655
Cdd:PRK06164 473 FVIPTDGASPDE----AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
274-657 |
3.26e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 85.05 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 274 DEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTggyavmlhwSMSSIYGlqpgeVWWAASDLGWV-VGHSYIC 352
Cdd:PRK13383 157 DPATAGAEESGGRPAVAAPGRIVLLTSGTTGKPKGVPRAP---------QLRSAVG-----VWVTILDRTRLrTGSRISV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 353 YGPLLHGN-----TTVLYEGKPVGTP---DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLFVA 424
Cdd:PRK13383 223 AMPMFHGLglgmlMLTIALGGTVLTHrhfDAEAALAQASLHRADAFTAVPVVLARILELPP--RVRARNPLPQLRVVMSS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 425 GERCDVETLEWSKNVFRVPVLDHWWQTEtgspitascVGLGNSKTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCL 499
Cdd:PRK13383 301 GDRLDPTLGQRFMDTYGDILYNGYGSTE---------VGIGALATPAdlrdaPETVGKPVAGCPVRILDRNNRPVGPRVT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 500 GNIVVKLPLPPGAFSGlwKNQEAFkhlyfekFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHG 579
Cdd:PRK13383 372 GRIFVGGELAGTRYTD--GGGKAV-------VDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHP 442
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13375727 580 TVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPvaafRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:PRK13383 443 AVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQP----RDINIVSSIPRNPTGKVLRKELPG 516
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
263-655 |
3.75e-17 |
|
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: 84.44 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 263 VPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLH-WSmsSIYGL--QPGEVWWAA 339
Cdd:cd17650 65 VPIDPDYPAERLQYMLEDSGAKLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHaWR--REYELdsFPVRLLQMA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 340 SdLGWVVGHSYICYGpLLHGNTTVLYegkPVGTP-DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRF 418
Cdd:cd17650 143 S-FSFDVFAGDFARS-LLNGGTLVIC---PDEVKlDPAALYDLILKSRITLMESTPALIRPVMAY----VYRNGLDLSAM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 419 KTLFVAGERCDVETLEWSKNVF--RVPVLDHWWQTET---GSPITASCVGLGNSKTPPpgqAGKSVPGYNVMILDDNMQk 493
Cdd:cd17650 214 RLLIVGSDGCKAQDFKTLAARFgqGMRIINSYGVTEAtidSTYYEEGRDPLGDSANVP---IGRPLPNTAMYVLDERLQ- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 494 lkarclgnivvklPLPPGAFSGLW---------------KNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDV 558
Cdd:cd17650 290 -------------PQPVGVAGELYiggagvargylnrpeLTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQ 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 559 INVAGHRISAGAIEESILSHGTVADCAVVGKEDPlKGHVPL-ALCVLRKDINATEeqVLEEIVKHVRQNIGPvAAFrnaV 637
Cdd:cd17650 357 VKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEARLcAYVVAAATLNTAE--LRAFLAKELPSYMIP-SYY---V 429
|
410
....*....|....*...
gi 13375727 638 FVKQLPKTRSGKIPRSAL 655
Cdd:cd17650 430 QLDALPLTPNGKVDRRAL 447
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
473-655 |
5.21e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 84.72 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 473 GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVM 552
Cdd:PRK08974 378 GSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK---GPQVMLGYWQRPEATDEVIKD---GWLATGDIAVMDEEGFLRIV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 553 SRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAA 632
Cdd:PRK08974 452 DRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA-VKIFVVKKDPSLTE----EELITHCRRHLTGYKV 526
|
170 180
....*....|....*....|...
gi 13375727 633 FRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK08974 527 PKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
202-657 |
1.34e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.83 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 202 FASKELS--------SRIDH------VKPKVVVtasfGIEPGRRVE--------------YVPLVEEalkigqHKPDKI- 252
Cdd:PRK12467 1595 FGEQELTygelnrraNRLAHrlialgVGPEVLV----GIAVERSLEmvvgllailkaggaYVPLDPE------YPRERLa 1664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 253 ----------LIYNRPNMEAVPLAPG-RDLDWDEEMAKAQSHDCV-PVLSEHP---LYILYTSGTTGLPKGVIRPTGGYA 317
Cdd:PRK12467 1665 ymiedsgielLLTQSHLQARLPLPDGlRSLVLDQEDDWLEGYSDSnPAVNLAPqnlAYVIYTSGSTGRPKGAGNRHGALV 1744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 318 VMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLyeGKPVGTPDAGAYFRVLAEHGVAALFTAPTAI 397
Cdd:PRK12467 1745 NRLCA-TQEAYQLSAADVVLQFTSFAFDVSVWEL-FWPLINGARLVI--APPGAHRDPEQLIQLIERQQVTTLHFVPSML 1820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 398 RAIRQQDPgaALGKQYSLTRfktLFVAGERCDVETLE-WSKNVFRVPVLDHWWQTETGSPIT---ASCVGLGNSKTPPPG 473
Cdd:PRK12467 1821 QQLLQMDE--QVEHPLSLRR---VVCGGEALEVEALRpWLERLPDTGLFNLYGPTETAVDVThwtCRRKDLEGRDSVPIG 1895
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 474 QAGKSVPGYnvmILDDNMQKLKARCLGNIVVKlplppGAfsGLWKNQEAFKHLYFEKF-------PG--YYDTMDAGYMD 544
Cdd:PRK12467 1896 QPIANLSTY---ILDASLNPVPIGVAGELYLG-----GV--GLARGYLNRPALTAERFvadpfgtVGsrLYRTGDLARYR 1965
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 545 EEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDP----LKGH-VPLALCVLRKDInatEEQVLEEI 619
Cdd:PRK12467 1966 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGAngkqLVAYvVPTDPGLVDDDE---AQVALRAI 2042
|
490 500 510
....*....|....*....|....*....|....*....
gi 13375727 620 VK-HVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:PRK12467 2043 LKnHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
256-657 |
1.62e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 83.15 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 256 NRPNMEAVPLAPGRDLD-----WDEEMAKAqsHDCVP---VLSEHPLYILYTSGTTGLPKGViRPTGGYAVMLHWSMSSI 327
Cdd:PRK13388 109 HRPLLDGLDLPGVRVLDvdtpaYAELVAAA--GALTPhreVDAMDPFMLIFTSGTTGAPKAV-RCSHGRLAFAGRALTER 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 328 YGLQPGEVwwaasdlgwvvghSYICYgPLLHGNTTV------LYEGKPVGTPDAGAYFRVLA---EHGvAALFT---APT 395
Cdd:PRK13388 186 FGLTRDDV-------------CYVSM-PLFHSNAVMagwapaVASGAAVALPAKFSASGFLDdvrRYG-ATYFNyvgKPL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 396 A-IRAIRQQDPGAalgkQYSLTR-FKTlfVAGERcDVEtlEWSKNvFRVPVLDHWWQTETGSPITAScvglgnsKTPPPG 473
Cdd:PRK13388 251 AyILATPERPDDA----DNPLRVaFGN--EASPR-DIA--EFSRR-FGCQVEDGYGSSEGAVIVVRE-------PGTPPG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 474 QAGKSVPGynVMILDDNMQKLKARC--------------LGNIVVKLPlpPGAFSGLWKNQEA----FKHlyfekfpGYY 535
Cdd:PRK13388 314 SIGRGAPG--VAIYNPETLTECAVArfdahgallnadeaIGELVNTAG--AGFFEGYYNNPEAtaerMRH-------GMY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 536 DTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQv 615
Cdd:PRK13388 383 WSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDA- 461
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 13375727 616 LEEIVkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:PRK13388 462 FAAFL-AAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
273-657 |
2.18e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 82.81 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 273 WDEEMAkAQSHDCVPVLSEHP--LYILY-TSGTTGLPKGVI---RPTGGYAVMLhwsmSSIYGLQPGEVwwaasdlgwvv 346
Cdd:PRK07867 132 WADELA-AHRDAEPPFRVADPddLFMLIfTSGTSGDPKAVRcthRKVASAGVML----AQRFGLGPDDV----------- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 347 ghSYICYgPLLHGNTTVlyegkpvgtpdaGAYFRVLAEHGVAAL---FTAPTAIRAIRQQdpGAA----LGK--QYSLT- 416
Cdd:PRK07867 196 --CYVSM-PLFHSNAVM------------AGWAVALAAGASIALrrkFSASGFLPDVRRY--GATyanyVGKplSYVLAt 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 417 ------RFKTLFVA----GERCDVETLEwskNVFRVPVLDHWWQTETGSPITascvglgnsKTP--PPGQAGKSVPGYNV 484
Cdd:PRK07867 259 perpddADNPLRIVygneGAPGDIARFA---RRFGCVVVDGFGSTEGGVAIT---------RTPdtPPGALGPLPPGVAI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 485 M-----------ILDDNMQKLKARCLGNIVVklPLPPGAFSGLWKNQEAFKhlyfEKF-PGYYDTMDAGYMDEEGYLYVM 552
Cdd:PRK07867 327 VdpdtgtecppaEDADGRLLNADEAIGELVN--TAGPGGFEGYYNDPEADA----ERMrGGVYWSGDLAYRDADGYAYFA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 553 SRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIvkHVRQNIGPVAA 632
Cdd:PRK07867 401 GRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFL--AAQPDLGPKQW 478
|
410 420
....*....|....*....|....*
gi 13375727 633 FRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:PRK07867 479 PSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
127-655 |
2.26e-16 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 82.62 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSPvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 206
Cdd:PRK07514 17 DAPFIETPDG-----LRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 LSSRIDHVKPKVVVTAsfgiePGRRVEYVPLVEEAlkigqhkpdkiliyNRPNMEavPLAPGRDLDWDEEMAKA-QSHDC 285
Cdd:PRK07514 92 LDYFIGDAEPALVVCD-----PANFAWLSKIAAAA--------------GAPHVE--TLDADGTGSLLEAAAAApDDFET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 286 VPVLSEHPLYILYTSGTTGLPKGvirptggyAVMLHWSMSSiYGLQPGEVW-WAASDlgwVVGHSYicygPLLH------ 358
Cdd:PRK07514 151 VPRGADDLAAILYTSGTTGRSKG--------AMLSHGNLLS-NALTLVDYWrFTPDD---VLIHAL----PIFHthglfv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 359 -GNTTVLYEGKPVGTP--DAGAYFRVLAE----HGVAALFTaptaiRAIrqQDPGaaLGKQysLTRFKTLFVAGErcdve 431
Cdd:PRK07514 215 aTNVALLAGASMIFLPkfDPDAVLALMPRatvmMGVPTFYT-----RLL--QEPR--LTRE--AAAHMRLFISGS----- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 432 tlewsknvfrVPVLD---HWWQTETGSPI------TASCVglgNSKTP-----PPGQAGKSVPGYNVMILD-DNMQKLKA 496
Cdd:PRK07514 279 ----------APLLAethREFQERTGHAIlerygmTETNM---NTSNPydgerRAGTVGFPLPGVSLRVTDpETGAELPP 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 497 RCLGNIVVKlplPPGAFSGLW----KNQEAFKHlyfekfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIE 572
Cdd:PRK07514 346 GEIGMIEVK---GPNVFKGYWrmpeKTAEEFRA------DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 573 ESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVkhvrqniGPVAAF---RNAVFVKQLPKTRSGK 649
Cdd:PRK07514 417 GEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALK-------GRLARFkqpKRVFFVDELPRNTMGK 489
|
....*.
gi 13375727 650 IPRSAL 655
Cdd:PRK07514 490 VQKNLL 495
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
144-623 |
2.95e-16 |
|
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: 82.13 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 144 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAS 223
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 224 FGIEPGRRveyvPLVEEALkigqhkpdkiliynrPNMEAVPLAPGRDLD-WDEEMAKAQ-SHDCVPVLSEHPLYILYTSG 301
Cdd:cd05932 87 LDDWKAMA----PGVPEGL---------------ISISLPPPSAANCQYqWDDLIAQHPpLEERPTRFPEQLATLIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 302 TTGLPKGVIRPTGGYAvmlhWSMSSI---YGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYE-----------G 367
Cdd:cd05932 148 TTGQPKGVMLTFGSFA----WAAQAGiehIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAEsldtfvedvqrA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 368 KP---VGTPDAGAYF--RVLAEHGVAA---LFTAPTAIRAIRQQdpgaaLGKQYSLTRFKTLFVAGERCDVETLEWSKNV 439
Cdd:cd05932 224 RPtlfFSVPRLWTKFqqGVQDKIPQQKlnlLLKIPVVNSLVKRK-----VLKGLGLDQCRLAGCGSAPVPPALLEWYRSL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 440 fRVPVLDHWWQTETgSPITASCVGlGNSKTpppGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKN 519
Cdd:cd05932 299 -GLNILEAYGMTEN-FAYSHLNYP-GRDKI---GTVGNAGPGVEVRISED----------GEILVR---SPALMMGYYKD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 520 QEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVA-GHRISAGAIEESILSHGTVADCAVVGKEDPlkghVP 598
Cdd:cd05932 360 PEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSGLP----AP 433
|
490 500 510
....*....|....*....|....*....|....*..
gi 13375727 599 LALCVL------------RKDINATEEQVLEEIVKHV 623
Cdd:cd05932 434 LALVVLseearlradafaRAELEASLRAHLARVNSTL 470
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
127-655 |
3.17e-16 |
|
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: 82.09 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSPvTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 206
Cdd:cd05915 9 GRKEVVSRLH-TGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 LSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIgqhkpdkiliynRPNMEAVPLAPGRDLDWDEEMAKAQSH--D 284
Cdd:cd05915 88 IAYILNHAEDKVLLFDP---------NLLPLVEAIRGE------------LKTVQHFVVMDEKAPEGYLAYEEALGEeaD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 285 CVPVLSEHPLYILYTSGTTGLPKGVIRP-TGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTV 363
Cdd:cd05915 147 PVRVPERAACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 364 LYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIrqQDPGAALGKQYSLTrfkTLFVAGERCDVETLEWSKNVFRVP 443
Cdd:cd05915 227 PGP-----RLDPASLVELFDGEGVTFTAGVPTVWLAL--ADYLESTGHRLKTL---RRLVVGGSAAPRSLIARFERMGVE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 444 VLDHWWQTETGSPITAsCVGLGNSKTPPPGQAG--KSVPGYN-----VMILDDNMQKLKARclGNIVVKLPLPPGA-FSG 515
Cdd:cd05915 297 VRQGYGLTETSPVVVQ-NFVKSHLESLSEEEKLtlKAKTGLPiplvrLRVADEEGRPVPKD--GKALGEVQLKGPWiTGG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 516 LWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKG 595
Cdd:cd05915 374 YYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQ 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13375727 596 HVPLALCVLrKDINATEeqvlEEIVKHVRQNIGPVAAF-RNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd05915 452 ERPLAVVVP-RGEKPTP----EELNEHLLKAGFAKWQLpDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
127-657 |
4.26e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.08 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 206
Cdd:PRK12316 2018 EAIAVVFG------DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY----------- 2080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 lssridhvkpkVVVTASFgiePGRRVEYvpLVEEAlkiGQHkpdkILIYNRPNMEAVPLAPG---RDLDWDEEMAKAQSH 283
Cdd:PRK12316 2081 -----------VPLDPNY---PAERLAY--MLEDS---GAA----LLLTQRHLLERLPLPAGvarLPLDRDAEWADYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 284 DCVPVLSEHPL-YILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYiCYGPLLHGNTT 362
Cdd:PRK12316 2138 APAVQLAGENLaYVIYTSGSTGLPKGVAVSHGALVAHCQA-AGERYELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARV 2215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 363 VLyegKPVGTPDAGAYFRVLAEHGVAALFTAPT-----AIRAIRQQDPGAAlgkqysltrfKTLFVAGERCDVETLE-WS 436
Cdd:PRK12316 2216 LI---RDDELWDPEQLYDEMERHGVTILDFPPVylqqlAEHAERDGRPPAV----------RVYCFGGEAVPAASLRlAW 2282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 437 KNVFRVPVLDHWWQTETG-SPITASC--VGLGNSKTPPPGQAGKSVPGYnvmILDDNMQklkarclgnivvklPLPPGAF 513
Cdd:PRK12316 2283 EALRPVYLFNGYGPTEAVvTPLLWKCrpQDPCGAAYVPIGRALGNRRAY---ILDADLN--------------LLAPGMA 2345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 514 SGLWKNQEAFKHLYFEKfPG-----------------YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 576
Cdd:PRK12316 2346 GELYLGGEGLARGYLNR-PGltaerfvpdpfsasgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQ 2424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 577 SHGTVADCAVVGKEDPlkGHVPLALCVLRKDInatEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALS 656
Cdd:PRK12316 2425 AHPAVREAVVVAQDGA--SGKQLVAYVVPDDA---AEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALP 2499
|
.
gi 13375727 657 A 657
Cdd:PRK12316 2500 K 2500
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
145-656 |
7.34e-16 |
|
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: 80.43 E-value: 7.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASkelsSRIDHVkpkvvVTASF 224
Cdd:cd17653 24 TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPS----ARIQAI-----LRTSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 225 GiepgrrveyvplveealkigqhkpdKILIYNrpnmeavplapgrdlDWDEEMAkaqshdcvpvlsehplYILYTSGTTG 304
Cdd:cd17653 95 A-------------------------TLLLTT---------------DSPDDLA----------------YIIFTSGSTG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 305 LPKGVIRPTGGYAVMLhWSMSSIYGLQPG----EVWWAASDLG-WVVghsyicYGPLLHGNTTVLyegkpvgtPDAGAYF 379
Cdd:cd17653 119 IPKGVMVPHRGVLNYV-SQPPARLDVGPGsrvaQVLSIAFDACiGEI------FSTLCNGGTLVL--------ADPSDPF 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 380 RVLAEHgVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKTLFVAGERCdvetlewSKnvfrvPVLDHWWQ--------- 450
Cdd:cd17653 184 AHVART-VDALMSTPSILSTLSPQD----------FPNLKTIFLGGEAV-------PP-----SLLDRWSPgrrlynayg 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 451 -TETgspitaSCVGLGNSKTppPGQA---GKSVPGYNVMILDDNMQKLKARCLGNIVVklpLPPGAFSGLWKNQEA---- 522
Cdd:cd17653 241 pTEC------TISSTMTELL--PGQPvtiGKPIPNSTCYILDADLQPVPEGVVGEICI---SGVQVARGYLGNPALtask 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 523 FKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL-SHGTVADCAVVGKEDPLKGHV-PLa 600
Cdd:cd17653 310 FVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLqSQPEVTQAAAIVVNGRLVAFVtPE- 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 13375727 601 lcvlrkdiNATEEQVLEEIVKHVRQNIGP---VAafrnavfVKQLPKTRSGKIPRSALS 656
Cdd:cd17653 389 --------TVDVDGLRSELAKHLPSYAVPdriIA-------LDSFPLTANGKVDRKALR 432
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
295-656 |
1.05e-15 |
|
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: 80.14 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 295 YILYTSGTTGLPKGVIRPTGGyAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSY--ICYGpLLHGNTTVLYEGKPVGT 372
Cdd:cd17648 98 YAIYTSGTTGKPKGVLVEHGS-VVNLRTSLSERYFGRDNGDEAVLFFSNYVFDFFVeqMTLA-LLNGQKLVVPPDEMRFD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 373 PDagAYFRVLAEHGVAALFTAPTAIRAIRqqdpgaaLGKQYSLTRfktLFVAGERCDVETLEWSKNVFRVPVLDHWWQTE 452
Cdd:cd17648 176 PD--RFYAYINREKVTYLSGTPSVLQQYD-------LARLPHLKR---VDAAGEEFTAPVFEKLRSRFAGLIINAYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 453 TGspITascvglgNSKTPPPGQA------GKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGL---------- 516
Cdd:cd17648 244 TT--VT-------NHKRFFPGDQrfdkslGRPVRNTKCYVLNDAMK--------------RVPVGAVGELylggdgvarg 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 517 WKNQEAfkhLYFEKF----------------PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGT 580
Cdd:cd17648 301 YLNRPE---LTAERFlpnpfqteqerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 581 VADCAVVGKEDPLKGHVPlalcvLRKDINA---TEEQVLEE--IVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd17648 378 VRECAVVAKEDASQAQSR-----IQKYLVGyylPEPGHVPEsdLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
.
gi 13375727 656 S 656
Cdd:cd17648 453 P 453
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
134-658 |
1.22e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 80.25 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 134 DSPV-TNTKATFTYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRI 211
Cdd:PRK12492 39 DRPAfSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 212 DHVKPKVVVTAS-FG-----IEPGRRVEYvpLVEeaLKIGQHKP-----------DKIL----IYNRPnmEAVP----LA 266
Cdd:PRK12492 119 KDSGARALVYLNmFGklvqeVLPDTGIEY--LIE--AKMGDLLPaakgwlvntvvDKVKkmvpAYHLP--QAVPfkqaLR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 267 PGRDLdwdEEMAKAQSHDCVPVLSehplyilYTSGTTGLPKGVIRPTGG--------YAVMLHWSMSSIYGLQPG-EVWW 337
Cdd:PRK12492 193 QGRGL---SLKPVPVGLDDIAVLQ-------YTGGTTGLAKGAMLTHGNlvanmlqvRACLSQLGPDGQPLMKEGqEVMI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 338 AASDLGWVVGHSYICYGPLLHGNTTVLyegkpVGTP-DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAalgKQYSLT 416
Cdd:PRK12492 263 APLPLYHIYAFTANCMCMMVSGNHNVL-----ITNPrDIPGFIKELGKWRFSALLGLNTLFVALMDH-PGF---KDLDFS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 417 RFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETgSPItASCVGLGNSKTPppGQAGKSVPGYNVMILDDNMQKLKA 496
Cdd:PRK12492 334 ALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTET-SPV-ASTNPYGELARL--GTVGIPVPGTALKVIDDDGNELPL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 497 RCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 576
Cdd:PRK12492 410 GERGELCIK---GPQVMKGYWQQPEATAEALDAE--GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 577 SHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATeeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALS 656
Cdd:PRK12492 485 AHPKVANCAAIGVPDERSGEA-VKLFVVARDPGLS----VEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
..
gi 13375727 657 AI 658
Cdd:PRK12492 560 DI 561
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
263-657 |
2.99e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.39 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 263 VPLAPG-RDLDWDEEMAKAQSHD-CVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAAS 340
Cdd:PRK12316 3166 LPLAQGvQVLDLDRGDENYAEANpAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCW-MQQAYGLGVGDRVLQFT 3244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 341 DLGWVVGHSYIcYGPLLHGNTTVLyeGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlgkqySLTRFKT 420
Cdd:PRK12316 3245 TFSFDVFVEEL-FWPLMSGARVVL--AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAF-LEEEDAH-----RCTSLKR 3315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 421 LFVAGERCDVETLEwsKNVFRVPVLDHWWQTETGSPITASCVGLGNSKTPPpgqAGKSVPGYNVMILDDNMQKLKARCLG 500
Cdd:PRK12316 3316 IVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAVP---IGRPIANRACYILDGSLEPVPVGALG 3390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 501 NIVVK-LPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHG 579
Cdd:PRK12316 3391 ELYLGgEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHP 3470
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13375727 580 TVADCAVVGKE-DPLKGHVPLalcvlrkdiNATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:PRK12316 3471 WVREAVVLAVDgRQLVAYVVP---------EDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
290-649 |
1.16e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 76.27 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 290 SEHPLYILYTSGTTGLPKGVirptggyavmlHWSMSSIYGLQPG----------EVWWAASDLGWVVGHSYICYGPLLHG 359
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGV-----------MWRQEDIFRMLMGgadfgtgeftPSEDAHKAAAAAAGTVMFPAPPLMHG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 360 NTTVLYEGKPVGTP---------DAGAYFRVLAEHGVAALFTAPTA-----IRAIRqqDPGAalgkqYSLTRFKTLFVAG 425
Cdd:cd05924 71 TGSWTAFGGLLGGQtvvlpddrfDPEEVWRTIEKHKVTSMTIVGDAmarplIDALR--DAGP-----YDLSSLFAISSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 426 ercdvetLEWSKNVfRVPVLDHWWQ---------TETGSpitascVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLK- 495
Cdd:cd05924 144 -------ALLSPEV-KQGLLELVPNitlvdafgsSETGF------TGSGHSAGSGPETGPFTRANPDTVVLDDDGRVVPp 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 496 -ARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEK--FPGYYDTMDAGymdeeGYLYVMSRVDDVINVAGHRISAGAIE 572
Cdd:cd05924 210 gSGGVGWIARRGHIPLGYYGDEAKTAETFPEVDGVRyaVPGDRATVEAD-----GTVTLLGRGSVCINTGGEKVFPEEVE 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13375727 573 ESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGK 649
Cdd:cd05924 285 EALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGVDL----EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
127-655 |
1.59e-14 |
|
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: 76.54 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSPVTntkatfTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 206
Cdd:cd12114 2 DATAVICGDGTL------TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAY----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 lssridhvkpkVVVTASfgiEPGRRVEYvpLVEEA---LKIGQHKPDKILIYNR--PNMEAVPLAPGRDldwdEEMAKAQ 281
Cdd:cd12114 65 -----------VPVDID---QPAARREA--ILADAgarLVLTDGPDAQLDVAVFdvLILDLDALAAPAP----PPPVDVA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 282 SHDcvpvlsehPLYILYTSGTTGLPKGV-IRPTGGYAVMLhwSMSSIYGLQPGEVWWAASDLGW---VvghsYICYGPLL 357
Cdd:cd12114 125 PDD--------LAYVIFTSGSTGTPKGVmISHRAALNTIL--DINRRFAVGPDDRVLALSSLSFdlsV----YDIFGALS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 358 HGNTTVLYEGKPVGTPDAGAyfRVLAEHGV--------------AALFTAPTAIRAIRQ---------QDPGAALGKQYS 414
Cdd:cd12114 191 AGATLVLPDEARRRDPAHWA--ELIERHGVtlwnsvpallemllDVLEAAQALLPSLRLvllsgdwipLDLPARLRALAP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 415 LTRFKTLFVAgercdVETLEWSkNVFRV-PVLDHWWQTETGSPItascvglgnsktppPGQAgksvpgYNVMildDNMQK 493
Cdd:cd12114 269 DARLISLGGA-----TEASIWS-IYHPIdEVPPDWRSIPYGRPL--------------ANQR------YRVL---DPRGR 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 494 lkarclgnivvklPLPP-----------GAFSGLWKNQEAFKHLYFEKFPG--YYDTMDAGYMDEEGYLYVMSRVDDVIN 560
Cdd:cd12114 320 -------------DCPDwvpgelwiggrGVALGYLGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 561 VAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATEEQVLEE-IVKHVRQNIGPvaafRNAVFV 639
Cdd:cd12114 387 VRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRL-AAFVVPDNDGTPIAPDALRAfLAQTLPAYMIP----SRVIAL 461
|
570
....*....|....*.
gi 13375727 640 KQLPKTRSGKIPRSAL 655
Cdd:cd12114 462 EALPLTANGKVDRAAL 477
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
532-657 |
2.24e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.08 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 532 PGYYDTMDAGYMDEeGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVlrKDINAT 611
Cdd:PRK07824 233 PGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV--GDGGPA 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 13375727 612 EeqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:PRK07824 310 P--TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
136-655 |
3.41e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 75.94 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 136 PVTNTkatfTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVK 215
Cdd:PRK06018 36 PIVRT----TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 216 PKVVVTasfgiepgrRVEYVPLVEealKIGQHKP--DKILIY-NRPNMEAVPLA---------PGRDLD--W---DEEMA 278
Cdd:PRK06018 112 DRVVIT---------DLTFVPILE---KIADKLPsvERYVVLtDAAHMPQTTLKnavayeewiAEADGDfaWktfDENTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 279 KAqshdcvpvlsehplyILYTSGTTGLPKGVIrptggYAvmlHWS--MSSIYGLQPGEVWWAASDLGW-VVghsyicygP 355
Cdd:PRK06018 180 AG---------------MCYTSGTTGDPKGVL-----YS---HRSnvLHALMANNGDALGTSAADTMLpVV--------P 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 356 LLHGNT-TVLYEGKPVGTP--------DAGAYFRVLAEHGVAalFTA--PTAIRAIRQQDPGAALgkqySLTRFKTLFVA 424
Cdd:PRK06018 229 LFHANSwGIAFSAPSMGTKlvmpgaklDGASVYELLDTEKVT--FTAgvPTVWLMLLQYMEKEGL----KLPHLKMVVCG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 425 GERCDVETLEWSKNvFRVPVLDHWWQTETgSPI-TASCVGLGNSKTPPPGQ------AGKSVPGYNVMILDDNMQKL--K 495
Cdd:PRK06018 303 GSAMPRSMIKAFED-MGVEVRHAWGMTEM-SPLgTLAALKPPFSKLPGDARldvlqkQGYPPFGVEMKITDDAGKELpwD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 496 ARCLGNIVVKLPLPPGAFSGLWKNQeafkhlyFEKfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESI 575
Cdd:PRK06018 381 GKTFGRLKVRGPAVAAAYYRVDGEI-------LDD-DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 576 LSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK06018 453 VGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR----EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
87-660 |
4.46e-14 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 75.41 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 87 YKPWTKTLENKHSPSTRWFVEGMLNIcynaVDRHIENgkgDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIK 166
Cdd:PRK10946 5 FTRWPEEFARRYREKGYWQDLPLTDI----LTRHAAS---DAIAVICGE------RQFSYRELNQASDNLACSLRRQGIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 167 KGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVtASFGIEPGRRVEYVplveEALKIGQ 246
Cdd:PRK10946 72 PGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNAYASQIEPALLI-ADRQHALFSDDDFL----NTLVAEH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 247 HKPDKILIYNRPnmeavplaPGRDLD-WDEEmaKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSmS 325
Cdd:PRK10946 147 SSLRVVLLLNDD--------GEHSLDdAINH--PAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRS-V 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 326 SIYGLQPGEVwwaasdlgwvvghsYICYGPLLH-------GNTTVLYEGKPV---GTPDAGAYFRVLAEHGVAALFTAPT 395
Cdd:PRK10946 216 EICGFTPQTR--------------YLCALPAAHnypmsspGALGVFLAGGTVvlaPDPSATLCFPLIEKHQVNVTALVPP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 396 AIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDvETLewsknVFRVPVL-------------------------DHWWQ 450
Cdd:PRK10946 282 AVSLWLQA--IAEGGSRAQLASLKLLQVGGARLS-ETL-----ARRIPAElgcqlqqvfgmaeglvnytrlddsdERIFT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 451 TEtGSPITascvglgnsktpppgqagksvPGYNVMILDDNmqklkarclGNivvklPLPPG-----------AFSGLWK- 518
Cdd:PRK10946 354 TQ-GRPMS---------------------PDDEVWVADAD---------GN-----PLPQGevgrlmtrgpyTFRGYYKs 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 519 ---NQEAFKHlyfekfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKG 595
Cdd:PRK10946 398 pqhNASAFDA------NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13375727 596 HVPLALCVLRKDINATeeqvleEIVKHVRQNigPVAAFR---NAVFVKQLPKTRSGKIPRSALSAIVN 660
Cdd:PRK10946 472 EKSCAFLVVKEPLKAV------QLRRFLREQ--GIAEFKlpdRVECVDSLPLTAVGKVDKKQLRQWLA 531
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
293-648 |
1.12e-13 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 72.72 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 293 PLYILYTSGTTGLPKGVIRPTGgyAVMLH-WSMSSIYGLQPGEVwwaasdlgwvvghsYICYGPLLH------GNTTVLY 365
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQ--ALLAQaLVLAVLQAIDEGTV--------------FLNSGPLFHigtlmfTLATFHA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 366 EGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgaalgkqysltrfktlFVAGERCDVETL-------EWS 436
Cdd:cd17636 66 GGTNVFVRrvDAEEVLELIEAERCTHAFLLPPTIDQIVE-------------------LNADGLYDLSSLrsspaapEWN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 437 KNVfrvPVLDHWW--------QTETGSPITAScvGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPL 508
Cdd:cd17636 127 DMA---TVDTSPWgrkpggygQTEVMGLATFA--ALGGGAI---GGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 509 ppgAFSGLWK----NQEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADC 584
Cdd:cd17636 199 ---VMAGYWNrpevNARRTRG-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADA 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13375727 585 AVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSG 648
Cdd:cd17636 269 AVIGVPDPRWAQSVKAIVVLKPGASVTE----AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
291-655 |
1.18e-13 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 73.62 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 291 EHPLYILYTSGTTGLPKGVIrPTGGYAVMLHWSMSSIYGL-QPGEVWWAASdLGWVVGHSYIcYGPLLHGNTTVLYEGKP 369
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVM-IEHQSLVNLSHGLIKEYGItSSDRVLQFAS-IAFDVAAEEI-YVTLLSGATLVLRPEEM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 370 VGTPDA----------------GAYFRVLAEHGVAALFTAPTAIRAIrqqdpgaalgkqysltrfktlFVAGERCDVETL 433
Cdd:cd17644 183 RSSLEDfvqyiqqwqltvlslpPAYWHLLVLELLLSTIDLPSSLRLV---------------------IVGGEAVQPELV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 434 E-WSKNVF-RVPVLDHWWQTEtgSPITASCVGL-----GNSKTPPpgqAGKSVPGYNVMILDDNMQKLKARCLGNIVV-K 505
Cdd:cd17644 242 RqWQKNVGnFIQLINVYGPTE--ATIAATVCRLtqlteRNITSVP---IGRPIANTQVYILDENLQPVPVGVPGELHIgG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 506 LPLPPGAFSGLWKNQEAFKHLYFEKFPG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVAD 583
Cdd:cd17644 317 VGLARGYLNRPELTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKT 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13375727 584 CAVVGKEDPLKGHVPLALCVLRKD-INATEEqvLEEIVKHVRQNIGPVAAFrnaVFVKQLPKTRSGKIPRSAL 655
Cdd:cd17644 397 AVVIVREDQPGNKRLVAYIVPHYEeSPSTVE--LRQFLKAKLPDYMIPSAF---VVLEELPLTPNGKIDRRAL 464
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
296-650 |
2.33e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 73.80 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 296 ILYTSGTTGLPKGVirptggyavML-HWS-MSSIygLQPGEVWWAASD------------LGWVVghsyICYGPLLHGNT 361
Cdd:PRK08633 787 IIFSSGSEGEPKGV---------MLsHHNiLSNI--EQISDVFNLRNDdvilsslpffhsFGLTV----TLWLPLLEGIK 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 362 TVlYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRA-IRQQ--DPgaalgkqyslTRFKTL--FVAG-ERCDVETLEW 435
Cdd:PRK08633 852 VV-YHPDPT---DALGIAKLVAKHRATILLGTPTFLRLyLRNKklHP----------LMFASLrlVVAGaEKLKPEVADA 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 436 SKNVFRVPVLDHWWQTETGSPITASC-----VGLGNSKTPPPGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplP 509
Cdd:PRK08633 918 FEEKFGIRILEGYGATETSPVASVNLpdvlaADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG---G 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 510 PGAFSGLWKNQ----EAFKHLyfeKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESI--LSHGTVAD 583
Cdd:PRK08633 995 PQVMKGYLGDPektaEVIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELakALGGEEVV 1071
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13375727 584 CAVVGKEDPLKGHvplALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFrnaVFVKQLPKTRSGKI 650
Cdd:PRK08633 1072 FAVTAVPDEKKGE---KLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRY---FKVEALPLLGSGKL 1132
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
537-652 |
2.56e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 72.38 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 537 TMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINateeqvL 616
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEID------P 368
|
90 100 110
....*....|....*....|....*....|....*.
gi 13375727 617 EEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 652
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSR 404
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
275-655 |
5.13e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 72.05 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 275 EEMAKAQSHDCV-PVLSEHPL-YILYTSGTTGLPKGVI---RPTggyavMLHWSMSSIyglqPGEVWWAASDLGW-VVgh 348
Cdd:PRK07008 158 ETLVGAQDGDYDwPRFDENQAsSLCYTSGTTGNPKGALyshRST-----VLHAYGAAL----PDAMGLSARDAVLpVV-- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 349 syicygPLLHGNTTVL-YEGKPVGTP--------DAGAYFRVLAEHGVAalFTA--PTAIRAIRQQDPGAALgkqySLTR 417
Cdd:PRK07008 227 ------PMFHVNAWGLpYSAPLTGAKlvlpgpdlDGKSLYELIEAERVT--FSAgvPTVWLGLLNHMREAGL----RFST 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 418 FKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETgSPITASCVgLGNSKTPPPGQA--------GKSVPGYNVMILDD 489
Cdd:PRK07008 295 LRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEM-SPLGTLCK-LKWKHSQLPLDEqrkllekqGRVIYGVDMKIVGD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 490 NMQKL--KARCLGNIVVKLPlppgafsglWKNQEAFKHlyfEKFP---GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGH 564
Cdd:PRK07008 373 DGRELpwDGKAFGDLQVRGP---------WVIDRYFRG---DASPlvdGWFPTGDVATIDADGFMQITDRSKDVIKSGGE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 565 RISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRqniGPVAAFR---NAVFVKQ 641
Cdd:PRK07008 441 WISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTR----EELLAFYE---GKVAKWWipdDVVFVDA 513
|
410
....*....|....
gi 13375727 642 LPKTRSGKIPRSAL 655
Cdd:PRK07008 514 IPHTATGKLQKLKL 527
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
251-655 |
1.07e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 72.12 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 251 KILIYNRPNMEAVPLAPGR---DLDWDEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSI 327
Cdd:PRK12467 3194 KLLLTQAHLLEQLPAPAGDtalTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCW-IAEA 3272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 328 YGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLYEGKpVGTPDagAYFRVLAEHGVAALFTAPTAIRAIrqqdpgA 407
Cdd:PRK12467 3273 YELDANDRVLLFMSFSFDGAQERF-LWTLICGGCLVVRDND-LWDPE--ELWQAIHAHRISIACFPPAYLQQF------A 3342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 408 ALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF-RVPVLDHWWQTETGSPITASCVGLGNSKTPPPGQAGKSVPGYNVMI 486
Cdd:PRK12467 3343 EDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLkPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYV 3422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 487 LDDNMQklkarclgnivvklPLPPGAFSGLWKNQEAFKHLYFEK------------FPG----YYDTMDAGYMDEEGYLY 550
Cdd:PRK12467 3423 LDGQLN--------------PVPVGVAGELYIGGVGLARGYHQRpsltaerfvadpFSGsggrLYRTGDLARYRADGVIE 3488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 551 VMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKeDPLKGHVPLALCVLrkdiNATEEQVLEEIVKHVRQNIGPV 630
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP----ADPQGDWRETLRDHLAASLPDY 3563
|
410 420
....*....|....*....|....*
gi 13375727 631 AAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:PRK12467 3564 MVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
142-618 |
5.26e-12 |
|
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: 68.64 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 142 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVvt 221
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 asfgiepgrrveyvplveealkIGqhkpdkiliynrpnmeaVPLApgrdldwDEEMAkaqshdcvpvlsehplyILYTSG 301
Cdd:cd05910 79 ----------------------IG-----------------IPKA-------DEPAA-----------------ILFTSG 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 302 TTGLPKGVIRPTGGYAVMLHwSMSSIYGLQPGEVWWAASDLgwvvghsYICYGPLLhGNTTVLYEGKPV--GTPDAGAYF 379
Cdd:cd05910 96 STGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGPAL-GLTSVIPDMDPTrpARADPQKLV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 380 RVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQysLTRFKTLFVAGERCDVETLEWSKNVF--RVPVLDHWWQTETgSPI 457
Cdd:cd05910 167 GAIRQYGVSIVFGSPALLERVARY--CAQHGIT--LPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEA-LPV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 458 TA-SCVGLGNSKTPPPGQA-----GKSVPGYNVMILD---------DNMQKLKARCLGNIVVKLPL---------PPGAF 513
Cdd:cd05910 242 SSiGSRELLATTTAATSGGagtcvGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTvtptyvnrpVATAL 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 514 SGLWKNQEAFKHlyfekfpgyyDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPL 593
Cdd:cd05910 322 AKIDDNSEGFWH----------RMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPG 391
|
490 500
....*....|....*....|....*
gi 13375727 594 KGHvPLaLCVLRKDINATEEQVLEE 618
Cdd:cd05910 392 CQL-PV-LCVEPLPGTITPRARLEQ 414
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
120-661 |
1.09e-11 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 67.61 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 120 HIENGKGDKIAIIYdspvtnTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIG------A 193
Cdd:PRK04813 10 EFAQTQPDFPAYDY------LGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayipvD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 194 IHSlifggfASKELSSRIDHVKPKVVVTASfgiepgrrveyvPLVEEALKIGQHKPDKIliynrpnMEAvpLAPGRDLDW 273
Cdd:PRK04813 84 VSS------PAERIEMIIEVAKPSLIIATE------------ELPLEILGIPVITLDEL-------KDI--FATGNPYDF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 274 DEEMakaQSHDCVpvlsehplYILYTSGTTGLPKGV-IRptggYAVML---HWsMSSIYGLQPGEVWWAAS----DLGwv 345
Cdd:PRK04813 137 DHAV---KGDDNY--------YIIFTSGTTGKPKGVqIS----HDNLVsftNW-MLEDFALPEGPQFLNQApysfDLS-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 346 VGHSYICygpLLHGNTTVLYEgKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRaIRQQDPGAAlGKQY-SLTRFktLFvA 424
Cdd:PRK04813 199 VMDLYPT---LASGGTLVALP-KDM-TANFKQLFETLPQLPINVWVSTPSFAD-MCLLDPSFN-EEHLpNLTHF--LF-C 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 425 GERCDVETLEwsKNVFRVP---VLDHWWQTETGSPITASCVG---LGNSKTPPPGQAgKsvPGYNVMILDDNMQKLKARC 498
Cdd:PRK04813 269 GEELPHKTAK--KLLERFPsatIYNTYGPTEATVAVTSIEITdemLDQYKRLPIGYA-K--PDSPLLIIDEEGTKLPDGE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 499 LGNIVVKLP-LPPGAFSGLWKNQEAFKHlyFEKFPGYYdTMDAGYMDEeGYLYVMSRVDDVINVAGHRISAGAIEESILS 577
Cdd:PRK04813 344 QGEIVISGPsVSKGYLNNPEKTAEAFFT--FDGQPAYH-TGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQ 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 578 HGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 657
Cdd:PRK04813 420 SSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
....
gi 13375727 658 IVNG 661
Cdd:PRK04813 500 EVNK 503
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
476-654 |
1.66e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 67.34 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 476 GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLyfeKFPGYYDTMDAGYMdEEGYLYVMSRV 555
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR---GPSLMSGYFRDEESQDVL---AADGWLDTGDLGYL-LDGYLYITGRA 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 556 DDVINVAGHRISAGAIEESILSHGTV--ADCAVVGKEDPlKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGpVAAF 633
Cdd:PRK09192 461 KDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVQCRISDEERRGQLIHALAALVRSEFG-VEAA 538
|
170 180
....*....|....*....|.
gi 13375727 634 RNAVFVKQLPKTRSGKIPRSA 654
Cdd:PRK09192 539 VELVPPHSLPRTSSGKLSRAK 559
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
271-655 |
1.72e-11 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 67.11 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 271 LDWDEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASdlgwvvgHSY 350
Cdd:cd17656 108 LEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFAT-------CSF 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 351 -ICY----GPLLHGNTtvLYEGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaalgKQYS---LTRFKTLF 422
Cdd:cd17656 181 dVCYqeifSTLLSGGT--LYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSE-------REFInrfPTCVKHII 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 423 VAGERCDVETLewSKNVFR---VPVLDHWWQTETgSPITASCVGLGNS--KTPPpgqAGKSVPGYNVMILDDNMQKLKAR 497
Cdd:cd17656 252 TAGEQLVITNE--FKEMLHehnVHLHNHYGPSET-HVVTTYTINPEAEipELPP---IGKPISNTWIYILDQEQQLQPQG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 498 CLGNIVVK-LPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 576
Cdd:cd17656 326 IVGELYISgASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLL 405
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13375727 577 SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINatEEQVLEEIVKHVRQNIGPvAAFrnaVFVKQLPKTRSGKIPRSAL 655
Cdd:cd17656 406 NHPGVSEAVVLDKADDKGEKYLCAYFVMEQELN--ISQLREYLAKQLPEYMIP-SFF---VPLDQLPLTPNGKVDRKAL 478
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
145-669 |
3.26e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 66.36 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT--- 221
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTdet 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 -ASFGIEPG----RRVEYVPLVEEALKIGQHKPDKILIYNrPNMEAVPLAPGRDLDWDEEMAkaqshdcvpVLsehplyI 296
Cdd:PLN02860 114 cSSWYEELQndrlPSLMWQVFLESPSSSVFIFLNSFLTTE-MLKQRALGTTELDYAWAPDDA---------VL------I 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 297 LYTSGTTGLPKGVirpTGGYAVMLHWSMSSIYglqpgevwwaasdlgwVVGHS----YICYGPLLH------GNTTVLYE 366
Cdd:PLN02860 178 CFTSGTTGRPKGV---TISHSALIVQSLAKIA----------------IVGYGeddvYLHTAPLCHigglssALAMLMVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 367 GKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF-RVP 443
Cdd:PLN02860 239 ACHVLLPkfDAKAALQAIKQHNVTSMITVPAMMADLIS--LTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFpNAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 444 VLDHWWQTETGSPIT----------------ASCVGLGNSKTPPPGQA--GKSVPGYNVMILDDNMQKLkarclGNIVVK 505
Cdd:PLN02860 317 LFSAYGMTEACSSLTfmtlhdptlespkqtlQTVNQTKSSSVHQPQGVcvGKPAPHVELKIGLDESSRV-----GRILTR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 506 lplPPGAFSGLW-KNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADC 584
Cdd:PLN02860 392 ---GPHVMLGYWgQNSETASVLSND---GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 585 AVVGKEDPLKGHVPLALCVLR---------KDINATEEQVLEEIVK-HVRQnigpvaafrnavfvkqlpKTRSG-KIPRs 653
Cdd:PLN02860 466 VVVGVPDSRLTEMVVACVRLRdgwiwsdneKENAKKNLTLSSETLRhHCRE------------------KNLSRfKIPK- 526
|
570
....*....|....*.
gi 13375727 654 alSAIVNGKPYKITST 669
Cdd:PLN02860 527 --LFVQWRKPFPLTTT 540
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
143-648 |
7.10e-11 |
|
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: 65.15 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVK-HGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIfggfaSKELSSRidhvkpkvvvt 221
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFI-----NYNLSGD----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 asfgiepgrrveyvPLVEeALKIGQhkpDKILIYNrpnmeavplapgrdldwdeemakaqshdcvpvlSEHPLYILYTSG 301
Cdd:cd05937 69 --------------PLIH-CLKLSG---SRFVIVD---------------------------------PDDPAILIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 302 TTGLPKGVIRPTGGYAVMLhWSMSSIYGLQPGEVWwaasdlgwvvghsYICYgPLLHGNTTVLyegkpvgtpdagAYFRV 381
Cdd:cd05937 98 TTGLPKAAAISWRRTLVTS-NLLSHDLNLKNGDRT-------------YTCM-PLYHGTAAFL------------GACNC 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 382 LAEHGVAAL---FTAPT------AIRAIRQQDPGAALgkQYSLT----------RFKTLFVAGERCDVetleWSK--NVF 440
Cdd:cd05937 151 LMSGGTLALsrkFSASQfwkdvrDSGATIIQYVGELC--RYLLStppspydrdhKVRVAWGNGLRPDI----WERfrERF 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 441 RVPVLDHWWQTETG---------SPITASCVG---------LGNSKTP----PPGQagksvpgynvMILDDNMQKLKARC 498
Cdd:cd05937 225 NVPEIGEFYAATEGvfaltnhnvGDFGAGAIGhhglirrwkFENQVVLvkmdPETD----------DPIRDPKTGFCVRA 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 499 L----GNIVVKLPLPP-GAFSGLWKNQEAFKHLY----FEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAG 569
Cdd:cd05937 295 PvgepGEMLGRVPFKNrEAFQGYLHNEDATESKLvrdvFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTT 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 570 AIEESILSHGTVADCAVVGKEDP-LKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNigpVAAFRNAVFVKQLPKTRSG 648
Cdd:cd05937 375 EVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEESSAVPTEFTKSLLASLARKN---LPSYAVPLFLRLTEEVATT 451
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
532-660 |
1.05e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 64.25 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 532 PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAt 611
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS- 401
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 13375727 612 eeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVN 660
Cdd:PRK07445 402 ----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
476-659 |
7.77e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.94 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 476 GKSVPGYNVMILDDNMQKLKARCLGNIVVKLP-LPPG--AFSGLWKNQEAfkhlyfekfPGYYDTMDAGYMDEEGYLYVM 552
Cdd:PRK07768 363 GPPLPGLEVRVVDEDGQVLPPRGVGVIELRGEsVTPGylTMDGFIPAQDA---------DGWLDTGDLGYLTEEGEVVVC 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 553 SRVDDVINVAGHRISAGAIEESILS-HGTVADCAV-VGKEDPLK--GHVPLALCVLRKDInATEEQVLEEIVKHVRQNIG 628
Cdd:PRK07768 434 GRVKDVIIMAGRNIYPTDIERAAARvEGVRPGNAVaVRLDAGHSreGFAVAVESNAFEDP-AEVRRIRHQVAHEVVAEVG 512
|
170 180 190
....*....|....*....|....*....|...
gi 13375727 629 pvAAFRNAVFVK--QLPKTRSGKIPRSALSAIV 659
Cdd:PRK07768 513 --VRPRNVVVLGpgSIPKTPSGKLRRANAAELV 543
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
145-591 |
1.15e-09 |
|
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: 61.08 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhvkpkVVVTAsf 224
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNI------------------------PIVTV-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 225 giepgrrveYVPLVEEALKIGQHKPDKILIYNRPNmeavplapgrdldwDEEMAkaqshdCvpvlsehplyILYTSGTTG 304
Cdd:cd17639 61 ---------YATLGEDALIHSLNETECSAIFTDGK--------------PDDLA------C----------IMYTSGSTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 305 LPKGVirptggyaVMLHWSM-SSIYGLqpgevwwaasdLGWVVGH-----SYICYGPLLH-----GNTTVLYEGKPVG-- 371
Cdd:cd17639 102 NPKGV--------MLTHGNLvAGIAGL-----------GDRVPELlgpddRYLAYLPLAHifelaAENVCLYRGGTIGyg 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 372 TP-------------DAGAyFR--VLAehGVAALF-TAPTAIRA-------IRQQ------------------------- 403
Cdd:cd17639 163 SPrtltdkskrgckgDLTE-FKptLMV--GVPAIWdTIRKGVLAklnpmggLKRTlfwtayqsklkalkegpgtplldel 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 404 ---DPGAALGkqyslTRFKTLFVAGERCDVETLEWSkNVFRVPVLDHWWQTET--GSPI------TASCVGLgnsktPPP 472
Cdd:cd17639 240 vfkKVRAALG-----GRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETcaGGTVqdpgdlETGRVGP-----PLP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 473 GQAGK--SVPGYNVMILDDNMQklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLY 550
Cdd:cd17639 309 CCEIKlvDWEEGGYSTDKPPPR-------GEILIR---GPNVFKGYYKNPEKTKEAFDGD--GWFHTGDIGEFHPDGTLK 376
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 13375727 551 VMSRVDD-VINVAGHRISAGAIEESILSHGTVADCAVVGKED 591
Cdd:cd17639 377 IIDRKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPD 418
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
143-541 |
1.67e-09 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 60.91 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVI-------YMPMIPQAMYTMLACARIGAIHSLIFGGFAskELSSRIDHVK 215
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLIlsgnsieHALMALAAMYAGVPAAPVSPAYSLMSQDLA--KLKHLFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 216 PKVVVtASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPlaPGRDLDwdeEMAKAQSHDCVPVLsehply 295
Cdd:cd05921 103 PGLVF-AQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISFAELAATP--PTAAVD---AAFAAVGPDTVAKF------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 296 iLYTSGTTGLPKGVI---RPTGGYAVMlhwsMSSIYGLQPGEVWWAASDLGWvvGHSY---ICYGPLLH-GNTTVLYEGK 368
Cdd:cd05921 171 -LFTSGSTGLPKAVIntqRMLCANQAM----LEQTYPFFGEEPPVLVDWLPW--NHTFggnHNFNLVLYnGGTLYIDDGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 369 PvgTPDA-GAYFRVLAEHGVAALFTAPTA----IRAIRQQDpgaALGKQYsLTRFKTLFVAGERCDVETLEWSKNV---- 439
Cdd:cd05921 244 P--MPGGfEETLRNLREISPTVYFNVPAGwemlVAALEKDE---ALRRRF-FKRLKLMFYAGAGLSQDVWDRLQALavat 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 440 --FRVPVLDHWWQTETGsPITASCVGL----GNSKTPPPGQAGKSVPgynvmilddNMQKLKARCLGnivvklplpPGAF 513
Cdd:cd05921 318 vgERIPMMAGLGATETA-PTATFTHWPtersGLIGLPAPGTELKLVP---------SGGKYEVRVKG---------PNVT 378
|
410 420
....*....|....*....|....*...
gi 13375727 514 SGLWKNQEAFKHLYFEKfpGYYDTMDAG 541
Cdd:cd05921 379 PGYWRQPELTAQAFDEE--GFYCLGDAA 404
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
142-645 |
1.78e-09 |
|
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: 60.45 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 142 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVt 221
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 222 asfgiepgrrveyvplVEEAlkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdcvpvlsehpLYIlYTSG 301
Cdd:cd05940 81 ----------------VDAA----------------------------------------------------LYI-YTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 302 TTGLPKGvirptggyAVMLHwsmssiyglqpgEVWWAAsdlGWVVGHSyicygpLLHGNTTVLYEGKPVgtpdagaYfrv 381
Cdd:cd05940 92 TTGLPKA--------AIISH------------RRAWRG---GAFFAGS------GGALPSDVLYTCLPL-------Y--- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 382 laeHGVAALFTAPTAIRAirqqdpGA--ALGKQYSLTRF--------KTLFV-AGERC---------------------- 428
Cdd:cd05940 133 ---HSTALIVGWSACLAS------GAtlVIRKKFSASNFwddirkyqATIFQyIGELCryllnqppkpterkhkvrmifg 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 429 -----DVetleWS--KNVFRVP-VLDHWWQTETGSpitascvGLGN--SKtppPGQAGKS------VPGYNVMILD-DNM 491
Cdd:cd05940 204 nglrpDI----WEefKERFGVPrIAEFYAATEGNS-------GFINffGK---PGAIGRNpsllrkVAPLALVKYDlESG 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 492 QKL---KARCL-------GNIVVKL-PLPPgaFSGLWKNQEAFKHLY---FEKFPGYYDTMDAGYMDEEGYLYVMSRVDD 557
Cdd:cd05940 270 EPIrdaEGRCIkvprgepGLLISRInPLEP--FDGYTDPAATEKKILrdvFKKGDAWFNTGDLMRLDGEGFWYFVDRLGD 347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 558 VINVAGHRISAGAIEESILSHGTVADCAVVGKEDP-LKGHVPLALCVLRkdinATEEQVLEEIVKHVRQNIGPVAAFRNA 636
Cdd:cd05940 348 TFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQ----PNEEFDLSALAAHLEKNLPGYARPLFL 423
|
....*....
gi 13375727 637 VFVKQLPKT 645
Cdd:cd05940 424 RLQPEMEIT 432
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
143-659 |
6.63e-09 |
|
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: 58.71 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEvLEQVS-KLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGaihslifGGFASKELS---SRIDH----V 214
Cdd:cd05918 24 SLTYAE-LDRLSsRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAG-------GAFVPLDPShplQRLQEilqdT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 215 KPKVVVTasfgiepgrrveyvplveealkigqHKPDkiliynrpnmeavplapgrdldwdeemakaqshdcvpvlseHPL 294
Cdd:cd05918 96 GAKVVLT-------------------------SSPS-----------------------------------------DAA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 295 YILYTSGTTGLPKGVIRPTGGYAVMLHwSMSSIYGLQPGEVWWAASdlgwvvghSY---IC----YGPLLHGNTTVLyeg 367
Cdd:cd05918 110 YVIFTSGSTGKPKGVVIEHRALSTSAL-AHGRALGLTSESRVLQFA--------SYtfdVSileiFTTLAAGGCLCI--- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 368 kpvgTPDA---GAYFRVLAEHGVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKTLFVAGE---RCDVETleWSKnvfR 441
Cdd:cd05918 178 ----PSEEdrlNDLAGFINRLRVTWAFLTPSVARLLDPED----------VPSLRTLVLGGEaltQSDVDT--WAD---R 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 442 VPVLDHWWQTETgspiTASCVGLGNSKTPPPGQAGKSVPGyNVMILD-DNMQKLkarclgnivvklpLPPGAFSGLW--- 517
Cdd:cd05918 239 VRLINAYGPAEC----TIAATVSPVVPSTDPRNIGRPLGA-TCWVVDpDNHDRL-------------VPIGAVGELLieg 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 518 ------------KNQEAF-KHLYFEKFPGY------YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSH 578
Cdd:cd05918 301 pilargylndpeKTAAAFiEDPAWLKQEGSgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQS 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 579 GTVAD--CAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRNA--------------VFVKQL 642
Cdd:cd05918 381 LPGAKevVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKlrqrlpsymvpsvfLPLSHL 460
|
570
....*....|....*..
gi 13375727 643 PKTRSGKIPRSALSAIV 659
Cdd:cd05918 461 PLTASGKIDRRALRELA 477
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
100-657 |
1.29e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.64 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 100 PSTRWFVEgMLNicynavdrHIENGKGDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIP 179
Cdd:PRK05691 1128 PAQAWLPE-LLN--------EQARQTPERIALVWDG------GSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSP 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 180 QAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASfgiepgRRVEYVPLVEEALKIGQhkpDKILIYNRPN 259
Cdd:PRK05691 1193 QLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS------HLLERLPQAEGVSAIAL---DSLHLDSWPS 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 260 MeavplAPGRDLDWDeemakaqshdcvpvlseHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAA 339
Cdd:PRK05691 1264 Q-----APGLHLHGD-----------------NLAYVIYTSGSTGQPKGVGNTHAALAERLQW-MQATYALDDSDVLMQK 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 340 SDLGWVVGhSYICYGPLLHGNTTVLyeGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkqySLTRFK 419
Cdd:PRK05691 1321 APISFDVS-VWECFWPLITGCRLVL--AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDE-PLAA-----ACTSLR 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 420 TLFVAGERCDVEtlewsknvFRVPVLDHWWQtetgspitascVGLGNSKTPPpgQAGKSVPGYNVMIlDDNMQKLKARCL 499
Cdd:PRK05691 1392 RLFSGGEALPAE--------LRNRVLQRLPQ-----------VQLHNRYGPT--ETAINVTHWQCQA-EDGERSPIGRPL 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 500 GNIVVKL------PLPPGAF-------SGLWKNQEAFKHLYFEKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDD 557
Cdd:PRK05691 1450 GNVLCRVldaelnLLPPGVAgelciggAGLARGYLGRPALTAERFvpdplgeDGarLYRTGDRARWNADGALEYLGRLDQ 1529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 558 VINVAGHRISAGAIEESILSHGTVADCAVVGKEDpLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRnav 637
Cdd:PRK05691 1530 QVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREG-AAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIR--- 1605
|
570 580
....*....|....*....|
gi 13375727 638 fVKQLPKTRSGKIPRSALSA 657
Cdd:PRK05691 1606 -LDQMPLGPSGKLDRRALPE 1624
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
145-594 |
1.69e-08 |
|
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: 57.61 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDT--VVIYMPMIPQAMYTMLACARigaiHSLIfggfaskelssridhvkpkvvvta 222
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYA----YSLV------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 sfgiepgrrveYVPLVEealKIGqhkPDKIL-IYNRPNMEAVPLAPGRDL-DWDE--EMAKAQSHDCVPVLSEHPLYILY 298
Cdd:cd05927 59 -----------TVPLYD---TLG---PEAIEyILNHAEISIVFCDAGVKVySLEEfeKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 299 TSGTTGLPKGVIrptggyavMLHWSMSSIYglqpgevwwAASDLGWVVGHS------YICYGPLLH-----GNTTVLYEG 367
Cdd:cd05927 122 TSGTTGNPKGVM--------LTHGNIVSNV---------AGVFKILEILNKinptdvYISYLPLAHifervVEALFLYHG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 368 KPVGtpdagaYF----RVLAEHgVAALftAPT--------------AIRAIRQQDPG-------AALG-KQYSLT----- 416
Cdd:cd05927 185 AKIG------FYsgdiRLLLDD-IKAL--KPTvfpgvprvlnriydKIFNKVQAKGPlkrklfnFALNyKLAELRsgvvr 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 417 -------------------RFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVG---LGNSKTPPPGQ 474
Cdd:cd05927 256 aspfwdklvfnkikqalggNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGdtsVGHVGGPLPCA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 475 AGK--SVPGYNVMILDDNMQklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVM 552
Cdd:cd05927 336 EVKlvDVPEMNYDAKDPNPR-------GEVCIR---GPNVFSGYYKDPEKTAEALDED--GWLHTGDIGEWLPNGTLKII 403
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 13375727 553 SRVDDVINVA-GHRISAGAIEESILSHGTVADCAVVGkeDPLK 594
Cdd:cd05927 404 DRKKNIFKLSqGEYVAPEKIENIYARSPFVAQIFVYG--DSLK 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
127-654 |
1.83e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.26 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSPVTNTKATFTYKEVLEQVSKLAGVLVKHGiKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 206
Cdd:PRK05691 24 DRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 207 -----LSSRIDHVKPKVVVTASfgiepgrrveyvPLVEEALKIGQHKPDkiliyNRPNMEAV-PLAPGRDLDWDEEMAKA 280
Cdd:PRK05691 103 hhqerLLSIIADAEPRLLLTVA------------DLRDSLLQMEELAAA-----NAPELLCVdTLDPALAEAWQEPALQP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 281 qshdcvpvlsEHPLYILYTSGTTGLPKGViRPTGGYAVMLHWSMSSIYGLQPGE----VWWAA--SDLGWVVGhsyiCYG 354
Cdd:PRK05691 166 ----------DDIAFLQYTSGSTALPKGV-QVSHGNLVANEQLIRHGFGIDLNPddviVSWLPlyHDMGLIGG----LLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 355 PLLHGNTTVL-----YEGKPV----------GTPDAGAYF-------RVlAEHGVAAL--------FTAPTAIRairqQD 404
Cdd:PRK05691 231 PIFSGVPCVLmspayFLERPLrwleaiseygGTISGGPDFayrlcseRV-SESALERLdlsrwrvaYSGSEPIR----QD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 405 PGAALGKQYSLTRFK-------------TLFVAGE---------RCDVETLewSKNVFrvpvldhwwQTETGSPITaSCv 462
Cdd:PRK05691 306 SLERFAEKFAACGFDpdsffasyglaeaTLFVSGGrrgqgipalELDAEAL--ARNRA---------EPGTGSVLM-SC- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 463 glgnsktpppgqaGKSVPGYNVMILDDN-MQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfPG--YYDTMD 539
Cdd:PRK05691 373 -------------GRSQPGHAVLIVDPQsLEVLGDNRVGEIWAS---GPSIAHGYWRNPEASAKTFVEH-DGrtWLRTGD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 540 AGYMdEEGYLYVMSRVDDVINVAGHRISAGAIEESI------LSHGTVADCAVvgKEDPLKGhVPLALCVLRKDINATEE 613
Cdd:PRK05691 436 LGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVerevevVRKGRVAAFAV--NHQGEEG-IGIAAEISRSVQKILPP 511
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 13375727 614 QVLeeiVKHVRQNIGpvAAFRNAVFV------KQLPKTRSGKIPRSA 654
Cdd:PRK05691 512 QAL---IKSIRQAVA--EACQEAPSVvlllnpGALPKTSSGKLQRSA 553
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
137-655 |
3.61e-08 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 56.41 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 137 VTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIfggfaskelssridhvKP 216
Cdd:cd17645 17 VVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI----------------DP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 217 KVvvtasfgiePGRRVEYVPLVEEAlkigqhkpdKILIYNRPNMeavplapgrdldwdeemakaqshdcvpvlsehpLYI 296
Cdd:cd17645 81 DY---------PGERIAYMLADSSA---------KILLTNPDDL---------------------------------AYV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 297 LYTSGTTGLPKGVIRPTGGYAVMLHWSMSSiYGLQPGEVWWAASDLG-----WVVgHSYICYGPLLHgnttVLYEGKPVG 371
Cdd:cd17645 110 IYTSGSTGLPKGVMIEHHNLVNLCEWHRPY-FGVTPADKSLVYASFSfdasaWEI-FPHLTAGAALH----VVPSERRLD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 372 TPDAGAYFRvlaEHGVAALFTaPTairairqqdPGAALGKQYSLTRFKTLFVAGERCDVetleWSKNVFRVpvLDHWWQT 451
Cdd:cd17645 184 LDALNDYFN---QEGITISFL-PT---------GAAEQFMQLDNQSLRVLLTGGDKLKK----IERKGYKL--VNNYGPT 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 452 ETGSPITASCVGLGNSKTPppgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVklplppgAFSGLWKNQEAFKHLYFEKF 531
Cdd:cd17645 245 ENTVVATSFEIDKPYANIP----IGKPIDNTRVYILDEALQLQPIGVAGELCI-------AGEGLARGYLNRPELTAEKF 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 532 ------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDplKGHVPlALCV 603
Cdd:cd17645 314 ivhpfvPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKED--ADGRK-YLVA 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 13375727 604 LrkdINATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 655
Cdd:cd17645 391 Y---VTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
143-592 |
5.26e-08 |
|
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: 55.89 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 222
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 sfgiepgrrveyvpLVEEALKIGQHKPdkiliynrpnmeavPLAPGRDLDwdeemakaqshdcvpvlseHPLYILYTSGT 302
Cdd:cd05939 83 --------------LLDPLLTQSSTEP--------------PSQDDVNFR-------------------DKLFYIYTSGT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 303 TGLPKGvirptggyAVMLHWSMSSI-------YGLQPGEVWW--------AASDLGwvVGHSyicygpLLHGNTTVLYEg 367
Cdd:cd05939 116 TGLPKA--------AVIVHSRYYRIaagayyaFGMRPEDVVYdclplyhsAGGIMG--VGQA------LLHGSTVVIRK- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 368 kpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKQysltRFKTLFVAGERCDVetleWSKNV--FRVP-V 444
Cdd:cd05939 179 ----KFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKH----NVRLAVGNGLRPQI----WEQFVrrFGIPqI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 445 LDHWWQTETGSPI-----TASCVGLgNSKTPPpgqagKSVPGYNVMILDDNMQKLKAR---CL-----------GNIVVK 505
Cdd:cd05939 247 GEFYGATEGNSSLvnidnHVGACGF-NSRILP-----SVYPIRLIKVDEDTGELIRDSdglCIpcqpgepgllvGKIIQN 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 506 LPLPpgAFSGLWKNQEAFKHLY---FEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIeESILSHGT-V 581
Cdd:cd05939 321 DPLR--RFDGYVNEGATNKKIArdvFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEV-EGILSNVLgL 397
|
490
....*....|.
gi 13375727 582 ADCAVVGKEDP 592
Cdd:cd05939 398 EDVVVYGVEVP 408
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
132-665 |
5.44e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.05 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 132 IYDSPVTNTkatFTYKEVLEQvSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLI-FGGFASKELSS- 209
Cdd:PRK06814 650 AVEDPVNGP---LTYRKLLTG-AFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMInFSAGIANILSAc 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 210 RIDHVKpkVVVTASFGIEPGRrveYVPLVE-----------EALKIGQHKPDKILIYNRPNMEAVPLaPGRDldwdeema 278
Cdd:PRK06814 726 KAAQVK--TVLTSRAFIEKAR---LGPLIEalefgiriiylEDVRAQIGLADKIKGLLAGRFPLVYF-CNRD-------- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 279 kaqshdcvpvlSEHPLYILYTSGTTGLPKGVirptggyaVMLHWSM-SSIYGLQpGEVWWAASDLgwV-----VGHSYIC 352
Cdd:PRK06814 792 -----------PDDPAVILFTSGSEGTPKGV--------VLSHRNLlANRAQVA-ARIDFSPEDK--VfnalpVFHSFGL 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 353 YG----PLLHGNTTVLYegkpvgtPDAGAYfRVLAE--HGVAA--LFTAPTAIRA-IRQQDPgaalgkqYSLTRFKTLFV 423
Cdd:PRK06814 850 TGglvlPLLSGVKVFLY-------PSPLHY-RIIPEliYDTNAtiLFGTDTFLNGyARYAHP-------YDFRSLRYVFA 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 424 AGERCDVETLEWSKNVFRVPVLDHWWQTETgSPITA---------SCVG----LGNSKTPP-PG--QAGK-SVPGYNVMi 486
Cdd:PRK06814 915 GAEKVKEETRQTWMEKFGIRILEGYGVTET-APVIAlntpmhnkaGTVGrllpGIEYRLEPvPGidEGGRlFVRGPNVM- 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 487 lddnMQKLKARCLGNIVvklPLPPGafsglWknqeafkhlyfekfpgyYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRI 566
Cdd:PRK06814 993 ----LGYLRAENPGVLE---PPADG-----W-----------------YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMI 1043
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 567 SAGAIEESILSHGTVADCAVVGKEDPLKGHvPLALCVLRKDINAteeqvlEEIVKHVRQN-IGPVAAFRNAVFVKQLPKT 645
Cdd:PRK06814 1044 SLAAVEELAAELWPDALHAAVSIPDARKGE-RIILLTTASDATR------AAFLAHAKAAgASELMVPAEIITIDEIPLL 1116
|
570 580
....*....|....*....|
gi 13375727 646 RSGKIPRSALSAIVNGKPYK 665
Cdd:PRK06814 1117 GTGKIDYVAVTKLAEEAAAK 1136
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
532-649 |
1.34e-06 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 51.63 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 532 PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHvplALCVLRKDINAT 611
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---ALVLFTTDSELT 666
|
90 100 110
....*....|....*....|....*....|....*....
gi 13375727 612 EEQVLeeivKHVRQNIGP-VAAFRNAVFVKQLPKTRSGK 649
Cdd:PRK08043 667 REKLQ----QYAREHGVPeLAVPRDIRYLKQLPLLGSGK 701
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
142-310 |
1.70e-06 |
|
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: 51.30 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 142 ATFTYKEVLEQVSKLAGVL-VKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVv 220
Cdd:cd17632 66 ETITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 221 TASfgiepgrrVEYVPLVEEALKIGQhKPDKILIYN-RPNMEA---------VPLAP-GR-----DLDWDEEMAKAQSHD 284
Cdd:cd17632 145 AVS--------AEHLDLAVEAVLEGG-TPPRLVVFDhRPEVDAhraalesarERLAAvGIpvttlTLIAVRGRDLPPAPL 215
|
170 180
....*....|....*....|....*..
gi 13375727 285 CVPVLSEHPLYIL-YTSGTTGLPKGVI 310
Cdd:cd17632 216 FRPEPDDDPLALLiYTSGSTGTPKGAM 242
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
145-546 |
2.91e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 50.43 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI-------HSLIFGGFAskELSSRIDHVKPK 217
Cdd:PRK12582 82 TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPaapvspaYSLMSHDHA--KLKHLFDLVKPR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 218 VVVtasfgiepgrrVEYVPLVEEALKI-GQHKPDKILIYNRPNMEA-VPLA------PGRDLdwdEEMAKAQSHDCVPvl 289
Cdd:PRK12582 160 VVF-----------AQSGAPFARALAAlDLLDVTVVHVTGPGEGIAsIAFAdlaatpPTAAV---AAAIAAITPDTVA-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 290 sehplYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVwwaASDLGWVVGH----SYICYGPLLHGNTTvLY 365
Cdd:PRK12582 224 -----KYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPP---PVSLDWMPWNhtmgGNANFNGLLWGGGT-LY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 366 --EGKPVgtpdAGAY---FRVLAEHGVAALFTAPTAIRAI---RQQDP----------------GAALgKQYSLTRFKTL 421
Cdd:PRK12582 295 idDGKPL----PGMFeetIRNLREISPTVYGNVPAGYAMLaeaMEKDDalrrsffknlrlmaygGATL-SDDLYERMQAL 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 422 FVAgercdvETLEwsknvfRVPVLDHWWQTETgSPITASC---------VGLgnsktPPPGQAGKSVPgynvmilddNMQ 492
Cdd:PRK12582 370 AVR------TTGH------RIPFYTGYGATET-APTTTGThwdtervglIGL-----PLPGVELKLAP---------VGD 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 13375727 493 KLKARCLGNIVVKlplppgafsGLWKNQEAFKHLYFEKfpGYYDTMDAG-YMDEE 546
Cdd:PRK12582 423 KYEVRVKGPNVTP---------GYHKDPELTAAAFDEE--GFYRLGDAArFVDPD 466
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
145-371 |
2.81e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.42 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 145 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACAR-------IGA-------IHSLifggfASKELSSR 210
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRqnitvvtIYAslgeealCHSL-----NETEVTTV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 211 I-DHVKPKVVVTASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVplapGRDLDWDEEMAKAQShdcVPVl 289
Cdd:PLN02387 183 IcDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKL----GKENPVDPDLPSPND---IAV- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 290 sehplyILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVwwaasdlgwvvghsYICYGPLLH-----GNTTVL 364
Cdd:PLN02387 255 ------IMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPLAHilelaAESVMA 314
|
....*..
gi 13375727 365 YEGKPVG 371
Cdd:PLN02387 315 AVGAAIG 321
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
127-334 |
3.49e-05 |
|
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: 46.74 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 127 DKIAIIYDSPVTNTKA-TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLifggfask 205
Cdd:cd17647 3 ERTCVVETPSLNSSKTrSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSV-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 206 elssrIDHVKPkvvvtasfgiePGRRVEYvplveealkIGQHKPdKILIynrpNMEAVPLAPGRdldwdeemakaqshDC 285
Cdd:cd17647 75 -----IDPAYP-----------PARQNIY---------LGVAKP-RGLI----VIRAAGVVVGP--------------DS 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13375727 286 VPVLSehplyilYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGE 334
Cdd:cd17647 111 NPTLS-------FTSGSEGIPKGVLGRHFSLAYYFPW-MAKRFNLSEND 151
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
535-658 |
8.77e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 535 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHvpLALCVLRKDINATEEQ 614
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKH--LVGYLVPHQTVLAQGA 4181
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 13375727 615 VLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 658
Cdd:PRK05691 4182 LLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPAL 4225
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
476-656 |
2.49e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 44.02 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 476 GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMdEEGYLYVMSRV 555
Cdd:cd05908 317 GKPIDETDIRICDEDNKILPDGYIGHIQIR---GKNVTPGYYNNPEATAKVFTDD--GWLKTGDLGFI-RNGRLVITGRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 556 DDVI-----NVAGHRISAGAIEESILSHGTVADCAVVGKEDplKGHVPLALCVLRKDINATEEQVlEEIVKHVRQNIGpv 630
Cdd:cd05908 391 KDIIfvngqNVYPHDIERIAEELEGVELGRVVACGVNNSNT--RNEEIFCFIEHRKSEDDFYPLG-KKIKKHLNKRGG-- 465
|
170 180
....*....|....*....|....*.
gi 13375727 631 AAFRNAVFVKQLPKTRSGKIPRSALS 656
Cdd:cd05908 466 WQINEVLPIRRIPKTTSGKVKRYELA 491
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
143-358 |
2.98e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 44.20 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 222
Cdd:PTZ00216 121 YITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 223 sfgiepGRRV-EYVPLVEEALKigqhkPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQShdcvpVLSEHPL------- 294
Cdd:PTZ00216 201 ------GKNVpNLLRLMKSGGM-----PNTTIIYLDSLPASVDTEGCRLVAWTDVVAKGHS-----AGSHHPLnipennd 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13375727 295 ---YILYTSGTTGLPKGVIRPTG----GYAVMLHWSMSSIYGLQPGEVwwaasdlgwvvghsYICYGPLLH 358
Cdd:PTZ00216 265 dlaLIMYTSGTTGDPKGVMHTHGsltaGILALEDRLNDLIGPPEEDET--------------YCSYLPLAH 321
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
143-575 |
4.44e-03 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 40.03 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 143 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYtmlacARIGAIHSlifGGFASKELSSR--------IDHV 214
Cdd:cd05933 8 TLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFI-----AAVGAIFA---GGIAVGIYTTNspeacqyvAETS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 215 KPKVVVtasfgIEPGRRVEYVPLVEEALKigqhKPDKILIYNRPNMEAVP--------LAPGRDLDWDEEMAKAQSHD-- 284
Cdd:cd05933 80 EANILV-----VENQKQLQKILQIQDKLP----HLKAIIQYKEPLKEKEPnlyswdefMELGRSIPDEQLDAIISSQKpn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 285 --CVpvlsehplyILYTSGTTGLPKGV------IRPTGGYAVMlhwSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPL 356
Cdd:cd05933 151 qcCT---------LIYTSGTTGMPKGVmlshdnITWTAKAASQ---HMDLRPATVGQESVVSYLPLSHIAAQILDIWLPI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 357 LHGNTT--------------VLYEGKP---VGTP---------------DAGAYFRVLAEHGVAALFTAPTAIRAIRQQD 404
Cdd:cd05933 219 KVGGQVyfaqpdalkgtlvkTLREVRPtafMGVPrvwekiqekmkavgaKSGTLKRKIASWAKGVGLETNLKLMGGESPS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 405 PG--------------AALGkqysLTRFKTLFVAGERCDVETLEW--SKNVfrvPVLDHWWQTETGSPITAScvGLGNSK 468
Cdd:cd05933 299 PLfyrlakklvfkkvrKALG----LDRCQKFFTGAAPISRETLEFflSLNI---PIMELYGMSETSGPHTIS--NPQAYR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13375727 469 TpppGQAGKSVPGYNVMILDDNMQKLKARCL-GNIVvklplppgaFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEG 547
Cdd:cd05933 370 L---LSCGKALPGCKTKIHNPDADGIGEICFwGRHV---------FMGYLNMEDKTEEAIDED--GWLHSGDLGKLDEDG 435
|
490 500
....*....|....*....|....*....
gi 13375727 548 YLYVMSRVDDVINVA-GHRISAGAIEESI 575
Cdd:cd05933 436 FLYITGRIKELIITAgGENVPPVPIEDAV 464
|
|
| |
